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Human Metabolome Database Version 2.5

 

Showing metabocard for 3a,7a-Dihydroxycoprostanic acid (HMDB00359)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2009-05-05 20:57:54
Accession Number HMDB00359
Secondary Accession Numbers HMDB01974
Common Name 3a,7a-Dihydroxycoprostanic acid
Description 3a,7a-Dihydroxycoprostanic acid is a bile acid excreted in small amounts in the urine of healthy subjects (PMID 864325) 3a,7a-Dihydroxycoprostanic acid is the precursor to chenodeoxycholic acid A bile acid. Bile acids are steroid acids found predominantly in bile of mammals. The distinction between different bile acids is minute, depends only on presence or absence of hydroxyl groups on positions 3, 7, and 12. Bile acids are physiological detergents that facilitate excretion, absorption, and transport of fats and sterols in the intestine and liver. Bile acids are also steroidal amphipathic molecules derived from the catabolism of cholesterol. They modulate bile flow and lipid secretion, are essential for the absorption of dietary fats and vitamins, and have been implicated in the regulation of all the key enzymes involved in cholesterol homeostasis. Bile acids recirculate through the liver, bile ducts, small intestine and portal vein to form an enterohepatic circuit. They exist as anions at physiological pH and, consequently, require a carrier for transport across the membranes of the enterohepatic tissues. The unique detergent properties of bile acids are essential for the digestion and intestinal absorption of hydrophobic nutrients. Bile acids have potent toxic properties (e.g., membrane disruption) and there are a plethora of mechanisms to limit their accumulation in blood and tissues.
Synonyms
  1. 3a,7a-Dihydroxy-5b-cholestan-26-oate
  2. 3a,7a-Dihydroxy-5b-cholestan-26-oic acid
  3. 3a,7a-Dihydroxy-5b-cholestanoate
  4. 3a,7a-Dihydroxy-5b-cholestanoic acid
  5. 3a,7a-Dihydroxycoprostanate
  6. 3a,7a-Dihydroxycoprostanic acid
  7. 3a,7a-Hydroxy-5b-cholestan-26-oate
  8. 3a,7a-Hydroxy-5b-cholestan-26-oic acid
  9. 3alpha,7alpha-Dihydroxy-5beta-cholestanate
  10. 3alpha,7alpha-Dihydroxy-5beta-cholestanoate
  11. 3alpha,7alpha-Dihydroxy-5beta-cholestan-26-oic acid
  12. 3alpha,7alpha-dihydroxy-5beta-cholestanic acid
  13. 3alpha,7alpha-dihydroxy-5beta-cholestanoic acid
  14. 3alpha,7alpha-Dihydroxy-5beta-cholestan-26-oate
Chemical IUPAC Name (6R)-6-[(3R,5S,7R,10S,13R)-3,7-dihydroxy-10,13-dimethyl-2,3,4,5,6,7,8,9,11,12,14,15,16,17-tetradecahydro-1H-cyclopenta[a]phenanthren-17-yl]-2-methylheptanoicacid
Chemical Formula C27H46O4
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Cholesterols and derivatives
Class
  • Bile Acids
Sub Class
  • Dihydroxy bile acids
Family
  • Mammalian Metabolite
Species
  • secondary alcohol
  • carboxylic acid
Biofunction
  • Fat solubilization and Waste products
Application
—
Source
  • Endogenous
Average Molecular Weight 434.652
Monoisotopic Molecular Weight 434.339600
Isomeric SMILES C[C@H](CCCC(C)C(O)=O)[C@H]1CC[C@H]2C3[C@H](O)C[C@@H]4C[C@H](O)CC[C@]4(C)[C@H]3CC[C@]12C
Canonical SMILES CC(CCCC(C)C(O)=O)C1CCC2C3C(O)CC4CC(O)CCC4(C)C3CCC12C
KEGG Compound ID Not Available
BioCyc ID Not Available
BiGG ID Not Available
Wikipedia Link Not Available
NuGOwiki Link HMDB00359 Link Image
Metagene Link HMDB00359 Link Image
METLIN ID 5348 Link Image
PubChem Compound 440384 Link Image
PubChem Substance 8143503 Link Image
ChEBI ID Not Available
CAS Registry Number 17974-66-2
InChI Identifier InChI=1/C27H46O4/c1-16(6-5-7-17(2)25(30)31)20-8-9-21-24-22(11-13-27(20,21)4)26(3)12-10-19(28)14-18(26)15-23(24)29/h16-24,28-29H,5-15H2,1-4H3,(H,30,31)/t16-,17?,18+,19-,20-,21+,22+,23-,24+,26+,27-/m1/s1
Synthesis Reference Hanson, Russell Floyd. Isolation, identification, formation, and metabolism of 3a, 7a-hydroxy-5b-cholestan-26-oic acid in man. (1972), 73 pp. CAN 78:27152 AN 1973:27152
Melting Point (Experimental) Not Available
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 4.36e-03 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge -1
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity 4.02 [Predicted by ALOGPS]; 6.1 [Predicted by PubChem via XLOGP] Calculated using ALOGPS
Material Safety Data Sheet (MSDS) Not Available
MOL File Show
SDF File Show
PDB File Show
2D Structure
3D Structure
Experimental PDB ID Not Available
Experimental 1H NMR Spectrum Not Available
Experimental 13C NMR Spectrum Not Available
Experimental 13C HSQC Spectrum Not Available
Predicted 1H NMR Spectrum Show Image
Show Peaklist
Predicted 13C NMR Spectrum Show Image
Show Peaklist
Mass Spectrum Not Available
Simplified TOCSY Spectrum Not Available
BMRB Spectrum Not Available
Cellular Location Not Available
Biofluid Location Not Available
Tissue Location Not Available
Concentrations (Normal) Not Available
Concentrations (Abnormal) Not Available
Associated Disorders Not Available
OMIM ID Not Available
Pathways
Name SMPDB Link KEGG Link
Bile Acid Biosynthesis SMP00035 Link Image map00120 Link Image
General References
  1. Alme B, Bremmelgaard A, Sjovall J, Thomassen P: Analysis of metabolic profiles of bile acids in urine using a lipophilic anion exchanger and computerized gas-liquid chromatorgaphy-mass spectrometry. J Lipid Res. 1977 May;18(3):339-62. [PubMed Link Image]
Metabolic Enzymes
  1. Aldehyde dehydrogenase, mitochondrial precursor
  2. Solute carrier organic anion transporter family member 1B3
  3. Solute carrier organic anion transporter family member 1B1
  4. Bile acid CoA:amino acid N-acyltransferase
  5. Canalicular multispecific organic anion transporter 2
  6. Bile salt export pump
  7. Ileal sodium/bile acid cotransporter
  8. Sodium/bile acid cotransporter
  9. Solute carrier organic anion transporter family member 1A2
  10. Bile acyl-CoA synthetase
  11. Solute carrier organic anion transporter family member 4A1
  12. Gastrotropin
Enzyme 1 [top]
Enzyme 1 ID 5530
Enzyme 1 Name Aldehyde dehydrogenase, mitochondrial precursor
Enzyme 1 Synonyms
  1. ALDH class 2
  2. ALDHI
  3. ALDH-E2
Enzyme 1 Gene Name ALDH2
Enzyme 1 Protein Sequence >Aldehyde dehydrogenase, mitochondrial precursor 
MLRAAARFGPRLGRRLLSAAATQAVPAPNQQPEVFCNQIFINNEWHDAVSRKTFPTVNPS
TGEVICQVAEGDKEDVDKAVKAARAAFQLGSPWRRMDASHRGRLLNRLADLIERDRTYLA
ALETLDNGKPYVISYLVDLDMVLKCLRYYAGWADKYHGKTIPIDGDFFSYTRHEPVGVCG
QIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLTALYVANLIKEAGFPPGVVNIVPG
FGPTAGAAIASHEDVDKVAFTGSTEIGRVIQVAAGSSNLKRVTLELGGKSPNIIMSDADM
DWAVEQAHFALFFNQGQCCCAGSRTFVQEDIYDEFVERSVARAKSRVVGNPFDSKTEQGP
QVDETQFKKILGYINTGKQEGAKLLCGGGIAADRGYFIQPTVFGDVQDGMTIAKEEIFGP
VMQILKFKTIEEVVGRANNSTYGLAAAVFTKDLDKANYLSQALQAGTVWVNCYDVFGAQS
PFGGYKMSGSGRELGEYGLQAYTEVKTVTVKVPQKNS
Enzyme 1 Number of Residues 517
Enzyme 1 Molecular Weight 56382
Enzyme 1 Theoretical pI 7.05
Enzyme 1 GO Classification
Function
  • catalytic activity
  • oxidoreductase activity
Process
  • metabolism
  • physiological process
Component
—
Enzyme 1 General Function Energy production and conversion
Enzyme 1 Specific Function An aldehyde + NAD(+) + H(2)O = an acid + NADH
Enzyme 1 Pathways
Enzyme 1 Reactions
  • an aldehyde + NAD+ + H2O = an acid + NADH + H+
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • 1-24
Enzyme 1 Transmembrane Regions Not Available
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 28606 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID P05091 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name ALDH2_HUMAN Link Image
Enzyme 1 PDB ID 1OF7 Link Image
Enzyme 1 PDB File Show
Enzyme 1 3D Structure
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >1551 bp 
ATGTTGCGCGCTGCCGCCGCTCGGGCCCCGCCTGGCCGCCGCCTCTTGTCAGCCGCCGCC
ACCCAGGCCGTGCCTGCCCCCAACCAGCAGCCCGAGGTCTTCTGCAACCAGATTTTCATA
AACAATGAATGGCACGATGCCGTCAGCAGGAAAACATTCCCCACCGTCAATCCGTCCACT
GGAGAGGTCATCTGTCAGGTAGCTGAAGGGGACAAGGAAGATGTGGACAAGGCACGTGAA
GGCCGCCCGGGCGCCTTCCAGCTGGGCTCACCTTGGCGCCGCATGGACGCATCACACAGC
GGCCGGCTGCTGAACCGCCTGGCCGATCTGATCGAGCGGGACCGGACCTACCTGGCGGCC
TTGGAGACCCTGGACAATGGCAAGCCCTATGTCATCTCCTACCTGGTGGATTTGGACATG
GTCCTCAAATGTCTCCGGTATTATGCCGGCTGGGCTGATAAGTACCACGGGAAAACCATC
CCCATTGACGGAGACTTCTTCAGCTACACACGCCATGAACCTGTGGGGGTGTGCGGGCAG
ATCATTCCGTGGAATTTCCCGCTCCTGATGCAAGCATGGAAGCTGGGCCCAGCCTTGGCA
ACTGGAAACGTGGTTGTGATGAAGGTAGCTGAGCAGACACCCCTCACCGCCCTCTATGTG
GCCAACCTGATCAAGGAGGCTGGCTTTCCCCCTGGTGTGGTCAACATTGTGCCTGGATTT
GGCCCCACGGCTGGGGCCGCCATTGCCTCCCATGAGGATGTGGACAAAGTGGCATTCACA
GGCTCCACTGAGATTGGCCGCGTAATCCAGGTTGCTGCTGGGAGCAGCAACCTCAAGAGA
GTGACCTTGGAGCTGGGGGGGAAGAGCCCCAACATCATCATGTCAGATGCCGATATGGAT
TGGGCCGTGGAACAGGCCCACTTCGCCCTGTTCTTCAACCAGGGCCAGTGCTGCTGTGCC
GGCTCCCGGACCTTCGTGCAGGAGGACATCTATGATGAGTTTGTGGTGCGGAGCGTTGCC
CGGGCCAAGTCTCGGGTGGTCGGGAACCCCTTTGATAGCAAGACCGAGCAGGGGCCGCAG
GTGGATGAAACTCAGTTTAAGAAGATCCTCGGCTACATCAACACGGGGAAGCAAGAGGGG
GCGAAGCTGCTGTGTGGTGGGGGCATTGCTGCTGACCGTGGTTACTTCATCCAGCCCACT
GTGTTTGGAGATGTGCAGGATGGCATGACCATCGCCAAGGAGGAGATCTTCGGGCCAGTG
ATGCAGATCCTGAAGTTCAAGACCATAGAGGAGGTTGTTGGGAGAGCCAACAATTCCACG
TACGGGCTGGCCGCAGCTGTCTTCACAAAGGATTTGGACAAGGCCAATTACCTGTCCCAG
GCCCTCCAGGCGGGCACTGTGTGGGTCAACTGCTATGATGTGTTTGGAGCCCAGTCACCC
TTTGGTGGCTACAAGATGTCGGGGAGTGGCCGGGAGTTGGGCGAGTACGGGCTGCAGGCA
TACACTGAAGTGAAAACTGTCACAGTCAAAGTGCCTCAGAAGAACTCATAA
Enzyme 1 GenBank Gene ID X05409 Link Image
Enzyme 1 GeneCard ID ALDH2 Link Image
Enzyme 1 GenAtlas ID ALDH2 Link Image
Enzyme 1 HGNC ID HGNC:404 Link Image
Enzyme 1 Chromosome Location 12
Enzyme 1 Locus 12q24.2
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Braun T, Bober E, Singh S, Agarwal DP, Goedde HW: Evidence for a signal peptide at the amino-terminal end of human mitochondrial aldehyde dehydrogenase. FEBS Lett. 1987 May 11;215(2):233-6. [PubMed Link Image]
  2. Braun T, Bober E, Singh S, Agarwal DP, Goedde HW: Isolation and sequence analysis of a full length cDNA clone coding for human mitochondrial aldehyde dehydrogenase. Nucleic Acids Res. 1987 Apr 10;15(7):3179. [PubMed Link Image]
  3. Hsu LC, Bendel RE, Yoshida A: Genomic structure of the human mitochondrial aldehyde dehydrogenase gene. Genomics. 1988 Jan;2(1):57-65. [PubMed Link Image]
  4. Hempel J, Kaiser R, Jornvall H: Mitochondrial aldehyde dehydrogenase from human liver. Primary structure, differences in relation to the cytosolic enzyme, and functional correlations. Eur J Biochem. 1985 Nov 15;153(1):13-28. [PubMed Link Image]
  5. Hsu LC, Tani K, Fujiyoshi T, Kurachi K, Yoshida A: Cloning of cDNAs for human aldehyde dehydrogenases 1 and 2. Proc Natl Acad Sci U S A. 1985 Jun;82(11):3771-5. [PubMed Link Image]
  6. Yoshida A, Ikawa M, Hsu LC, Tani K: Molecular abnormality and cDNA cloning of human aldehyde dehydrogenases. Alcohol. 1985 Jan-Feb;2(1):103-6. [PubMed Link Image]
  7. Agarwal DP, Goedde HW: Human aldehyde dehydrogenase isozymes and alcohol sensitivity. Isozymes Curr Top Biol Med Res. 1987;16:21-48. [PubMed Link Image]
  8. Hempel J, Hoog JO, Jornvall H: Mitochondrial aldehyde dehydrogenase. Homology of putative targeting sequence to that of carbamyl phosphate synthetase I revealed by correlation of cDNA and protein data. FEBS Lett. 1987 Sep 28;222(1):95-8. [PubMed Link Image]
  9. Yoshida A, Huang IY, Ikawa M: Molecular abnormality of an inactive aldehyde dehydrogenase variant commonly found in Orientals. Proc Natl Acad Sci U S A. 1984 Jan;81(1):258-61. [PubMed Link Image]
  10. Novoradovsky A, Tsai SJ, Goldfarb L, Peterson R, Long JC, Goldman D: Mitochondrial aldehyde dehydrogenase polymorphism in Asian and American Indian populations: detection of new ALDH2 alleles. Alcohol Clin Exp Res. 1995 Oct;19(5):1105-10. [PubMed Link Image]
  11. Ni L, Zhou J, Hurley TD, Weiner H: Human liver mitochondrial aldehyde dehydrogenase: three-dimensional structure and the restoration of solubility and activity of chimeric forms. Protein Sci. 1999 Dec;8(12):2784-90. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 5684
Enzyme 2 Name Solute carrier organic anion transporter family member 1B3
Enzyme 2 Synonyms
  1. Solute carrier family 21 member 8
  2. Organic anion transporter 8
  3. Organic anion-transporting polypeptide 8
  4. OATP8
  5. Liver-specific organic anion transporter 2
  6. LST-2
Enzyme 2 Gene Name SLCO1B3
Enzyme 2 Protein Sequence >Solute carrier organic anion transporter family member 1B3 
MDQHQHLNKTAESASSEKKKTRRCNGFKMFLAALSFSYIAKALGGIIMKISITQIERRFD
ISSSLAGLIDGSFEIGNLLVIVFVSYFGSKLHRPKLIGIGCLLMGTGSILTSLPHFFMGY
YRYSKETHINPSENSTSSLSTCLINQTLSFNGTSPEIVEKDCVKESGSHMWIYVFMGNML
RGIGETPIVPLGISYIDDFAKEGHSSLYLGSLNAIGMIGPVIGFALGSLFAKMYVDIGYV
DLSTIRITPKDSRWVGAWWLGFLVSGLFSIISSIPFFFLPKNPNKPQKERKISLSLHVLK
TNDDRNQTANLTNQGKNVTKNVTGFFQSLKSILTNPLYVIFLLLTLLQVSSFIGSFTYVF
KYMEQQYGQSASHANFLLGIITIPTVATGMFLGGFIIKKFKLSLVGIAKFSFLTSMISFL
FQLLYFPLICESKSVAGLTLTYDGNNSVASHVDVPLSYCNSECNCDESQWEPVCGNNGIT
YLSPCLAGCKSSSGIKKHTVFYNCSCVEVTGLQNRNYSAHLGECPRDNTCTRKFFIYVAI
QVINSLFSATGGTTFILLTVKIVQPELKALAMGFQSMVIRTLGGILAPIYFGALIDKTCM
KWSTNSCGAQGACRIYNSVFFGRVYLGLSIALRFPALVLYIVFIFAMKKKFQGKDTKASD
NERKVMDEANLEFLNNGEHFVPSAGTDSKTCNLDMQDNAAAN
Enzyme 2 Number of Residues 702
Enzyme 2 Molecular Weight 77404
Enzyme 2 Theoretical pI 8.95
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 transport of organic anions such as 17-beta-glucuronosyl estradiol, taurocholate, triiodothyronine (T3), leukotriene C4, dehydroepiandrosterone sulfate (DHEAS), methotrexate and sulfobromophthalein (BSP)
Enzyme 2 Pathways Not Available
Enzyme 2 Reactions Not Available
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • None
Enzyme 2 Transmembrane Regions
  • 30-50 65-85 97-117 171-191 207-227 259-279 336-356 377-397 410-430 538-558 575-595 626-646
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 9188300 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID Q9NPD5 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name SO1B3_HUMAN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >84 bp 
ATGGACCAACATCAACATTTGAATAAAACAGCAGAGTCAGCATCTTCAGAGAAAAAGAAA
ACAAGACGCTGCAATGGATTCAAG
Enzyme 2 GenBank Gene ID AJ400763 Link Image
Enzyme 2 GeneCard ID SLCO1B3 Link Image
Enzyme 2 GenAtlas ID SLCO1B3 Link Image
Enzyme 2 HGNC ID HGNC:10961 Link Image
Enzyme 2 Chromosome Location 12
Enzyme 2 Locus 12p12
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. 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]
  2. Abe T, Unno M, Onogawa T, Tokui T, Kondo TN, Nakagomi R, Adachi H, Fujiwara K, Okabe M, Suzuki T, Nunoki K, Sato E, Kakyo M, Nishio T, Sugita J, Asano N, Tanemoto M, Seki M, Date F, Ono K, Kondo Y, Shiiba K, Suzuki M, Ohtani H, Shimosegawa T, Iinuma K, Nagura H, Ito S, Matsuno S: LST-2, a human liver-specific organic anion transporter, determines methotrexate sensitivity in gastrointestinal cancers. Gastroenterology. 2001 Jun;120(7):1689-99. [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
  1. 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]
Enzyme 4 [top]
Enzyme 4 ID 5821
Enzyme 4 Name Bile acid CoA:amino acid N-acyltransferase
Enzyme 4 Synonyms
  1. BAT
  2. BACAT
  3. Glycine N-choloyltransferase
  4. Long-chain fatty-acyl-CoA hydrolase
Enzyme 4 Gene Name BAAT
Enzyme 4 Protein Sequence >Bile acid CoA:amino acid N-acyltransferase 
MIQLTATPVSALVDEPVHIRATGLIPFQMVSFQASLEDENGDMFYSQAHYRANEFGEVDL
NHASSLGGDYMGVHPMGLFWSLKPEKLLTRLLKRDVMNRPFQVQVKLYDLELIVNNKVAS
APKASLTLERWYVAPGVTRIKVREGRLRGALFLPPGEGLFPGVIDLFGGLGGLLEFRASL
LASRGFASLALAYHNYEDLPRKPEVTDLEYFEEAANFLLRHPKVFGSGVGVVSVCQGVQI
GLSMAIYLKQVTATVLINGTNFPFGIPQVYHGQIHQPLPHSAQLISTNALGLLELYRTFE
TTQVGASQYLFPIEEAQGQFLFIVGEGDKTINSKAHAEQAIGQLKRHGKNNWTLLSYPGA
GHLIEPPYSPLCCASTTHDLRLHWGGEVIPHAAAQEHAWKEIQRFLRKHLIPDVTSQL
Enzyme 4 Number of Residues 418
Enzyme 4 Molecular Weight 46300
Enzyme 4 Theoretical pI 7.00
Enzyme 4 GO Classification
Function
  • CoA hydrolase activity
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • palmitoyl-CoA hydrolase activity
  • thiolester hydrolase activity
Process
  • lipid metabolism
  • metabolism
  • physiological process
  • primary metabolism
Component
—
Enzyme 4 General Function Not Available
Enzyme 4 Specific Function Involved in bile acid metabolism. In liver hepatocytes catalyzes the second step in the conjugation of C24 bile acids (choloneates) to glycine and taurine before excretion into bile canaliculi. The major components of bile are cholic acid and chenodeoxycholic acid. In a first step the bile acids are converted to an acyl-CoA thioester, either in peroxisomes (primary bile acids deriving from the cholesterol pathway), or cytoplasmic at the endoplasmic reticulum (secondary bile acids). May catalyze the conjugation of primary or secondary bile acids, or both. The conjugation increases the detergent properties of bile acids in the intestine, which facilitates lipid and fat-soluble vitamin absorption. In turn, bile acids are deconjugated by bacteria in the intestine and are recycled back to the liver for reconjugation (secondary bile acids). May also act as an acyl-CoA thioesterase that regulates intracellular levels of free fatty acids. In vitro, catalyzes the hydrolysis of long- and very long-chain saturated acyl-CoAs to the free fatty acid and coenzyme A (CoASH), and conjugates glycine to these acyl-CoAs
Enzyme 4 Pathways
Enzyme 4 Reactions
  • palmitoyl-CoA + H2O = CoA + palmitate
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • None
Enzyme 4 Transmembrane Regions
  • None
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein 532505 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID Q14032 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name BAAT_HUMAN Link Image
Enzyme 4 PDB ID Not Available
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence >1257 bp 
ATGATCCAGTTGACAGCTACCCCTGTGAGTGCACTTGTTGATGAGCCAGTGCATATCCGA
GCTACAGGCCTGATTCCCTTTCAGATGGTGAGTTTTCAGGCATCACTGGAAGATGAAAAC
GGAGACATGTTTTATTCTCAAGCCCACTATAGGGCCAATGAATTCGGTGAGGTGGACCTG
AATCATGCTTCTTCACTTGGAGGGGATTATATGGGAGTCCACCCCATGGGTCTCTTCTGG
TCTCTGAAACCTGAAAAGCTATTAACAAGACTGTTGAAAAGAGATGTGATGAATAGGCCT
TTCCAGGTCCAAGTAAAACTTTATGACTTAGAGTTAATAGTGAACAATAAAGTTGCCAGT
GCTCCAAAGGCCAGCCTGACTTTGGAGAGGTGGTATGTGGCACCTGGTGTCACACGAATT
AAGGTTCGAGAAGGCCGCCTTCGAGGAGCTCTCTTTCTCCCTCCAGGAGAGGGTCTCTTC
CCAGGGGTAATTGATTTGTTTGGTGGTTTGGGTGGGCTGCTTGAATTTCGGGCCAGCCTC
CTAGCCAGTCGTGGCTTCGCCTCCTTGGCCTTGGCTTACCATAACTATGAAGACCTGCCC
CGCAAACCAGAAGTAACAGATTTGGAATATTTTGAGGAGGCTGCCAACTTTCTCCTGAGA
CATCCAAAGGTCTTTGGCTCAGGCGTTGGGGTAGTCTCTGTATGTCAAGGAGTACAGATT
GGACTATCTATGGCTATTTACCTAAAGCAAGTCACAGCCACGGTACTTATTAATGGGACC
AACTTTCCTTTTGGCATTCCACAGGTATATCATGGTCAGATCCATCAGCCCCTTCCCCAT
TCTGCACAATTAATATCCACCAATGCCTTGGGGTTACTAGAGCTCTATCGCACTTTTGAG
ACAACTCAAGTTGGGGCCAGTCAATATTTGTTTCCTATTGAAGAGGCCCAGGGGCAATTC
CTCTTCATTGTAGGAGAAGGTGATAAGACTATCAACAGCAAAGCACACGCTGAACAAGCC
ATAGGACAGCTGAAGAGACATGGGAAGAACAACTGGACCCTGCTATCTTACCCTGGGGCA
GGCCACCTGATAGAACCTCCCTATTCTCCTCTGTGCTGTGCCTCAACGACCCACGATTTG
AGGTTACACTGGGGAGGAGAGGTGATCCCACACGCAGCTGCACAGGAACATGCTTGGAAG
GAGATCCAGAGATTTCTCAGGAAGCACCTCATTCCAGATGTGACCAGTCAACTCTAA
Enzyme 4 GenBank Gene ID L34081 Link Image
Enzyme 4 GeneCard ID BAAT Link Image
Enzyme 4 GenAtlas ID BAAT Link Image
Enzyme 4 HGNC ID HGNC:932 Link Image
Enzyme 4 Chromosome Location 9
Enzyme 4 Locus 9q22.3
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References
  1. Falany CN, Johnson MR, Barnes S, Diasio RB: Glycine and taurine conjugation of bile acids by a single enzyme. Molecular cloning and expression of human liver bile acid CoA:amino acid N-acyltransferase. J Biol Chem. 1994 Jul 29;269(30):19375-9. [PubMed Link Image]
  2. Carlton VE, Harris BZ, Puffenberger EG, Batta AK, Knisely AS, Robinson DL, Strauss KA, Shneider BL, Lim WA, Salen G, Morton DH, Bull LN: Complex inheritance of familial hypercholanemia with associated mutations in TJP2 and BAAT. Nat Genet. 2003 May;34(1):91-6. [PubMed Link Image]
Enzyme 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 7519
Enzyme 5 Name Canalicular multispecific organic anion transporter 2
Enzyme 5 Synonyms
  1. ATP-binding cassette sub-family C member 3
  2. Multidrug resistance-associated protein 3
  3. Multi-specific organic anion transporter-D
  4. MOAT-D
Enzyme 5 Gene Name ABCC3
Enzyme 5 Protein Sequence >Canalicular multispecific organic anion transporter 2 
MDALCGSGELGSKFWDSNLSVHTENPDLTPCFQNSLLAWVPCIYLWVALPCYLLYLRHHC
RGYIILSHLSKLKMVLGVLLWCVSWADLFYSFHGLVHGRAPAPVFFVTPLVVGVTMLLAT
LLIQYERLQGVQSSGVLIIFWFLCVVCAIVPFRSKILLAKAEGEISDPFRFTTFYIHFAL
VLSALILACFREKPPFFSAKNVDPNPYPETSAGFLSRLFFWWFTKMAIYGYRHPLEEKDL
WSLKEEDRSQMVVQQLLEAWRKQEKQTARHKASAAPGKNASGEDEVLLGARPRPRKPSFL
KALLATFGSSFLISACFKLIQDLLSFINPQLLSILIRFISNPMAPSWWGFLVAGLMFLCS
MMQSLILQHYYHYIFVTGVKFRTGIMGVIYRKALVITNSVKRASTVGEIVNLMSVDAQRF
MDLAPFLNLLWSAPLQIILAIYFLWQNLGPSVLAGVAFMVLLIPLNGAVAVKMRAFQVKQ
MKLKDSRIKLMSEILNGIKVLKLYAWEPSFLKQVEGIRQGELQLLRTAAYLHTTTTFTWM
CSPFLVTLITLWVYVYVDPNNVLDAEKAFVSVSLFNILRLPLNMLPQLISNLTQASVSLK
RIQQFLSQEELDPQSVERKTISPGYAITIHSGTFTWAQDLPPTLHSLDIQVPKGALVAVV
GPVGCGKSSLVSALLGEMEKLEGKVHMKGSVAYVPQQAWIQNCTLQENVLFGKALNPKRY
QQTLEACALLADLEMLPGGDQTEIGEKGINLSGGQRQRVSLARAVYSDADIFLLDDPLSA
VDSHVAKHIFDHVIGPEGVLAGKTRVLVTHGISFLPQTDFIIVLADGQVSEMGPYPALLQ
RNGSFANFLCNYAPDEDQGHLEDSWTALEGAEDKEALLIEDTLSNHTDLTDNDPVTYVVQ
KQFMRQLSALSSDGEGQGRPVPRRHLGPSEKVQVTEAKADGALTQEEKAAIGTVELSVFW
DYAKAVGLCTTLAICLLYVGQSAAAIGANVWLSAWTNDAMADSRQNNTSLRLGVYAALGI
LQGFLVMLAAMAMAAGGIQAARVLHQALLHNKIRSPQSFFDTTPSGRILNCFSKDIYVVD
EVLAPVILMLLNSFFNAISTLVVIMASTPLFTVVILPLAVLYTLVQRFYAATSRQLKRLE
SVSRSPIYSHFSETVTGASVIRAYNRSRDFEIISDTKVDANQRSCYPYIISNRWLSIGVE
FVGNCVVLFAALFAVIGRSSLNPGLVGLSVSYSLQVTFALNWMIRMMSDLESNIVAVERV
KEYSKTETEAPWVVEGSRPPEGWPPRGEVEFRNYSVRYRPGLDLVLRDLSLHVHGGEKVG
IVGRTGAGKSSMTLCLFRILEAAKGEIRIDGLNVADIGLHDLRSQLTIIPQDPILFSGTL
RMNLDPFGSYSEEDIWWALELSHLHTFVSSQPAGLDFQCSEGGENLSVGQRQLVCLARAL
LRKSRILVLDEATAAIDLETDNLIQATIRTQFDTCTVLTIAHRLNTIMDYTRVLVLDKGV
VAEFDSPANLIAARGIFYGMARDAGLA
Enzyme 5 Number of Residues 1527
Enzyme 5 Molecular Weight 169345
Enzyme 5 Theoretical pI 7.20
Enzyme 5 GO Classification
Function
  • ATP binding
  • ATPase activity
  • ATPase activity, coupled to transmembrane movement of substances
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on acid anhydrides
  • hydrolase activity, acting on acid anhydrides, catalyzing transmembrane movement of substances
  • hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides
  • nucleoside-triphosphatase activity
  • nucleotide binding
  • purine nucleotide binding
  • pyrophosphatase activity
  • transporter activity
Process
  • cellular physiological process
  • physiological process
  • transport
Component
  • cell
  • integral to membrane
  • intrinsic to membrane
  • membrane
Enzyme 5 General Function Defense mechanisms
Enzyme 5 Specific Function May act as an inducible transporter in the biliary and intestinal excretion of organic anions
Enzyme 5 Pathways Not Available
Enzyme 5 Reactions Not Available
Enzyme 5 Pfam Domain Function
Enzyme 5 Signals
  • None
Enzyme 5 Transmembrane Regions
  • 33-53 74-94 100-120 133-153 172-192 303-323 350-370 427-447 451-471 534-554 577-597 964-984 1022-1042 1086-1106 1108-1128 1200-1220 1223-1243
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein 3132270 Link Image
Enzyme 5 UniProtKB/Swiss-Prot ID O15438 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name MRP3_HUMAN Link Image
Enzyme 5 PDB ID Not Available
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence >4584 bp 
ATGGACGCCCTGTGCGGTTCCGGGGAGCTCGGCTCCAAGTTCTGGGACTCCAACCTGTCT
GTGCACACAGAAAACCCGGACCTCACTCCCTGCTTCCAGAACTCCCTGCTGGCCTGGGTG
CCCTGCATCTACCTGTGGGTCGCCCTGCCCTGCTACTTGCTCTACCTGCGGCACCATTGT
CGTGGCTACATCATCCTCTCCCACCTGTCCAAGCTCAAGATGGTCCTGGGTGTCCTGCTG
TGGTGCGTCTCCTGGGCAGACCTTTTTTACTCCTTCCATGGCCTGGTCCATGGCCGGGCC
CCTGCCCCTGTTTTCTTTGTCACCCCCTTGGTGGTGGGGGTCACCATGCTGCTGGCCACC
CTGCTGATACAGTATGAGCGGCTGCAGGGCGTACAGTCTTCGGGGGTCCTCATTATCTTC
TGGTTCCTGTGTGTGGTCTGCGCCATCGTCCCATTCCGCTCCAAGATCCTTTTAGCCAAG
GCAGAGGGTGAGATCTCAGACCCCTTCCGCTTCACCACCTTCTACATCCACTTTGCCCTG
GTACTCTCTGCCCTCATCTTGGCCTGCTTCAGGGAGAAACCTCCATTTTTCTCCGCAAAG
AATGTCGACCCTAACCCCTACCCTGAGACCAGCGCTGGCTTTCTCTCCCGCCTGTTTTTC
TGGTGGTTCACAAAGATGGCCATCTATGGCTACCGGCATCCCCTGGAGGAGAAGGACCTC
TGGTCCCTAAAGGAAGAGGACAGATCCCAGATGGTGGTGCAGCAGCTGCTGGAGGCATGG
AGGAAGCAGGAAAAGCAGACGGCACGACACAAGGCTTCAGCAGCACCTGGGAAAAATGCC
TCCGGCGAGGACGAGGTGCTGCTGGGTGCCCGGCCCAGGCCCCGGAAGCCCTCCTTCCTG
AAGGCCCTGCTGGCCACCTTCGGCTCCAGCTTCCTCATCAGTGCCTGCTTCAAGCTTATC
CAGGACCTGCTCTCCTTCATCAATCCACAGCTGCTCAGCATCCTGATCAGGTTTATCTCC
AACCCCATGGCCCCCTCCTGGTGGGGCTTCCTGGTGGCTGGGCTGATGTTCCTGTGCTCC
ATGATGCAGTCGCTGATCTTACAACACTATTACCACTACATCTTTGTGACTGGGGTGAAG
TTTCGTACTGGGATCATGGGTGTCATCTACAGGAAGGCTCTGGTTATCACCAACTCAGTC
AAACGTGCGTCCACTGTGGGGGAAATTGTCAACCTCATGTCAGTGGATGCCCAGCGCTTC
ATGGACCTTGCCCCCTTCCTCAATCTGCTGTGGTCAGCACCCCTGCAGATCATCCTGGCG
ATCTACTTCCTCTGGCAGAACCTAGGTCCCTCTGTCCTGGCTGGAGTCGCTTTCATGGTC
TTGCTGATTCCACTCAACGGAGCTGTGGCCGTGAAGATGCGCGCCTTCCAGGTAAAGCAA
ATGAAATTGAAGGACTCGCGCATCAAGCTGATGAGTGAGATCCTGAACGGCATCAAGGTG
CTGAAGCTGTACGCCTGGGAGCCCAGCTTCCTGAAGCAGGTGGAGGGCATCAGGCAGGGT
GAGCTCCAGCTGCTGCGCACGGCGGCCTACCTCCACACCACAACCACCTTCACCTGGATG
TGCAGCCCCTTCCTGGTGACCCTGATCACCCTCTGGGTGTACGTGTACGTGGACCCAAAC
AATGTGCTGGACGCCGAGAAGGCCTATGTGTCTGTGTCCTTGTTTAATATCTTAAGACTT
CCCCTCAACATGCTGCCCCAGTTAATCAGCAACCTGACTCAGGCCAGTGTGTCTCTGAAA
CGGATCCAGCAATTCCTGAGCCAAGAGGAACTTGACCCCCAGAGTGTGGAAAGAAAGACC
ATCTCCCCAGGCTATGCCATCACCATACACAGTGGCACCTTCACCTGGGCCCAGGACCTG
CCCCCCACTCTGCACAGCCTAGACATCCAGGTCCCGAAAGGGGCACTGGTGGCCGTGGTG
GGGCCTGTGGGCTGTGGGAAGTCCTCCCTGGTGTCTGCCCTGCTGGGAGAGATGGAGAAG
CTAGAAGGCAAAGTGCACATGAAGGGCTCCGTGGCCTATGTGCCCCAGCAGGCATGGATC
CAGAACTGCACTCTTCAGGAAAACGTGCTTTTCGGCAAAGCCCTGAACCCCAAGCGCTAC
CAGCAGACTCTGGAGGCCTGTGCCTTGCTAGCTGACCTGGAGATGCTGCCTGGTGGGGAT
CAGACAGAGATTGGAGAGAAGGGCATTAACCTGTCTGGGGGCCAGCGGCAGCGGGTCAGT
CTGGCTCGAGCTGTTTACAGTGATGCCGATATTTTCTTGCTGGATGACCCACTGTCCGCG
GTGGACTCTCATGTGGCCAAGCACATCTTTGACCACGTCATCGGGCCAGAAGGCGTGCTG
GCAGGCAAGACGCGAGTGCTGGTGACGCACGGCATTAGCTTCCTGCCCCAGACAGACTTC
ATCATTGTGCTAGCTGATGGACAGGTGTCTGAGATGGGCCCGTACCCAGCCCTGCTGCAG
CGCAACGGCTCCTTTGCCAACTTTCTCTGCAACTATGCCCCCGATGAGGACCAAGGGCAC
CTGGAGGACAGCTGGACCGCGTTGGAAGGTGCAGAGGATAAGGAGGCACTGCTGATTGAA
GACACACTCAGCAACCACACGGATCTGACAGACAATGATCCAGTCACCTATGTGGTCCAG
AAGCAGTTTATGAGACAGCTGAGTGCCCTGTCCTCAGATGGGGAGGGACAGGGTCGGCCT
GTACCCCGGAGGCACCTGGGTCCATCAGAGAAGGTGCAGGTGACAGAGGCGAAGGCAGAT
GGGGCACTGACCCAGGAGGAGAAAGCAGCCATTGGCACTGTGGAGCTCAGTGTGTTCTGG
GATTATGCCAAGGCCGTGGGGCTCTGTACCACGCTGGCCATCTGTCTCCTGTATGTGGGT
CAAAGTGCGGCTGCCATTGGAGCCAATGTGTGGCTCAGTGCCTGGACAAATGATGCCATG
GCAGACAGTAGACAGAACAACACTTCCCTGAGGCTGGGCGTCTATGCTGCTTTAGGAATT
CTGCAAGGGTTCTTGGTGATGCTGGCAGCCATGGCCATGGCAGCGGGTGGCATCCAGGCT
GCCCGTGTGTTGCACCAGGCACTGCTGCACAACAAGATACGCTCGCCACAGTCCTTCTTT
GACACCACACCATCAGGCCGCATCCTGAACTGCTTCTCCAAGGACATCTATGTCGTTGAT
GAGGTTCTGGCCCCTGTCATCCTCATGCTGCTCAATTCCTTCTTCAACGCCATCTCCACT
CTTGTGGTCATCATGGCCAGCACGCCGCTCTTCACTGTGGTCATCCTGCCCCTGGCTGTG
CTCTACACCTTAGTGCAGCGCTTCTATGCAGCCACATCACGGCAACTGAAGCGGCTGGAA
TCAGTCAGCCGCTCACCTATCTACTCCCACTTTTCGGAGACAGTGACTGGTGCCAGTGTC
ATCCGGGCCTACAACCGCAGCCGGGATTTTGAGATCATCAGTGATACTAAGGTGGATGCC
AACCAGAGAAGCTGCTACCCCTACATCATCTCCAACCGGTGGCTGAGCATCGGAGTGGAG
TTCGTGGGGAACTGCGTGGTGCTCTTTGCTGCACTATTTGCCGTCATCGGGAGGAGCAGC
CTGAACCCGGGGCTGGTGGGCCTTTCTGTGTCCTACTCCTTGCAGGTGACATTTGCTCTG
AACTGGATGATACGAATGATGTCAGATTTGGAATCTAACATCGTGGCTGTGGAGAGGGTC
AAGGAGTACTCCAAGACAGAGACAGAGGCGCCCTGGGTGGTGGAAGGCAGCCGCCCTCCC
GAAGGTTGGCCCCCACGTGGGGAGGTGGAGTTCCGGAATTATTCTGTGCGCTACCGGCCG
GGCCTAGACCTGGTGCTGAGAGACCTGAGTCTGCATGTGCATGGTGGCGAGAAGGTGGGG
ATCGTGGGCCGCACTGGGGCTGGCAAGTCTTCCATGACCCTTTGCCTGTTCCGCATCCTG
GAGGCGGCAAAGGGTGAAATCCGCATTGATGGCCTCAATGTGGCAGACATCGGCCTCCAT
GACCTGCGCTCTCAGCTGACCATCATCCCGCAGGACCCCATCCTGTTCTCGGGGACCCTG
CGCATGAACCTGGACCCCTTCGGCAGCTACTCAGAGGAGGACATTTGGTGGGCTTTGGAG
CTGTCCCACCTGCACACGTTTGTGAGCTCCCAGCCGGCAGGCCTGGACTTCCAGTGCTCA
GAGGGCGGGGAGAATCTCAGCGTGGGCCAGAGGCAGCTCGTGTGCCTGGCCCGAGCCCTG
CTCCGCAAGAGCCGCATCCTGGTTTTAGACGAGGCCACAGCTGCCATCGACCTGGAGACT
GACAACCTCATCCAGGCTACCATCCGCACCCAGTTTGATACCTGCACTGTCCTGACCATC
GCACACCGGCTTAACACTATCATGGACTACACCAGGGTCCTGGTCCTGGACAAAGGAGTA
GTAGCTGAGTTTGATTCTCCAGCCAACCTCATTGCAGCTAGAGGCATCTTCTACGGGATG
GCCAGAGATGCTGGACTTGCCTAA
Enzyme 5 GenBank Gene ID AB010887 Link Image
Enzyme 5 GeneCard ID ABCC3 Link Image
Enzyme 5 GenAtlas ID ABCC3 Link Image
Enzyme 5 HGNC ID HGNC:54 Link Image
Enzyme 5 Chromosome Location 17
Enzyme 5 Locus 17q22
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 General References
  1. Kiuchi Y, Suzuki H, Hirohashi T, Tyson CA, Sugiyama Y: cDNA cloning and inducible expression of human multidrug resistance associated protein 3 (MRP3). FEBS Lett. 1998 Aug 14;433(1-2):149-52. [PubMed Link Image]
  2. Konig J, Rost D, Cui Y, Keppler D: Characterization of the human multidrug resistance protein isoform MRP3 localized to the basolateral hepatocyte membrane. Hepatology. 1999 Apr;29(4):1156-63. [PubMed Link Image]
  3. Uchiumi T, Hinoshita E, Haga S, Nakamura T, Tanaka T, Toh S, Furukawa M, Kawabe T, Wada M, Kagotani K, Okumura K, Kohno K, Akiyama S, Kuwano M: Isolation of a novel human canalicular multispecific organic anion transporter, cMOAT2/MRP3, and its expression in cisplatin-resistant cancer cells with decreased ATP-dependent drug transport. Biochem Biophys Res Commun. 1998 Nov 9;252(1):103-10. [PubMed Link Image]
  4. Fromm MF, Leake B, Roden DM, Wilkinson GR, Kim RB: Human MRP3 transporter: identification of the 5'-flanking region, genomic organization and alternative splice variants. Biochim Biophys Acta. 1999 Jan 8;1415(2):369-74. [PubMed Link Image]
  5. Belinsky MG, Bain LJ, Balsara BB, Testa JR, Kruh GD: Characterization of MOAT-C and MOAT-D, new members of the MRP/cMOAT subfamily of transporter proteins. J Natl Cancer Inst. 1998 Nov 18;90(22):1735-41. [PubMed Link Image]
  6. Kool M, de Haas M, Scheffer GL, Scheper RJ, van Eijk MJ, Juijn JA, Baas F, Borst P: Analysis of expression of cMOAT (MRP2), MRP3, MRP4, and MRP5, homologues of the multidrug resistance-associated protein gene (MRP1), in human cancer cell lines. Cancer Res. 1997 Aug 15;57(16):3537-47. [PubMed Link Image]
Enzyme 5 Metabolite References Not Available
Enzyme 6 [top]
Enzyme 6 ID 7531
Enzyme 6 Name Bile salt export pump
Enzyme 6 Synonyms
  1. ATP-binding cassette sub-family B member 11
Enzyme 6 Gene Name ABCB11
Enzyme 6 Protein Sequence >Bile salt export pump 
MSDSVILRSIKKFGEENDGFESDKSYNNDKKSRLQDEKKGDGVRVGFFQLFRFSSSTDIW
LMFVGSLCAFLHGIAQPGVLLIFGTMTDVFIDYDVELQELQIPGKACVNNTIVWTNSSLN
QNMTNGTRCGLLNIESEMIKFASYYAGIAVAVLITGYIQICFWVIAAARQIQKMRKFYFR
RIMRMEIGWFDCNSVGELNTRFSDDINKINDAIADQMALFIQRMTSTICGFLLGFFRGWK
LTLVIISVSPLIGIGAATIGLSVSKFTDYELKAYAKAGVVADEVISSMRTVAAFGGEKRE
VERYEKNLVFAQRWGIRKGIVMGFFTGFVWCLIFLCYAVAFWYGSTLVLDEGEYTPGTLV
QIFLSVIVGALNLGNASPCLEAFATGRAAATSIFETIDRKPIIDCMSEDGYKLDRIKGEI
EFHNVTFHYPSRPEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVT
VDGHDIRSLNIQWLRDQIGIVEQEPVLFSTTIAENIRYGREDATMEDIVQAAKEANAYNF
IMDLPQQFDTLVGEGGGQMSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEV
LSKIQHGHTIISVAHRLSTVRAADTIIGFEHGTAVERGTHEELLERKGVYFTLVTLQSQG
NQALNEEDIKDATEDDMLARTFSRGSYQDSLRASIRQRSKSQLSYLVHEPPLAVVDHKST
YEEDRKDKDIPVQEEVEPAPVRRILKFSAPEWPYMLVGSVGAAVNGTVTPLYAFLFSQIL
GTFSIPDKEEQRSQINGVCLLFVAMGCVSLFTQFLQGYAFAKSGELLTKRLRKFGFRAML
GQDIAWFDDLRNSPGALTTRLATDASQVQGAAGSQIGMIVNSFTNVTVAMIIAFSFSWKL
SLVILCFFPFLALSGATQTRMLTGFASRDKQALEMVGQITNEALSNIRTVAGIGKERRFI
EALETELEKPFKTAIQKANIYGFCFAFAQCIMFIANSASYRYGGYLISNEGLHFSYVFRV
ISAVVLSATALGRAFSYTPSYAKAKISAARFFQLLDRQPPISVYNTAGEKWDNFQGKIDF
VDCKFTYPSRPDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMID
GHDSKKVNVQFLRSNIGIVSQEPVLFACSIMDNIKYGDNTKEIPMERVIAAAKQAQLHDF
VMSLPEKYETNVGSQGSQLSRGEKQRIAIARAIVRDPKILLLDEATSALDTESEKTVQVA
LDKAREGRTCIVIAHRLSTIQNADIIAVMAQGVVIEKGTHEELMAQKGAYYKLVTTGSPI
S
Enzyme 6 Number of Residues 1321
Enzyme 6 Molecular Weight 146395
Enzyme 6 Theoretical pI 6.52
Enzyme 6 GO Classification
Function
  • ATP binding
  • ATPase activity
  • ATPase activity, coupled to transmembrane movement of substances
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on acid anhydrides
  • hydrolase activity, acting on acid anhydrides, catalyzing transmembrane movement of substances
  • hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides
  • nucleoside-triphosphatase activity
  • nucleotide binding
  • purine nucleotide binding
  • pyrophosphatase activity
Process
  • cellular physiological process
  • physiological process
  • transport
Component
  • cell
  • integral to membrane
  • intrinsic to membrane
  • membrane
Enzyme 6 General Function Defense mechanisms
Enzyme 6 Specific Function Involved in the ATP-dependent secretion of bile salts into the canaliculus of hepatocytes
Enzyme 6 Pathways Not Available
Enzyme 6 Reactions Not Available
Enzyme 6 Pfam Domain Function
Enzyme 6 Signals
  • None
Enzyme 6 Transmembrane Regions
  • 63-83 148-168 216-236 241-261 320-340 354-374 756-776 795-815 870-890 891-911 980-1000 1012-1032
Enzyme 6 Essentiality Not Available
Enzyme 6 GenBank ID Protein 3873243 Link Image
Enzyme 6 UniProtKB/Swiss-Prot ID O95342 Link Image
Enzyme 6 UniProtKB/Swiss-Prot Entry Name ABCBB_HUMAN Link Image
Enzyme 6 PDB ID Not Available
Enzyme 6 Cellular Location Not Available
Enzyme 6 Gene Sequence >3966 bp 
ATGTCTGACTCAGTAATTCTTCGAAGTATAAAGAAATTTGGAGAGGAGAATGATGGTTTT
GAGTCAGATAAATCATATAATAATGATAAGAAATCAAGGTTACAAGATGAGAAGAAAGGT
GATGGCGTTAGAGTTGGCTTCTTTCAATTGTTTCGGTTTTCTTCATCAACTGACATTTGG
CTGATGTTTGTGGGAAGTTTGTGTGCATTTCTCCATGGAATAGCCCAGCCAGGCGTGCTA
CTCATTTTTGGCACAATGACAGATGTTTTTATTGACTACGACGTTGAGTTACAAGAACTC
CAGATTCCAGGAAAAGCATGTGTGAATAACACCATTGTATGGACTAACAGTTCCCTCAAC
CAGAACATGACAAATGGAACACGTTGTGGGTTGCTGAACATCGAGAGCGAAATGATCAAA
TTTGCCAGTTACTATGCTGGAATTGCTGTCGCAGTACTTATCACAGGATATATTCAAATA
TGCTTTTGGGTCATTGCCGCAGCTCGTCAGATACAGAAAATGAGAAAATTTTACTTTAGG
AGAATAATGAGAATGGAAATAGGGTGGTTTGACTGCAATTCAGTGGGGGAGCTGAATACA
AGATTCTCTGATGATATTAATAAAATCAATGATGCCATAGCTGACCAAATGGCCCTTTTC
ATTCAGCGCATGACCTCGACCATCTGTGGTTTCCTGTTGGGATTTTTCAGGGGTTGGAAA
CTGACCTTGGTTATTATTTCTGTCAGCCCTCTCATTGGGATTGGAGCAGCCACCATTGGT
CTGAGTGTGTCCAAGTTTACGGACTATGAGCTGAAGGCCTATGCCAAAGCAGGGGTGGTG
GCTGATGAAGTCATTTCATCAATGAGAACAGTGGCTGCTTTTGGTGGTGAGAAAAGAGAG
GTTGAAAGGTATGAGAAAAATCTTGTGTTCGCCCAGCGTTGGGGAATTAGAAAAGGAATA
GTGATGGGATTCTTTACTGGATTCGTGTGGTGTCTCATCTTTTTGTGTTATGCAGTGGCC
TTCTGGTACGGCTCCACACTTGTCCTGGATGAAGGAGAATATACACCAGGAACCCTTGTC
CAGATTTTCCTCAGTGTCATAGTAGGAGCTTTAAATCTTGGCAATGCCTCTCCTTGTTTG
GAAGCCTTTGCAACTGGACGTGCAGCAGCCACCAGCATTTTTGAGACAATAGACAGGAAA
CCCATCATTGACTGCATGTCAGAAGATGGTTACAAGTTGGATCGAATCAAGGGTGAAATT
GAATTCCATAATGTGACCTTCCATTATCCTTCCAGACCAGAGGTGAAGATTCTAAATGAC
CTCAACATGGTCATTAAACCAGGGGAAATGACAGCTCTGGTAGGACCCAGTGGAGCTGGA
AAAAGTACAGCACTGCAACTCATTCAGCGATTCTATGACCCCTGTGAAGGAATGGTGACC
GTGGATGGCCATGACATTCGCTCTCTTAACATTCAGTGGCTTAGAGATCAGATTGGGATA
GTGGAGCAAGAGCCAGTTCTGTTCTCTACCACCATTGCAGAAAATATTCGCTATGGCAGA
GAAGATGCAACAATGGAAGACATAGTCCAAGCTGCCAAGGAGGCCAATGCCTACAACTTC
ATCATGGACCTGCCACAGCAATTTGACACCCTTGTTGGAGAAGGAGGAGGCCAGATGAGT
GGTGGCCAGAAACAAAGGGTAGCTATCGCCAGAGCCCTCATCCGAAATCCCAAGATTCTG
CTTTTGGACATGGCCACCTCAGCTCTGGACAATGAGAGTGAAGCCATGGTGCAAGAAGTG
CTGAGTAAGATTCAGCATGGGCACACAATCATTTCAGTTGCTCATCGCTTGTCTACGGTC
AGAGCTGCAGATACCATCATTGGTTTTGAACATGGCACTGCAGTGGAAAGAGGGACCCAT
GAAGAATTACTGGAAAGGAAAGGTGTTTACTTCACTCTAGTGACTTTGCAAAGCCAGGGA
AATCAAGCTCTTAATGAAGAGGACATAAAGGATGCAACTGAAGATGACATGCTTGCGAGG
ACCTTTAGCAGAGGGAGCTACCAGGATAGTTTAAGGGCTTCCATCCGGCAACGCTCCAAG
TCTCAGCTTTCTTACCTGGTGCACGAACCTCCATTAGCTGTTGTAGATCATAAGTCTACC
TATGAAGAAGATAGAAAGGACAAGGACATTCCTGTGCAGGAAGAAGTTGAACCTGCCCCA
GTTAGGAGGATTCTGAAATTCAGTGCTCCAGAATGGCCCTACATGCTGGTAGGGTCTGTG
GGTGCAGCTGTGAACGGGACAGTCACACCCTTGTATGCCTTTTTATTCAGCCAGATTCTT
GGGACTTTTTCAATTCCTGATAAAGAGGAACAAAGGTCACAGATCAATGGTGTGTGCCTA
CTTTTTGTAGCAATGGGCTGTGTATCTCTTTTCACCCAATTTCTACAGGGATATGCCTTT
GCTAAATCTGGGGAGCTCCTAACAAAAAGGCTACGTAAATTTGGTTTCAGGGCAATGCTG
GGGCAAGATATTGCCTGGTTTGATGACCTCAGAAATAGCCCTGGAGCATTGACAACAAGA
CTTGCTACAGATGCTTCCCAAGTTCAAGGGGCTGCCGGCTCTCAGATCGGGATGATAGTC
AATTCCTTCACTAACGTCACTGTGGCCATGATCATTGCCTTCTCCTTTAGCTGGAAGCTG
AGCCTGGTCATCTTGTGCTTCTTCCCCTTCTTGGCTTTATCAGGAGCCACACAGACCAGG
ATGTTGACAGGATTTGCCTCTCGAGATAAGCAGGCCCTGGAGATGGTGGGACAGATTACA
AATGAAGCCCTCAGTAACATCCGCACTGTTGCTGGAATTGGAAAGGAGAGGCGGTTCATT
GAAGCACTTGAGACTGAGCTGGAGAAGCCCTTCAAGACAGCCATTCAGAAAGCCAATATT
TACGGATTCTGCTTTGCCTTTGCCCAGTGCATCATGTTTATTGCGAATTCTGCTTCCTAC
AGATATGGAGGTTACTTAATCTCCAATGAGGGGCTCCATTTCAGCTATGTGTTCAGGGTG
ATCTCTGCAGTTGTACTGAGTGCAACAGCTCTTGGAAGAGCCTTCTCTTACACCCCAAGT
TATGCAAAAGCTAAAATATCAGCTGCACGCTTTTTTCAACTGCTGGACCGACAACCCCCA
ATCAGTGTATACAATACTGCAGGTGAAAAATGGGACAACTTCCAGGGGAAGATTGATTTT
GTTGATTGTAAATTTACATATCCTTCTCGACCTGACTCGCAAGTTCTGAATGGTCTCTCA
GTGTCGATTAGTCCAGGGCAGACACTGGCGTTTGTTGGGAGCAGTGGATGTGGCAAAAGC
ACTAGCATTCAGCTGTTGGAACGTTTCTATGATCCTGATCAAGGGAAGGTGATGATAGAT
GGTCATGACAGCAAAAAAGTAAATGTCCAGTTCCTCCGCTCAAACATTGGAATTGTTTCC
CAGGAACCAGTGTTGTTTGCCTGTAGCATAATGGACAATATCAAGTATGGAGACAACACC
AAAGAAATTCCCATGGAAAGAGTCATAGCAGCTGCAAAACAGGCTCAGCTGCATGATTTT
GTCATGTCACTCCCAGAGAAATATGAAACTAACGTTGGGTCCCAGGGGTCTCAACTCTCT
AGAGGGGAGAAACAACGCATTGCTATTGCTCGGGCCATTGTACGAGATCCTAAAATCTTG
CTACTAGATGAAGCCACTTCTGCCTTAGACACAGAAAGTGAAAAGACGGTGCAGGTTGCT
CTAGACAAAGCCAGAGAGGGTCGGACCTGCATTGTCATTGCCCATCGCTTGTCCACCATC
CAGAACGCGGATATCATTGCTGTCATGGCACAGGGGGTGGTGATTGAAAAGGGGACCCAT
GAAGAACTGATGGCCCAAAAAGGAGCCTACTACAAACTAGTCACCACTGGATCCCCCATC
AGTTGA
Enzyme 6 GenBank Gene ID AF091582 Link Image
Enzyme 6 GeneCard ID ABCB11 Link Image
Enzyme 6 GenAtlas ID ABCB11 Link Image
Enzyme 6 HGNC ID HGNC:42 Link Image
Enzyme 6 Chromosome Location 2
Enzyme 6 Locus 2q24
Enzyme 6 SNPs SNPJam Report Link Image
Enzyme 6 General References
  1. Strautnieks SS, Bull LN, Knisely AS, Kocoshis SA, Dahl N, Arnell H, Sokal E, Dahan K, Childs S, Ling V, Tanner MS, Kagalwalla AF, Nemeth A, Pawlowska J, Baker A, Mieli-Vergani G, Freimer NB, Gardiner RM, Thompson RJ: A gene encoding a liver-specific ABC transporter is mutated in progressive familial intrahepatic cholestasis. Nat Genet. 1998 Nov;20(3):233-8. [PubMed Link Image]
  2. Saito S, Iida A, Sekine A, Miura Y, Ogawa C, Kawauchi S, Higuchi S, Nakamura Y: Three hundred twenty-six genetic variations in genes encoding nine members of ATP-binding cassette, subfamily B (ABCB/MDR/TAP), in the Japanese population. J Hum Genet. 2002;47(1):38-50. [PubMed Link Image]
  3. Chen HL, Chang PS, Hsu HC, Ni YH, Hsu HY, Lee JH, Jeng YM, Shau WY, Chang MH: FIC1 and BSEP defects in Taiwanese patients with chronic intrahepatic cholestasis with low gamma-glutamyltranspeptidase levels. J Pediatr. 2002 Jan;140(1):119-24. [PubMed Link Image]
Enzyme 6 Metabolite References Not Available
Enzyme 7 [top]
Enzyme 7 ID 7956
Enzyme 7 Name Ileal sodium/bile acid cotransporter
Enzyme 7 Synonyms
  1. Ileal Na(+/bile acid cotransporter
  2. Na(+-dependent ileal bile acid transporter
  3. Ileal sodium-dependent bile acid transporter
  4. ISBT
  5. IBAT
  6. Apical sodium- dependent bile acid transporter
  7. ASBT
  8. Sodium/taurocholate cotransporting polypeptide, ileal
  9. Solute carrier family 10 member 2
Enzyme 7 Gene Name SLC10A2
Enzyme 7 Protein Sequence >Ileal sodium/bile acid cotransporter 
MNDPNSCVDNATVCSGASCVVPESNFNNILSVVLSTVLTILLALVMFSMGCNVEIKKFLG
HIKRPWGICVGFLCQFGIMPLTGFILSVAFDILPLQAVVVLIIGCCPGGTASNILAYWVD
GDMDLSVSMTTCSTLLALGMMPLCLLIYTKMWVDSGSIVIPYDNIGTSLVALVVPVSIGM
FVNHKWPQKAKIILKIGSIAGAILIVLIAVVGGILYQSAWIIAPKLWIIGTIFPVAGYSL
GFLLARIAGLPWYRCRTVAFETGMQNTQLCSTIVQLSFTPEELNVVFTFPLIYSIFQLAF
AAIFLGFYVAYKKCHGKNKAEIPESKENGTEPESSFYKANGGFQPDEK
Enzyme 7 Number of Residues 348
Enzyme 7 Molecular Weight 37698
Enzyme 7 Theoretical pI 7.13
Enzyme 7 GO Classification
Function
  • bile acid:sodium symporter activity
  • organic acid transporter activity
  • organic acid:sodium symporter activity
  • transporter activity
Process
  • anion transport
  • cation transport
  • cellular physiological process
  • ion transport
  • monovalent inorganic cation transport
  • organic anion transport
  • physiological process
  • sodium ion transport
  • transport
Component
  • cell
  • integral to membrane
  • intrinsic to membrane
  • membrane
Enzyme 7 General Function Not Available
Enzyme 7 Specific Function Plays a critical role in the sodium-dependent reabsorption of bile acids from the lumen of the small intestine. Plays a key role in cholesterol metabolism
Enzyme 7 Pathways Not Available
Enzyme 7 Reactions Not Available
Enzyme 7 Pfam Domain Function
Enzyme 7 Signals
  • None
Enzyme 7 Transmembrane Regions
  • 29-49 83-103 127-147 158-178 196-216 225-245 285-305
Enzyme 7 Essentiality Not Available
Enzyme 7 GenBank ID Protein 595399 Link Image
Enzyme 7 UniProtKB/Swiss-Prot ID Q12908 Link Image
Enzyme 7 UniProtKB/Swiss-Prot Entry Name NTCP2_HUMAN Link Image
Enzyme 7 PDB ID Not Available
Enzyme 7 Cellular Location Not Available
Enzyme 7 Gene Sequence >1047 bp 
ATGAATGATCCGAACAGCTGTGTGGACAATGCAACAGTTTGCTCTGGTGCATCCTGTGTG
GTACCTGAGAGCAATTTCAATAACATCCTAAGTGTGGTCCTAAGTACGGTGCTGACCATC
CTGTTGGCCTTGGTGATGTTCTCCATGGGATGCAACGTGGAAATCAAGAAATTTCTAGGG
CACATAAAGCGGCCGTGGGGCATTTGTGTTGGCTTCCTCTGTCAGTTTGGAATCATGCCC
CTCACAGGATTCATCCTGTCGGTGGCCTTTGACATCCTCCCGCTCCAGGCCGTAGTGGTG
CTCATTATAGGATGCTGCCCTGGAGGAACTGCCTCCAATATCTTGGCCTATTGGGTCGAT
GGCGACATGGACCTGAGCGTCAGCATGACCACATGCTCCACACTGCTTGCCCTCGGAATG
ATGCCGCTGTGCCTCCTTATCTATACCAAAATGTGGGTCGACTCTGGGAGCATCGTAATT
CCCTATGATAACATAGGTACATCTCTGGTTGCTCTCGTTGTTCCTGTTTCCATTGGAATG
TTTGTTAATCACAAATGGCCCCAAAAAGCAAAGATCATACTTAAAATTGGGTCCATCGCG
GGCGCCATCCTCATTGTGCTCATAGCTGTGGTTGGAGGAATATTGTACCAAAGCGCCTGG
ATCATTGCTCCCAAACTGTGGATTATAGGAACAATATTTCCTGTGGCGGGTTACTCCCTG
GGGTTTCTTCTGGCTAGAATTGCTGGTCTACCCTGGTACAGGTGCCGAACGGTTGCTTTT
GAAACGGGGATGCAGAACACGCAGCTATGTTCCACCATCGTTCAGCTCTCCTTCACTCCT
GAGGAGCTCAATGTCGTATTCACCTTCCCGCTCATCTACAGCATTTTCCAGCTCGCCTTT
GCCGCAATATTCTTAGGATTTTATGTGGCATACAAGAAATGTCATGGAAAAAACAAGGCA
GAAATTCCAGAGAGCAAAGAAAATGGAACGGAGCCAGAGTCATCGTTTTATAAGGCAAAT
GGAGGATTTCAACCTGACGAAAAGTAG
Enzyme 7 GenBank Gene ID U10417 Link Image
Enzyme 7 GeneCard ID SLC10A2 Link Image
Enzyme 7 GenAtlas ID SLC10A2 Link Image
Enzyme 7 HGNC ID HGNC:10906 Link Image
Enzyme 7 Chromosome Location 13
Enzyme 7 Locus 13q33
Enzyme 7 SNPs SNPJam Report Link Image
Enzyme 7 General References
  1. Wong MH, Oelkers P, Dawson PA: Identification of a mutation in the ileal sodium-dependent bile acid transporter gene that abolishes transport activity. J Biol Chem. 1995 Nov 10;270(45):27228-34. [PubMed Link Image]
  2. Oelkers P, Kirby LC, Heubi JE, Dawson PA: Primary bile acid malabsorption caused by mutations in the ileal sodium-dependent bile acid transporter gene (SLC10A2). J Clin Invest. 1997 Apr 15;99(8):1880-7. [PubMed Link Image]
  3. Chumakov I, Blumenfeld M, Guerassimenko O, Cavarec L, Palicio M, Abderrahim H, Bougueleret L, Barry C, Tanaka H, La Rosa P, Puech A, Tahri N, Cohen-Akenine A, Delabrosse S, Lissarrague S, Picard FP, Maurice K, Essioux L, Millasseau P, Grel P, Debailleul V, Simon AM, Caterina D, Dufaure I, Malekzadeh K, Belova M, Luan JJ, Bouillot M, Sambucy JL, Primas G, Saumier M, Boubkiri N, Martin-Saumier S, Nasroune M, Peixoto H, Delaye A, Pinchot V, Bastucci M, Guillou S, Chevillon M, Sainz-Fuertes R, Meguenni S, Aurich-Costa J, Cherif D, Gimalac A, Van Duijn C, Gauvreau D, Ouellette G, Fortier I, Raelson J, Sherbatich T, Riazanskaia N, Rogaev E, Raeymaekers P, Aerssens J, Konings F, Luyten W, Macciardi F, Sham PC, Straub RE, Weinberger DR, Cohen N, Cohen D: Genetic and physiological data implicating the new human gene G72 and the gene for D-amino acid oxidase in schizophrenia. Proc Natl Acad Sci U S A. 2002 Oct 15;99(21):13675-80. Epub 2002 Oct 3. [PubMed Link Image]
  4. Montagnani M, Love MW, Rossel P, Dawson PA, Qvist P: Absence of dysfunctional ileal sodium-bile acid cotransporter gene mutations in patients with adult-onset idiopathic bile acid malabsorption. Scand J Gastroenterol. 2001 Oct;36(10):1077-80. [PubMed Link Image]
Enzyme 7 Metabolite References
  1. Kramer W, Girbig F, Glombik H, Corsiero D, Stengelin S, Weyland C: Identification of a ligand-binding site in the Na+/bile acid cotransporting protein from rabbit ileum. J Biol Chem. 2001 Sep 21;276(38):36020-7. Epub 2001 Jul 10. [PubMed Link Image]
Enzyme 8 [top]
Enzyme 8 ID 8049
Enzyme 8 Name Sodium/bile acid cotransporter
Enzyme 8 Synonyms
  1. Na(+/bile acid cotransporter
  2. Na(+/taurocholate transport protein
  3. Sodium/taurocholate cotransporting polypeptide
  4. Solute carrier family 10 member 1
  5. Cell growth-inhibiting gene 29 protein
Enzyme 8 Gene Name SLC10A1
Enzyme 8 Protein Sequence >Sodium/bile acid cotransporter 
MEAHNASAPFNFTLPPNFGKRPTDLALSVILVFMLFFIMLSLGCTMEFSKIKAHLWKPKG
LAIALVAQYGIMPLTAFVLGKVFRLKNIEALAILVCGCSPGGNLSNVFSLAMKGDMNLSI
VMTTCSTFCALGMMPLLLYIYSRGIYDGDLKDKVPYKGIVISLVLVLIPCTIGIVLKSKR
PQYMRYVIKGGMIIILLCSVAVTVLSAINVGKSIMFAMTPLLIATSSLMPFIGFLLGYVL
SALFCLNGRCRRTVSMETGCQNVQLCSTILNVAFPPEVIGPLFFFPLLYMIFQLGEGLLL
IAIFWCYEKFKTPKDKTKMIYTAATTEETIPGALGNGTYKGEDCSPCTA
Enzyme 8 Number of Residues 349
Enzyme 8 Molecular Weight 38120
Enzyme 8 Theoretical pI 8.94
Enzyme 8 GO Classification
Function
  • bile acid:sodium symporter activity
  • organic acid transporter activity
  • organic acid:sodium symporter activity
  • transporter activity
Process
  • anion transport
  • cation transport
  • cellular physiological process
  • ion transport
  • monovalent inorganic cation transport
  • organic anion transport
  • physiological process
  • sodium ion transport
  • transport
Component
  • cell
  • integral to membrane
  • intrinsic to membrane
  • membrane
Enzyme 8 General Function Not Available
Enzyme 8 Specific Function The hepatic sodium/bile acid uptake system exhibits broad substrate specificity and transports various non-bile acid organic compounds as well. It is strictly dependent on the extracellular presence of sodium
Enzyme 8 Pathways Not Available
Enzyme 8 Reactions Not Available
Enzyme 8 Pfam Domain Function
Enzyme 8 Signals
  • None
Enzyme 8 Transmembrane Regions
  • 25-45 60-80 91-111 120-140 156-176 191-211 220-240 283-303
Enzyme 8 Essentiality Not Available
Enzyme 8 GenBank ID Protein 410214 Link Image
Enzyme 8 UniProtKB/Swiss-Prot ID Q14973 Link Image
Enzyme 8 UniProtKB/Swiss-Prot Entry Name NTCP_HUMAN Link Image
Enzyme 8 PDB ID Not Available
Enzyme 8 Cellular Location Not Available
Enzyme 8 Gene Sequence >1050 bp 
ATGGAGGCCCACAACGCGTCTGCCCCATTCAACTTCACCCTGCCACCCAACTTTGGCAAG
CGCCCCACAGACCTGGCACTGAGCGTCATCCTGGTGTTCATGTTGTTCTTCATCATGCTC
TCGCTGGGCTGCACCATGGAGTTCAGCAAGATCAAGGCTCACTTATGGAAGCCTAAAGGG
CTGGCCATCGCCCTGGTGGCACAGTATGGCATCATGCCCCTCACGGCCTTTGTGCTGGGC
AAGGTCTTCCGGCTGAAGAACATTGAGGCACTGGCCATCTTGGTCTGTGGCTGCTCACCT
GGAGGGAACCTGTCCAATGTCTTCAGTCTGGCCATGAAGGGGGACATGAACCTCAGCATT
GTGATGACCACCTGCTCCACCTTCTGTGCCCTTGGCATGATGCCTCTCCTCCTGTACATC
TACTCCAGGGGGATCTATGATGGGGACCTGAAGGACAAGGTGCCCTATAAAGGCATCGTG
ATATCACTGGTCCTGGTTCTCATTCCTTGCACCATAGGGATCGTCCTCAAATCCAAACGG
CCACAATACATGCGCTATGTCATCAAGGGAGGGATGATCATCATTCTCTTGTGCAGTGTG
GCCGTCACAGTTCTCTCTGCCATCAATGTGGGGAAGAGCATCATGTTTGCCATGACACCA
CTCTTGATTGCCACCTCCTCCCTGATGCCTTTTATTGGCTTTCTGCTGGGTTATGTTCTC
TCTGCTCTCTTCTGCCTCAATGGACGGTGCAGACGCACTGTCAGCATGGAGACTGGATGC
CAAAATGTCCAACTCTGTTCCACCATCCTCAATGTGGCCTTTCCACCTGAAGTCATTGGA
CCACTTTTCTTCTTTCCCCTCCTCTACATGATTTTCCAGCTTGGAGAAGGGCTTCTCCTC
ATTGCCATATTTTGGTGCTATGAGAAATTCAAGACTCCCAAGGATAAAACAAAAATGATC
TACACAGCTGCCACAACTGAAGAAACAATTCCAGGAGCTCTGGGAAATGGCACCTACAAA
GGGGAGGACTGCTCCCCTTGCACAGCCTAG
Enzyme 8 GenBank Gene ID L21893 Link Image
Enzyme 8 GeneCard ID SLC10A1 Link Image
Enzyme 8 GenAtlas ID SLC10A1 Link Image
Enzyme 8 HGNC ID HGNC:10905 Link Image
Enzyme 8 Chromosome Location 14
Enzyme 8 Locus 14q24.1
Enzyme 8 SNPs SNPJam Report Link Image
Enzyme 8 General References
  1. Hagenbuch B, Meier PJ: Molecular cloning, chromosomal localization, and functional characterization of a human liver Na+/bile acid cotransporter. J Clin Invest. 1994 Mar;93(3):1326-31. [PubMed Link Image]
Enzyme 8 Metabolite References Not Available
Enzyme 9 [top]
Enzyme 9 ID 8186
Enzyme 9 Name Solute carrier organic anion transporter family member 1A2
Enzyme 9 Synonyms
  1. Solute carrier family 21 member 3
  2. Sodium-independent organic anion transporter
  3. Organic anion-transporting polypeptide 1
  4. OATP1
  5. OATP- A
Enzyme 9 Gene Name SLCO1A2
Enzyme 9 Protein Sequence >Solute carrier organic anion transporter family member 1A2 
MGETEKRIETHRIRCLSKLKMFLLAITCAFVSKTLSGSYMNSMLTQIERQFNIPTSLVGF
INGSFEIGNLLLIIFVSYFGTKLHRPIMIGIGCVVMGLGCFLKSLPHFLMNQYEYESTVS
VSGNLSSNSFLCMENGTQILRPTQDPSECTKEVKSLMWVYVLVGNIVRGMGETPILPLGI
SYIEDFAKFENSPLYIGLVETGAIIGPLIGLLLASFCANVYVDTGFVNTDDLIITPTDTR
WVGAWWFGFLICAGVNVLTAIPFFFLPNTLPKEGLETNADIIKNENEDKQKEEVKKEKYG
ITKDFLPFMKSLSCNPIYMLFILVSVIQFNAFVNMISFMPKYLEQQYGISSSDAIFLMGI
YNLPPICIGYIIGGLIMKKFKITVKQAAHIGCWLSLLEYLLYFLSFLMTCENSSVVGINT
SYEGIPQDLYVENDIFADCNVDCNCPSKIWDPVCGNNGLSYLSACLAGCETSIGTGINMV
FQNCSCIQTSGNSSAVLGLCDKGPDCSLMLQYFLILSAMSSFIYSLAAIPGYMVLLRCMK
SEEKSLGVGLHTFCTRVFAGIPAPIYFGALMDSTCLHWGTLKCGESGACRIYDSTTFRYI
YLGLPAALRGSSFVPALIILILLRKCHLPGENASSGTELIETKVKGKENECKDIYQKSTV
LKDDELKTKL
Enzyme 9 Number of Residues 670
Enzyme 9 Molecular Weight 74146
Enzyme 9 Theoretical pI 5.75
Enzyme 9 GO Classification
Function
  • transporter activity
Process
  • cellular physiological process
  • physiological process
  • transport
Component
  • cell
  • integral to membrane
  • intrinsic to membrane
  • membrane
Enzyme 9 General Function Not Available
Enzyme 9 Specific Function Mediates the Na(+)-independent transport of organic anions such as sulfobromophthalein (BSP) and conjugated (taurocholate) and unconjugated (cholate) bile acids
Enzyme 9 Pathways Not Available
Enzyme 9 Reactions Not Available
Enzyme 9 Pfam Domain Function
Enzyme 9 Signals
  • 1-36
Enzyme 9 Transmembrane Regions Not Available
Enzyme 9 Essentiality Not Available
Enzyme 9 GenBank ID Protein 885978 Link Image
Enzyme 9 UniProtKB/Swiss-Prot ID P46721 Link Image
Enzyme 9 UniProtKB/Swiss-Prot Entry Name SO1A2_HUMAN Link Image
Enzyme 9 PDB ID Not Available
Enzyme 9 Cellular Location Not Available
Enzyme 9 Gene Sequence >2013 bp 
ATGGGAGAAACTGAGAAAAGAATTGAAACCCATAGAATAAGATGTCTTTCCAAGTTGAAG
ATGTTTCTGTTGGCAATAACATGTGCATTTGTATCCAAAACACTGTCTGGATCTTATATG
AATTCCATGCTCACACAAATAGAGAGACAATTCAACATCCCAACATCTCTAGTTGGATTC
ATTAATGGAAGCTTTGAGATTGGAAATCTTTTGTTGATTATATTTGTGAGTTATTTTGGA
ACCAAACTGCATAGACCTATAATGATTGGCATTGGATGTGTGGTTATGGGCTTAGGCTGT
TTCTTAAAATCACTACCTCATTTCCTCATGAACCAATATGAATATGAATCTACAGTTTCA
GTTTCAGGCAACTTGTCCTCAAACAGTTTCTTGTGTATGGAAAATGGAACCCAGATTTTA
AGACCAACGCAGGATCCATCAGAGTGTACAAAGGAAGTTAAATCATTAATGTGGGTGTAC
GTCCTAGTAGGCAATATTGTACGTGGAATGGGTGAAACTCCCATCCTGCCTTTGGGTATT
TCCTATATAGAAGATTTTGCCAAATTTGAAAATTCTCCTTTATATATTGGGCTTGTAGAA
ACAGGAGCTATTATTGGTCCTTTGATTGGACTTTTGTTGGCATCATTCTGTGCAAATGTT
TATGTTGACACTGGATTTGTGAACACAGATGATCTGATCATAACTCCCACTGACACTCGT
TGGGTCGGTGCATGGTGGTTTGGCTTTCTGATTTGTGCAGGAGTTAACGTGCTCACTGCC
ATTCCTTTTTTCTTTTTGCCCAACACACTTCCAAAGGAAGGACTAGAGACTAATGCTGAC
ATCATTAAAAATGAAAATGAAGACAAACAAAAAGAAGAGGTCAAGAAGGAAAAATATGGA
ATCACTAAAGATTTTCTACCTTTCATGAAAAGTCTTTCCTGCAATCCAATTTATATGCTT
TTCATACTTGTAAGTGTGATACAGTTCAATGCATTCGTTAACATGATCTCCTTCATGCCT
AAATACCTAGAACAGCAATATGGAATATCATCTTCAGATGCAATCTTTCTAATGGGTATT
TATAACTTACCTCCAATATGTATTGGATATATAATTGGTGGTTTAATTATGAAGAAGTTC
AAGATTACTGTCAAACAAGCTGCCCACATAGGATGTTGGTTATCCTTACTTGAGTATCTT
CTCTATTTTTTATCTTTTCTCATGACTTGTGAAAATTCTTCAGTTGTTGGAATAAATACC
TCTTATGAAGGAATTCCACAAGATTTATATGTGGAAAATGACATCTTTGCTGATTGCAAT
GTGGATTGCAACTGTCCATCTAAAATATGGGATCCTGTGTGTGGAAACAATGGCTTGTCA
TATCTGTCAGCTTGTCTTGCTGGTTGTGAGACATCCATTGGAACGGGAATAAACATGGTG
TTCCAAAATTGCAGCTGTATTCAAACATCAGGAAATTCATCTGCAGTTCTTGGGCTGTGC
GACAAAGGACCTGACTGTTCCTTGATGCTCCAGTACTTCCTAATCTTGTCAGCGATGAGC
AGTTTCATTTATTCTTTGGCTGCCATACCTGGATATATGGTTCTCTTGAGGTGTATGAAA
TCTGAAGAGAAGTCCCTTGGTGTGGGATTACATACATTTTGCACAAGAGTATTTGCTGGC
ATTCCTGCACCTATATATTTTGGCGCTTTAATGGATTCCACATGTTTACACTGGGGAACT
TTGAAATGTGGTGAGTCAGGGGCATGCAGGATATATGATTCCACCACCTTCAGATACATC
TACCTCGGATTGCCGGCAGCACTAAGAGGATCAAGCTTTGTTCCAGCCTTAATCATCTTA
ATTCTTTTGAGGAAGTGTCATCTACCTGGTGAAAATGCCTCTTCAGGAACAGAGCTTATA
GAGACAAAAGTCAAAGGGAAGGAAAATGAGTGCAAAGATATATACCAAAAGTCCACGGTT
TTGAAAGATGATGAATTGAAAACTAAATTGTAA
Enzyme 9 GenBank Gene ID U21943 Link Image
Enzyme 9 GeneCard ID SLCO1A2 Link Image
Enzyme 9 GenAtlas ID SLCO1A2 Link Image
Enzyme 9 HGNC ID HGNC:10956 Link Image
Enzyme 9 Chromosome Location 12
Enzyme 9 Locus 12p12
Enzyme 9 SNPs SNPJam Report Link Image
Enzyme 9 General References
  1. Kullak-Ublick GA, Hagenbuch B, Stieger B, Schteingart CD, Hofmann AF, Wolkoff AW, Meier PJ: Molecular and functional characterization of an organic anion transporting polypeptide cloned from human liver. Gastroenterology. 1995 Oct;109(4):1274-82. [PubMed Link Image]
  2. 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]
  3. Speek M: Antisense promoter of human L1 retrotransposon drives transcription of adjacent cellular genes. Mol Cell Biol. 2001 Mar;21(6):1973-85. [PubMed Link Image]
Enzyme 9 Metabolite References Not Available
Enzyme 10 [top]
Enzyme 10 ID 8587
Enzyme 10 Name Bile acyl-CoA synthetase
Enzyme 10 Synonyms
  1. BACS
  2. Bile acid CoA ligase
  3. BA-CoA ligase
  4. BAL
  5. Cholate--CoA ligase
  6. Very long-chain acyl-CoA synthetase homolog 2
  7. VLCSH2
  8. VLCS-H2
  9. Very long chain acyl-CoA synthetase-related protein
  10. VLACS-related
  11. VLACSR
  12. Fatty-acid- coenzyme A ligase, very long-chain 3
  13. Fatty acid transport protein 5
  14. FATP-5
  15. Solute carrier family 27 member 5
Enzyme 10 Gene Name SLC27A5
Enzyme 10 Protein Sequence >Bile acyl-CoA synthetase 
MGVRQQLALLLLLLLLLWGLGQPVWPVAVALTLRWLLGDPTCCVLLGLAMLARPWLGPWV
PHGLSLAAAALALTLLPARLPPGLRWLPADVIFLAKILHLGLKIRGCLSRQPPDTFVDAF
ERRARAQPGRALLVWTGPGAGSVTFGELDARACQAAWALKAELGDPASLCAGEPTALLVL
ASQAVPALCMWLGLAKLGCPTAWINPHGRGMPLAHSVLSSGARVLVVDPDLRESLEEILP
KLQAENIRCFYLSHTSPTPGVGALGAALDAAPSHPVPADLRAGITWRSPALFIYTSGTTG
LPKPAILTHERVLQMSKMLSLSGATADDVVYTVLPLYHVMGLVVGILGCLDLGATCVLAP
KFSTSCFWDDCRQHGVTVILYVGELLRYLCNIPQQPEDRTHTVRLAMGNGLRADVWETFQ
QRFGPIRIWEVYGSTEGNMGLVNYVGRCGALGKMSCLLRMLSPFELVQFDMEAAEPVRDN
QGFCIPVGLGEPGLLLTKVVSQQPFVGYRGPRELSERKLVRNVRQSGDVYYNTGDVLAMD
REGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQVDFLQQVNVYGVCVPGCEGKVGMAAVQ
LAPGQTFDGEKLYQHVRAWLPAYATPHFIRIQDAMEVTSTFKLMKTRLVREGFNVGIVVD
PLFVLDNRAQSFRPLTAEMYQAVCEGTWRL
Enzyme 10 Number of Residues 690
Enzyme 10 Molecular Weight 75386
Enzyme 10 Theoretical pI 7.70
Enzyme 10 GO Classification
Function
  • catalytic activity
Process
  • metabolism
  • physiological process
Component
—
Enzyme 10 General Function Lipid transport and metabolism
Enzyme 10 Specific Function Acyl-CoA synthetase involved in bile acid metabolism. Proposed to catalyze the first step in the conjugation of C24 bile acids (choloneates) to glycine and taurine before excretion into bile canaliculi by activating them to their CoA thioesters. Seems to activate secondary bile acids entering the liver from the enterohepatic circulation. In vitro, also activates 3-alpha,7- alpha,12-alpha-trihydroxy-5-beta-cholestanate (THCA), the C27 precursor of cholic acid deriving from the de novo synthesis from cholesterol
Enzyme 10 Pathways
Enzyme 10 Reactions
  • ATP + cholate + CoA = AMP + diphosphate + choloyl-CoA
Enzyme 10 Pfam Domain Function
Enzyme 10 Signals
  • 1-21
Enzyme 10 Transmembrane Regions
  • 9-29 31-51 56-76
Enzyme 10 Essentiality Not Available
Enzyme 10 GenBank ID Protein 4768277 Link Image
Enzyme 10 UniProtKB/Swiss-Prot ID Q9Y2P5 Link Image
Enzyme 10 UniProtKB/Swiss-Prot Entry Name S27A5_HUMAN Link Image
Enzyme 10 PDB ID Not Available
Enzyme 10 Cellular Location Not Available
Enzyme 10 Gene Sequence >2073 bp 
ATGGGTGTCAGGCAACAGTTGGCCTTGCTGCTGCTGCTGCTGCTCCTGCTCTGGGGCCTG
GGGCAGCCAGTGTGGCCAGTCGCTGTGGCCTTGACCCTGCGCTGGCTCCTGGGGGATCCC
ACATGTTGCGTGCTACTTGGGCTGGCCATGTTAGCACGGCCCTGGCTCGGCCCCTGGGTG
CCCCATGGGCTGAGCCTGGCAGCTGCGGCCCTGGCACTAACCCTCCTGCCAGCACGGCTG
CCCCCAGGACTACGCTGGCTGCCGGCTGATGTGATCTTCTTGGCCAAGATCCTCCACCTG
GGCCTGAAGATCAGGGGATGCTTGAGCCGGCAGCCGCCTGACACCTTTGTAGATGCCTTC
GAGCGGCGAGCACGAGCGCAGCCTGGCAGGGCACTCTTGGTGTGGACGGGGCCTGGGGCC
GGCTCAGTCACCTTTGGTGAGCTGGATGCCCGGGCCTGCCAGGCGGCATGGGCCCTGAAG
GCTGAGCTGGGTGACCCTGCGAGCCTGTGTGCCGGGGAGCCTACTGCCCTCCTTGTGCTG
GCTTCCCAGGCCGTTCCAGCCCTGTGTATGTGGCTGGGGCTGGCCAAGCTGGGCTGCCCA
ACAGCCTGGATCAACCCGCATGGCCGGGGGATGCCCCTGGCGCACTCTGTGCTGAGCTCT
GGGGCCCGGGTGCTGGTGGTGGACCCAGACCTCCGGGAGAGCCTGGAGGAGATCCTTCCC
AAGCTGCAGGCTGAGAACATCCGCTGCTTCTACCTCAGCCATACCTCCCCTACACCAGGG
GTGGGGGCTCTGGGGGCTGCCCTGGATGCAGCGCCCTCCCACCCAGTGCCTGCTGACCTG
CGTGCTGGGATCACATGGAGAAGCCCTGCCCTCTTCATCTATACCTCGGGGACCACTGGC
CTCCCGAAGCCAGCCATCCTCACGCATGAGCGGGTACTGCAGATGAGCAAGATGCTGTCC
TTATCTGGGGCCACAGCTGATGATGTGGTTTACACGGTCCTGCCTCTGTACCACGTGATG
GGACTTGTCGTTGGGATCCTCGGCTGCTTAGATCTCGGAGCCACCTGTGTTCTGGCCCCC
AAGTTCTCTACTTCCTGCTTCTGGGATGACTGTCGGCAGCATGGCGTGACAGTGATCCTG
TATGTGGGCGAGCTCCTGCGGTACTTGTGTAACATTCCCCAGCAACCAGAGGACCGGACA
CATACAGTCCGCCTGGCAATGGGCAATGGACTACGGGCTGATGTGTGGGAGACCTTCCAG
CAGCGCTTCGGTCCTATTCGGATCTGGGAAGTCTACGGCTCCACAGAAGGCAACATGGGC
TTAGTCAACTATGTGGGGCGCTGCGGGGCCCTGGGCAAGATGAGCTGCCTCCTCCGAATG
CTGTCCCCCTTTGAGCTGGTGCAGTTCGACATGGAGGCGGCGGAGCCTGTGAGGGACAAT
CAGGGCTTCTGCATCCCTGTAGGGCTAGGGGAGCCGGGGCTGCTGCTGACCAAGGTGGTA
AGCCAGCAACCCTTCGTGGGCTACCGCGGCCCCCGAGAGCTGTCGGAACGGAAGCTGGTG
CGCAACGTGCGGCAATCGGGCGACGTTTACTACAACACCGGGGACGTACTGGCCATGGAC
CGCGAAGGCTTCCTCTACTTCCGCGACCGCCTCGGGGACACCTTCCGATGGAAGGGCGAG
AACGTGTCCACGCACGAGGTGGAGGGCGTGTTGTCGCAGGTGGACTTCTTGCAACAGGTT
AACGTGTATGGCGTGTGCGTGCCAGGTTGTGAGGGTAAGGTGGGCATGGCTGCTGTGCAG
CTAGCCCCCGGCCAGACTTTCGACGGGGAGAAGTTGTACCAGCACGTTCGCGCTTGGCTC
CCTGCCTACGCTACCCCCCATTTCATCCGCATCCAGGACGCCATGGAGGTCACCAGCACG
TTCAAACTGATGAAGACCCGGTTGGTGCGTGAGGGCTTCAATGTGGGGATCGTGGTTGAC
CCTCTGTTTGTACTGGACAACCGGGCCCAGTCCTTCCGGCCCCTGACGGCAGAAATGTAC
CAGGCTGTGTGTGAGGGAACCTGGAGGCTCTGA
Enzyme 10 GenBank Gene ID AF064255 Link Image
Enzyme 10 GeneCard ID SLC27A5 Link Image
Enzyme 10 GenAtlas ID SLC27A5 Link Image
Enzyme 10 HGNC ID HGNC:10999 Link Image
Enzyme 10 Chromosome Location 19
Enzyme 10 Locus 19q13.43
Enzyme 10 SNPs SNPJam Report Link Image
Enzyme 10 General References
  1. Steinberg SJ, Wang SJ, McGuinness MC, Watkins PA: Human liver-specific very-long-chain acyl-coenzyme A synthetase: cDNA cloning and characterization of a second enzymatically active protein. Mol Genet Metab. 1999 Sep;68(1):32-42. [PubMed Link Image]
Enzyme 10 Metabolite References Not Available
Enzyme 11 [top]
Enzyme 11 ID 8766
Enzyme 11 Name Solute carrier organic anion transporter family member 4A1
Enzyme 11 Synonyms
  1. Solute carrier family 21 member 12
  2. Sodium-independent organic anion transporter E
  3. Organic anion-transporting polypeptide E
  4. OATP-E
  5. Colon organic anion transporter
  6. Organic anion transporter polypeptide-related protein 1
  7. OATP-RP1
  8. OATPRP1
  9. POAT
Enzyme 11 Gene Name SLCO4A1
Enzyme 11 Protein Sequence >Solute carrier organic anion transporter family member 4A1 
MPLHQLGDKPLTFPSPNSAMENGLDHTPPSRRASPGTPLSPGSLRSAAHSPLDTSKQPLC
QLWAEKHGARGTHEVRYVSAGQSVACGWWAFAPPCLQVLNTPKGILFFLCAAAFLQGMTV
NGFINTVITSLERRYDLHSYQSGLIASSYDIAACLCLTFVSYFGGSGHKPRWLGWGVLLM
GTGSLVFALPHFTAGRYEVELDAGVRTCPANPGAVCADSTSGLSRYQLVFMLGQFLHGVG
ATPLYTLGVTYLDENVKSSCSPVYIAIFYTAAILGPAAGYLIGGALLNIYTEMGRRTELT
TESPLWVGAWWVGFLGSGAAAFFTAVPILGYPRQLPGSQRYAVMRAAEMHQLKDSSRGEA
SNPDFGKTIRDLPLSIWLLLKNPTFILLCLAGATEATLITGMSTFSPKFLESQFSLSASE
AATLFGYLVVPAGGGGTFLGGFFVNKLRLRGSAVIKFCLFCTVVSLLGILVFSLHCPSVP
MAGVTASYGGSLLPEGHLNLTAPCNAACSCQPEHYSPVCGSDGLMYFSLCHAGCPAATET
NVDGQKVYRDCSCIPQNLSSGFGHATAGKCTSTCQRKPLLLVFIFVVIFFTFLSSIPALT
ATLRCVRDPQRSFALGIQWIVVRILGGIPGPIAFGWVIDKACLLWQDQCGQQGSCLVYQN
SAMSRYILIMGLLYKVLGVLFFAIACFLYKPLSESSDGLETCLPSQSSAPDSATDSQLQS
SV
Enzyme 11 Number of Residues 722
Enzyme 11 Molecular Weight 77194
Enzyme 11 Theoretical pI 7.85
Enzyme 11 GO Classification
Function
  • transporter activity
Process
  • cellular physiological process
  • physiological process
  • transport
Component
  • cell
  • integral to membrane
  • intrinsic to membrane
  • membrane
Enzyme 11 General Function Not Available
Enzyme 11 Specific Function Mediates the Na(+)-independent transport of organic anions such as the thyroid hormones T3 (triiodo-L-thyronine), T4 (thyroxine) and rT3, and of estrone-3-sulfate and taurocholate
Enzyme 11 Pathways Not Available
Enzyme 11 Reactions Not Available
Enzyme 11 Pfam Domain Function
Enzyme 11 Signals
  • 1-188
Enzyme 11 Transmembrane Regions
  • 104-124 144-164 172-192 229-249 263-283 309-329 372-392 424-444 454-474 579-599 617-637 667-687
Enzyme 11 Essentiality Not Available
Enzyme 11 GenBank ID Protein 6683743 Link Image
Enzyme 11 UniProtKB/Swiss-Prot ID Q96BD0 Link Image
Enzyme 11 UniProtKB/Swiss-Prot Entry Name SO4A1_HUMAN Link Image
Enzyme 11 PDB ID Not Available
Enzyme 11 Cellular Location Not Available
Enzyme 11 Gene Sequence >2169 bp 
ATGCCCCTGCATCAGCTGGGGGACAAGCCGCTCACCTTCCCCAGCCCCAACTCAGCCATG
GAAAACGGGCTTGACCACACCCCACCCAGCAGGAGGGCATCCCCGGGCACACCCCTGAGC
CCCGGCTCCCTCCGCTCCGCTGCCCATAGCCCCCTGGACACCAGCAAGCAGCCCCTCTGC
CAGCTCTGGGCCGAGAAGCATGGCGCCCGGGGGACCCATGAGGTGCGGTACGTCTCGGCC
GGGCAGAGCGTGGCGTGCGGCTGGTGGGCCTTCGCACCGCCGTGCCTGCAGGTCCTCAAC
ACGCCCAAGGGCATCCTGTTCTTCCTGTGTGCGGCCGCATTCCTGCAGGGGATGACTGTG
AATGGCTTCATCAACACAGTCATCACCTCCCTGGAGCGCCGCTATGACCTGCACAGCTAC
CAGAGCGGGCTCATCGCCAGCTCCTACGACATTGCCGCCTGCCTCTGCCTCACCTTCGTC
AGCTACTTCGGGGGCTCAGGGCACAAGCCGCGCTGGCTGGGCTGGGGCGTGCTGCTTATG
GGCACGGGGTCGCTGGTGTTCGCGCTGCCCCACTTCACGGCTGGCCGCTATGAGGTGGAG
TTGGACGCGGGTGTCAGGACGTGCCCTGCCAACCCCGGCGCGGTGTGTGCGGACAGCACC
TCGGGCCTGTCCCGCTACCAGCTGGTCTTCATGCTGGGCCAGTTCCTGCATGGCGTGGGT
GCCACACCCCTCTACACGCTGGGCGTCACCTACCTGGATGAGAACGTCAAGTCCAGCTGC
TCGCCCGTCTACATTGCCATCTTCTACACAGCGGCCATCCTGGGCCCAGCTGCCGGCTAC
CTGATTGGAGGTGCCCTGCTGAATATCTACACGGAAATGGGCCGACGGACGGAGCTGACC
ACCGAGAGCCCACTGTGGGTCGGCGCCTGGTGGGTCGGCTTCCTGGGCTCTGGGGCCGCT
GCTTTCTTCACCGCCGTTCCCATCCTTGGTTACCCTCGGCAGCTGCCAGGCTCCCAGCGC
TACGCGGTCATGAGAGCGGCGGAAATGCACCAGTTGAAGGACAGCAGCCGTGGGGAGGCG
AGCAACCCGGACTTTGGGAAAACCATCAGAGACCTGCCTCTCTCCATCTGGCTCCTGCTG
AAGAACCCCACGTTCATCCTGCTCTGCCTGGCCGGGGCCACCGAGGCCACTCTCATCACC
GGCATGTCCACGTTCAGCCCCAAGTTCTTGGAGTCCCAGTTCAGCCTGAGTGCCTCAGAA
GCTGCCACCTTGTTTGGGTACCTGGTGGTGCCAGCGGGTGGTGGCGGCACCTTCCTGGGC
GGCTTCTTTGTGAACAAGCTCAGGCTCCGGGGCTCCGCGGTCATCAAGTTCTGCCTGTTC
TGCACCGTTGTCAGCCTGCTGGGCATCCTCGTCTTCTCACTGCACTGCCCCAGTGTGCCC
ATGGCGGGCGTCACAGCCAGCTACGGCGGGAGCCTCCTGCCCGAAGGCCACCTGAACCTA
ACGGCTCCCTGCAACGCTGCCTGCAGCTGCCAGCCAGAACACTACAGCCCTGTGTGCGGC
TCGGACGGCCTCATGTACTTCTCACTGTGCCACGCAGGGTGCCCTGCAGCCACGGAGACG
AATGTGGACGGCCAGAAGGTGTACCGAGACTGTAGCTGTATCCCTCAGAATCTTTCCTCT
GGTTTTGGCCATGCCACTGCAGGGAAATGCACTTCAACTTGTCAGAGAAAGCCCCTCCTT
CTGGTTTTCATATTCGTTGTAATTTTCTTTACATTCCTCAGCAGCATTCCTGCACTAACG
GCAACTCTACGATGTGTCCGTGACCCTCAGAGATCCTTTGCCCTGGGAATCCAGTGGATT
GTAGTTAGAATACTAGGGGGCATCCCGGGGCCCATCGCCTTCGGCTGGGTGATCGACAAG
GCCTGTCTGCTGTGGCAGGACCAGTGTGGCCAGCAGGGCTCCTGCTTGGTGTACCAGAAT
TCGGCCATGAGCCGCTACATACTCATCATGGGGCTCCTGTACAAGGTGCTGGGCGTCCTC
TTCTTTGCCATAGCCTGCTTCTTATACAAGCCCCTGTCGGAGTCTTCAGATGGCCTGGAA
ACTTGTCTGCCCAGCCAGTCCTCAGCCCCTGACAGTGCCACAGATAGCCAGCTCCAGAGC
AGCGTCTGA
Enzyme 11 GenBank Gene ID AB031051 Link Image
Enzyme 11 GeneCard ID SLCO4A1 Link Image
Enzyme 11 GenAtlas ID SLCO4A1 Link Image
Enzyme 11 HGNC ID HGNC:10953 Link Image
Enzyme 11 Chromosome Location 20
Enzyme 11 Locus 20q13.33
Enzyme 11 SNPs SNPJam Report Link Image
Enzyme 11 General References
  1. Tamai I, Nezu J, Uchino H, Sai Y, Oku A, Shimane M, Tsuji A: Molecular identification and characterization of novel members of the human organic anion transporter (OATP) family. Biochem Biophys Res Commun. 2000 Jun 24;273(1):251-60. [PubMed Link Image]
  2. Fujiwara K, Adachi H, Nishio T, Unno M, Tokui T, Okabe M, Onogawa T, Suzuki T, Asano N, Tanemoto M, Seki M, Shiiba K, Suzuki M, Kondo Y, Nunoki K, Shimosegawa T, Iinuma K, Ito S, Matsuno S, Abe T: Identification of thyroid hormone transporters in humans: different molecules are involved in a tissue-specific manner. Endocrinology. 2001 May;142(5):2005-12. [PubMed Link Image]
  3. Deloukas P, Matthews LH, Ashurst J, Burton J, Gilbert JG, Jones M, Stavrides G, Almeida JP, Babbage AK, Bagguley CL, Bailey J, Barlow KF, Bates KN, Beard LM, Beare DM, Beasley OP, Bird CP, Blakey SE, Bridgeman AM, Brown AJ, Buck D, Burrill W, Butler AP, Carder C, Carter NP, Chapman JC, Clamp M, Clark G, Clark LN, Clark SY, Clee CM, Clegg S, Cobley VE, Collier RE, Connor R, Corby NR, Coulson A, Coville GJ, Deadman R, Dhami P, Dunn M, Ellington AG, Frankland JA, Fraser A, French L, Garner P, Grafham DV, Griffiths C, Griffiths MN, Gwilliam R, Hall RE, Hammond S, Harley JL, Heath PD, Ho S, Holden JL, Howden PJ, Huckle E, Hunt AR, Hunt SE, Jekosch K, Johnson CM, Johnson D, Kay MP, Kimberley AM, King A, Knights A, Laird GK, Lawlor S, Lehvaslaiho MH, Leversha M, Lloyd C, Lloyd DM, Lovell JD, Marsh VL, Martin SL, McConnachie LJ, McLay K, McMurray AA, Milne S, Mistry D, Moore MJ, Mullikin JC, Nickerson T, Oliver K, Parker A, Patel R, Pearce TA, Peck AI, Phillimore BJ, Prathalingam SR, Plumb RW, Ramsay H, Rice CM, Ross MT, Scott CE, Sehra HK, Shownkeen R, Sims S, Skuce CD, Smith ML, Soderlund C, Steward CA, Sulston JE, Swann M, Sycamore N, Taylor R, Tee L, Thomas DW, Thorpe A, Tracey A, Tromans AC, Vaudin M, Wall M, Wallis JM, Whitehead SL, Whittaker P, Willey DL, Williams L, Williams SA, Wilming L, Wray PW, Hubbard T, Durbin RM, Bentley DR, Beck S, Rogers J: The DNA sequence and comparative analysis of human chromosome 20. Nature. 2001 Dec 20-27;414(6866):865-71. [PubMed Link Image]
Enzyme 11 Metabolite References Not Available
Enzyme 12 [top]
Enzyme 12 ID 14865
Enzyme 12 Name Gastrotropin
Enzyme 12 Synonyms Not Available
Enzyme 12 Gene Name FABP6
Enzyme 12 Protein Sequence >MAFTGKFEMESEKNYDEFMKLLGISSDVIEKARNFKIVTEVQQDGQDFTWSQHYSGGHTMTNKFTVGKES 
NIQTMGGKTFKATVQMEGGKLVVNFPNYHQTSEIVGDKLVEVSTIGGVTYERVSKRLA
Enzyme 12 Number of Residues 128
Enzyme 12 Molecular Weight 14371
Enzyme 12 Theoretical pI 6.81
Enzyme 12 GO Classification
Function
  • binding
  • lipid binding
Process
  • cellular physiological process
  • physiological process
  • transport
Component
—
Enzyme 12 General Function Not Available
Enzyme 12 Specific Function Ileal protein which stimulates gastric acid and pepsinogen secretion. Seems to be able to bind to bile salts and bilirubins
Enzyme 12 Pathways Not Available
Enzyme 12 Reactions Not Available
Enzyme 12 Pfam Domain Function
Enzyme 12 Signals
  • None
Enzyme 12 Transmembrane Regions
  • None
Enzyme 12 Essentiality Not Available
Enzyme 12 GenBank ID Protein 894183 Link Image
Enzyme 12 UniProtKB/Swiss-Prot ID P51161 Link Image
Enzyme 12 UniProtKB/Swiss-Prot Entry Name FABP6_HUMAN Link Image
Enzyme 12 PDB ID 1O1V Link Image
Enzyme 12 PDB File Show
Enzyme 12 3D Structure
Enzyme 12 Cellular Location Not Available
Enzyme 12 Gene Sequence >387 bp 
ATGGCTTTCACCGGCAAGTTCGAGATGGAGAGTGAGAAGAATTATGATGAGTTCATGAAG
CTCCTTGGGATCTCCAGCGATGTAATCGAAAAGGCCCGCAACTTCAAGATCGTCACGGAG
GTGCAGCAGGATGGGCAGGACTTCACTTGGTCCCAGCACTACTCCGGGGGCCACACCATG
ACCAACAAGTTCACTGTTGGCAAGGAAAGCAACATACAGACAATGGGGGGCAAGACGTTC
AAGGCCACTGTGCAGATGGAGGGCGGGAAGCTGGTGGTGAATTTCCCCAACTATCACCAG
ACCTCAGAGATCGTGGGTGACAAGCTGGTGGAGGTCTCCACCATCGGAGGCGTGACCTAT
GAGCGCGTGAGCAAGAGACTGGCCTAA
Enzyme 12 GenBank Gene ID U19869 Link Image
Enzyme 12 GeneCard ID P51161 Link Image
Enzyme 12 GenAtlas ID FABP6 Link Image
Enzyme 12 HGNC ID HGNC:3561 Link Image
Enzyme 12 Chromosome Location Not Available
Enzyme 12 Locus Not Available
Enzyme 12 SNPs SNPJam Report Link Image
Enzyme 12 General References
  1. Oelkers P, Dawson PA: Cloning and chromosomal localization of the human ileal lipid-binding protein. Biochim Biophys Acta. 1995 Jul 13;1257(2):199-202. [PubMed Link Image]
  2. Fujita M, Fujii H, Kanda T, Sato E, Hatakeyama K, Ono T: Molecular cloning, expression, and characterization of a human intestinal 15-kDa protein. Eur J Biochem. 1995 Oct 15;233(2):406-13. [PubMed Link Image]
Enzyme 12 Metabolite References
  1. Kurz M, Brachvogel V, Matter H, Stengelin S, Thuring H, Kramer W: Insights into the bile acid transportation system: the human ileal lipid-binding protein-cholyltaurine complex and its comparison with homologous structures. Proteins. 2003 Feb 1;50(2):312-28. [PubMed Link Image]