ID TYR1_HUMAN STANDARD; PRT; 537 AA. AC P17643; Q15679; P78469; P78468; Q13721; DT 01-AUG-1990 (Rel. 15, Created) DT 01-OCT-2000 (Rel. 40, Last sequence update) DT 01-OCT-2000 (Rel. 40, Last annotation update) DE 5,6-DIHYDROXYINDOLE-2-CARBOXYLIC ACID OXIDASE PRECURSOR (EC 1.14.18.-) DE (DHICA OXIDASE) (TYROSINASE-RELATED PROTEIN 1) (TRP-1) (TRP1) (TRP) DE (CATALASE B) (GLYCOPROTEIN-75) (MELANOMA ANTIGEN GP75). GN TYRP1 OR TYRP OR CAS2 OR TYRRP. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Melanoma; RX MEDLINE=90251459; PubMed=2111010; RA Cohen T., Muller R.M., Tomita Y., Shibahara S.; RT "Nucleotide sequence of the cDNA encoding human tyrosinase-related RT protein."; RL Nucleic Acids Res. 18:2807-2807(1990). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=91298952; PubMed=1906272; RA Chintamaneni C.D., Ramsay M., Colman M.-A., Fox M.F., Pickard R.T., RA Kwon B.S.; RT "Mapping the human CAS2 gene, the homologue of the mouse brown (b) RT locus, to human chromosome 9p22-pter."; RL Biochem. Biophys. Res. Commun. 178:227-235(1991). RN [3] RP SEQUENCE FROM N.A. RX MEDLINE=98096585; PubMed=9434945; RA Box N.F., Wyeth J.R., Mayne C.J., O'Gorman L.E., Martin N.G., RA Sturm R.A.; RT "Complete sequence and polymorphism study of the human TYRP1 gene RT encoding tyrosinase-related protein 1."; RL Mamm. Genome 9:50-53(1998). RN [4] RP SEQUENCE OF 1-128 FROM N.A. RC TISSUE=Liver; RX MEDLINE=96079088; PubMed=8530077; RA Sturm R.A., O'Sullivan B.J., Box N.F., Smith A.G., Smit S.E., RA Puttick E.R.J., Parsons P.G., Dunn I.S.; RT "Chromosomal structure of the human TYRP1 and TYRP2 loci and RT comparison of the tyrosinase-related protein gene family."; RL Genomics 29:24-34(1995). RN [5] RP SEQUENCE OF 1-17 FROM N.A. RX MEDLINE=92246935; PubMed=1575733; RA Shibata K., Takeda K., Tomita Y., Tagami H., Shibahara S.; RT "Downstream region of the human tyrosinase-related protein gene RT enhances its promoter activity."; RL Biochem. Biophys. Res. Commun. 184:568-575(1992). RN [6] RP SEQUENCE OF 218-465 FROM N.A., AND PARTIAL SEQUENCE. RC TISSUE=Melanoma; RX MEDLINE=90217958; PubMed=2324688; RA Vijayasaradhi S., Bouchard B., Houghton A.N.; RT "The melanoma antigen gp75 is the human homologue of the mouse b RT (brown) locus gene product."; RL J. Exp. Med. 171:1375-1380(1990). RN [7] RP SEQUENCE OF 481-537 FROM N.A. RC TISSUE=Blood, and Root hairs; RX MEDLINE=92051358; PubMed=1945866; RA Urquhart A.J.; RT "Human tyrosinase-like protein (TYRL) carboxy terminus: closer RT homology with the mouse protein than previously reported."; RL Nucleic Acids Res. 19:5803-5803(1991). RN [8] RP POSSIBLE FUNCTION. RX MEDLINE=90280465; PubMed=1693779; RA Halaban R., Moellmann G.; RT "Murine and human b locus pigmentation genes encode a glycoprotein RT (gp75) with catalase activity."; RL Proc. Natl. Acad. Sci. U.S.A. 87:4809-4813(1990). CC -!- FUNCTION: OXIDATION OF 5,6-DIHYDROXYINDOLE-2-CARBOXYLIC ACID CC (DHICA) INTO INDOLE-5,6-QUINONE-2-CARBOXYLIC ACID. MAY REGULATE OR CC INFLUENCE THE TYPE OF MELANIN SYNTHESIZED. CC -!- COFACTOR: BINDS TWO COPPER IONS (BY SIMILARITY). CC -!- PATHWAY: MELANIN BIOSYNTHESIS. CC -!- SUBCELLULAR LOCATION: TYPE I MEMBRANE PROTEIN. MELANOSOMAL CC (POTENTIAL). CC -!- TISSUE SPECIFICITY: PIGMENT CELLS. CC -!- DISEASE: DEFECTS IN TYRP1 ARE LINKED WITH ALBINISM TYPE III (OCA- CC III OR OCA3 OR BROWN ALIBINISM), A FORM OF ALBINISM WITH ONLY CC MODERATE REDUCTION OF PIGMENT. INDIVIDUALS WITH OCA-III ARE CC RECOGNIZED BY THEIR REDDISH SKIN AND HAIR COLOR. CC -!- SIMILARITY: BELONGS TO THE TYROSINASE FAMILY. CC -!- DATABASE: NAME=Albinism database (ADB); CC NOTE=OCA-III mutations; CC WWW="http://www.cbc.umn.edu/tad/". CC -!- DATABASE: NAME=Mutations of the TYRP1 gene; CC NOTE=Retina International's Scientific Newsletter; CC WWW="http://www.irpa.org/sci-news/trp1mut.htm". CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X51420; CAA35785.1; -. DR EMBL; AF001295; AAC15468.1; -. DR EMBL; L38952; AAC41924.1; -. DR EMBL; D83059; BAA11759.1; -. DR EMBL; X51455; CAA35820.1; -. DR EMBL; X60955; CAA43288.1; -. DR PIR; S09999; S09999. DR MIM; 115501; -. DR MIM; 203290; -. DR MIM; 278400; -. DR InterPro; IPR002227; Tyrosinase. DR Pfam; PF00264; tyrosinase; 1. DR PRINTS; PR00092; TYROSINASE. DR PROSITE; PS00497; TYROSINASE_1; 1. DR PROSITE; PS00498; TYROSINASE_2; 1. KW Oxidoreductase; Monooxygenase; Copper; Glycoprotein; Signal; KW Transmembrane; Melanin biosynthesis; Albinism; Antigen. FT SIGNAL 1 24 FT CHAIN 25 537 5,6-DIHYDROXYINDOLE-2-CARBOXYLIC ACID FT OXIDASE. FT DOMAIN 25 477 LUMENAL, MELANOSOME (POTENTIAL). FT TRANSMEM 478 501 POTENTIAL. FT DOMAIN 502 537 CYTOPLASMIC (POTENTIAL). FT METAL 192 192 COPPER A (BY SIMILARITY). FT METAL 215 215 COPPER A (BY SIMILARITY). FT METAL 224 224 COPPER A (BY SIMILARITY). FT METAL 377 377 COPPER B (BY SIMILARITY). FT METAL 381 381 COPPER B (BY SIMILARITY). FT METAL 404 404 COPPER B (BY SIMILARITY). FT CARBOHYD 96 96 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 104 104 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 181 181 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 304 304 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 350 350 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 385 385 N-LINKED (GLCNAC...) (POTENTIAL). FT CONFLICT 526 537 YEKLQNPNQSVV -> RI (IN REF. 1 AND 2). FT CONFLICT 395 396 PN -> SQ (IN REF. 6). SQ SEQUENCE 537 AA; 60724 MW; 1051CEEF52908CCA CRC64; MSAPKLLSLG CIFFPLLLFQ QARAQFPRQC ATVEALRSGM CCPDLSPVSG PGTDRCGSSS GRGRCEAVTA DSRPHSPQYP HDGRDDREVW PLRFFNRTCH CNGNFSGHNC GTCRPGWRGA ACDQRVLIVR RNLLDLSKEE KNHFVRALDM AKRTTHPLFV IATRRSEEIL GPDGNTPQFE NISIYNYFVW THYYSVKKTF LGVGQESFGE VDFSHEGPAF LTWHRYHLLR LEKDMQEMLQ EPSFSLPYWN FATGKNVCDI CTDDLMGSRS NFDSTLISPN SVFSQWRVVC DSLEDYDTLG TLCNSTEDGP IRRNPAGNVA RPMVQRLPEP QDVAQCLEVG LFDTPPFYSN STNSFRNTVE GYSDPTGKYD PAVRSLHNLA HLFLNGTGGQ THLSPNDPIF VLLHTFTDAV FDEWLRRYNA DISTFPLENA PIGHNRQYNM VPFWPPVTNT EMFVTAPDNL GYTYEIQWPS REFSVPEIIA IAVVGALLLV ALIFGTASYL IRARRSMDEA NQPLLTDQYQ CYAEEYEKLQ NPNQSVV //