1. GSSG
2. Glutathione disulfide
3. Oxiglutatione
4. L(-)-Glutathione(oxidized)

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• Cytoplasm (Predicted from LogP)
• Extracellular
• mitochondria

• Blood
• Cerebrospinal Fluid

• 271900 (Canavan disease)
• 126200 (Multiple sclerosis)

1. Slivka A, Spina MB, Cohen G: Reduced and oxidized glutathione in human and monkey brain. Neurosci Lett. 1987 Feb 10;74(1):112-8. [PubMed ]
2. Aukrust P, Svardal AM, Muller F, Lunden B, Berge RK, Ueland PM, Froland SS: Increased levels of oxidized glutathione in CD4+ lymphocytes associated with disturbed intracellular redox balance in human immunodeficiency virus type 1 infection. Blood. 1995 Jul 1;86(1):258-67. [PubMed ]
3. Sakhi AK, Russnes KM, Smeland S, Blomhoff R, Gundersen TE: Simultaneous quantification of reduced and oxidized glutathione in plasma using a two-dimensional chromatographic system with parallel porous graphitized carbon columns coupled with fluorescence and coulometric electrochemical detection. J Chromatogr A. 2006 Feb 3;1104(1-2):179-89. [PubMed ]
4. Glazyrin AL, Kolesnikov SI, Safronov AYu: Histochemical localization of oxidized glutathione-catalysing enzymes in human term placenta. Histochem J. 1993 Jan;25(1):45-50. [PubMed ]
5. Calabrese V, Scapagnini G, Ravagna A, Bella R, Butterfield DA, Calvani M, Pennisi G, Giuffrida Stella AM: Disruption of thiol homeostasis and nitrosative stress in the cerebrospinal fluid of patients with active multiple sclerosis: evidence for a protective role of acetylcarnitine. Neurochem Res. 2003 Sep;28(9):1321-8. [PubMed ]
6. Carru C, Zinellu A, Pes GM, Marongiu G, Tadolini B, Deiana L: Ultrarapid capillary electrophoresis method for the determination of reduced and oxidized glutathione in red blood cells. Electrophoresis. 2002 Jun;23(11):1716-21. [PubMed ]
7. Tauler P, Sureda A, Cases N, Aguilo A, Rodriguez-Marroyo JA, Villa G, Tur JA, Pons A: Increased lymphocyte antioxidant defences in response to exhaustive exercise do not prevent oxidative damage. J Nutr Biochem. 2006 Oct;17(10):665-71. Epub 2005 Nov 28. [PubMed ]
8. Tohgi H, Abe T, Saheki M, Hamato F, Sasaki K, Takahashi S: Reduced and oxidized forms of glutathione and alpha-tocopherol in the cerebrospinal fluid of parkinsonian patients: comparison between before and after L-dopa treatment. Neurosci Lett. 1995 Jan 16;184(1):21-4. [PubMed ]
9. Yoshida T: Determination of reduced and oxidized glutathione in erythrocytes by high-performance liquid chromatography with ultraviolet absorbance detection. J Chromatogr B Biomed Appl. 1996 Apr 12;678(2):157-64. [PubMed ]
10. Sofic E, Lange KW, Jellinger K, Riederer P: Reduced and oxidized glutathione in the substantia nigra of patients with Parkinson's disease. Neurosci Lett. 1992 Aug 17;142(2):128-30. [PubMed ]
11. Kondo T, Ohtsuka Y, Shimada M, Kawakami Y, Hiyoshi Y, Tsuji Y, Fujii H, Miwa S: Erythrocyte-oxidized glutathione transport in pyrimidine 5'-nucleotidase deficiency. Am J Hematol. 1987 Sep;26(1):37-45. [PubMed ]
12. Muda P, Kampus P, Zilmer M, Zilmer K, Kairane C, Ristimae T, Fischer K, Teesalu R: Homocysteine and red blood cell glutathione as indices for middle-aged untreated essential hypertension patients. J Hypertens. 2003 Dec;21(12):2329-33. [PubMed ]
13. Satoh T, Yoshioka Y: Contribution of reduced and oxidized glutathione to signals detected by magnetic resonance spectroscopy as indicators of local brain redox state. Neurosci Res. 2006 May;55(1):34-9. Epub 2006 Feb 24. [PubMed ]
14. Srivastava SK, Beutler E: Oxidized glutathione levels in erythrocytes of glucose-6-phosphate-dehydrogenase-deficient subjects. Lancet. 1968 Jul 6;2(7558):23-4. [PubMed ]
15. Board P, Nishida T, Gatmaitan Z, Che M, Arias IM: Erythrocyte membrane transport of glutathione conjugates and oxidized glutathione in the Dubin-Johnson syndrome and in rats with hereditary hyperbilirubinemia. Hepatology. 1992 Apr;15(4):722-5. [PubMed ]
16. Wikipedia

1. Glutathione reductase, mitochondrial precursor
2. Aminopeptidase N
3. Glutathione peroxidase 7 precursor
4. Epididymal secretory glutathione peroxidase precursor
5. Glutathione peroxidase 6 precursor
6. Glutathione peroxidase 1
7. Phospholipid hydroperoxide glutathione peroxidase, mitochondrial precursor
8. Glutathione peroxidase 3 precursor
9. Glutathione peroxidase 2
10. Thioredoxin domain-containing protein 12 precursor
11. cDNA PSEC0100 fis, clone NT2RP2002927, highly similar to Thioredoxin domain-containing protein 12 (Thioredoxin domain containing 12) (Endoplasmic reticulum)

1. GR
2. GRase

MALLPRALSAGAGPSWRRAARAFRGFLLLLPEPAALTRALSRAMACRQEPQPQGPPPAAG
AVASYDYLVIGGGSGGLASARRAAELGARAAVVESHKLGGTCVNVGCVPKKVMWNTAVHS
EFMHDHADYGFPSCEGKFNWRVIKEKRDAYVSRLNAIYQNNLTKSHIEIIRGHAAFTSDP
KPTIEVSGKKYTAPHILIATGGMPSTPHESQIPGASLGITSDGFFQLEELPGRSVIVGAG
YIAVEMAGILSALGSKTSLMIRHDKVLRSFDSMISTNCTEELENAGVEVLKFSQVKEVKK
TLSGLEVSMVTAVPGRLPVMTMIPDVDCLLWAIGRVPNTKDLSLNKLGIQTDDKGHIIVD
EFQNTNVKGIYAVGDVCGKALLTPVAIAAGRKLAHRLFEYKEDSKLDYNNIPTVVFSHPP
IGTVGLTEDEAIHKYGIENVKTYSTSFTPMYHAVTKRKTKCVMKMVCANKEEKVVGIHMQ
GLGCDEMLQGFAVAVKMGATKADFDNTVAIHPTSSEELVTLR

• Glutamate Metabolism (map00251 )
• Glutathione Metabolism (map00480 )

• 2 glutathione + NADP+ = glutathione disulfide + NADPH + H+

• Pyr_redox (PF00070 )
• Pyr_redox_2 (PF07992 )
• Pyr_redox_dim (PF02852 )

• 1-37

ATGGCCTGCAGGCAGGAGCCGCAGCCGCAGGGCCCGCCGCCCGCTGCTGGCGCCGTGGCC
TCCTATGACTACCTGGTGATCGGGGGCGGCTCGGGCGGGCTGGCCAGCGCGCGCAGGGCG
GCCGAGCTGGGTGCCAGGGCCGCCGTGGTGGAGAGCCACAAGCTGGGTGGCACTTGCGTG
AATGTTGGATGTGTACCCAAAAAGGTAATGTGGAACACAGCTGTCCACTCTGAATTCATG
CATGATCATGCTGATTATGGCTTTCCAAGTTGTGAGGGTAAATTCAATTGGCGTGTTATT
AAGGAAAAGCGGGATGCCTATGTGAGCCGCCTGAATGCCATCTATCAAAACAATCTCACC
AAGTCCCATATAGAAATCATCCGTGGCCATGCAGCCTTCACGAGTGATCCCAAGCCCACA
ATAGAGGTCAGTGGGAAAAAGTACACCGCCCCACACATCCTGATCGCCACAGGTGGTATG
CCCTCCACCCCTCATGAGAGCCAGATCCCCGGTGCCAGCTTAGGAATAACCAGCGATGGA
TTTTTTCAGCTGGAAGAATTGCCCGGCCGCAGCGTCATTGTTGGTGCAGGTTACATTGCT
GTGGAGATGGCAGGGATCCTGTCAGCCCTGGGTTCTAAGACATCACTGATGATACGGCAT
GATAAGGTACTTAGAAGTTTTGATTCAATGATCAGCACCAACTGCACGGAGGAGCTGGAG
AACGCTGGCGTGGAGGTGCTGAAGTTCTCCCAGGTCAAGGAGGTTAAAAAGACTTTGTCG
GGCTTGGAAGTCAGCATGGTTACTGCAGTTCCCGGTAGGCTACCAGTCATGACCATGATT
CCAGATGTTGACTGCCTGCTCTGGGCCATTGGGCGGGTCCCGAATACCAAGGACCTGAGT
TTAAACAAACTGGGGATTCAAACCGATGACAAGGGTCATATCATCGTAGACGAATTCCAG
AATACCAACGTCAAAGGCATCTATGCAGTTGGGGATGTATGTGGAAAAGCTCTTCTTACT
CCAGTTGCAATAGCTGCTGGCCGAAAACTTGCCCATCGACTTTTTGAATATAAGGAAGAT
TCCAAATTAGATTATAACAACATCCCAACTGTGGTCTTCAGCCACCCCCCTATTGGGACA
GTGGGACTCACGGAAGATGAAGCCATTCATAAATATGGAATAGAAAATGTGAAGACCTAT
TCAACGAGCTTTACCCCGATGTATCACGCAGTTACCAAAAGGAAAACAAAATGTGTGATG
AAAATGGTCTGTGCTAACAAGGAAGAAAAGGTGGTTGGGATCCATATGCAGGGACTTGGG
TGTGATGAAATGCTGCAGGGTTTTGCTGTTGCAGTGAAGATGGGAGCAACGAAGGCAGAC
TTTGACAACACAGTCGCCATTCACCCTACCTCTTCAGAAGAGCTGGTCACACTTCGTTGA

1. Tutic M, Lu XA, Schirmer RH, Werner D: Cloning and sequencing of mammalian glutathione reductase cDNA. Eur J Biochem. 1990 Mar 30;188(3):523-8. [PubMed ]
2. Kelner MJ, Montoya MA: Structural organization of the human glutathione reductase gene: determination of correct cDNA sequence and identification of a mitochondrial leader sequence. Biochem Biophys Res Commun. 2000 Mar 16;269(2):366-8. [PubMed ]
3. Krauth-Siegel RL, Blatterspiel R, Saleh M, Schiltz E, Schirmer RH, Untucht-Grau R: Glutathione reductase from human erythrocytes. The sequences of the NADPH domain and of the interface domain. Eur J Biochem. 1982 Jan;121(2):259-67. [PubMed ]
4. Krohne-Ehrich G, Schirmer RH, Untucht-Grau R: Glutathione reductase from human erythrocytes. Isolation of the enzyme and sequence analysis of the redox-active peptide. Eur J Biochem. 1977 Oct 17;80(1):65-71. [PubMed ]
5. Thieme R, Pai EF, Schirmer RH, Schulz GE: Three-dimensional structure of glutathione reductase at 2 A resolution. J Mol Biol. 1981 Nov 15;152(4):763-82. [PubMed ]
6. Karplus PA, Schulz GE: Refined structure of glutathione reductase at 1.54 A resolution. J Mol Biol. 1987 Jun 5;195(3):701-29. [PubMed ]
7. Savvides SN, Karplus PA: Kinetics and crystallographic analysis of human glutathione reductase in complex with a xanthene inhibitor. J Biol Chem. 1996 Apr 5;271(14):8101-7. [PubMed ]
8. Stoll VS, Simpson SJ, Krauth-Siegel RL, Walsh CT, Pai EF: Glutathione reductase turned into trypanothione reductase: structural analysis of an engineered change in substrate specificity. Biochemistry. 1997 May 27;36(21):6437-47. [PubMed ]
9. Becker K, Savvides SN, Keese M, Schirmer RH, Karplus PA: Enzyme inactivation through sulfhydryl oxidation by physiologic NO-carriers. Nat Struct Biol. 1998 Apr;5(4):267-71. [PubMed ]

1. hAPN
2. Alanyl aminopeptidase
3. Microsomal aminopeptidase
4. Aminopeptidase M
5. gp150
6. Myeloid plasma membrane glycoprotein CD13
7. CD13 antigen

MAKGFYISKSLGILGILLGVAAVCTIIALSVVYSQEKNKNANSSPVASTTPSASATTNPA
SATTLDQSKAWNRYRLPNTLKPDSYRVTLRPYLTPNDRGLYVFKGSSTVRFTCKEATDVI
IIHSKKLNYTLSQGHRVVLRGVGGSQPPDIDKTELVEPTEYLVVHLKGSLVKDSQYEMDS
EFEGELADDLAGFYRSEYMEGNVRKVVATTQMQAADARKSFPCFDEPAMKAEFNITLIHP
KDLTALSNMLPKGPSTPLPEDPNWNVTEFHTTPKMSTYLLAFIVSEFDYVEKQASNGVLI
RIWARPSAIAAGHGDYALNVTGPILNFFAGHYDTPYPLPKSDQIGLPDFNAGAMENWGLV
TYRENSLLFDPLSSSSSNKERVVTVIAHELAHQWFGNLVTIEWWNDLWLNEGFASYVEYL
GADYAEPTWNLKDLMVLNDVYRVMAVDALASSHPLSTPASEINTPAQISELFDAISYSKG
ASVLRMLSSFLSEDVFKQGLASYLHTFAYQNTIYLNLWDHLQEAVNNRSIQLPTTVRDIM
NRWTLQMGFPVITVDTSTGTLSQEHFLLDPDSNVTRPSEFNYVWIVPITSIRDGRQQQDY
WLIDVRAQNDLFSTSGNEWVLLNLNVTGYYRVNYDEENWRKIQTQLQRDHSAIPVINRAQ
IINDAFNLASAHKVPVTLALNNTLFLIEERQYMPWEAALSSLSYFKLMFDRSEVYGPMKN
YLKKQVTPLFIHFRNNTNNWREIPENLMDQYSEVNAISTACSNGVPECEEMVSGLFKQWM
ENPNNNPIHPNLRSTVYCNAIAQGGEEEWDFAWEQFRNATLVNEADKLRAALACSKELWI
LNRYLSYTLNPDLIRKQDATSTIISITNNVIGQGLVWDFVQSNWKKLFNDYGGGSFSFSN
LIQAVTRRFSTEYELQQLEQFKKDNEETGFGSGTRALEQALEKTKANIKWVKENKEVVLQ
WFTENSK

• Glutathione Metabolism (map00480 )

• Release of an N-terminal amino acid, Xaa-|-Yaa- from a peptide, amide or arylamide. Xaa is preferably Ala, but may be most amino acids including Pro (slow action). When a terminal hydrophobic residue is followed by a prolyl residue, the two may be released as an intact Xaa-Pro dipeptide

• 1-22

ATGGCCAAGGGCTTCTATATTTCCAAGTCCCTGGGCATCCTGGGGATCCTCCTGGGCGTG
GCAGCCGTGTGCACAATCATCGCACTGTCAGTGGTGTACTCCCAGGAGAAGAACAAGAAC
GCCAACAGCTCCCCCGTGGCCTCCACCACCCCGTCCGCCTCAGCCACCACCAACCCCGCC
TCGGCCACCACCTTGGACCAAAGTAAAGCGTGGAATCGTTACCGCCTCCCCAACACGCTG
AAACCCGATTCCTACCAGGTGACGCTGAGACCGTACCTCACCCCCAATGACAGGGGCCTG
TACGTTTTTAAGGGCTCCAGCACCGTCCGTTTCACCTGCAAGGAGGCCACTGACGTCATC
ATCATCCACAGCAAGAAGCTCAACTACACCCTCAGCCAGGGGCACAGGGTGGTCCTGCGT
GGTGTGGGAGGCTCCCAGCCCCCCGACATTGACAAGACTGAGCTGGTGGAGCCCACCGAG
TACCTGGTGGTGCACCTCAAGGGCTCCCTGGTGAAGGACAGCCAGTATGAGATGGACAGC
GAGTTCGAGGGGGAGTTGGCAGATGACCTGGCGGGCTTCTACCGCAGCGAGTACATGGAG
GGCAATGTCAGAAAGGTGGTGGCCACTACACAGATGCAGGCTGCAGATGCCCGGAAGTCC
TTCCCATGCTTCGATGAGCCGGCCATGAAGGCCGAGTTCAACATCACGCTTATCCACCCC
AAGGACCTGACAGCCCTGTCCAACATGCTTCCCAAAGGTCCCAGCACCCCACTTCCAGAA
GACCCCAACTGGAATGTCACTGAGTTCCACACCACGCCCAAGATGTCCACGTACTTGCTG
GCCTTCATTGTCAGTGAGTTCGACTACGTGGAGAAGCAGGCATCCAATGGTGTCTTGATC
CGGATCTGGGCCCGGCCCAGTGCCATTGCGGCGGGCCACGGCGATTATGCCCTGAACGTG
ACGGGCCCCATCCTTAACTTCTTTGCTGGTCATTATGACACACCCTACCCACTCCCAAAA
TCAGACCAGATTGGCCTGCCAGACTTCAACGCCGGCGCCATGGAGAACTGGGGACTGGTG
ACCTACCGGGAGAACTCCCTGCTGTTCGACCCCCTGTCCTCCTCCAGCAGCAACAAGGAG
CGGGTGGTCACTGTGATTGCTCATGAGCTGGCCCACCAGTGGTTCGGGAACCTGGTGACC
ATAGAGTGGTGGAATGACCTGTGGCTGAACGAGGGCTTCGCCTCCTACGTGGAGTACCTG
GGTGCTGACTATGCGGAGCCCACCTGGAACTTGAAAGACCTCATGGTGCTGAATGATGTG
TACCGCGTGATGGCAGTGGATGCACTGGCCTCCTCCCACCCGCTGTCCACACCCGCCTCG
GAGATCAACACGCCGGCCCAGATCAGTGAGCTGTTTGACGCCATCTCCTACAGCAAGGGC
GCCTCAGTCCTCAGGATGCTCTCCAGCTTCCTGTCCGAGGACGTATTCAAGCAGGGCCTG
GCGTCCTACCTCCACACCTTTGCCTACCAGAACACCATCTACCTGAACCTGTGGGACCAC
CTGCAGGAGGCTGTGAACAACCGGTCCATCCAACTCCCCACCACCGAGCGGGACATCATG
AACCGCTGGACCCTGCAGATGGGCTTCCCGGTCATCACGGTGGATACCAGCACGGGGACC
CTTTCCCAGGAGCACTTCCTCCTTGACCCCGATTCCAATGTTACCCGCCCCTCAGAATTC
AACTACGTGTGGATTGTGCCCATCACATCCATCAGAGATGGCAGACAGCAGCAGGACTAC
TGGCTGATGGATGTAAGAGCCCAGAACGATCTCTTCAGCACATCAGGCAATGAGTGGGTC
CTGCTGAACCTCAATGTGACGGGCTATTACCGGGTGAACTACGACGAAGAGAACTGGAGG
AAGATTCAGACTCAGCTGCAGAGAGACCACTCGGCCATCCCTGTCATCAATCGGGCACAG
ATCATTAATGACGCCTTCAACCTGGCCAGTGCCCATAAGGTCCCTGTCACTCTGGCGCTG
AACAACACCCTCTTCCTGATTGAAGAGAGACAGTACATGCCCTGGGAGGCCGCCCTGAGC
AGCCTGAGCTACTTCAAGCTCATGTTTGACCGCTCCGAGGTCTATGGCCCCATGAAGAAC
TACCTGAAGAAGCAGGTCACACCCCTCTTCATTCACTTCAGAAATAATACCAACAACTGG
AGGGAGATCCCAGAAAACCTGATGGACCAGTACAGCGAGGTTAATGCCATCAGCACCGCC
TGCTCCAACGGAGTTCCAGAGTGTGAGGAGATGGTCTCTGGCCTTTTCAAGCAGTGGATG
GAGAACCCCAATAATAACCCGATCCACCCCAACCTGCGGTCCACCGTCTACTGCAACGCT
ATCGCCCAGGGCGGGGAGGAGGAGTGGGACTTCGCCTGGGAGCAGTTCCGAAATGCCACA
CTGGTCAATGAGGCTGACAAGCTCCGGGCAGCCCTGGCCTGCAGCAAAGAGTTGTGGATC
CTGAACAGGTACCTGAGCTACACCCTGAACCCGGACTTAATCCGGAAGCAGGACGCCACC
TCTACCATCATCAGCATTACCAACAACGTCATTGGGCAAGGTCTGGTCTGGGACTTTGTC
CAGAGCAACTGGAAGAAGCCTTTTAACGATTATGGTGGTGGCTCGTTCTCCTTCTCCAAC
CTCATCCAGGCAGTGACACGACGATTCTCCACCGAGTATGAGCTGCAGCAGCTGGAGCAG
TTCAAGAAGGACAACGAGGAAACAGGCTTCGGCTCAGGCACCCGGGCCCTGGAGCAAGCC
CTGGAGAAGACGAAAGCCAACATCAAGTGGGTGAAGGAGAACAAGGAGGTGGTGCTCCAG
TGGTTCACAGAAAACAGCAAATAG

1. Olsen J, Cowell GM, Konigshofer E, Danielsen EM, Moller J, Laustsen L, Hansen OC, Welinder KG, Engberg J, Hunziker W, et al.: Complete amino acid sequence of human intestinal aminopeptidase N as deduced from cloned cDNA. FEBS Lett. 1988 Oct 10;238(2):307-14. [PubMed ]
2. Look AT, Ashmun RA, Shapiro LH, Peiper SC: Human myeloid plasma membrane glycoprotein CD13 (gp150) is identical to aminopeptidase N. J Clin Invest. 1989 Apr;83(4):1299-307. [PubMed ]
3. Shapiro LH, Ashmun RA, Roberts WM, Look AT: Separate promoters control transcription of the human aminopeptidase N gene in myeloid and intestinal epithelial cells. J Biol Chem. 1991 Jun 25;266(18):11999-2007. [PubMed ]
4. Watanabe Y, Iwaki-Egawa S, Mizukoshi H, Fujimoto Y: Identification of an alanine aminopeptidase in human maternal serum as a membrane-bound aminopeptidase N. Biol Chem Hoppe Seyler. 1995 Jul;376(7):397-400. [PubMed ]
5. Nunez L, Amigo L, Rigotti A, Puglielli L, Mingrone G, Greco AV, Nervi F: Cholesterol crystallization-promoting activity of aminopeptidase-N isolated from the vesicular carrier of biliary lipids. FEBS Lett. 1993 Aug 23;329(1-2):84-8. [PubMed ]
6. Tokioka-Terao M, Hiwada K, Kokubu T: Purification and characterization of aminopeptidase N from human plasma. Enzyme. 1984;32(2):65-75. [PubMed ]
7. O'Connell PJ, Gerkis V, d'Apice AJ: Variable O-glycosylation of CD13 (aminopeptidase N). J Biol Chem. 1991 Mar 5;266(7):4593-7. [PubMed ]
8. Yeager CL, Ashmun RA, Williams RK, Cardellichio CB, Shapiro LH, Look AT, Holmes KV: Human aminopeptidase N is a receptor for human coronavirus 229E. Nature. 1992 Jun 4;357(6377):420-2. [PubMed ]
9. Favaloro EJ, Browning T, Facey D: CD13 (GP150; aminopeptidase-N): predominant functional activity in blood is localized to plasma and is not cell-surface associated. Exp Hematol. 1993 Dec;21(13):1695-701. [PubMed ]
10. Soderberg C, Giugni TD, Zaia JA, Larsson S, Wahlberg JM, Moller E: CD13 (human aminopeptidase N) mediates human cytomegalovirus infection. J Virol. 1993 Nov;67(11):6576-85. [PubMed ]
11. Kolb AF, Maile J, Heister A, Siddell SG: Characterization of functional domains in the human coronavirus HCV 229E receptor. J Gen Virol. 1996 Oct;77 ( Pt 10):2515-21. [PubMed ]
12. Noren K, Hansen GH, Clausen H, Noren O, Sjostrom H, Vogel LK: Defectively N-glycosylated and non-O-glycosylated aminopeptidase N (CD13) is normally expressed at the cell surface and has full enzymatic activity. Exp Cell Res. 1997 Feb 25;231(1):112-8. [PubMed ]
13. Kolb AF, Hegyi A, Siddell SG: Identification of residues critical for the human coronavirus 229E receptor function of human aminopeptidase N. J Gen Virol. 1997 Nov;78 ( Pt 11):2795-802. [PubMed ]
14. Hegyi A, Kolb AF: Characterization of determinants involved in the feline infectious peritonitis virus receptor function of feline aminopeptidase N. J Gen Virol. 1998 Jun;79 ( Pt 6):1387-91. [PubMed ]
15. Dong X, An B, Salvucci Kierstead L, Storkus WJ, Amoscato AA, Salter RD: Modification of the amino terminus of a class II epitope confers resistance to degradation by CD13 on dendritic cells and enhances presentation to T cells. J Immunol. 2000 Jan 1;164(1):129-35. [PubMed ]
16. Pasqualini R, Koivunen E, Kain R, Lahdenranta J, Sakamoto M, Stryhn A, Ashmun RA, Shapiro LH, Arap W, Ruoslahti E: Aminopeptidase N is a receptor for tumor-homing peptides and a target for inhibiting angiogenesis. Cancer Res. 2000 Feb 1;60(3):722-7. [PubMed ]
17. Seli E, Senturk LM, Bahtiyar OM, Kayisli UA, Arici A: Expression of aminopeptidase N in human endometrium and regulation of its activity by estrogen. Fertil Steril. 2001 Jun;75(6):1172-6. [PubMed ]
18. Wentworth DE, Holmes KV: Molecular determinants of species specificity in the coronavirus receptor aminopeptidase N (CD13): influence of N-linked glycosylation. J Virol. 2001 Oct;75(20):9741-52. [PubMed ]
19. van Hensbergen Y, Broxterman HJ, Hanemaaijer R, Jorna AS, van Lent NA, Verheul HM, Pinedo HM, Hoekman K: Soluble aminopeptidase N/CD13 in malignant and nonmalignant effusions and intratumoral fluid. Clin Cancer Res. 2002 Dec;8(12):3747-54. [PubMed ]
20. Bonavia A, Zelus BD, Wentworth DE, Talbot PJ, Holmes KV: Identification of a receptor-binding domain of the spike glycoprotein of human coronavirus HCoV-229E. J Virol. 2003 Feb;77(4):2530-8. [PubMed ]
21. Lendeckel U, Wex T, Arndt M, Frank K, Franke A, Ansorge S: Identification of point mutations in the aminopeptidase N gene by SSCP analysis and sequencing. Hum Mutat. 1998;Suppl 1:S158-60. [PubMed ]

1. CL683

MVAATVAAAWLLLWAAACAQQEQDFYDFKAVNIRGKLVSLEKYRGSVSLVVNVASECGFT
DQHYRALQQLQRDLGPHHFNVLAFPCNQFGQQEPDSNKEIESFARRTYSVSFPMFSKIAV
TGTGAHPAFKYLAQTSGKEPTWNFWKYLVAPDGKVVGAWDPTVSVEEVRPQITALVRKLI
LLKREDL

• Glutathione Metabolism (map00480 )

• 2 glutathione + H2O2 = glutathione disulfide + 2 H2O

• GSHPx (PF00255 )

• 1-19

ATGGTGGCGGCGACGGTGGCAGCGGCGTGGCTGCTCCTGTGGGCTGCGGCCTGCGCGCAG
CAGGAGCAGGACTTCTACGACTTCAAGGCGGTCAACATCCGGGGCAAACTGGTGTCGCTG
GAGAAGTACCGCGGATCGGTGTCCCTGGTGGTGAATGTGGCCAGCGAGTGCGGCTTCACA
GACCAGCACTACCGAGCCCTGCAGCAGCTGCAGCGAGACCTGGGCCCCCACCACTTTAAC
GTGCTCGCCTTCCCCTGCAACCAGTTTGGCCAACAGGAGCCTGACAGCAACAAGGAGATT
GAGAGCTTTGCCCGCCGCACCTACAGTGTCTCATTCCCCATGTTTAGCAAGATTGCAGTC
ACCGGTACTGGTGCCCATCCTGCCTTCAAGTACCTGGCCCAGACTTCTGGGAAGGAGCCC
ACCTGGAACTTCTGGAAGTACCTAGTAGCCCCAGATGGAAAGGTGGTAGGGGCTTGGGAC
CCAACTGTGTCAGTGGAGGAGGTCAGACCCCAGATCACAGCGCTCGTGAGGAAGCTCATC
CTACTGAAGCGAGAAGACTTATAA

1. Clark HF, Gurney AL, Abaya E, Baker K, Baldwin D, Brush J, Chen J, Chow B, Chui C, Crowley C, Currell B, Deuel B, Dowd P, Eaton D, Foster J, Grimaldi C, Gu Q, Hass PE, Heldens S, Huang A, Kim HS, Klimowski L, Jin Y, Johnson S, Lee J, Lewis L, Liao D, Mark M, Robbie E, Sanchez C, Schoenfeld J, Seshagiri S, Simmons L, Singh J, Smith V, Stinson J, Vagts A, Vandlen R, Watanabe C, Wieand D, Woods K, Xie MH, Yansura D, Yi S, Yu G, Yuan J, Zhang M, Zhang Z, Goddard A, Wood WI, Godowski P, Gray A: The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. Genome Res. 2003 Oct;13(10):2265-70. Epub 2003 Sep 15. [PubMed ]

1. Epididymis-specific glutathione peroxidase-like protein
2. EGLP

MTTQLRVVHLLPLLLACFVQTSPKQEKMKMDCHKDEKGTIYDYEAIALNKNEYVSFKQYV
GKHILFVNVATYCGLTAQYPELNALQEELKPYGLVVLGFPCNQFGKQEPGDNKEILPGLK
YVRPGGGFVPSFQLFEKGDVNGEKEQKVFSFLKHSCPHPSEILGTFKSISWDPVKVHDIR
WNFEKFLVGPDGIPVMRWSHRATVSSVKTDILAYLKQFKTK

• Glutathione Metabolism (map00480 )

• 2 glutathione + H2O2 = glutathione disulfide + 2 H2O

• GSHPx (PF00255 )

• 1-21

ATGACTACACAGTTAAGGGTCGTCCATCTGCTTCCCCTTCTCCTAGCCTGCTTTGTGCAA
ACAAGTCCCAAGCAGGAGAAGATGAAGATGGATTGCCACAAAGACGAGAAAGGCACCATC
TATGACTATGAGGCCATCGCACTTAATAAGAATGAATATGTTTCCTTCAAGCAGTATGTG
GGCAAGCACATCCTCTTCGTCAACGTGGCCACCTACTGTGGTCTGACAGCGCAATATCCT
GAACTAAATGCACTCCAGGAGGAGCTGAAGCCCTATGGTCTAGTTGTGTTGGGCTTTCCC
TGCAACCAATTTGGAAAGCAAGAACCAGGAGATAACAAAGAGATTCTTCCTGGGCTCAAG
TATGTCCGTCCAGGGGGAGGATTTGTACCTAGTTTCCAGCTTTTTGAGAAAGGGGATGTG
AATGGTGAAAAAGAACAGAAAGTCTTCAGTTTCTTGAAGCACTCCTGTCCTCATCCCTCT
GAGATTTTGGGCACATTCAAATCTATATCCTGGGACCCTGTAAAGGTCCATGACATCCGT
TGGAACTTTGAAAAGTTCCTGGTGGGGCCTGATGGAATCCCTGTCATGCGCTGGTCCCAC
CGGGCTACGGTCAGCTCAGTCAAGACAGACATCCTGGCGTACTTGAAGCAATTCAAAACC
AAATAG

1. Hall L, Williams K, Perry AC, Frayne J, Jury JA: The majority of human glutathione peroxidase type 5 (GPX5) transcripts are incorrectly spliced: implications for the role of GPX5 in the male reproductive tract. Biochem J. 1998 Jul 1;333 ( Pt 1):5-9. [PubMed ]
2. Mungall AJ, Palmer SA, Sims SK, Edwards CA, Ashurst JL, Wilming L, Jones MC, Horton R, Hunt SE, Scott CE, Gilbert JG, Clamp ME, Bethel G, Milne S, Ainscough R, Almeida JP, Ambrose KD, Andrews TD, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beare DM, Beasley H, Beasley O, Bird CP, Blakey S, Bray-Allen S, Brook J, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Clark SY, Clark G, Clee CM, Clegg S, Cobley V, Collier RE, Collins JE, Colman LK, Corby NR, Coville GJ, Culley KM, Dhami P, Davies J, Dunn M, Earthrowl ME, Ellington AE, Evans KA, Faulkner L, Francis MD, Frankish A, Frankland J, French L, Garner P, Garnett J, Ghori MJ, Gilby LM, Gillson CJ, Glithero RJ, Grafham DV, Grant M, Gribble S, Griffiths C, Griffiths M, Hall R, Halls KS, Hammond S, Harley JL, Hart EA, Heath PD, Heathcott R, Holmes SJ, Howden PJ, Howe KL, Howell GR, Huckle E, Humphray SJ, Humphries MD, Hunt AR, Johnson CM, Joy AA, Kay M, Keenan SJ, Kimberley AM, King A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd CR, Lloyd DM, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, Maslen GL, Matthews L, McCann OT, McLaren SJ, McLay K, McMurray A, Moore MJ, Mullikin JC, Niblett D, Nickerson T, Novik KL, Oliver K, Overton-Larty EK, Parker A, Patel R, Pearce AV, Peck AI, Phillimore B, Phillips S, Plumb RW, Porter KM, Ramsey Y, Ranby SA, Rice CM, Ross MT, Searle SM, Sehra HK, Sheridan E, Skuce CD, Smith S, Smith M, Spraggon L, Squares SL, Steward CA, Sycamore N, Tamlyn-Hall G, Tester J, Theaker AJ, Thomas DW, Thorpe A, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, White SS, Whitehead SL, Whittaker H, Wild A, Willey DJ, Wilmer TE, Wood JM, Wray PW, Wyatt JC, Young L, Younger RM, Bentley DR, Coulson A, Durbin R, Hubbard T, Sulston JE, Dunham I, Rogers J, Beck S: The DNA sequence and analysis of human chromosome 6. Nature. 2003 Oct 23;425(6960):805-11. [PubMed ]

MFQQFQASCLVLFFLVGFAQQTLKPQNRKVDCNKGVTGTIYEYGALTLNGEEYIQFKQFA
GKHVLFVNVAAYCGLAAQYPELNALQEELKNFGVIVLAFPCNQFGKQEPGTNSEILLGLK
YVCPGSGFVPSFQLFEKGDVNGEKEQKVFTFLKNSCPPTSDLLGSSSQLFWEPMKVHDIR
WNFEKFLVGPDGVPVMHWFHQAPVSTVKSDILEYLKQFNTH

• Glutathione Metabolism (map00480 )

• 2 glutathione + H2O2 = glutathione disulfide + 2 H2O

• GSHPx (PF00255 )

• 1-19

ATGTTCCAGCAGTTCCAGGCCTCCTGTCTTGTCCTGTTTTTCCTGGTTGGCTTTGCTCAG
CAGACCCTAAAGCCTCAAAATAGGAAGGTGGATTGCAACAAAGGGGTAACAGGCACCATC
TATGAGTATGGAGCCCTCACCCTCAACGGCGAGGAGTACATCCAATTCAAGCAGTTTGCA
GGCAAGCACGTCCTGTTTGTCAATGTGGCCGCCTATTGAGGCTTGGCAGCTCAGTATCCT
GAACTGAATGCACTACAGGAGGAGCTGAAGAATTTTGGTGTCATTGTGTTGGCCTTTCCC
TGCAACCAGTTTGGAAAACAAGAACCAGGAACAAACTCAGAAATACTTCTTGGTCTCAAG
TATGTGTGTCCAGGTAGTGGCTTTGTCCCCAGTTTCCAGCTCTTTGAGAAAGGGGATGTG
AATGGAGAAAAAGAACAGAAGGTCTTTACTTTCCTGAAGAACTCCTGCCCTCCGACCTCT
GATCTTTTGGGCTCATCAAGCCAACTCTTCTGGGAGCCCATGAAGGTCCATGATATCCGC
TGGAACTTTGAGAAATTTCTGGTGGGGCCCGATGGAGTCCCTGTCATGCATTGGTTCCAC
CAGGCTCCAGTCAGCACAGTCAAGTCAGACATCCTGGAGTACCTAAAGCAGTTCAATACC
CACTAG

1. Kryukov GV, Castellano S, Novoselov SV, Lobanov AV, Zehtab O, Guigo R, Gladyshev VN: Characterization of mammalian selenoproteomes. Science. 2003 May 30;300(5624):1439-43. [PubMed ]

1. GSHPx-1
2. GPx-1
3. Cellular glutathione peroxidase

MCAARLAAAAAQSVYAFSARPLAGGEPVSLGSLRGKVLLIENVASLCGTTVRDYTQMNEL
QRRLGPRGLVVLGFPCNQFGHQENAKNEEILNSLKYVRPGGGFEPNFMLFEKCEVNGAGA
HPLFAFLREALPAPSDDATALMTDPKLITWSPVCRNDVAWNFEKFLVGPDGVPLRRYSRR
FQTIDIEPDIEALLSQGPSCA

• Glutathione Metabolism (map00480 )

• 2 glutathione + H2O2 = glutathione disulfide + 2 H2O

• GSHPx (PF00255 )

• 1-16

ATGTGTGCTGCTCGGCTAGCGGCGGCGGCGGCCCAGTCGGTGTATGCCTTCTCGGCGCGC
CCGTTGGCCGGCGGGGAGCCTGTGAGCCTGGGCTCCCTGCGGGGCAAGGTACTACTTATC
GAGAATGTGGCGTCCCTCTGAGGCACCACGGTCCGGGACTACACCCAGATGAACGAGCTG
CAGCGGCGCCTCGGACCCCGGGGCCTGGTGGTGCTCGGCTTCCCGTGCAACCAGTTTGGG
CATCAGGAGAACGCCAAGAACGAAGAGATTCTGAATTCCCTCAAGTACGTCCGGCCTGGT
GGTGGGTTCGAGCCCAACTTCATGCTCTTCGAGAAGTGCGAGGTGAACGGTGCGGGGGCG
CACCCTCTCTTCGCCTTCCTGCGGGAGGCCCTGCCAGCTCCCAGCGACGACGCCACCGCG
CTTATGACCGACCCCAAGCTCATCACCTGGTCTCCGGTGTGTCGCAACGATGTTGCCTGG
AACTTTGAGAAGTTCCTGGTGGGCCCTGACGGTGTGCCCCTACGCAGGTACAGCCGCCGC
TTCCAGACCATTGACATCGAGCCTGACATCGAAGCCCTGCTGTCTCAAGGGCCCAGCTGT
GCCTAG

1. Sukenaga Y, Ishida K, Takeda T, Takagi K: cDNA sequence coding for human glutathione peroxidase. Nucleic Acids Res. 1987 Sep 11;15(17):7178. [PubMed ]
2. Ishida K, Morino T, Takagi K, Sukenaga Y: Nucleotide sequence of a human gene for glutathione peroxidase. Nucleic Acids Res. 1987 Dec 10;15(23):10051. [PubMed ]
3. Mullenbach GT, Tabrizi A, Irvine BD, Bell GI, Hallewell RA: Sequence of a cDNA coding for human glutathione peroxidase confirms TGA encodes active site selenocysteine. Nucleic Acids Res. 1987 Jul 10;15(13):5484. [PubMed ]
4. Chada S, Le Beau MM, Casey L, Newburger PE: Isolation and chromosomal localization of the human glutathione peroxidase gene. Genomics. 1990 Feb;6(2):268-71. [PubMed ]
5. Moscow JA, Morrow CS, He R, Mullenbach GT, Cowan KH: Structure and function of the 5'-flanking sequence of the human cytosolic selenium-dependent glutathione peroxidase gene (hgpx1). J Biol Chem. 1992 Mar 25;267(9):5949-58. [PubMed ]
6. Forsberg L, de Faire U, Morgenstern R: Low yield of polymorphisms from EST blast searching: analysis of genes related to oxidative stress and verification of the P197L polymorphism in GPX1. Hum Mutat. 1999;13(4):294-300. [PubMed ]
7. Kote-Jarai Z, Durocher F, Edwards SM, Hamoudi R, Jackson RA, Ardern-Jones A, Murkin A, Dearnaley DP, Kirby R, Houlston R, Easton DF, Eeles R: Association between the GCG polymorphism of the selenium dependent GPX1 gene and the risk of young onset prostate cancer. Prostate Cancer Prostatic Dis. 2002;5(3):189-92. [PubMed ]

1. PHGPx
2. GPX-4

MSLGRLCRLLKPALLCGALAAPGLAGTMCASRDDWRCARSMHEFSAKDIDGHMVNLDKYR
GFVCIVTNVASQCGKTEVNYTQLVDLHARYAECGLRILAFPCNQFGKQEPGSNEEIKEFA
AGYNVKFDMFSKICVNGDDAHPLWKWMKIQPKGKGILGNAIKWNFTKFLIDKNGCVVKRY
GPMEEPLVIEKDLPHYF

• Glutathione Metabolism (map00480 )

• 2 glutathione + a lipid hydroperoxide = glutathione disulfide + lipid + 2 H2O

• GSHPx (PF00255 )

• 1-25

ATGAGCCTCGGCCGCCTTTGCCGCCTACTGAAGCCGGCGCTGCTCTGTGGGGCTCTGGCC
GCGCCTGGCCTGGCCGGGACCATGTGCGCGTCCCGGGACGACTGGCGCTGTGCGCGCTCC
ATGCACGAGTTTTCCGCCAAGGACATCGACGGGCACATGGTTAACCTGGACAAGTACCGG
GGCTTCGTGTGCATCGTCACCAACGTGGCCTCCCAGTGAGGCAAGACCGAAGTAAACTAC
ACTCAGCTCGTCGACCTGCACGCCCGATACGCTGAGTGTGGTTTGCGGATCCTGGCCTTC
CCGTGTAACCAGTTCGGGAAGCAGGAGCCAGGGAGTAACGAAGAGATCAAAGAGTTCGCC
GCGGGCTACAACGTCAAATTCGATATGTTCAGCAAGATCTGCGTGAACGGGGACGACGCC
CACCCGCTGTGGAAGTGGATGAAGATCCAACCCAAGGGCAAGGGCATCCTGGGAAATGCC
ATCAAGTGGAACTTCACCAAGTTCCTCATCGACAAGAACGGCTGCGTGGTGAAGCGCTAC
GGACCCATGGAGGAGCCCCTGGTGATAGAGAAGGACCTGCCCCACTATTTCTAG

1. Esworthy RS, Doan K, Doroshow JH, Chu FF: Cloning and sequencing of the cDNA encoding a human testis phospholipid hydroperoxide glutathione peroxidase. Gene. 1994 Jul 8;144(2):317-8. [PubMed ]
2. Kelner MJ, Montoya MA: Structural organization of the human selenium-dependent phospholipid hydroperoxide glutathione peroxidase gene (GPX4): chromosomal localization to 19p13.3. Biochem Biophys Res Commun. 1998 Aug 10;249(1):53-5. [PubMed ]
3. Maiorino M, Bosello V, Ursini F, Foresta C, Garolla A, Scapin M, Sztajer H, Flohe L: Genetic variations of gpx-4 and male infertility in humans. Biol Reprod. 2003 Apr;68(4):1134-41. Epub 2002 Nov 27. [PubMed ]

1. GSHPx-3
2. GPx-3
3. Plasma glutathione peroxidase
4. GSHPx-P
5. Extracellular glutathione peroxidase
6. GPx-P

MARLLQASCLLSLLLAGFVSQSRGQEKSKMDCHGGISGTIYEYGALTIDGEEYIPFKQYA
GKYVLFVNVASYCGLTGQYIELNALQEELAPFGLVILGFPCNQFGKQEPGENSEILPTLK
YVRPGGGFVPNFQLFEKGDVNGEKEQKFYTFLKNSCPPTSELLGTSDRLFWEPMKVHDIR
WNFEKFLVGPDGIPIMRWHHRTTVSNVKMDILSYMRRQAALGVKRK

• Glutathione Metabolism (map00480 )

• 2 glutathione + H2O2 = glutathione disulfide + 2 H2O

• GSHPx (PF00255 )

• 1-20

ATGGCCCGGCTGCTGCAGGCGTCCTGCCTGCTTTCCCTGCTCCTGGCCGGCTTCGTCTCG
CAGAGCCGGGGACAAGAGAAGTCGAAGATGGACTGCCATGGTGGCATAAGTGGCACCATT
TACGAGTACGGAGCCCTCACCATTGATGGGGAGGAGTACATCCCCTTCAAGCAGTATGCT
GGCAAATACGTCCTCTTTGTCAACGTGGCCAGCTACTGAGGCCTGACGGGCCAGTACATT
GAACTGAATGCACTACAGGAAGAGCTTGCACCATTCGGTCTGGTCATTCTGGGCTTTCCC
TGCAACCAATTTGGAAAACAGGAACCAGGAGAGAACTCAGAGATCCTTCCTACCCTCAAG
TATGTCCGACCAGGTGGAGGCTTTGTCCCTAATTTCCAGCTCTTTGAGAAAGGGGATGTC
AATGGAGAGAAAGAGCAGAAATTCTACACTTTCCTAAAGAACTCCTGTCCTCCCACCTCG
GAGCTCCTGGGTACATCTGACCGCCTCTTCTGGGAACCCATGAAGGTTCACGACATCCGC
TGGAACTTTGAGAAGTTCCTGGTGGGGCCAGATGGTATACCCATCATGCGCTGGCACCAC
CGGACCACGGTCAGCAACGTCAAGATGGACATCCTGTCCTACATGAGGCGGCAGGCAGCC
CTGGGGGTCAAGAGGAAGTAA

1. Takahashi K, Akasaka M, Yamamoto Y, Kobayashi C, Mizoguchi J, Koyama J: Primary structure of human plasma glutathione peroxidase deduced from cDNA sequences. J Biochem (Tokyo). 1990 Aug;108(2):145-8. [PubMed ]
2. Chu FF, Esworthy RS, Doroshow JH, Doan K, Liu XF: Expression of plasma glutathione peroxidase in human liver in addition to kidney, heart, lung, and breast in humans and rodents. Blood. 1992 Jun 15;79(12):3233-8. [PubMed ]
3. Yoshimura S, Suemizu H, Taniguchi Y, Arimori K, Kawabe N, Moriuchi T: The human plasma glutathione peroxidase-encoding gene: organization, sequence and localization to chromosome 5q32. Gene. 1994 Aug 5;145(2):293-7. [PubMed ]
4. Comhair SA, Thomassen MJ, Erzurum SC: Differential induction of extracellular glutathione peroxidase and nitric oxide synthase 2 in airways of healthy individuals exposed to 100% O(2) or cigarette smoke. Am J Respir Cell Mol Biol. 2000 Sep;23(3):350-4. [PubMed ]
5. Esworthy RS, Chu FF, Paxton RJ, Akman S, Doroshow JH: Characterization and partial amino acid sequence of human plasma glutathione peroxidase. Arch Biochem Biophys. 1991 May 1;286(2):330-6. [PubMed ]

1. GSHPx-2
2. GPx-2
3. Glutathione peroxidase-gastrointestinal
4. GSHPx-GI
5. Glutathione peroxidase- related protein 2
6. Gastrointestinal glutathione peroxidase
7. GPRP

MAFIAKSFYDLSAISLDGEKVDFNTFRGRAVLIENVASLCGTTTRDFTQLNELQCRFPRR
LVVLGFPCNQFGHQENCQNEEILNSLKYVRPGGGYQPTFTLVQKCEVNGQNEHPVFAYLK
DKLPYPYDDPFSLMTDPKLIIWSPVRRSDVAWNFEKFLIGPEGEPFRRYSRTFPTINIEP
DIKRLLKVAI

• Glutathione Metabolism (map00480 )

• 2 glutathione + H2O2 = glutathione disulfide + 2 H2O

• GSHPx (PF00255 )

• None

• None

ATGGCTTTCATTGCCAAGTCCTTCTATGACCTCAGTGCCATCAGCCTGGATGGGGAGAAG
GTAGATTTCAATACGTTCCGGGGCAGGGCCGTGCTGATTGAGAATGTGCGTTCGCTCTGA
GGCACAACCACCCGGGACTTCACCCAGCTCAACGAGCTGCAATGCCGCTTTCCCAGGCGC
CTGGTGGTCCTTGGCTTCCCTTGCAACCAATTTGGACATCAGGAGAACAGTCAGAATGAG
GAGATCCTGAACAGTCTCAAGTATGTCCGTCCTGGGGGTGGATACCAGCCCACCTTCACC
CTTGTCCAAAAATGTGAGGTGAATGGGCAGAACGAGCATCCTGTCTTCGCCTACCTGAAG
GACAAGCTCCCCTACCCTTATGATGACCCATTTTCCCTCATGACCGATCCCAAGCTCATC
ATTTGGAGCCCTGTGCGCCGCTCAGATGTGGCCTGGAACTTTGAGAAGTTCCTCATAGGG
CCGGAGGGAGAGCCCTTCCGACGCTACAGCCGCACCTTCCCAACCATCAACATTGAGCCT
GACATCAAGCGCCTCCTTAAAGTTGCCATATAG

1. Akasaka M, Mizoguchi J, Takahashi K: A human cDNA sequence of a novel glutathione peroxidase-related protein. Nucleic Acids Res. 1990 Aug 11;18(15):4619. [PubMed ]
2. Chu FF, Doroshow JH, Esworthy RS: Expression, characterization, and tissue distribution of a new cellular selenium-dependent glutathione peroxidase, GSHPx-GI. J Biol Chem. 1993 Feb 5;268(4):2571-6. [PubMed ]
3. Kelner MJ, Bagnell RD, Montoya MA, Lanham KA: Structural organization of the human gastrointestinal glutathione peroxidase (GPX2) promoter and 3'-nontranscribed region: transcriptional response to exogenous redox agents. Gene. 2000 May 2;248(1-2):109-16. [PubMed ]

1. Thioredoxin-like protein p19
2. Endoplasmic reticulum protein ERp19
3. ERp18
4. hTLP19

METRPRLGATCLLGFSFLLLVISSDGHNGLGKGFGDHIHWRTLEDGKKEAAASGLPLMVI
IHKSWCGACKALKPKFAESTEISELSHNFVMVNLEDEEEPKDEDFSPDGGYIPRILFLDP
SGKVHPEIINENGNPSYKYFYVSAEQVVQGMKEAQERLTGDAFRKKHLEDEL

• Glutathione Metabolism (map00480 )

• 2 glutathione + protein-disulfide = glutathione disulfide + protein-dithiol [RN:R03915] ALL_REAC R03915
• (other) R02824

• 1-26

• None

1. Liu F, Rong YP, Zeng LC, Zhang X, Han ZG: Isolation and characterization of a novel human thioredoxin-like gene hTLP19 encoding a secretory protein. Gene. 2003 Oct 2;315:71-8. [PubMed ]
2. Clark HF, Gurney AL, Abaya E, Baker K, Baldwin D, Brush J, Chen J, Chow B, Chui C, Crowley C, Currell B, Deuel B, Dowd P, Eaton D, Foster J, Grimaldi C, Gu Q, Hass PE, Heldens S, Huang A, Kim HS, Klimowski L, Jin Y, Johnson S, Lee J, Lewis L, Liao D, Mark M, Robbie E, Sanchez C, Schoenfeld J, Seshagiri S, Simmons L, Singh J, Smith V, Stinson J, Vagts A, Vandlen R, Watanabe C, Wieand D, Woods K, Xie MH, Yansura D, Yi S, Yu G, Yuan J, Zhang M, Zhang Z, Goddard A, Wood WI, Godowski P, Gray A: The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. Genome Res. 2003 Oct;13(10):2265-70. Epub 2003 Sep 15. [PubMed ]

METRPRLGATCLLGFSFLLLVISSDGHNGLGKGFGDHIHWRTLEDGKKEAAASGLPLMVI
IHKSWCGACKALKPKFAESTEISELSHNFVMVNLEDEEEPKDEDFSPDGGYIPRILFLDP
SGKVHPEIINENGNPSYKYFYVSAEQVVQGMKEAQERLTGDAFRKKHLEDEL

• None

• None