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Human Metabolome Database Version 2.5

 

Showing metabocard for Thyroxine (HMDB00248)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2009-08-10 13:49:37
Accession Number HMDB00248
Secondary Accession Numbers HMDB01918
Common Name Thyroxine
Description The thyronamines function via some unknown mechanism to inhibit neuronal activity; this plays an important role in the hibernation cycles of mammals. One effect of administering the thyronamines is a severe drop in body temperature.; Iodide is actively absorbed from the bloodstream and concentrated in the thyroid follicles. (If there is a deficiency of dietary iodine, the thyroid enlarges in an attempt to trap more iodine, resulting in goitre.) Via a reaction with the enzyme thyroperoxidase, iodine is covalently bound to tyrosine residues in the thyroglobulin molecules, forming monoiodotyrosine (MIT) and diiodotyrosine (DIT). Linking two moieties of DIT produces thyroxine. Combining one particle of MIT and one particle of DIT produces triiodothyronine.; Both T3 and T4 are used to treat thyroid hormone deficiency (hypothyroidism). They are both absorbed well by the gut, so can be given orally. Levothyroxine, the most commonly used synthetic thyroxine form, is a stereoisomer of physiological thyroxine, which is metabolized more slowly and hence usually only needs once-daily administration. Natural desiccated thyroid hormones, which are derived from pig thyroid glands, are a "natural" hypothyroid treatment containing 20% T3 and traces of T2, T1 and calcitonin.; this plays an important role in the hibernation cycles of mammals. One effect of administering the thyronamines is a severe drop in body temperature.; The major hormone derived from the thyroid gland. Thyroxine is synthesized via the iodination of tyrosines (monoiodotyrosine) and the coupling of iodotyrosines (diiodotyrosine) in the thyroglobulin. Thyroxine is released from thyroglobulin by proteolysis and secreted into the blood. Thyroxine is peripherally deiodinated to form triiodothyronine which exerts a broad spectrum of stimulatory effects on cell metabolism.; The thyronamines function via some unknown mechanism to inhibit neuronal activity
Synonyms
  1. (-)-Thyroxine
  2. 3,3',5,5''-Tetraiodo-L-thyronine
  3. 3,3',5,5'-Tetraiodo-L-thyronine
  4. 3,5,3',5'-Tetraiodo-L-Thyronine
  5. 3,5,3',5'-Tetraiodothyronine
  6. 3,5,3'5'-Tetraiodo-L-thyronine
  7. DL-Thyroxin
  8. Henning
  9. L-3,5,3',5'-Tetraiodothyronine
  10. L-Thyroxin
  11. L-Thyroxine
  12. Laevothyroxinum
  13. Levothroid
  14. Levothyroxin
  15. Levothyroxine
  16. Levothyroxine sodium
  17. Levothyroxinum
  18. Levoxyl
  19. Prestwick_548
  20. Synthroid
  21. T4
  22. THX
  23. Tetraiodothyronine
  24. Tetramet
  25. Thyratabs
  26. Thyrax
  27. Thyreoideum
  28. Thyroxin
  29. Thyroxinal
  30. Thyroxine
  31. Thyroxine I 125
  32. Thyroxine iodine
  33. d-Thyroxine
Chemical IUPAC Name 2-amino-3-[4-(4-hydroxy-3,5-diiodo-phenoxy)-3,5-diiodo-phenyl]-propanoic acid
Chemical Formula C15H11I4NO4
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Amino acids and Amino Acid conjugates
Class
  • Amino Acids
Sub Class
  • NA
Family
  • Mammalian Metabolite
Species
  • phenol or hydroxyhetarene
  • diaryl ether
  • primary amine
  • primary aliphatic amine (alkylamine)
  • aryl iodide
  • carboxylic acid
  • aromatic compound
  • alpha-aminoacid
Biofunction
  • Protein synthesis, amino acid biosynthesis
Application
Source
  • Endogenous
Average Molecular Weight 776.870
Monoisotopic Molecular Weight 776.686707
Isomeric SMILES N[C@@H](CC1=CC(I)=C(OC2=CC(I)=C(O)C(I)=C2)C(I)=C1)C(O)=O
Canonical SMILES NC(CC1=CC(I)=C(OC2=CC(I)=C(O)C(I)=C2)C(I)=C1)C(O)=O
KEGG Compound ID C01829 Link Image
BioCyc ID L-THYROXINE Link Image
BiGG ID 38499 Link Image
Wikipedia Link Thyroxine Link Image
NuGOwiki Link HMDB00248 Link Image
Metagene Link HMDB00248 Link Image
METLIN ID 439 Link Image
PubChem Compound 5819 Link Image
PubChem Substance 821887 Link Image
ChEBI ID 18332 Link Image
CAS Registry Number 51-48-9
InChI Identifier InChI=1/C15H11I4NO4/c16-8-4-7(5-9(17)13(8)21)24-14-10(18)1-6(2-11(14)19)3-12(20)15(22)23/h1-2,4-5,12,21H,3,20H2,(H,22,23)/t12-/m0/s1
Synthesis Reference Martinovich, V. P.; Katok, Ya. M.; Fil'chenkov, N. A.; Sviridov, O. V. Conjugated synthesis of L-thyroxine and L-triiodothyronine. Vestsi Natsyyanal'nai Akademii Navuk Belarusi, Seryya Khimichnykh Navuk (2004), (1), 85-92.
Melting Point (Experimental) 235.5 oC
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 1.05e-07 mg/mL [MEYLAN,WM et al. (1996)]; 8.98e-03 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge 0
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity 1.15 [Predicted by ALOGPS]; 4 [Predicted by PubChem via XLOGP]; 4.12 [MEYLAN,WM & HOWARD,PH (1995)] Calculated using ALOGPS
Material Safety Data Sheet (MSDS)
MOL File Show
SDF File Show
PDB File Show
2D Structure
3D Structure
Experimental PDB ID Not Available
Experimental 1H NMR Spectrum Download Spectrum
Download FID (Bruker)
Show Experimental Conditions Link Image
Experimental 13C NMR Spectrum Not Available
Experimental 13C HSQC Spectrum Download Spectrum
Download FID (Bruker)
Show Experimental Conditions Link Image
Predicted 1H NMR Spectrum Show Image
Show Peaklist
Predicted 13C NMR Spectrum Show Image
Show Peaklist
Mass Spectrum
Low Energy
Download File
Show Experimental Conditions Link Image
Medium Energy
Download File
Show Experimental Conditions Link Image
High Energy
Download File
Show Experimental Conditions Link Image
Simplified TOCSY Spectrum Not Available
BMRB Spectrum Not Available
Cellular Location
  • Membrane (Predicted from LogP)
  • Cytoplasm
  • Extracellular
Biofluid Location
  • Blood
  • Saliva
  • Urine
Tissue Location
Tissue References
Adipose Tissue
Fibroblasts
Gonads
Intestine
Muscle
Myelin
Nerve Cells
Neuron
Placenta
Platelet
Skeletal Muscle
Spleen
Testes
Thyroid Gland
Concentrations (Normal)
Biofluid Blood
Value 0.0000144 +/- 0.0000036 uM
Age Adolescent:13-18 yrs old
Sex Female
Patient information Normal
Comments Not Available
References
  • Capo-chichi CD, Gueant JL, Lefebvre E, Bennani N, Lorentz E, Vidailhet C, Vidailhet M: Riboflavin and riboflavin-derived cofactors in adolescent girls with anorexia nervosa. Am J Clin Nutr. 1999 Apr;69(4):672-8. [PubMed Link Image]
Biofluid Blood
Value 0.32 (0.16-0.47) uM
Age Adult:>18 yrs old
Sex Both
Patient information Thyroxine iodine
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 80-82. Edited by C. Lentner, West Cadwell, N.J.: Medical education Div., Ciba-Geigy Corp., Basel, Switzerland c1981-1992.
Biofluid Blood
Value 0.00002 (0.00001-0.00003) uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Wu AHB. Tietz clinical guide to laboratory tests. 4th ed. St. Louis: Saunders/Elsevier, 2006.
Biofluid Blood
Value 0.000016 (0.0000064-0.000064) uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Gu J, Soldin OP, Soldin SJ: Simultaneous quantification of free triiodothyronine and free thyroxine by isotope dilution tandem mass spectrometry. Clin Biochem. 2007 Dec;40(18):1386-91. Epub 2007 Aug 24. [PubMed Link Image]
Biofluid Blood
Value 0.12 +/- 0.0061 uM
Age Children:1-13 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Capo-Chichi CD, Feillet F, Gueant JL, Amouzou K, Zonon N, Sanni A, Lefebvre E, Assimadi K, Vidailhet M: Concentrations of riboflavin and related organic acids in children with protein-energy malnutrition. Am J Clin Nutr. 2000 Apr;71(4):978-86. [PubMed Link Image]
Biofluid Saliva
Value 0.0 - 1.0 uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Gil'miiarova FN, Pervova IuV, Radomskaia VM, Gergel' NI, Tarasova SV: [Levels of unified metabolites and thyroid hormones in blood and oral fluid of children with minimal brain dysfunction] Biomed Khim. 2004 Mar-Apr;50(2):204-10. [PubMed Link Image]
Biofluid Urine
Value 0.00032 +/- 0.00015 umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Chandurkar V, Shik J, Randell E: Exacerbation of underlying hypothyroidism caused by proteinuria and induction of urinary thyroxine loss: case report and subsequent investigation. Endocr Pract. 2008 Jan-Feb;14(1):97-103. [PubMed Link Image]
Concentrations (Abnormal)
Biofluid Blood
Value 0.000011 +/- 0.0000016 uM
Age Adolescent:13-18 yrs old
Sex Female
Condition Anorexia nervosa
Comments Not Available
References
  • Capo-chichi CD, Gueant JL, Lefebvre E, Bennani N, Lorentz E, Vidailhet C, Vidailhet M: Riboflavin and riboflavin-derived cofactors in adolescent girls with anorexia nervosa. Am J Clin Nutr. 1999 Apr;69(4):672-8. [PubMed Link Image]
Biofluid Blood
Value 0.0000185 +/- 0.0000052 uM
Age Adult:>18 yrs old
Sex Both
Condition Hypothyroidism
Comments Not Available
References
  • Sjoberg S, Eriksson M, Nordin C: L-thyroxine treatment and neurotransmitter levels in the cerebrospinal fluid of hypothyroid patients: a pilot study. Eur J Endocrinol. 1998 Nov;139(5):493-7. [PubMed Link Image]
Biofluid Blood
Value 0.057 +/- 0.0058 uM
Age Children:1-13 yrs old
Sex Both
Comments Not Available
References
  • Capo-Chichi CD, Feillet F, Gueant JL, Amouzou K, Zonon N, Sanni A, Lefebvre E, Assimadi K, Vidailhet M: Concentrations of riboflavin and related organic acids in children with protein-energy malnutrition. Am J Clin Nutr. 2000 Apr;71(4):978-86. [PubMed Link Image]
Biofluid Urine
Value 0.0015 +/- 0.00154 umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Condition Proteinuria
Comments Not Available
References
  • Chandurkar V, Shik J, Randell E: Exacerbation of underlying hypothyroidism caused by proteinuria and induction of urinary thyroxine loss: case report and subsequent investigation. Endocr Pract. 2008 Jan-Feb;14(1):97-103. [PubMed Link Image]
Associated Disorders
Condition References
Anorexia nervosa
  • Capo-chichi CD, Gueant JL, Lefebvre E, Bennani N, Lorentz E, Vidailhet C, Vidailhet M: Riboflavin and riboflavin-derived cofactors in adolescent girls with anorexia nervosa. Am J Clin Nutr. 1999 Apr;69(4):672-8. [PubMed Link Image]
Hypothyroidism
  • Sjoberg S, Eriksson M, Nordin C: L-thyroxine treatment and neurotransmitter levels in the cerebrospinal fluid of hypothyroid patients: a pilot study. Eur J Endocrinol. 1998 Nov;139(5):493-7. [PubMed Link Image]
Proteinuria
  • Chandurkar V, Shik J, Randell E: Exacerbation of underlying hypothyroidism caused by proteinuria and induction of urinary thyroxine loss: case report and subsequent investigation. Endocr Pract. 2008 Jan-Feb;14(1):97-103. [PubMed Link Image]
OMIM ID
Pathways
Name SMPDB Link KEGG Link
Tyrosine Metabolism SMP00006 Link Image map00350 Link Image
General References
  1. Kahan IL, Varsanyi-Nagy M, Toth M, Nadrai A: The possible role of tear fluid thyroxine in keratoconus development. Exp Eye Res. 1990 Apr;50(4):339-43. [PubMed Link Image]
  2. Jagannathan NR, Tandon N, Raghunathan P, Kochupillai N: Reversal of abnormalities of myelination by thyroxine therapy in congenital hypothyroidism: localized in vivo proton magnetic resonance spectroscopy (MRS) study. Brain Res Dev Brain Res. 1998 Aug 8;109(2):179-86. [PubMed Link Image]
  3. Kurz W, Wittlinger G, Litmanovitch YI, Romanoff H, Pfeifer Y, Tal E, Sulman FG: Effect of manual lymph drainage massage on urinary excretion of neurohormones and minerals in chronic lymphedema. Angiology. 1978 Oct;29(10):764-72. [PubMed Link Image]
  4. Randolph VS: Four clinical chemistry analyses for pediatric patients: glycosylated hemoglobin, free bilirubin, sweat electrolytes, neonatal thyroxine. Am J Med Technol. 1982 Jan;48(1):15-22. [PubMed Link Image]
  5. van Wassenaer AG, Stulp MR, Valianpour F, Tamminga P, Ris Stalpers C, de Randamie JS, van Beusekom C, de Vijlder JJ: The quantity of thyroid hormone in human milk is too low to influence plasma thyroid hormone levels in the very preterm infant. Clin Endocrinol (Oxf). 2002 May;56(5):621-7. [PubMed Link Image]
  6. Etling N, Gehin-Fouque F, Vielh JP, Gautray JP: The iodine content of amniotic fluid and placental transfer of iodinated drugs. Obstet Gynecol. 1979 Mar;53(3):376-80. [PubMed Link Image]
  7. Zenovko EI, Pavlov BA, Koreshkov GG, Gudukina GN, Sonkina EG: [Hypothalamo-pituitary-thyroid system in patients with rheumatoid arthritis] Ter Arkh. 1998;70(1):49-52. [PubMed Link Image]
  8. Hays MT, McGuire RA, Hoogeveen JT, Diezeraad KN: Measurement method for radioactive thyroxine, triiodothyronine, iodide, and iodoprotein in samples with low activity. J Nucl Med. 1980 Mar;21(3):225-32. [PubMed Link Image]
  9. Benvenga S, Alesci S, Trimarchi F: High-density lipoprotein-facilitated entry of thyroid hormones into cells: a mechanism different from the low-density lipoprotein-facilitated entry. Thyroid. 2002 Jul;12(7):547-56. [PubMed Link Image]
  10. Gil'miiarova FN, Pervova IuV, Radomskaia VM, Gergel' NI, Tarasova SV: [Levels of unified metabolites and thyroid hormones in blood and oral fluid of children with minimal brain dysfunction] Biomed Khim. 2004 Mar-Apr;50(2):204-10. [PubMed Link Image]
  11. Hausman GJ, Wright JT, Latimer A, Watson R, Martin RJ: The influence of human growth hormone (GH) and thyroxine (T4) on the differentiation of adipose tissue in the fetus. Obes Res. 1993 Sep;1(5):345-56. [PubMed Link Image]
  12. Gil-Loyzaga P, Remezal M, Mollicone R, Ibanez A, Oriol R: H and B human blood-group antigen expression in cochlear hair cells is modulated by thyroxine. Cell Tissue Res. 1994 May;276(2):239-43. [PubMed Link Image]
  13. Escobar-Morreale HF, Botella-Carretero JI, Gomez-Bueno M, Galan JM, Barrios V, Sancho J: Thyroid hormone replacement therapy in primary hypothyroidism: a randomized trial comparing L-thyroxine plus liothyronine with L-thyroxine alone. Ann Intern Med. 2005 Mar 15;142(6):412-24. [PubMed Link Image]
  14. Bode HH, Vanjonack WJ, Crawford JD: Mitigation of cretinism by breast-feeding. Pediatrics. 1978 Jul;62(1):13-6. [PubMed Link Image]
  15. Marks P, Anderson J, Vincent R: Aldosterone in myxoedema. Lancet. 1978 Dec 16;2(8103):1277-8. [PubMed Link Image]
  16. Sutherland RL, Simpson-Morgan MW: The thyroxine-binding properties of serum proteins. A competitive binding technique employing sephadex G-25. J Endocrinol. 1975 Jun;65(3):319-32. [PubMed Link Image]
  17. Braley-Mullen H, Sharp GC: A thyroxine-containing thyroglobulin peptide induces both lymphocytic and granulomatous forms of experimental autoimmune thyroiditis. J Autoimmun. 1997 Dec;10(6):531-40. [PubMed Link Image]
  18. Raghu P, Reddy GB, Sivakumar B: Inhibition of transthyretin amyloid fibril formation by 2,4-dinitrophenol through tetramer stabilization. Arch Biochem Biophys. 2002 Apr 1;400(1):43-7. [PubMed Link Image]
  19. Hekimsoy Z, Oktem IK: Serum creatine kinase levels in overt and subclinical hypothyroidism. Endocr Res. 2005;31(3):171-5. [PubMed Link Image]
  20. Wikipedia Link Image
Metabolic Enzymes
  1. Thyroid peroxidase precursor
  2. Solute carrier organic anion transporter family member 1C1
  3. Solute carrier organic anion transporter family member 1B1
  4. Type I iodothyronine deiodinase
  5. Type II iodothyronine deiodinase
  6. Transthyretin precursor
  7. Thyroxine-binding globulin precursor
  8. 4F2 cell-surface antigen heavy chain
  9. Type III iodothyronine deiodinase
Enzyme 1 [top]
Enzyme 1 ID 5508
Enzyme 1 Name Thyroid peroxidase precursor
Enzyme 1 Synonyms
  1. TPO
Enzyme 1 Gene Name TPO
Enzyme 1 Protein Sequence >Thyroid peroxidase precursor
MRALAVLSVTLVMACTEAFFPFISRGKELLWGKPEESRVSSVLEESKRLVDTAMYATMQR
NLKKRGILSPAQLLSFSKLPEPTSGVIARAAEIMETSIQAMKRKVNLKTQQSQHPTDALS
EDLLSIIANMSGCLPYMLPPKCPNTCLANKYRPITGACNNRDHPRWGASNTALARWLPPV
YEDGFSQPRGWNPGFLYNGFPLPPVREVTRHVIQVSNEVVTDDDRYSDLLMAWGQYIDHD
IAFTPQSTSKAAFGGGADCQMTCENQNPCFPIQLPEEARPAAGTACLPFYRSSAACGTGD
QGALFGNLSTANPRQQMNGLTSFLDASTVYGSSPALERQLRNWTSAEGLLRVHARLRDSG
RAYLPFVPPRAPAACAPEPGIPGETRGPCFLAGDGRASEVPSLTALHTLWLREHNRLAAA
LKALNAHWSADAVYQEARKVVGALHQIITLRDYIPRILGPEAFQQYVGPYEGYDSTANPT
VSNVFSTAAFRFGHATIHPLVRRLDASFQEHPDLPGLWLHQAFFSPWTLLRGGGLDPLIR
GLLARPAKLQVQDQLMNEELTERLFVLSNSSTLDLASINLQRGRDHGLPGYNEWREFCGL
PRLETPADLSTAIASRSVADKILDLYKHPDNIDVWLGGLAENFLPRARTGPLFACLIGKQ
MKALRDGDWFWWENSHVFTDAQRRELEKHSLSRVICDNTGLTRVPMDAFQVGKFPEDFES
CDSIPGMNLEAWRETFPQDDKCGFPESVENGDFVHCEESGRRVLVYSCRHGYELQGREQL
TCTQEGWDFQPPLCKDVNECADGAHPPCHASARCRNTKGGFQCLCADPYELGDDGRTCVD
SGRLPRATWISMSLAALLIGGFAGLTSTVICRWTRTGTKSTLPISETGGGTPELRCGKHQ
AVGTSPQRAAAQDSEQESAGMEGRDTHRLPRAL
Enzyme 1 Number of Residues 933
Enzyme 1 Molecular Weight 102932
Enzyme 1 Theoretical pI 6.75
Enzyme 1 GO Classification
Function
  • antioxidant activity
  • binding
  • calcium ion binding
  • cation binding
  • ion binding
  • peroxidase activity
Process
  • cellular metabolism
  • metabolism
  • oxygen and reactive oxygen species metabolism
  • physiological process
  • response to oxidative stress
Component
Enzyme 1 General Function Not Available
Enzyme 1 Specific Function Iodination and coupling of the hormonogenic tyrosines in thyroglobulin to yield the thyroid hormones T(3) and T(4)
Enzyme 1 Pathways
Enzyme 1 Reactions
  • iodide + H2O2 = iodine + 2 H2O
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • 1-14
Enzyme 1 Transmembrane Regions
  • 847-871
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 339867 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID P07202 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name PERT_HUMAN Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >2802 bp
ATGAGAGCGCTCGCTGTGCTGTCTGTCACGCTGGTTATGGCCTGCACAGAAGCCTTCTTC
CCCTTCATCTCGAGAGGGAAAGAACTCCTTTGGGGAAAGCCTGAGGAGTCTCGTGTCTCT
AGCGTCTTGGAGGAAAGCAAGCGCCTGGTGGACACCGCCATGTACGCCACGATGCAGAGA
AACCTCAAGAAAAGAGGAATCCTTTCTCCAGCTCAGCTTCTGTCTTTTTCCAAACTTCCT
GAGCCAACAAGCGGAGTGATTGCCCGAGCAGCAGAGATAATGGAAACATCAATACAAGCG
ATGAAAAGAAAAGTCAACCTGAAAACTCAACAATCACAGCATCCAACGGATGCTTTATCA
GAAGATCTGCTGAGCATCATTGCAAACATGTCTGGATGTCTCCCTTACATGCTGCCCCCA
AAATGCCCAAACACTTGCCTGGCGAACAAATACAGGCCCATCACAGGAGCTTGCAACAAC
AGAGACCACCCCAGATGGGGCGCCTCCAACACGGCCCTGGCACGATGGCTCCCTCCAGTC
TATGAGGACGGCTTCAGTCAGCCCCGAGGCTGGAACCCCGGCTTCTTGTACAACGGGTTC
CCACTGCCCCCGGTCCGGGAGGTGACAAGACATGTCATTCAAGTTTCAAATGAGGTTGTC
ACAGATGATGACCGCTATTCTGACCTCCTGATGGCATGGGGACAATACATCGACCACGAC
ATCGCGTTCACACCACAGAGCACCAGCAAAGCTGCCTTCGGGGGAGGGGCTGACTGCCAG
ATGACTTGTGAGAACCAAAACCCATGTTTTCCCATACAACTCCCGGAGGAGGCCCGGCCG
GCCGCGGGCACCGCCTGTCTGCCCTTCTACCGCTCTTCGGCCGCCTGCGGCACCGGGGAC
CAAGGCGCGCTCTTTGGGAACCTGTCCACGGCCAACCCGCGGCAGCAGATGAACGGGTTG
ACCTCGTTCCTGGACGCGTCCACCGTGTATGGCAGCTCCCCGGCCCTAGAGAGGCAGCTG
CGGAACTGGACCAGTGCCGAAGGGCTGCTCCGCGTCCACGCGCGCCTCCGGGACTCCGGC
CGCGCCTACCTGCCCTTCGTGCCGCCACGGCGGCCTGCGGCCTGTGCGCCCGAGCCCGGC
ATCCCCGGAGAGACCCGCGGGCCCTGCTTCCTGGCCGGAGACGGCCGCGCCAGCGAGGTC
CCCTCCCTGACGGCACTGCACACGCTGTGGCTGCGCGAGCACAACCGCCTGGCCGCGGCG
CTCAAGGCCCTCAATGCGCACTGGAGCGCGGACGCCGTGTACCAGGAGGCGCGCAAGGTC
GTGGGCGCTCTGCACCAGATCATCACCCTGAGGGATTACATCCCCAGGATCCTGGGACCC
GAGGCCTTCCAGCAGTACGTGGGTCCCTATGAAGGCTATGACTCCACCGCCAACCCCACT
GTGTCCAACGTGTTCTCCACAGCCGCCTTCCGCTTCGGCCATGCCACGATCCACCCGCTG
GTGAGGAGGCTGGACGCCAGCTTCCAGGAGCACCCCGACCTGCCCGGGCTGTGGCTGCAC
CAGGCTTTCTTCAGCCCATGGACATTACTCCGTGGAGGTGGTTTGGACCCACTAATACGA
GGCCTTCTTGCAAGACCAGCCAAACTGCAGGTGCAGGATCAGCTGATGAACGAGGAGCTG
ACGGAAAGGCTCTTTGTGCTGTCCAATTCCAGCACCTTGGATCTGGCGTCCATCAACCTG
CAGAGGGGCCGGGACCACGGGCTGCCAGGTTACAATGAGTGGAGGGAGTTCTGCGGCCTG
CCTCGCCTGGAGACCCCCGCTGACCTGAGCACAGCCATCGCCAGCAGGAGCGTGGCCGAC
AAGATCCTGGACTTGTACAAGCATCCTGACAACATCGATGTCTGGCTGGGAGGCTTAGCT
GAAAACTTCCTCCCCAGGGCTCGGACAGGGCCCCTGTTTGCCTGTCTCATTGGGAAGCAG
ATGAAGGCTCTGCGGGATGGTGACTGGTTTTGGTGGGAGAACAGCCACGTCTTCACGGAT
GCACAGAGGCGTGAGCTGGAGAAGCACTCCCTGTCTCGGGTCATCTGTGACAACACTGGC
CTCACCAGGGTGCCCATGGATGCCTTCCAAGTCGGCAAATTCCCTGAAGACTTTGAGTCT
TGTGACAGCATCCCTGGCATGAACCTGGAGGCCTGGAGGGAAACCTTTCCTCAAGACGAC
AAGTGTGGCTTCCCAGAGAGCGTGGAGAATGGGGACTTTGTGCACTGTGAGGAGTCTGGG
AGGCGCGTGCTGGTGTATTCCTGCCGGCACGGGTATGAGCTCCAAGGCCGGGAGCAGCTC
ACTTGCACCCAGGAAGGATGGGATTTCCAGCCTCCCCTCTGCAAAGATGTGAACGAGTGT
GCAGACGGTGCCCACCCCCCCTGCCACGCCTCTGCGAGGTGCAGAAACACCAAAGGCGGC
TTCCAGTGTCTCTGCGCGGACCCCTACGAGTTAGGAGACGATGGGAGAACCTGCGTAGAC
TCCGGGAGGCTCCCTCGGGCGACTTGGATCTCCATGTCGCTGGCTGCTCTGCTGATCGGA
GGCTTCGCAGGTCTCACCTCGACGGTGATTTGCAGGTGGACACGCACTGGCACTAAATCC
ACACTGCCCATCTCGGAGACAGGCGGAGGAACTCCCGAGCTGAGATGCGGAAAGCACCAG
GCCGTAGGGACCTCACCGCAGCGGGCCGCAGCTCAGGACTCGGAGCAGGAGAGTGCTGGG
ATGGAAGGCCGGGATACTCACAGGCTGCCGAGAGCCCTCTGA
Enzyme 1 GenBank Gene ID J02969 Link Image
Enzyme 1 GeneCard ID TPO Link Image
Enzyme 1 GenAtlas ID TPO Link Image
Enzyme 1 HGNC ID HGNC:12015 Link Image
Enzyme 1 Chromosome Location 2
Enzyme 1 Locus 2p25
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Kimura S, Kotani T, McBride OW, Umeki K, Hirai K, Nakayama T, Ohtaki S: Human thyroid peroxidase: complete cDNA and protein sequence, chromosome mapping, and identification of two alternately spliced mRNAs. Proc Natl Acad Sci U S A. 1987 Aug;84(16):5555-9. [PubMed Link Image]
  2. Libert F, Ruel J, Ludgate M, Swillens S, Alexander N, Vassart G, Dinsart C: Complete nucleotide sequence of the human thyroperoxidase-microsomal antigen cDNA. Nucleic Acids Res. 1987 Aug 25;15(16):6735. [PubMed Link Image]
  3. Kimura S, Hong YS, Kotani T, Ohtaki S, Kikkawa F: Structure of the human thyroid peroxidase gene: comparison and relationship to the human myeloperoxidase gene. Biochemistry. 1989 May 16;28(10):4481-9. [PubMed Link Image]
  4. Barnett PS, Banga JP, Watkins J, Huang GC, Gluckman DR, Page MJ, McGregor AM: Nucleotide sequence of the alternatively spliced human thyroid peroxidase cDNA, TPO-2. Nucleic Acids Res. 1990 Feb 11;18(3):670. [PubMed Link Image]
  5. Ferrand M, Le Fourn V, Franc JL: Increasing diversity of human thyroperoxidase generated by alternative splicing. Characterized by molecular cloning of new transcripts with single- and multispliced mRNAs. J Biol Chem. 2003 Feb 7;278(6):3793-800. Epub 2002 Nov 25. [PubMed Link Image]
  6. Seto P, Hirayu H, Magnusson RP, Gestautas J, Portmann L, DeGroot LJ, Rapoport B: Isolation of a complementary DNA clone for thyroid microsomal antigen. Homology with the gene for thyroid peroxidase. J Clin Invest. 1987 Oct;80(4):1205-8. [PubMed Link Image]
  7. Zanelli E, Henry M, Charvet B, Malthiery Y: Evidence for an alternate splicing in the thyroperoxidase messenger from patients with Graves' disease. Biochem Biophys Res Commun. 1990 Jul 31;170(2):735-41. [PubMed Link Image]
  8. Bikker H, Vulsma T, Baas F, de Vijlder JJ: Identification of five novel inactivating mutations in the human thyroid peroxidase gene by denaturing gradient gel electrophoresis. Hum Mutat. 1995;6(1):9-16. [PubMed Link Image]
  9. Bikker H, Baas F, De Vijlder JJ: Molecular analysis of mutated thyroid peroxidase detected in patients with total iodide organification defects. J Clin Endocrinol Metab. 1997 Feb;82(2):649-53. [PubMed Link Image]
  10. Santos CL, Bikker H, Rego KG, Nascimento AC, Tambascia M, De Vijlder JJ, Medeiros-Neto G: A novel mutation in the TPO gene in goitrous hypothyroid patients with iodide organification defect. Clin Endocrinol (Oxf). 1999 Aug;51(2):165-72. [PubMed Link Image]
  11. Pannain S, Weiss RE, Jackson CE, Dian D, Beck JC, Sheffield VC, Cox N, Refetoff S: Two different mutations in the thyroid peroxidase gene of a large inbred Amish kindred: power and limits of homozygosity mapping. J Clin Endocrinol Metab. 1999 Mar;84(3):1061-71. [PubMed Link Image]
  12. Kotani T, Umeki K, Yamamoto I, Maesaka H, Tachibana K, Ohtaki S: A novel mutation in the human thyroid peroxidase gene resulting in a total iodide organification defect. J Endocrinol. 1999 Feb;160(2):267-73. [PubMed Link Image]
  13. Bakker B, Bikker H, Vulsma T, de Randamie JS, Wiedijk BM, De Vijlder JJ: Two decades of screening for congenital hypothyroidism in The Netherlands: TPO gene mutations in total iodide organification defects (an update). J Clin Endocrinol Metab. 2000 Oct;85(10):3708-12. [PubMed Link Image]
  14. Ambrugger P, Stoeva I, Biebermann H, Torresani T, Leitner C, Gruters A: Novel mutations of the thyroid peroxidase gene in patients with permanent congenital hypothyroidism. Eur J Endocrinol. 2001 Jul;145(1):19-24. [PubMed Link Image]
  15. Umeki K, Kotani T, Kawano J, Suganuma T, Yamamoto I, Aratake Y, Furujo M, Ichiba Y: Two novel missense mutations in the thyroid peroxidase gene, R665W and G771R, result in a localization defect and cause congenital hypothyroidism. Eur J Endocrinol. 2002 Apr;146(4):491-8. [PubMed Link Image]
  16. Niu DM, Hwang B, Chu YK, Liao CJ, Wang PL, Lin CY: High prevalence of a novel mutation (2268 insT) of the thyroid peroxidase gene in Taiwanese patients with total iodide organification defect, and evidence for a founder effect. J Clin Endocrinol Metab. 2002 Sep;87(9):4208-12. [PubMed Link Image]
  17. Wu JY, Shu SG, Yang CF, Lee CC, Tsai FJ: Mutation analysis of thyroid peroxidase gene in Chinese patients with total iodide organification defect: identification of five novel mutations. J Endocrinol. 2002 Mar;172(3):627-35. [PubMed Link Image]
  18. Rivolta CM, Esperante SA, Gruneiro-Papendieck L, Chiesa A, Moya CM, Domene S, Varela V, Targovnik HM: Five novel inactivating mutations in the thyroid peroxidase gene responsible for congenital goiter and iodide organification defect. Hum Mutat. 2003 Sep;22(3):259. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 5689
Enzyme 2 Name Solute carrier organic anion transporter family member 1C1
Enzyme 2 Synonyms
  1. Solute carrier family 21 member 14
  2. Organic anion transporter F
  3. OATP-F
  4. Organic anion-transporting polypeptide 14
  5. Organic anion transporter polypeptide-related protein 5
  6. OAT-RP-5
  7. OATPRP5
Enzyme 2 Gene Name SLCO1C1
Enzyme 2 Protein Sequence >Solute carrier organic anion transporter family member 1C1
MDTSSKENIQLFCKTSVQPVGRPSFKTEYPSSEEKQPCCGELKVFLCALSFVYFAKALAE
GYLKSTITQIERRFDIPSSLVGVIDGSFEIGNLLVITFVSYFGAKLHRPKIIGAGCVIMG
VGTLLIAMPQFFMEQYKYERYSPSSNSTLSISPCLLESSSQLPVSVMEKSKSKISNECEV
DTSSSMWIYVFLGNLLRGIGETPIQPLGIAYLDDFASEDNAAFYIGCVQTVAIIGPIFGF
LLGSLCAKLYVDIGFVNLDHITITPKDPQWVGAWWLGYLIAGIISLLAAVPFWYLPKSLP
RSQSREDSNSSSEKSKFIIDDHTDYQTPQGENAKIMEMARDFLPSLKNLFGNPVYFLYLC
TSTVQFNSLFGMVTYKPKYIEQQYGQSSSRANFVIGLINIPAVALGIFSGGIVMKKFRIS
VCGAAKLYLGSSVFGYLLFLSLFALGCENSDVAGLTVSYQGTKPVSYHERALFSDCNSRC
KCSETKWEPMCGENGITYVSACLAGCQTSNRSGKNIIFYNCTCVGIAASKSGNSSGIVGR
CQKDNGCPQMFLYFLVISVITSYTLSLGGIPGYILLLRCIKPQLKSFALGIYTLAIRVLA
GIPAPVYFGVLIDTSCLKWGFKRCGSRGSCRLYDSNVFRHIYLGLTVILGTVSILLSIAV
LFILKKNYVSKHRSFITKRERTMVSTRFQKENYTTSDHLLQPNYWPGKETQL
Enzyme 2 Number of Residues 712
Enzyme 2 Molecular Weight 78697
Enzyme 2 Theoretical pI 8.59
Enzyme 2 GO Classification
Function
  • transporter activity
Process
  • cellular physiological process
  • physiological process
  • transport
Component
  • cell
  • integral to membrane
  • intrinsic to membrane
  • membrane
Enzyme 2 General Function Not Available
Enzyme 2 Specific Function Mediates the Na(+)-independent high affinity transport of organic anions such as the thyroid hormones thyroxine (T4) and rT3. Other potential substrates, such as triiodothyronine (T3), 17-beta-glucuronosyl estradiol, estrone-3-sulfate and sulfobromophthalein (BSP) are transported with much lower efficiency
Enzyme 2 Pathways Not Available
Enzyme 2 Reactions Not Available
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • None
Enzyme 2 Transmembrane Regions
  • 80-100 111-131 222-242 270-290 353-373 393-413 427-447 550-570 592-612 643-663
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 7839587 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID Q9NYB5 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name SO1C1_HUMAN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >2139 bp
ATGGACACTTCATCCAAAGAAAATATCCAGTTGTTCTGCAAAACTTCAGTGCAACCTGTT
GGAAGGCCTTCTTTTAAAACAGAATATCCCTCCTCAGAAGAAAAGCAACCATGCTGTGGT
GAACTAAAGGTGTTCTTGTGTGCCTTGTCTTTTGTTTACTTTGCCAAAGCATTGGCAGAA
GGCTATCTGAAGAGCACCATCACTCAGATAGAGAGAAGGTTTGATATCCCTTCTTCACTG
GTGGGAGTTATTGATGGTAGTTTTGAAATTGGGAATCTCTTAGTTATAACATTTGTTAGC
TACTTTGGAGCCAAACTTCACAGGCCAAAAATAATTGGAGCAGGGTGTGTAATCATGGGA
GTTGGAACACTGCTCATTGCAATGCCTCAGTTCTTCATGGAGCAGTACAAATATGAGAGA
TATTCTCCTTCCTCCAATTCCACTCTCAGCATCTCTCCGTGTCTCCTAGAGTCAAGCAGT
CAATTACCAGTTTCAGTTATGGAAAAATCAAAATCCAAAATAAGTAACGAATGTGAAGTG
GACACTAGCTCTTCCATGTGGATTTATGTTTTCCTGGGCAATCTTCTTCGTGGAATAGGA
GAAACTCCCATTCAGCCTTTGGGCATTGCCTACCTGGATGATTTTGCCAGTGAAGACAAT
GCAGCTTTCTATATTGGGTGTGTGCAGACGGTTGCAATTATAGGACCAATCTTTGGTTTC
CTGTTAGGCTCATTATGTGCCAAACTATATGTTGACATTGGCTTTGTAAACCTAGATCAC
ATAACCATTACCCCAAAAGATCCCCAGTGGGTAGGAGCCTGGTGGCTTGGCTATCTAATA
GCAGGAATCATAAGTCTTCTTGCAGCTGTGCCTTTCTGGTATTTACCAAAGAGTTTACCA
AGATCCCAAAGTAGAGAGGATTCTAATTCTTCCTCTGAGAAATCCAAGTTTATTATAGAT
GATCACACAGACTACCAAACACCCCAGGGAGAAAATGCAAAAATAATGGAAATGGCAAGA
GATTTTCTTCCATCACTGAAGAATCTTTTTGGAAACCCAGTATACTTCCTATATTTATGT
ACAAGCACTGTTCAGTTCAATTCTCTGTTCGGCATGGTGACGTACAAACCAAAGTACATT
GAGCAGCAGTATGGACAGTCATCCTCCAGGGCCAACTTTGTGATCGGGCTCATCAACATT
CCAGCAGTGGCCCTTGGAATATTCTCTGGGGGGATAGTTATGAAAAAATTCAGAATCAGT
GTGTGTGGAGCTGCAAAACTCTACTTGGGATCATCTGTCTTTGGTTACCTCCTATTTCTT
TCCCTGTTTGCACTGGGCTGTGAAAATTCTGATGTGGCAGGACTAACTGTCTCCTACCAA
GGAACCAAACCTGTCTCTTATCATGAACGAGCTCTCTTTTCAGATTGCAACTCAAGATGC
AAATGTTCAGAGACAAAATGGGAACCCATGTGCGGTGAAAATGGAATCACATATGTATCA
GCTTGTCTTGCTGGTTGTCAAACCTCCAACAGGAGTGGAAAAAATATTATATTTTACAAC
TGCACTTGTGTGGGAATTGCAGCTTCTAAATCCGGAAATTCCTCAGGCATAGTGGGAAGA
TGTCAGAAAGACAATGGATGTCCCCAAATGTTTCTGTATTTCCTTGTAATTTCAGTCATC
ACATCCTATACTTTATCCCTAGGTGGCATACCTGGATACATATTACTTCTGAGGTGCATT
AAGCCACAGCTTAAGTCTTTTGCCTTGGGTATCTACACATTAGCAATAAGAGTTCTTGCA
GGAATCCCAGCTCCAGTGTATTTTGGAGTTTTGATTGATACTTCATGCCTCAAATGGGGA
TTTAAAAGATGTGGAAGTAGAGGATCATGCAGATTATATGATTCAAATGTCTTCAGACAT
ATATATCTGGGACTAACTGTGATACTGGGCACAGTGTCAATTCTCCTAAGCATTGCAGTA
CTTTTCATTTTAAAGAAAAATTATGTTTCAAAACACAGAAGTTTTATAACCAAGAGAGAA
AGAACAATGGTGTCTACAAGATTCCAAAAGGAAAATTACACTACAAGTGATCATCTGCTA
CAACCCAACTACTGGCCAGGCAAGGAAACTCAACTTTAG
Enzyme 2 GenBank Gene ID AF260704 Link Image
Enzyme 2 GeneCard ID SLCO1C1 Link Image
Enzyme 2 GenAtlas ID SLCO1C1 Link Image
Enzyme 2 HGNC ID HGNC:13819 Link Image
Enzyme 2 Chromosome Location 12
Enzyme 2 Locus 12p12.2
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Pizzagalli F, Hagenbuch B, Stieger B, Klenk U, Folkers G, Meier PJ: Identification of a novel human organic anion transporting polypeptide as a high affinity thyroxine transporter. Mol Endocrinol. 2002 Oct;16(10):2283-96. [PubMed Link Image]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 5692
Enzyme 3 Name Solute carrier organic anion transporter family member 1B1
Enzyme 3 Synonyms
  1. Solute carrier family 21 member 6
  2. Sodium-independent organic anion- transporting polypeptide 2
  3. OATP 2
  4. Liver-specific organic anion transporter 1
  5. LST-1
  6. OATP-C
Enzyme 3 Gene Name SLCO1B1
Enzyme 3 Protein Sequence >Solute carrier organic anion transporter family member 1B1
MDQNQHLNKTAEAQPSENKKTRYCNGLKMFLAALSLSFIAKTLGAIIMKSSIIHIERRFE
ISSSLVGFIDGSFEIGNLLVIVFVSYFGSKLHRPKLIGIGCFIMGIGGVLTALPHFFMGY
YRYSKETNINSSENSTSTLSTCLINQILSLNRASPEIVGKGCLKESGSYMWIYVFMGNML
RGIGETPIVPLGLSYIDDFAKEGHSSLYLGILNAIAMIGPIIGFTLGSLFSKMYVDIGYV
DLSTIRITPTDSRWVGAWWLNFLVSGLFSIISSIPFFFLPQTPNKPQKERKASLSLHVLE
TNDEKDQTANLTNQGKNITKNVTGFFQSFKSILTNPLYVMFVLLTLLQVSSYIGAFTYVF
KYVEQQYGQPSSKANILLGVITIPIFASGMFLGGYIIKKFKLNTVGIAKFSCFTAVMSLS
FYLLYFFILCENKSVAGLTMTYDGNNPVTSHRDVPLSYCNSDCNCDESQWEPVCGNNGIT
YISPCLAGCKSSSGNKKPIVFYNCSCLEVTGLQNRNYSAHLGECPRDDACTRKFYFFVAI
QVLNLFFSALGGTSHVMLIVKIVQPELKSLALGFHSMVIRALGGILAPIYFGALIDTTCI
KWSTNNCGTRGSCRTYNSTSFSRVYLGLSSMLRVSSLVLYIILIYAMKKKYQEKDINASE
NGSVMDEANLESLNKNKHFVPSAGADSETHC
Enzyme 3 Number of Residues 691
Enzyme 3 Molecular Weight 76450
Enzyme 3 Theoretical pI 8.68
Enzyme 3 GO Classification
Function
  • transporter activity
Process
  • cellular physiological process
  • physiological process
  • transport
Component
  • cell
  • integral to membrane
  • intrinsic to membrane
  • membrane
Enzyme 3 General Function Carbohydrate transport and metabolism
Enzyme 3 Specific Function Mediates the Na(+)-independent transport of organic anions such as pravastatin, taurocholate, methotrexate, dehydroepiandrosterone sulfate, 17-beta-glucuronosyl estradiol, estrone sulfate, prostaglandin E2, thromboxane B2, leukotriene C3, leukotriene E4, thyroxine and triiodothyronine. May play an important role in the clearance of bile acids and organic anions from the liver
Enzyme 3 Pathways Not Available
Enzyme 3 Reactions Not Available
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • None
Enzyme 3 Transmembrane Regions
  • 97-117 207-227 259-279 336-356 376-396 410-430 575-595
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 5051630 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID Q9Y6L6 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name SO1B1_HUMAN Link Image
Enzyme 3 PDB ID Not Available
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >2076 bp
ATGGACCAAAATCAACATTTGAATAAAACAGCAGAGGCACAACCTTCAGAGAATAAGAAA
ACAAGATACTGCAATGGATTGAAGATGTTCTTGGCAGCTCTGTCACTCAGCTTTATTGCT
AAGACACTAGGTGCAATTATTATGAAAAGTTCCATCATTCATATAGAACGGAGATTTGAG
ATATCCTCTTCTCTTGTTGGTTTTATTGACGGAAGCTTTGAAATTGGAAATTTGCTTGTG
ATTGTATTTGTGAGTTACTTTGGATCCAAACTACATAGACCAAAGTTAATTGGAATCGGT
TGTTTCATTATGGGAATTGGAGGTGTTTTGACTGCTTTGCCACATTTCTTCATGGGATAT
TACAGGTATTCTAAAGAAACTAATATCAATTCATCAGAAAATTCAACATCGACCTTATCC
ACTTGTTTAATTAATCAAATTTTATCACTCAATAAAGCATCACCTGAGATAGTGGGAAAA
GGTTGTTTAAAGGAATCTGGGTCATACATGTGGATATATGTGTTCATGGGTAATATGCTT
CGTGGAATAGGGGAGACTCCCATAGTACCACTGGGGCTTTCTTACATTGATGATTTCGCT
AAAGAAGGACATTCTTCTTTGTATTTAGGTATATTGAATGCAATAGCAATGATTGGTCCA
ATCATTGGCTTTACCCTGGGATCTCTGTTTTCTAAAATGTACGTGGATATTGGATATGTT
AATCTAAGCACTATCAGGATAACTCCTACTGATTCTCGATGGGTTGGAGCTTGGTGGCTT
AATTTCCTTGTGTCTGGACTATTCTCCATTATTTCTTCCATACCATTCTTTTTCTTGCCC
CAAACTCCAAATAAACCACAAAAAGAAAGAAAAGCTTCACTGTCTTTGCATGTGCTGGAA
ACAAATGATGAAAAGGATCAAACAGCTAATTTGACCAATCAAGGAAAAAATATTACCAAA
AATGTGACTGGTTTTTTCCAGTCTTTTAAAAGCATCCTTACTAATCCCCTGTATGTTATG
TTTGTGCTTTTGACGTTGTTACAAGTAAGCAGCTATATTGGTGCTTTTACTTATGTCTTC
AAATACGTAGAGCAACAGTATGGTCAGCCTTCATCTAAGGCTAACATCTTATTGGGAGTC
ATAACCATACCTATTTTTGCAAGTGGAATGTTTTTAGGAGGATATATCATTAAAAAATTC
AAACTGAACACCGTTGGAATTGCCAAATTCTCATGTTTTACTGCTGTGATGTCATTGTCC
TTTTACCTATTATATTTTTTCATACTCTGTGAAAACAAATCAGTTGCCGGACTAACCATG
ACCTATGATGGAAATAATCCAGTGACATCTCATAGAGATGTACCACTTTCTTATTGCAAC
TCAGACTGCAATTGTGATGAAAGTCAATGGGAACCAGTCTGTGGAAACAATGGAATAACT
TACATCTCACCCTGTCTAGCAGGTTGCAAATCTTCAAGTGGCAATAAAAAGCCTATAGTG
TTTTACAACTGCAGTTGTTTGGAAGTAACTGGTCTCCAGAACAGAAATTACTCAGCCCAT
TTGGGTGAATGCCCAAGAGATGATGCTTGTACAAGGAAATTTTACTTTTTTGTTGCAATA
CAAGTCTTGAATTTATTTTTCTCTGCACTTGGAGGCACCTCACATGTCATGCTGATTGTT
AAAATTGTTCAACCTGAATTGAAATCACTTGCACTGGGTTTCCACTCAATGGTTATACGA
GCACTAGGAGGAATTCTAGCTCCTATATATTTTGGGGCTCTGATTGATACAACGTGTATA
AAGTGGTCCACCAACAACTGTGGCACACGTGGGTCATGTAGGACATATAATTCCACATCA
TTTTCAAGGGTCTACTTGGGCTTGTCTTCAATGTTAAGAGTCTCATCACTTGTTTTATAT
ATTATATTAATTTATGCCATGAAGAAAAAATATCAAGAGAAAGATATCAATGCATCAGAA
AATGGAAGTGTCATGGATGAAGCAAACTTAGAATCCTTAAATAAAAATAAACATTTTGTC
CCTTCTGCTGGGGCAGATAGTGAAACACATTGTTAA
Enzyme 3 GenBank Gene ID AF060500 Link Image
Enzyme 3 GeneCard ID SLCO1B1 Link Image
Enzyme 3 GenAtlas ID SLCO1B1 Link Image
Enzyme 3 HGNC ID HGNC:10959 Link Image
Enzyme 3 Chromosome Location 12
Enzyme 3 Locus 12p
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  1. Abe T, Kakyo M, Tokui T, Nakagomi R, Nishio T, Nakai D, Nomura H, Unno M, Suzuki M, Naitoh T, Matsuno S, Yawo H: Identification of a novel gene family encoding human liver-specific organic anion transporter LST-1. J Biol Chem. 1999 Jun 11;274(24):17159-63. [PubMed Link Image]
  2. Hsiang B, Zhu Y, Wang Z, Wu Y, Sasseville V, Yang WP, Kirchgessner TG: A novel human hepatic organic anion transporting polypeptide (OATP2). Identification of a liver-specific human organic anion transporting polypeptide and identification of rat and human hydroxymethylglutaryl-CoA reductase inhibitor transporters. J Biol Chem. 1999 Dec 24;274(52):37161-8. [PubMed Link Image]
  3. Konig J, Cui Y, Nies AT, Keppler D: A novel human organic anion transporting polypeptide localized to the basolateral hepatocyte membrane. Am J Physiol Gastrointest Liver Physiol. 2000 Jan;278(1):G156-64. [PubMed Link Image]
  4. Konig J, Cui Y, Nies AT, Keppler D: Localization and genomic organization of a new hepatocellular organic anion transporting polypeptide. J Biol Chem. 2000 Jul 28;275(30):23161-8. [PubMed Link Image]
  5. Tirona RG, Leake BF, Merino G, Kim RB: Polymorphisms in OATP-C: identification of multiple allelic variants associated with altered transport activity among European- and African-Americans. J Biol Chem. 2001 Sep 21;276(38):35669-75. Epub 2001 Jul 26. [PubMed Link Image]
  6. Michalski C, Cui Y, Nies AT, Nuessler AK, Neuhaus P, Zanger UM, Klein K, Eichelbaum M, Keppler D, Konig J: A naturally occurring mutation in the SLC21A6 gene causing impaired membrane localization of the hepatocyte uptake transporter. J Biol Chem. 2002 Nov 8;277(45):43058-63. Epub 2002 Aug 23. [PubMed Link Image]
  7. Nozawa T, Nakajima M, Tamai I, Noda K, Nezu J, Sai Y, Tsuji A, Yokoi T: Genetic polymorphisms of human organic anion transporters OATP-C (SLC21A6) and OATP-B (SLC21A9): allele frequencies in the Japanese population and functional analysis. J Pharmacol Exp Ther. 2002 Aug;302(2):804-13. [PubMed Link Image]
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 6350
Enzyme 4 Name Type I iodothyronine deiodinase
Enzyme 4 Synonyms
  1. Type-I 5' deiodinase
  2. DIOI
  3. Type 1 DI
  4. 5DI
Enzyme 4 Gene Name DIO1
Enzyme 4 Protein Sequence >Type I iodothyronine deiodinase
MGLPQPGLWLKRLWVLLEVAVHVVVGKVLLILFPDRVKRNILAMGEKTGMTRNPHFSHDN
WIPTFFSTQYFWFVLKVRWQRLEDTTELGGLAPNCPVVRLSGQRCNIWEFMQGNRPLVLN
FGSCTCPSFMFKFDQFKRLIEDFSSIADFLVIYIEEAHASDGWAFKNNMDIRNHQNLQDR
LQAAHLLLARSPQCPVVVDTMQNQSSQLYAALPERLYIIQEGRILYKGKSGPWNYNPEEV
RAVLEKLHS
Enzyme 4 Number of Residues 249
Enzyme 4 Molecular Weight 28878
Enzyme 4 Theoretical pI 8.72
Enzyme 4 GO Classification
Function
  • catalytic activity
  • oxidoreductase activity
  • thyroxine 5'-deiodinase activity
Process
Component
Enzyme 4 General Function Not Available
Enzyme 4 Specific Function Responsible for the deiodination of T4 (3,5,3',5'- tetraiodothyronine) into T3 (3,5,3'-triiodothyronine) and of T3 into T2 (3,3'-diiodothyronine). Plays a role in providing a source of plasma T3 by deiodination of T4 in peripheral tissues such as liver and kidney
Enzyme 4 Pathways Not Available
Enzyme 4 Reactions
  • 3,5,3'-triiodo-L-thyronine + iodide + A + H+ = L-thyroxine + AH2
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • 1-26
Enzyme 4 Transmembrane Regions Not Available
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein 13195755 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID P49895 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name IOD1_HUMAN Link Image
Enzyme 4 PDB ID Not Available
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence >750 bp
ATGGGGCTGCCCCAGCCAGGGCTGTGGCTGAAGAGGCTCTGGGTGCTCTTGGAGGTGGCT
GTGCATGTGGTCGTGGGTAAAGTGCTTCTGATATTGTTTCCAGACAGAGTCAAGCGGAAC
ATCCTGGCCATGGGCGAGAAGACGGGTATGACCAGGAACCCCCATTTCAGCCACGACAAC
TGGATACCAACCTTTTTCAGCACCCAGTATTTCTGGTTCGTCTTGAAGGTCCGTTGGCAG
CGACTAGAGGACACGACTGAGCTAGGGGGTCTGGCCCCAAACTGCCCGGTGGTCCGCCTC
TCAGGACAGAGGTGCAACATTTGGGAGTTTATGCAAGGTAATAGGCCACTGGTGCTGAAT
TTTGGAAGTTGTACCTGACCTTCATTTATGTTCAAATTTGACCAGTTCAAGAGGCTTATT
GAAGACTTTAGTTCCATAGCAGATTTTCTTGTCATTTACATTGAAGAAGCACATGCATCA
GATGGCTGGGCTTTTAAGAACAACATGGACATCAGAAATCACCAGAACCTTCAGGATCGC
CTGCAGGCAGCCCATCTACTGCTGGCCAGGAGCCCCCAGTGCCCTGTGGTGGTGGACACC
ATGCAGAACCAGAGCAGCCAGCTCTACGCAGCACTGCCTGAGAGGCTCTACATAATCCAG
GAGGGCAGGATCCTCTACAAGGGTAAATCTGGCCCTTGGAACTACAACCCAGAGGAAGTT
CGTGCTGTTCTGGAAAAGCTCCACAGTTAA
Enzyme 4 GenBank Gene ID S48220 Link Image
Enzyme 4 GeneCard ID DIO1 Link Image
Enzyme 4 GenAtlas ID DIO1 Link Image
Enzyme 4 HGNC ID HGNC:2883 Link Image
Enzyme 4 Chromosome Location 1
Enzyme 4 Locus 1p33-p32
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References
  1. Mandel SJ, Berry MJ, Kieffer JD, Harney JW, Warne RL, Larsen PR: Cloning and in vitro expression of the human selenoprotein, type I iodothyronine deiodinase. J Clin Endocrinol Metab. 1992 Oct;75(4):1133-9. [PubMed Link Image]
  2. Toyoda N, Zavacki AM, Maia AL, Harney JW, Larsen PR: A novel retinoid X receptor-independent thyroid hormone response element is present in the human type 1 deiodinase gene. Mol Cell Biol. 1995 Sep;15(9):5100-12. [PubMed Link Image]
Enzyme 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 6351
Enzyme 5 Name Type II iodothyronine deiodinase
Enzyme 5 Synonyms
  1. Type-II 5' deiodinase
  2. DIOII
  3. Type 2 DI
  4. 5DII
Enzyme 5 Gene Name DIO2
Enzyme 5 Protein Sequence >Type II iodothyronine deiodinase
MGILSVDLLITLQILPVFFSNCLFLALYDSVILLKHVVLLLSRSKSTRGEWRRMLTSEGL
RCVWKSFLLDAYKQVKLGEDAPNSSVVHVSSTEGGDNSGNGTQEKIAEGATCHLLDFASP
ERPLVVNFGSATCPPFTSQLPAFRKLVEEFSSVADFLLVYIDEAHPSDGWAIPGDSSLSF
EVKKHQNQEDRCAAAQQLLERFSLPPQCRVVADRMDNNANIAYGVAFERVCIVQRQKIAY
LGGKGPFSYNLQEVRHWLEKNFSKR
Enzyme 5 Number of Residues 265
Enzyme 5 Molecular Weight 29600
Enzyme 5 Theoretical pI 7.07
Enzyme 5 GO Classification
Function
  • catalytic activity
  • oxidoreductase activity
  • thyroxine 5'-deiodinase activity
Process
Component
Enzyme 5 General Function Not Available
Enzyme 5 Specific Function Responsible for the deiodination of T4 (3,5,3',5'- tetraiodothyronine) into T3 (3,5,3'-triiodothyronine). Essential for providing the brain with appropriate levels of T3 during the critical period of development
Enzyme 5 Pathways Not Available
Enzyme 5 Reactions
  • 3,5,3'-triiodo-L-thyronine + iodide + A + H+ = L-thyroxine + AH2
Enzyme 5 Pfam Domain Function
Enzyme 5 Signals
  • 1-22
Enzyme 5 Transmembrane Regions Not Available
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein 1518542 Link Image
Enzyme 5 UniProtKB/Swiss-Prot ID Q92813 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name IOD2_HUMAN Link Image
Enzyme 5 PDB ID Not Available
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence >822 bp
ATGGGCATCCTCAGCGTAGACTTGCTGATCACACTGCAAATTCTGCCAGTTTTTTTCTCC
AACTGCCTCTTCCTGGCTCTCTATGACTCGGTCATTCTGCTCAAGCACGTGGTGCTGCTG
TTGAGCCGCTCCAAGTCCACTCGCGGAGAGTGGCGGCGCATGCTGACCTCAGAGGGACTG
CGCTGCGTCTGGAAGAGCTTCCTCCTCGATGCCTACAAACAGGTGAAATTGGGTGAGGAT
GCCCCCAATTCCAGTGTGGTGCATGTCTCCAGTACAGAAGGAGGTGACAACAGTGGCAAT
GGTACCCAGGAGAAGATAGCTGAGGGAGCCACATGCCACCTTCTTGACTTTGCCAGCCCT
GAGCGCCCACTAGTGGTCAACTTTGGCTCAGCCACTTGACCTCCTTTCACGAGCCAGCTG
CCAGCCTTCCGCAAACTGGTGGAAGAGTTCTCCTCAGTGGCTGACTTCCTGCTGGTCTAC
ATTGATGAGGCTCATCCATCAGATGGCTGGGCGATACCGGGGGACTCCTCTTTGTCTTTT
GAGGTGAAGAAGCACCAGAACCAGGAAGATCGATGTGCAGCAGCCCAGCAGCTTCTGGAG
CGTTTCTCCTTGCCGCCCCAGTGCCGAGTTGTGGCTGACCGCATGGACAATAACGCCAAC
ATAGCTTACGGGGTAGCCTTTGAACGTGTGTGCATTGTGCAGAGACAGAAAATTGCTTAT
CTGGGAGGAAAGGGCCCCTTCTCCTACAACCTTCAAGAAGTCCGGCATTGGCTGGAGAAG
AATTTCAGCAAGAGATGAAAGAAAACTAGATTAGCTGGTTAA
Enzyme 5 GenBank Gene ID U53506 Link Image
Enzyme 5 GeneCard ID DIO2 Link Image
Enzyme 5 GenAtlas ID DIO2 Link Image
Enzyme 5 HGNC ID HGNC:2884 Link Image
Enzyme 5 Chromosome Location 14
Enzyme 5 Locus 14q24.2-q24.3
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 General References
  1. Croteau W, Davey JC, Galton VA, St Germain DL: Cloning of the mammalian type II iodothyronine deiodinase. A selenoprotein differentially expressed and regulated in human and rat brain and other tissues. J Clin Invest. 1996 Jul 15;98(2):405-17. [PubMed Link Image]
  2. Buettner C, Harney JW, Larsen PR: The 3'-untranslated region of human type 2 iodothyronine deiodinase mRNA contains a functional selenocysteine insertion sequence element. J Biol Chem. 1998 Dec 11;273(50):33374-8. [PubMed Link Image]
Enzyme 5 Metabolite References Not Available
Enzyme 6 [top]
Enzyme 6 ID 7194
Enzyme 6 Name Transthyretin precursor
Enzyme 6 Synonyms
  1. Prealbumin
  2. TBPA
  3. TTR
  4. ATTR
Enzyme 6 Gene Name TTR
Enzyme 6 Protein Sequence >Transthyretin precursor
MASHRLLLLCLAGLVFVSEAGPTGTGESKCPLMVKVLDAVRGSPAINVAVHVFRKAADDT
WEPFASGKTSESGELHGLTTEEEFVEGIYKVEIDTKSYWKALGISPFHEHAEVVFTANDS
GPRRYTIAALLSPYSYSTTAVVTNPKE
Enzyme 6 Number of Residues 147
Enzyme 6 Molecular Weight 15887
Enzyme 6 Theoretical pI 5.58
Enzyme 6 GO Classification
Function
  • binding
  • carrier activity
  • steroid binding
  • transporter activity
Process
  • cellular physiological process
  • physiological process
  • transport
Component
Enzyme 6 General Function Not Available
Enzyme 6 Specific Function Thyroid hormone-binding protein. Probably transports thyroxine from the bloodstream to the brain
Enzyme 6 Pathways Not Available
Enzyme 6 Reactions Not Available
Enzyme 6 Pfam Domain Function
Enzyme 6 Signals
  • 1-20
Enzyme 6 Transmembrane Regions Not Available
Enzyme 6 Essentiality Not Available
Enzyme 6 GenBank ID Protein 189582 Link Image
Enzyme 6 UniProtKB/Swiss-Prot ID P02766 Link Image
Enzyme 6 UniProtKB/Swiss-Prot Entry Name TTHY_HUMAN Link Image
Enzyme 6 PDB ID 1KED Link Image
Enzyme 6 PDB File Show
Enzyme 6 3D Structure
Enzyme 6 Cellular Location Not Available
Enzyme 6 Gene Sequence >444 bp
ATGGCTTCTCATCGTCTGCTCCTCCTCTGCCTTGCTGGACTGGTATTTGTGTCTGAGGCT
GGCCCTACGGGCACCGGTGAATCCAAGTGTCCTCTGATGGTCAAAGTTCTAGATGCTGTC
CGAGGCAGTCCTGCCATCAATGTGGCCGTGCATGTGTTCAGAAAGGCTGCTGATGACACC
TGGGAGCCATTTGCCTCTGGGAAAACCAGTGAGTCTGGAGAGCTGCATGGGCTCACAACT
GAGGAGGAATTTGTAGAAGGGATATACAAAGTGGAAATAGACACCAAATCTTACTGGAAG
GCACTTGGCATCTCCCCATTCCATGAGCATGCAGAGGTGGTATTCACAGCCAACGACTCC
GGCCCCCGCCGCTACACCATTGCCGCCCTGCTGAGCCCCTACTCCTATTCCACCACGGCT
GTCGTCACCAATCCCAAGGAATGA
Enzyme 6 GenBank Gene ID K02091 Link Image
Enzyme 6 GeneCard ID TTR Link Image
Enzyme 6 GenAtlas ID TTR Link Image
Enzyme 6 HGNC ID HGNC:12405 Link Image
Enzyme 6 Chromosome Location 18
Enzyme 6 Locus 18q12.1
Enzyme 6 SNPs SNPJam Report Link Image
Enzyme 6 General References
  1. Mita S, Maeda S, Shimada K, Araki S: Cloning and sequence analysis of cDNA for human prealbumin. Biochem Biophys Res Commun. 1984 Oct 30;124(2):558-64. [PubMed Link Image]
  2. Wallace MR, Naylor SL, Kluve-Beckerman B, Long GL, McDonald L, Shows TB, Benson MD: Localization of the human prealbumin gene to chromosome 18. Biochem Biophys Res Commun. 1985 Jun 28;129(3):753-8. [PubMed Link Image]
  3. Sasaki H, Yoshioka N, Takagi Y, Sakaki Y: Structure of the chromosomal gene for human serum prealbumin. Gene. 1985;37(1-3):191-7. [PubMed Link Image]
  4. Tsuzuki T, Mita S, Maeda S, Araki S, Shimada K: Structure of the human prealbumin gene. J Biol Chem. 1985 Oct 5;260(22):12224-7. [PubMed Link Image]
  5. Mita S, Maeda S, Shimada K, Araki S: Analyses of prealbumin mRNAs in individuals with familial amyloidotic polyneuropathy. J Biochem (Tokyo). 1986 Nov;100(5):1215-22. [PubMed Link Image]
  6. Maeda S, Mita S, Araki S, Shimada K: Structure and expression of the mutant prealbumin gene associated with familial amyloidotic polyneuropathy. Mol Biol Med. 1986 Aug;3(4):329-38. [PubMed Link Image]
  7. Christmanson L, Betsholtz C, Gustavsson A, Johansson B, Sletten K, Westermark P: The transthyretin cDNA sequence is normal in transthyretin-derived senile systemic amyloidosis. FEBS Lett. 1991 Apr 9;281(1-2):177-80. [PubMed Link Image]
  8. Gu JR, Jiang HQ, He LP, Li DZ, Zhou XM, Dai WL, Qian LF, Chen YQ, Schweinfest C, Papas T: Transthyretin (prealbumin) gene in human primary hepatic cancer. Sci China B. 1991 Nov;34(11):1312-8. [PubMed Link Image]
  9. Kanda Y, Goodman DS, Canfield RE, Morgan FJ: The amino acid sequence of human plasma prealbumin. J Biol Chem. 1974 Nov 10;249(21):6796-805. [PubMed Link Image]
  10. Pras M, Prelli F, Franklin EC, Frangione B: Primary structure of an amyloid prealbumin variant in familial polyneuropathy of Jewish origin. Proc Natl Acad Sci U S A. 1983 Jan;80(2):539-42. [PubMed Link Image]
  11. Tawara S, Nakazato M, Kangawa K, Matsuo H, Araki S: Identification of amyloid prealbumin variant in familial amyloidotic polyneuropathy (Japanese type). Biochem Biophys Res Commun. 1983 Nov 15;116(3):880-8. [PubMed Link Image]
  12. Dwulet FE, Benson MD: Primary structure of an amyloid prealbumin and its plasma precursor in a heredofamilial polyneuropathy of Swedish origin. Proc Natl Acad Sci U S A. 1984 Feb;81(3):694-8. [PubMed Link Image]
  13. Cornwell GG 3rd, Sletten K, Johansson B, Westermark P: Evidence that the amyloid fibril protein in senile systemic amyloidosis is derived from normal prealbumin. Biochem Biophys Res Commun. 1988 Jul 29;154(2):648-53. [PubMed Link Image]
  14. Kametani F, Ikeda S, Yanagisawa N, Ishi T, Hanyu N: Characterization of a transthyretin-related amyloid fibril protein from cerebral amyloid angiopathy in type I familial amyloid polyneuropathy. J Neurol Sci. 1992 Apr;108(2):178-83. [PubMed Link Image]
  15. Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J: Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. Nat Biotechnol. 2003 May;21(5):566-9. Epub 2003 Mar 31. [PubMed Link Image]
  16. Harding J, Skare J, Skinner M: A second transthyretin mutation at position 33 (Leu/Phe) associated with familial amyloidotic polyneuropathy. Biochim Biophys Acta. 1991 Oct 21;1097(3):183-6. [PubMed Link Image]
  17. Skare J, Jones LA, Myles N, Kane K, Milunsky A, Cohen A, Skinner M: Two transthyretin mutations (glu42gly, his90asn) in an Italian family with amyloidosis. Clin Genet. 1994 Jun;45(6):281-4. [PubMed Link Image]
  18. Soprano DR, Herbert J, Soprano KJ, Schon EA, Goodman DS: Demonstration of transthyretin mRNA in the brain and other extrahepatic tissues in the rat. J Biol Chem. 1985 Sep 25;260(21):11793-8. [PubMed Link Image]
  19. Moses AC, Rosen HN, Moller DE, Tsuzaki S, Haddow JE, Lawlor J, Liepnieks JJ, Nichols WC, Benson MD: A point mutation in transthyretin increases affinity for thyroxine and produces euthyroid hyperthyroxinemia. J Clin Invest. 1990 Dec;86(6):2025-33. [PubMed Link Image]
  20. Gustavsson A, Jahr H, Tobiassen R, Jacobson DR, Sletten K, Westermark P: Amyloid fibril composition and transthyretin gene structure in senile systemic amyloidosis. Lab Invest. 1995 Nov;73(5):703-8. [PubMed Link Image]
  21. Blake CC, Oatley SJ: Protein-DNA and protein-hormone interactions in prealbumin: a model of the thyroid hormone nuclear receptor? Nature. 1977 Jul 14;268(5616):115-20. [PubMed Link Image]
  22. Blake CC, Geisow MJ, Oatley SJ, Rerat B, Rerat C: Structure of prealbumin: secondary, tertiary and quaternary interactions determined by Fourier refinement at 1.8 A. J Mol Biol. 1978 May 25;121(3):339-56. [PubMed Link Image]
  23. Blake CC, Geisow MJ, Swan ID, Rerat C, Rerat B: Strjcture of human plasma prealbumin at 2-5 A resolution. A preliminary report on the polypeptide chain conformation, quaternary structure and thyroxine binding. J Mol Biol. 1974 Sep 5;88(1):1-12. [PubMed Link Image]
  24. Terry CJ, Damas AM, Oliveira P, Saraiva MJ, Alves IL, Costa PP, Matias PM, Sakaki Y, Blake CC: Structure of Met30 variant of transthyretin and its amyloidogenic implications. EMBO J. 1993 Feb;12(2):735-41. [PubMed Link Image]
  25. Hamilton JA, Steinrauf LK, Braden BC, Liepnieks J, Benson MD, Holmgren G, Sandgren O, Steen L: The x-ray crystal structure refinements of normal human transthyretin and the amyloidogenic Val-30-->Met variant to 1.7-A resolution. J Biol Chem. 1993 Feb 5;268(4):2416-24. [PubMed Link Image]
  26. Monaco HL, Rizzi M, Coda A: Structure of a complex of two plasma proteins: transthyretin and retinol-binding protein. Science. 1995 May 19;268(5213):1039-41. [PubMed Link Image]
  27. Naylor HM, Newcomer ME: The structure of human retinol-binding protein (RBP) with its carrier protein transthyretin reveals an interaction with the carboxy terminus of RBP. Biochemistry. 1999 Mar 2;38(9):2647-53. [PubMed Link Image]
  28. Peterson SA, Klabunde T, Lashuel HA, Purkey H, Sacchettini JC, Kelly JW: Inhibiting transthyretin conformational changes that lead to amyloid fibril formation. Proc Natl Acad Sci U S A. 1998 Oct 27;95(22):12956-60. [PubMed Link Image]
  29. Schormann N, Murrell JR, Benson MD: Tertiary structures of amyloidogenic and non-amyloidogenic transthyretin variants: new model for amyloid fibril formation. Amyloid. 1998 Sep;5(3):175-87. [PubMed Link Image]
  30. Klabunde T, Petrassi HM, Oza VB, Raman P, Kelly JW, Sacchettini JC: Rational design of potent human transthyretin amyloid disease inhibitors. Nat Struct Biol. 2000 Apr;7(4):312-21. [PubMed Link Image]
  31. Saraiva MJ: Transthyretin mutations in health and disease. Hum Mutat. 1995;5(3):191-6. [PubMed Link Image]
  32. Nakazato M, Kangawa K, Minamino N, Tawara S, Matsuo H, Araki S: Revised analysis of amino acid replacement in a prealbumin variant (SKO-III) associated with familial amyloidotic polyneuropathy of Jewish origin. Biochem Biophys Res Commun. 1984 Sep 28;123(3):921-8. [PubMed Link Image]
  33. Wallace MR, Dwulet FE, Conneally PM, Benson MD: Biochemical and molecular genetic characterization of a new variant prealbumin associated with hereditary amyloidosis. J Clin Invest. 1986 Jul;78(1):6-12. [PubMed Link Image]
  34. Strahler JR, Rosenblum BB, Hanash SM: Identification and characterization of a human transthyretin variant. Biochem Biophys Res Commun. 1987 Oct 14;148(1):471-7. [PubMed Link Image]
  35. Wallace MR, Dwulet FE, Williams EC, Conneally PM, Benson MD: Identification of a new hereditary amyloidosis prealbumin variant, Tyr-77, and detection of the gene by DNA analysis. J Clin Invest. 1988 Jan;81(1):189-93. [PubMed Link Image]
  36. Ueno S, Uemichi T, Yorifuji S, Tarui S: A novel variant of transthyretin (Tyr114 to Cys) deduced from the nucleotide sequences of gene fragments from familial amyloidotic polyneuropathy in Japanese sibling cases. Biochem Biophys Res Commun. 1990 May 31;169(1):143-7. [PubMed Link Image]
  37. Ueno S, Uemichi T, Takahashi N, Soga F, Yorifuji S, Tarui S: Two novel variants of transthyretin identified in Japanese cases with familial amyloidotic polyneuropathy: transthyretin (Glu42 to Gly) and transthyretin (Ser50 to Arg). Biochem Biophys Res Commun. 1990 Jun 29;169(3):1117-21. [PubMed Link Image]
  38. Harrison HH, Gordon ED, Nichols WC, Benson MD: Biochemical and clinical characterization of prealbuminCHICAGO: an apparently benign variant of serum prealbumin (transthyretin) discovered with high-resolution two-dimensional electrophoresis. Am J Med Genet. 1991 Jun 15;39(4):442-52. [PubMed Link Image]
  39. Saeki Y, Ueno S, Yorifuji S, Sugiyama Y, Ide Y, Matsuzawa Y: New mutant gene (transthyretin Arg 58) in cases with hereditary polyneuropathy detected by non-isotope method of single-strand conformation polymorphism analysis. Biochem Biophys Res Commun. 1991 Oct 15;180(1):380-5. [PubMed Link Image]
  40. Skare JC, Milunsky JM, Milunsky A, Skare IB, Cohen AS, Skinner M: A new transthyretin variant from a patient with familial amyloidotic polyneuropathy has asparagine substituted for histidine at position 90. Clin Genet. 1991 Jan;39(1):6-12. [PubMed Link Image]
  41. Ii S, Minnerath S, Ii K, Dyck PJ, Sommer SS: Two-tiered DNA-based diagnosis of transthyretin amyloidosis reveals two novel point mutations. Neurology. 1991 Jun;41(6):893-8. [PubMed Link Image]
  42. Saraiva MJ, Almeida Mdo R, Sherman W, Gawinowicz M, Costa P, Costa PP, Goodman DS: A new transthyretin mutation associated with amyloid cardiomyopathy. Am J Hum Genet. 1992 May;50(5):1027-30. [PubMed Link Image]
  43. Murakami T, Maeda S, Yi S, Ikegawa S, Kawashima E, Onodera S, Shimada K, Araki S: A novel transthyretin mutation associated with familial amyloidotic polyneuropathy. Biochem Biophys Res Commun. 1992 Jan 31;182(2):520-6. [PubMed Link Image]
  44. Murakami T, Atsumi T, Maeda S, Tanase S, Ishikawa K, Mita S, Kumamoto T, Araki S, Ando M: A novel transthyretin mutation at position 30 (Leu for Val) associated with familial amyloidotic polyneuropathy. Biochem Biophys Res Commun. 1992 Aug 31;187(1):397-403. [PubMed Link Image]
  45. Nishi H, Kimura A, Harada H, Hayashi Y, Nakamura M, Sasazuki T: Novel variant transthyretin gene (Ser50 to Ile) in familial cardiac amyloidosis. Biochem Biophys Res Commun. 1992 Aug 31;187(1):460-6. [PubMed Link Image]
  46. Jones LA, Skare JC, Cohen AS, Harding JA, Milunsky A, Skinner M: Familial amyloidotic polyneuropathy: a new transthyretin position 30 mutation (alanine for valine) in a family of German descent. Clin Genet. 1992 Feb;41(2):70-3. [PubMed Link Image]
  47. Jacobson DR, McFarlin DE, Kane I, Buxbaum JN: Transthyretin Pro55, a variant associated with early-onset, aggressive, diffuse amyloidosis with cardiac and neurologic involvement. Hum Genet. 1992 May;89(3):353-6. [PubMed Link Image]
  48. Almeida MR, Ferlini A, Forabosco A, Gawinowicz M, Costa PP, Salvi F, Plasmati R, Tassinari CA, Altland K, Saraiva MJ: Two transthyretin variants (TTR Ala-49 and TTR Gln-89) in two Sicilian kindreds with hereditary amyloidosis. Hum Mutat. 1992;1(3):211-5. [PubMed Link Image]
  49. Uemichi T, Murrell JR, Zeldenrust S, Benson MD: A new mutant transthyretin (Arg 10) associated with familial amyloid polyneuropathy. J Med Genet. 1992 Dec;29(12):888-91. [PubMed Link Image]
  50. Izumoto S, Younger D, Hays AP, Martone RL, Smith RT, Herbert J: Familial amyloidotic polyneuropathy presenting with carpal tunnel syndrome and a new transthyretin mutation, asparagine 70. Neurology. 1992 Nov;42(11):2094-102. [PubMed Link Image]
  51. Shiomi K, Nakazato M, Matsukura S, Ohnishi A, Hatanaka H, Tsuji S, Murai Y, Kojima M, Kangawa K, Matsuo H: A basic transthyretin variant (Glu61-->Lys) causes familial amyloidotic polyneuropathy: protein and DNA sequencing and PCR-induced mutation restriction analysis. Biochem Biophys Res Commun. 1993 Aug 16;194(3):1090-6. [PubMed Link Image]
  52. Hesse A, Altland K, Linke RP, Almeida MR, Saraiva MJ, Steinmetz A, Maisch B: Cardiac amyloidosis: a review and report of a new transthyretin (prealbumin) variant. Br Heart J. 1993 Aug;70(2):111-5. [PubMed Link Image]
  53. Almeida Mdo R, Lopez-Andreu F, Munar-Ques M, Costa PP, Saraiva MJ: Transthyretin ALA 71: a new transthyretin variant in a Spanish family with familial amyloidotic polyneuropathy. Hum Mutat. 1993;2(5):420-1. [PubMed Link Image]
  54. Benson MD 2nd, Turpin JC, Lucotte G, Zeldenrust S, LeChevalier B, Benson MD: A transthyretin variant (alanine 71) associated with familial amyloidotic polyneuropathy in a French family. J Med Genet. 1993 Feb;30(2):120-2. [PubMed Link Image]
  55. Jacobson DR, Buxbaum JN: A double-variant transthyretin allele (Ser 6, Ile 33) in the Israeli patient "SKO" with familial amyloidotic polyneuropathy. Hum Mutat. 1994;3(3):254-60. [PubMed Link Image]
  56. Jacobson DR, Gertz MA, Buxbaum JN: Transthyretin VAL107, a new variant associated with familial cardiac and neuropathic amyloidosis. Hum Mutat. 1994;3(4):399-401. [PubMed Link Image]
  57. Berni R, Malpeli G, Folli C, Murrell JR, Liepnieks JJ, Benson MD: The Ile-84-->Ser amino acid substitution in transthyretin interferes with the interaction with plasma retinol-binding protein. J Biol Chem. 1994 Sep 23;269(38):23395-8. [PubMed Link Image]
  58. Uemichi T, Gertz MA, Benson MD: Amyloid polyneuropathy in two German-American families: a new transthyretin variant (Val 107). J Med Genet. 1994 May;31(5):416-7. [PubMed Link Image]
  59. Yasuda T, Sobue G, Doyu M, Nakazato M, Shiomi K, Yanagi T, Mitsuma T: Familial amyloidotic polyneuropathy with late-onset and well-preserved autonomic function: a Japanese kindred with novel mutant transthyretin (Ala97 to Gly). J Neurol Sci. 1994 Jan;121(1):97-102. [PubMed Link Image]
  60. Yamamoto K, Hsu SP, Yoshida K, Ikeda S, Nakazato M, Shiomi K, Cheng SY, Furihata K, Ueno I, Yanagisawa N: Familial amyloid polyneuropathy in Taiwan: identification of transthyretin variant (Leu55-->Pro). Muscle Nerve. 1994 Jun;17(6):637-41. [PubMed Link Image]
  61. Murakami T, Tachibana S, Endo Y, Kawai R, Hara M, Tanase S, Ando M: Familial carpal tunnel syndrome due to amyloidogenic transthyretin His 114 variant. Neurology. 1994 Feb;44(2):315-8. [PubMed Link Image]
  62. Booth DR, Tan SY, Hawkins PN, Pepys MB, Frustaci A: A novel variant of transthyretin, 59Thr-->Lys, associated with autosomal dominant cardiac amyloidosis in an Italian family. Circulation. 1995 Feb 15;91(4):962-7. [PubMed Link Image]
  63. Vidal R, Garzuly F, Budka H, Lalowski M, Linke RP, Brittig F, Frangione B, Wisniewski T: Meningocerebrovascular amyloidosis associated with a novel transthyretin mis-sense mutation at codon 18 (TTRD 18G) Am J Pathol. 1996 Feb;148(2):361-6. [PubMed Link Image]
  64. Jacobson DR, Pan T, Kyle RA, Buxbaum JN: Transthyretin ILE20, a new variant associated with late-onset cardiac amyloidosis. Hum Mutat. 1997;9(1):83-5. [PubMed Link Image]
  65. Nakamura M, Hamidi Asl K, Benson MD: A novel variant of transthyretin (Glu89Lys) associated with familial amyloidotic polyneuropathy. Amyloid. 2000 Mar;7(1):46-50. [PubMed Link Image]
  66. de Carvalho M, Moreira P, Evangelista T, Ducla-Soares JL, Bento M, Fernandes R, Saraiva MJ: New transthyretin mutation V28M in a Portuguese kindred with amyloid polyneuropathy. Muscle Nerve. 2000 Jul;23(7):1016-21. [PubMed Link Image]
  67. Blevins G, Macaulay R, Harder S, Fladeland D, Yamashita T, Yazaki M, Hamidi Asl K, Benson MD, Donat JR: Oculoleptomeningeal amyloidosis in a large kindred with a new transthyretin variant Tyr69His. Neurology. 2003 May 27;60(10):1625-30. [PubMed Link Image]
Enzyme 6 Metabolite References Not Available
Enzyme 7 [top]
Enzyme 7 ID 8393
Enzyme 7 Name Thyroxine-binding globulin precursor
Enzyme 7 Synonyms
  1. T4-binding globulin
  2. Serpin A7
Enzyme 7 Gene Name SERPINA7
Enzyme 7 Protein Sequence >Thyroxine-binding globulin precursor
MSPFLYLVLLVLGLHATIHCASPEGKVTACHSSQPNATLYKMSSINADFAFNLYRRFTVE
TPDKNIFFSPVSISAALVMLSFGACCSTQTEIVETLGFNLTDTPMVEIQHGFQHLICSLN
FPKKELELQIGNALFIGKHLKPLAKFLNDVKTLYETEVFSTDFSNISAAKQEINSHVEMQ
TKGKVVGLIQDLKPNTIMVLVNYIHFKAQWANPFDPSKTEDSSSFLIDKTTTVQVPMMHQ
MEQYYHLVDMELNCTVLQMDYSKNALALFVLPKEGQMESVEAAMSSKTLKKWNRLLQKGW
VDLFVPKFSISATYDLGATLLKMGIQHAYSENADFSGLTEDNGLKLSNAAHKAVLHIGEK
GTEAAAVPEVELSDQPENTFLHPIIQIDRSFMLLILERSTRSILFLGKVVNPTEA
Enzyme 7 Number of Residues 415
Enzyme 7 Molecular Weight 46325
Enzyme 7 Theoretical pI 6.27
Enzyme 7 GO Classification
Function
  • endopeptidase inhibitor activity
  • enzyme inhibitor activity
  • enzyme regulator activity
  • protease inhibitor activity
  • serine-type endopeptidase inhibitor activity
Process
Component
Enzyme 7 General Function Not Available
Enzyme 7 Specific Function Major thyroid hormone transport protein in serum
Enzyme 7 Pathways Not Available
Enzyme 7 Reactions Not Available
Enzyme 7 Pfam Domain Function
Enzyme 7 Signals
  • 1-20
Enzyme 7 Transmembrane Regions Not Available
Enzyme 7 Essentiality Not Available
Enzyme 7 GenBank ID Protein 338697 Link Image
Enzyme 7 UniProtKB/Swiss-Prot ID P05543 Link Image
Enzyme 7 UniProtKB/Swiss-Prot Entry Name THBG_HUMAN Link Image
Enzyme 7 PDB ID Not Available
Enzyme 7 Cellular Location Not Available
Enzyme 7 Gene Sequence >1248 bp
ATGTCACCATTCCTGTACCTGGTTCTCTTGGTACTTGGGCTTCATGCTACAATCCACTGT
GCATCACCTGAAGGCAAAGTAACAGCCTGCCATTCATCCCAACCAAATGCCACTCTCTAC
AAGATGTCATCCATTAATGCTGACTTTGCATTCAATCTGTACCGGAGGTTCACTGTGGAG
ACCCCAGATAAGAACATCTTCTTTTCCCCTGTGAGCATTTCTGCAGCTTTGGTTATGCTT
TCCTTTGGGGCCTGCTGCAGCACCCAAACTGAGATTGTGGAGACCTTGGGGTTCAACCTC
ACAGACACTCCAATGGTAGAGATCCAGCATGGCTTCCAGCATCTGATCTGTTCACTGAAT
TTTCCAAAGAAGGAACTGGAATTGCAGATAGGAAATGCCCTCTTCATTGGCAAGCATCTG
AAACCACTGGCAAAGTTCTTGAATGATGTCAAGACCCTCTATGAGACTGAAGTCTTTTCT
ACCGACTTCTCCAACATTTCTGCAGCCAAGCAGGAGATTAACAGTCATGTGGAGATGCAA
ACCAAAGGGAAAGTTGTGGGTCTAATTCAAGACCTCAAGCCAAACACCACTATGGTCTTA
GTGAACTATATTCACTTTAAAGCCCAGTGGGCAAATCCTTTTGATCCATCCAAGACAGAA
GACAGTTCCAGCTTCTTAATAGACAAGACCACCACTGTTCAAGTGCCCATGATGCACCAG
ATGGAACAATACTATCACCTAGTGGATATGGAATTGAACTGCACAGTTCTGCAAATGGAC
TACAGCAAGAATGCTCTGGCACTCTTTGTTCTTCCCAAGGAGGGACAGATGGAGTCAGTG
GAAGCTGCCATGTCATCTAAAACACTGAAGAAGTGGAACCGCTTACTACAGAAGGGATGG
GTTGACTTGTTTGTTCCAAAGTTTTCCATTTCTGCCACATATGACCTTGGAGCCACACTT
TTGAAGATGGGCATTCAGCATGCCTATTCTGAAAATGCTGATTTTTCTGGACTCACAGAG
GACAATGGTCTGAAACTTTCCAATGCTGCCCATAAGGCTGTGCTGCACATTGGTGAAAAG
GGAACTGAAGCTGCAGCTGTCCCTGAAGTTGAACTTTCGGATCAGCCTGAAAACACTTTC
CTACACCCTATTATCCAAATTGATAGATCTTTCATGTTGTTGATTTTGGAGAGAAGCACA
AGGAGTATTCTCTTTCTAGGGAAAGTTGTGAACCCAACGGAAGCGTAG
Enzyme 7 GenBank Gene ID M14091 Link Image
Enzyme 7 GeneCard ID SERPINA7 Link Image
Enzyme 7 GenAtlas ID SERPINA7 Link Image
Enzyme 7 HGNC ID HGNC:11583 Link Image
Enzyme 7 Chromosome Location X
Enzyme 7 Locus Xq22.2
Enzyme 7 SNPs SNPJam Report Link Image
Enzyme 7 General References
  1. Flink IL, Bailey TJ, Gustafson TA, Markham BE, Morkin E: Complete amino acid sequence of human thyroxine-binding globulin deduced from cloned DNA: close homology to the serine antiproteases. Proc Natl Acad Sci U S A. 1986 Oct;83(20):7708-12. [PubMed Link Image]
  2. Akbari MT, Kapadi A, Farmer MJ, Fitch NJ, McCann KP, Kordestani S, Flink IL, Sheppard MC, Ramsden DB: The structure of the human thyroxine binding globulin (TBG) gene. Biochim Biophys Acta. 1993 Dec 14;1216(3):446-54. [PubMed Link Image]
  3. Hayashi Y, Mori Y, Janssen OE, Sunthornthepvarakul T, Weiss RE, Takeda K, Weinberg M, Seo H, Bell GI, Refetoff S: Human thyroxine-binding globulin gene: complete sequence and transcriptional regulation. Mol Endocrinol. 1993 Aug;7(8):1049-60. [PubMed Link Image]
  4. Cheng SY: Partial amino acid sequence of human thyroxine-binding globulin. Further evidence for a single polypeptide chain. Biochem Biophys Res Commun. 1977 Dec 21;79(4):1212-8. [PubMed Link Image]
  5. Mori Y, Takeda K, Charbonneau M, Refetoff S: Replacement of Leu227 by Pro in thyroxine-binding globulin (TBG) is associated with complete TBG deficiency in three of eight families with this inherited defect. J Clin Endocrinol Metab. 1990 Mar;70(3):804-9. [PubMed Link Image]
  6. Mori Y, Seino S, Takeda K, Flink IL, Murata Y, Bell GI, Refetoff S: A mutation causing reduced biological activity and stability of thyroxine-binding globulin probably as a result of abnormal glycosylation of the molecule. Mol Endocrinol. 1989 Mar;3(3):575-9. [PubMed Link Image]
  7. Shirotani T, Kishikawa H, Wake N, Miyamura N, Hashimoto Y, Motoyoshi S, Yamaguchi K, Shichiri M: Thyroxine-binding globulin variant (TBG-Kumamoto): identification of a point mutation and genotype analysis of its family. Endocrinol Jpn. 1992 Dec;39(6):577-84. [PubMed Link Image]
  8. Janssen OE, Takeda K, Refetoff S: Sequence of the variant thyroxine-binding globulin (TBG) in a Montreal family with partial TBG deficiency. Hum Genet. 1991 Jun;87(2):119-22. [PubMed Link Image]
  9. Bertenshaw R, Takeda K, Refetoff S: Sequencing of the variant thyroxine-binding globulin (TBG)-Quebec reveals two nucleotide substitutions. Am J Hum Genet. 1991 Apr;48(4):741-4. [PubMed Link Image]
  10. Bertenshaw R, Sarne D, Tornari J, Weinberg M, Refetoff S: Sequencing of the variant thyroxine-binding globulin (TBG)-San Diego reveals two nucleotide substitutions. Biochim Biophys Acta. 1992 Aug 25;1139(4):307-10. [PubMed Link Image]
  11. Takeda K, Mori Y, Sobieszczyk S, Seo H, Dick M, Watson F, Flink IL, Seino S, Bell GI, Refetoff S: Sequence of the variant thyroxine-binding globulin of Australian aborigines. Only one of two amino acid replacements is responsible for its altered properties. J Clin Invest. 1989 Apr;83(4):1344-8. [PubMed Link Image]
  12. Waltz MR, Pullman TN, Takeda K, Sobieszczyk P, Refetoff S: Molecular basis for the properties of the thyroxine-binding globulin-slow variant in American blacks. J Endocrinol Invest. 1990 Apr;13(4):343-9. [PubMed Link Image]
Enzyme 7 Metabolite References Not Available
Enzyme 8 [top]
Enzyme 8 ID 8627
Enzyme 8 Name 4F2 cell-surface antigen heavy chain
Enzyme 8 Synonyms
  1. 4F2hc
  2. Lymphocyte activation antigen 4F2 large subunit
  3. 4F2 heavy chain antigen
  4. CD98 antigen
Enzyme 8 Gene Name SLC3A2
Enzyme 8 Protein Sequence >4F2 cell-surface antigen heavy chain
MSQDTEVDMKEVELNELEPEKQPMNAASGAAMSLAGAEKNGLVKIKVAEDEAEAAAAAKF
TGLSKEELLKVAGSPGWVRTRWALLLLFWLGWLGMLAGAVVIIVRAPRCRELPAQKWWHT
GALYRIGDLQAFQGHGAGNLAGLKGRLDYLSSLKVKGLVLGPIHKNQKDDVAQTDLLQID
PNFGSKEDFDSLLQSAKKKSIRVILDLTPNYRGENSWFSTQVDTVATKVKDALEFWLQAG
VDGFQVRDIENLKDASSFLAEWQNITKGFSEDRLLIAGTNSSDLQQILSLLESNKDLLLT
SSYLSDSGSTGEHTKSLVTQYLNATGNRWCSWSLSQARLLTSFLPAQLLRLYQLMLFTLP
GTPVFSYGDEIGLDAAALPGQPMEAPVMLWDESSFPDIPGAVSANMTVKGQSEDPGSLLS
LFRRLSDQRSKERSLLHGDFHAFSAGPGLFSYIRHWDQNERFLVVLNFGDVGLSAGLQAS
DLPASASLPAKADLLLSTQPGREEGSPLELERLKLEPHEGLLLRFPYAA
Enzyme 8 Number of Residues 529
Enzyme 8 Molecular Weight 57945
Enzyme 8 Theoretical pI 4.99
Enzyme 8 GO Classification
Function
  • alpha-amylase activity
  • amylase activity
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on glycosyl bonds
  • hydrolase activity, hydrolyzing O-glycosyl compounds
Process
  • carbohydrate metabolism
  • macromolecule metabolism
  • metabolism
  • physiological process
Component
Enzyme 8 General Function Carbohydrate transport and metabolism
Enzyme 8 Specific Function Involved in sodium-independent, high-affinity transport of large neutral amino acids. Required for normal and neoplastic cell growth
Enzyme 8 Pathways Not Available
Enzyme 8 Reactions Not Available
Enzyme 8 Pfam Domain Function
Enzyme 8 Signals
  • 1-98
Enzyme 8 Transmembrane Regions
  • 82-104
Enzyme 8 Essentiality Not Available
Enzyme 8 GenBank ID Protein 182865 Link Image
Enzyme 8 UniProtKB/Swiss-Prot ID P08195 Link Image
Enzyme 8 UniProtKB/Swiss-Prot Entry Name 4F2_HUMAN Link Image
Enzyme 8 PDB ID Not Available
Enzyme 8 Cellular Location Not Available
Enzyme 8 Gene Sequence >1590 bp
ATGAGCCAGGACACCGAGGTGGATATGAAGGAGGTGGAGCTGAATGAGTTAGAGCCCGAG
AAGCAGCCGATGAACGCGGCGTCTGGGGCGGCCATGTCCCTGGCGGGAGCCGAGAAGAAT
GGTCTGGTGAAGATCAAGGTGGCGGAAGACGAGGCGGAGGCGGCAGCCGCGGCTAAGTTC
ACGGGCCTGTCCAAGGAGGAGCTGCTGAAGGTGGCAGGCAGCCCCGGCTGGGTACGCACC
CGCTGGGCACTGCTGCTGCTCTTCTGGCTCGGCTGGCTCGGCATGCTTGCTGGTGCCGTG
GTCATAATCGTGCGAGCGCCGCGTTGTCGCGAGCTACCGGCGCAGAAGTGGTGGCACACG
GGCGCCCTCTACCGCATCGGCGACCTTCAGGCCTTCCAGGGCCACGGCGCGGGCAACCTG
GCGGGTCTGAAGGGGCGTCTCGATTACCTGAGCTCTCTGAAGGTGAAGGGCCTTGTGCTG
GGTCCAATTCACAAGAACCAGAAGGATGATGTCGCTCAGACTGACTTGCTGCAGATCGAC
CCCAATTTTGGCTCCAAGGAAGATTTTGACAGTCTCTTGCAATCGGCTAAAAAAAAGAGC
ATCCGTGTCATTCTGGACCTTACTCCCAACTACCGGGGTGAGAACTCGTGGTTCTCCACT
CAGGTTGACACTGTGGCCACCAAGGTGAAGGATGCTCTGGAGTTTTGGCTGCAAGCTGGC
GTGGATGGGTTCCAGGTTCGGGACATAGAGAATCTGAAGGATGCATCCTCATTCTTGGCT
GAGTGGCAAAATATCACCAAGGGCTTCAGTGAAGACAGGCTCTTGATTGCGGGGACTAAC
TCCTCCGACCTTCAGCAGATCCTGAGCCTACTCGAATCCAACAAAGACTTGCTGTTGACT
AGCTCATACCTGTCTGATTCTGGTTCTACTGGGGAGCATACAAAATCCCTAGTCACACAG
TATTTGAATGCCACTGGCAATCGCTGGTGCAGCTGGAGTTTGTCTCAGGCAAGGCTCCTG
ACTTCCTTCTTGCCGGCTCAACTTCTCCGACTCTACCAGCTGATGCTCTTCACCCTGCCA
GGGACCCCTGTTTTCAGCTACGGGGATGAGATTGGCCTGGATGCAGCTGCCCTTCCTGGA
CAGCCTATGGAGGCTCCAGTCATGCTGTGGGATGAGTCCAGCTTCCCTGACATCCCAGGG
GCTGTAAGTGCCAACATGACTGTGAAGGGCCAGAGTGAAGACCCTGGCTCCCTCCTTTCC
TTGTTCCGGCGGCTGAGTGACCAGCGGAGTAAGGAGCGCTCCCTACTGCATGGGGACTTC
CACGCGTTCTCCGCTGGGCCTGGACTCTTCTCCTATATCCGCCACTGGGACCAGAATGAG
CGTTTTCTGGTAGTGCTTAACTTTGGGGATGTGGGCCTCTCGGCTGGACTGCAGGCCTCC
GACCTGCCTGCCAGCGCCAGCCTCCCAGCCAAGGCTGACCTCCTGCTCAGCACCCAGCCA
GGCCGTGAGGAGGGCTCCCCTCTTGAGCTGGAACGCCTGAAACTGGAGCCTCACGAAGGG
CTGCTGCTCCGCTTCCCCTACGCGGCCTGA
Enzyme 8 GenBank Gene ID J02939 Link Image
Enzyme 8 GeneCard ID SLC3A2 Link Image
Enzyme 8 GenAtlas ID SLC3A2 Link Image
Enzyme 8 HGNC ID HGNC:11026 Link Image
Enzyme 8 Chromosome Location 11
Enzyme 8 Locus 11q13
Enzyme 8 SNPs SNPJam Report Link Image
Enzyme 8 General References
  1. Quackenbush E, Clabby M, Gottesdiener KM, Barbosa J, Jones NH, Strominger JL, Speck S, Leiden JM: Molecular cloning of complementary DNAs encoding the heavy chain of the human 4F2 cell-surface antigen: a type II membrane glycoprotein involved in normal and neoplastic cell growth. Proc Natl Acad Sci U S A. 1987 Sep;84(18):6526-30. [PubMed Link Image]
  2. Teixeira S, Di Grandi S, Kuhn LC: Primary structure of the human 4F2 antigen heavy chain predicts a transmembrane protein with a cytoplasmic NH2 terminus. J Biol Chem. 1987 Jul 15;262(20):9574-80. [PubMed Link Image]
  3. Lumadue JA, Glick AB, Ruddle FH: Cloning, sequence analysis, and expression of the large subunit of the human lymphocyte activation antigen 4F2. Proc Natl Acad Sci U S A. 1987 Dec;84(24):9204-8. [PubMed Link Image]
  4. Gottesdiener KM, Karpinski BA, Lindsten T, Strominger JL, Jones NH, Thompson CB, Leiden JM: Isolation and structural characterization of the human 4F2 heavy-chain gene, an inducible gene involved in T-lymphocyte activation. Mol Cell Biol. 1988 Sep;8(9):3809-19. [PubMed Link Image]
  5. Zhang H, Li XJ, Martin DB, Aebersold R: Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry. Nat Biotechnol. 2003 Jun;21(6):660-6. Epub 2003 May 18. [PubMed Link Image]
  6. Harris RA, Yang A, Stein RC, Lucy K, Brusten L, Herath A, Parekh R, Waterfield MD, O'Hare MJ, Neville MA, Page MJ, Zvelebil MJ: Cluster analysis of an extensive human breast cancer cell line protein expression map database. Proteomics. 2002 Feb;2(2):212-23. [PubMed Link Image]
  7. He X, Di Y, Li J, Xie Y, Tang Y, Zhang F, Wei L, Zhang Y, Qin W, Huo K, Li Y, Wan D, Gu J: Molecular cloning and characterization of CT120, a novel membrane-associated gene involved in amino acid transport and glutathione metabolism. Biochem Biophys Res Commun. 2002 Sep 27;297(3):528-36. [PubMed Link Image]
Enzyme 8 Metabolite References Not Available
Enzyme 9 [top]
Enzyme 9 ID 15249
Enzyme 9 Name Type III iodothyronine deiodinase
Enzyme 9 Synonyms
  1. Type-III 5'-deiodinase
  2. Type 3 DI
  3. DIOIII
  4. 5DIII
Enzyme 9 Gene Name DIO3
Enzyme 9 Protein Sequence >Type III iodothyronine deiodinase
MLRSLLLHSLRLCAQTASCLVLFPRFLGTAFMLWLLDFLCIRKHFLGRRRRGQPEPEVEL
NSEGEEVPPDDPPICVSDDNRLCTLASLKAVWHGQKLDFFKQAHEGGPAPNSEVVLPDGF
QSQHILDYAQGNRPLVLNFGSCTUPPFMARMSAFQRLVTKYQRDVDFLIIYIEEAHPSDG
WVTTDSPYIIPQHRSLEDRVSAARVLQQGAPGCALVLDTMANSSSSAYGAYFERLYVIQS
GTIMYQGGRGPDGYQVSELRTWLERYDEQLHGARPRRV
Enzyme 9 Number of Residues 278
Enzyme 9 Molecular Weight 31451
Enzyme 9 Theoretical pI 6.71
Enzyme 9 GO Classification
Function
  • catalytic activity
  • oxidoreductase activity
  • thyroxine 5'-deiodinase activity
Process
Component
Enzyme 9 General Function Not Available
Enzyme 9 Specific Function Responsible for the deiodination of T4 (3,5,3',5'- tetraiodothyronine) into RT3 (3,3',5'-triiodothyronine) and of T3 (3,5,3'-triiodothyronine) into T2 (3,3'-diiodothyronine). RT3 and T2 are inactive metabolites. May play a role in preventing premature exposure of developing fetal tissues to adult levels of thyroid hormones. Can regulate circulating fetal thyroid hormone concentrations throughout gestation. Essential role for regulation of thyroid hormone inactivation during embryological development
Enzyme 9 Pathways Not Available
Enzyme 9 Reactions Not Available
Enzyme 9 Pfam Domain Function
Enzyme 9 Signals
  • None
Enzyme 9 Transmembrane Regions
  • 17-36
Enzyme 9 Essentiality Not Available
Enzyme 9 GenBank ID Protein 13242866 Link Image
Enzyme 9 UniProtKB/Swiss-Prot ID P55073 Link Image
Enzyme 9 UniProtKB/Swiss-Prot Entry Name IOD3_HUMAN Link Image
Enzyme 9 PDB ID Not Available
Enzyme 9 Cellular Location Not Available
Enzyme 9 Gene Sequence >837 bp
ATGCTCCACTCCCTGCTGCTTCACTCCTTGAGGCTCTGCGCCCAGACCGCCTCGTGCCTC
GTGCTCTTCCCGCGCTTCCTCGGCACGGCCTTCATGCTCTGGCTTCTCGATTTCTTGTGT
ATCCGCAAGCATTTCCTGGGCCGCCGCCGCCGGGGCAAGCCCGAGCCCGAAGTGGAGCTC
AACAGTGAAGGCGAGGAGGTGCCTCCCGATGACCCGCCCATCTGCGTGTCCGACGACAAC
CGCCTGTGCACCCTGGCGTCGCTCAAGGCGGTGTGGCATGGCCAGAAGTTGGATTTCTTC
AAGCAGGCGCACGAGGGCGGTCCGGCGCCCAACTCCGAGGTGGTTCTGCCCGACGGCTTC
CAGAGCCAGCACATCCTCGACTACGCGCAAGGGAACCGCCCGCTGGTTCTCAATTTCGGC
AGCTGCACCTGACCACCGTTCATGGCGCGCATGAGCGCCTTCCAGCGCCTGGTCACTAAG
TACCAGCGCGACGTCGACTTCCTCATCATCTACATCGAGGAAGCGCACCCCTCCGACGGC
TGGGTCACCACGGACTCTCCCTACATCATCCCACAGCACCGGAGCCTGGAGGACCGGGTC
AGCGCAGCGAGGGTACTGCAGCAAGGTGCACCCGGCTGCGCTCTGGTCCTCGACACCATG
GCCAACTCCAGCAGCTCGGCCTATGGCGCCTACTTCGAGCGTCTCTATGTCATCCAGAGT
GGCACTATTATGTACCAGGGCGGCCGTGGCCCCGACGGCTACCAGGTCTCTGAGCTGCGC
ACTTGGTTGGAACGCTATGATGAGCAACTGCACGGCGCTCGGCCCCGGAGGGTGTAA
Enzyme 9 GenBank Gene ID S79854 Link Image
Enzyme 9 GeneCard ID P55073 Link Image
Enzyme 9 GenAtlas ID DIO3 Link Image
Enzyme 9 HGNC ID HGNC:2885 Link Image
Enzyme 9 Chromosome Location 14
Enzyme 9 Locus 14q32
Enzyme 9 SNPs SNPJam Report Link Image
Enzyme 9 General References
  1. Salvatore D, Low SC, Berry M, Maia AL, Harney JW, Croteau W, St Germain DL, Larsen PR: Type 3 lodothyronine deiodinase: cloning, in vitro expression, and functional analysis of the placental selenoenzyme. J Clin Invest. 1995 Nov;96(5):2421-30. [PubMed Link Image]
Enzyme 9 Metabolite References Not Available