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5,6-dihydroxyindole-2-carboxylic acid oxidase (DHICA oxidase) (EC 1.14.18.-) (Brown locus protein) (Catalase B) (Tyrosinase-related protein 1) (TRP) (TRP-1) (TRP1)

 TYRP1_MOUSE             Reviewed;         537 AA.
P07147;
01-APR-1988, integrated into UniProtKB/Swiss-Prot.
01-APR-1988, sequence version 1.
12-SEP-2018, entry version 163.
RecName: Full=5,6-dihydroxyindole-2-carboxylic acid oxidase;
Short=DHICA oxidase;
EC=1.14.18.-;
AltName: Full=Brown locus protein;
AltName: Full=Catalase B;
AltName: Full=Tyrosinase-related protein 1;
Short=TRP;
Short=TRP-1;
Short=TRP1;
Flags: Precursor;
Name=Tyrp1; Synonyms=Tyrp-1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Melanoma;
PubMed=3008090; DOI=10.1093/nar/14.6.2413;
Shibahara S., Tomita Y., Sakakura T., Nager C., Chaudhuri B.,
Mueller R.;
"Cloning and expression of cDNA encoding mouse tyrosinase.";
Nucleic Acids Res. 14:2413-2427(1986).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Eye;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
IDENTIFICATION OF PROTEIN.
PubMed=3132713; DOI=10.1073/pnas.85.12.4392;
Jackson I.J.;
"A cDNA encoding tyrosinase-related protein maps to the brown locus in
mouse.";
Proc. Natl. Acad. Sci. U.S.A. 85:4392-4396(1988).
[4]
POSSIBLE FUNCTION.
PubMed=1693779; DOI=10.1073/pnas.87.12.4809;
Halaban R., Moellmann G.;
"Murine and human b locus pigmentation genes encode a glycoprotein
(gp75) with catalase activity.";
Proc. Natl. Acad. Sci. U.S.A. 87:4809-4813(1990).
[5]
FUNCTION, AND GLYCOSYLATION.
PubMed=1537333;
Tsukamoto K., Jackson I.J., Urabe K., Montague P.M., Hearing V.J.;
"A second tyrosinase-related protein, TRP-2, is a melanogenic enzyme
termed DOPAchrome tautomerase.";
EMBO J. 11:519-526(1992).
[6]
POSSIBLE FUNCTION.
PubMed=8270621;
Winder A.J., Wittbjer A., Rosengren E., Rorsman H.;
"The mouse brown (b) locus protein has dopachrome tautomerase activity
and is located in lysosomes in transfected fibroblasts.";
J. Cell Sci. 106:153-166(1993).
[7]
FUNCTION.
PubMed=7813420;
Kobayashi T., Urabe K., Winder A., Jimenez-Cervantes C., Imokawa G.,
Brewington T., Solano F., Garcia-Borron J.C., Hearing V.J.;
"Tyrosinase related protein 1 (TRP1) functions as a DHICA oxidase in
melanin biosynthesis.";
EMBO J. 13:5818-5825(1994).
[8]
SUBCELLULAR LOCATION.
PubMed=17182842; DOI=10.1091/mbc.E06-12-1066;
Setty S.R., Tenza D., Truschel S.T., Chou E., Sviderskaya E.V.,
Theos A.C., Lamoreux M.L., Di Pietro S.M., Starcevic M., Bennett D.C.,
Dell'Angelica E.C., Raposo G., Marks M.S.;
"BLOC-1 is required for cargo-specific sorting from vacuolar early
endosomes toward lysosome-related organelles.";
Mol. Biol. Cell 18:768-780(2007).
[9]
SUBCELLULAR LOCATION.
PubMed=26620560; DOI=10.1074/jbc.M115.684043;
Marubashi S., Shimada H., Fukuda M., Ohbayashi N.;
"RUTBC1 functions as a GTPase-activating protein for Rab32/38 and
regulates melanogenic enzyme trafficking in melanocytes.";
J. Biol. Chem. 291:1427-1440(2016).
[10]
VARIANTS BROWN TYR-110 AND HIS-326, FUNCTION, AND PATHWAY.
PubMed=2245916;
Zdarsky E., Favor J., Jackson I.J.;
"The molecular basis of brown, an old mouse mutation, and of an
induced revertant to wild type.";
Genetics 126:443-449(1990).
-!- FUNCTION: Catalyzes the oxidation of 5,6-dihydroxyindole-2-
carboxylic acid (DHICA) into indole-5,6-quinone-2-carboxylic acid
(PubMed:7813420). May regulate or influence the type of melanin
synthesized (PubMed:7813420, PubMed:2245916). Also to a lower
extent, capable of hydroxylating tyrosine and producing melanin
(PubMed:1537333). {ECO:0000269|PubMed:1537333,
ECO:0000269|PubMed:2245916, ECO:0000269|PubMed:7813420}.
-!- COFACTOR:
Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
Evidence={ECO:0000250|UniProtKB:Q9ZP19};
Note=Binds 2 copper ions per subunit.
{ECO:0000250|UniProtKB:Q9ZP19};
-!- PATHWAY: Pigment biosynthesis; melanin biosynthesis.
{ECO:0000269|PubMed:2245916}.
-!- INTERACTION:
P11344:Tyr; NbExp=2; IntAct=EBI-821614, EBI-821603;
-!- SUBCELLULAR LOCATION: Melanosome membrane
{ECO:0000269|PubMed:17182842}; Single-pass type I membrane protein
{ECO:0000269|PubMed:17182842}. Melanosome
{ECO:0000269|PubMed:26620560}. Note=Located to mature stage III
and IV melanosomes and apposed endosomal tubular membranes.
Transported to pigmented melanosomes by the BLOC-1 complex. Proper
trafficking to melanosome is regulated by SGSM2, ANKRD27, RAB9A,
RAB32 and RAB38. {ECO:0000269|PubMed:17182842,
ECO:0000269|PubMed:26620560}.
-!- TISSUE SPECIFICITY: Pigment cells.
-!- PTM: Glycosylated. {ECO:0000269|PubMed:1537333}.
-!- DISEASE: Note=Defects in Tyrp1 are the cause of the brown (b)
phenotype. Brown mice have a brown or hypopigmented coat.
{ECO:0000269|PubMed:2245916}.
-!- SIMILARITY: Belongs to the tyrosinase family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; X03687; CAA27323.1; -; mRNA.
EMBL; BC076598; AAH76598.1; -; mRNA.
CCDS; CCDS18290.1; -.
PIR; A24933; YRMSB6.
RefSeq; NP_001268943.1; NM_001282014.1.
RefSeq; NP_001268944.1; NM_001282015.1.
RefSeq; NP_112479.1; NM_031202.3.
UniGene; Mm.30438; -.
ProteinModelPortal; P07147; -.
SMR; P07147; -.
IntAct; P07147; 1.
STRING; 10090.ENSMUSP00000006151; -.
BindingDB; P07147; -.
ChEMBL; CHEMBL3638355; -.
iPTMnet; P07147; -.
PhosphoSitePlus; P07147; -.
PaxDb; P07147; -.
PRIDE; P07147; -.
Ensembl; ENSMUST00000006151; ENSMUSP00000006151; ENSMUSG00000005994.
Ensembl; ENSMUST00000102831; ENSMUSP00000099895; ENSMUSG00000005994.
GeneID; 22178; -.
KEGG; mmu:22178; -.
UCSC; uc008tjq.3; mouse.
CTD; 7306; -.
MGI; MGI:98881; Tyrp1.
eggNOG; ENOG410IEEB; Eukaryota.
eggNOG; ENOG410XSJD; LUCA.
GeneTree; ENSGT00500000044790; -.
HOGENOM; HOG000118376; -.
HOVERGEN; HBG003553; -.
InParanoid; P07147; -.
KO; K00506; -.
OMA; TCHCNGN; -.
OrthoDB; EOG091G03YR; -.
PhylomeDB; P07147; -.
TreeFam; TF315865; -.
BioCyc; MetaCyc:MONOMER-15620; -.
Reactome; R-MMU-5662702; Melanin biosynthesis.
UniPathway; UPA00785; -.
ChiTaRS; Tyrp1; mouse.
PRO; PR:P07147; -.
Proteomes; UP000000589; Chromosome 4.
Bgee; ENSMUSG00000005994; Expressed in 73 organ(s), highest expression level in iris.
CleanEx; MM_TYRP1; -.
ExpressionAtlas; P07147; baseline and differential.
Genevisible; P07147; MM.
GO; GO:0030669; C:clathrin-coated endocytic vesicle membrane; ISO:MGI.
GO; GO:0010008; C:endosome membrane; ISO:MGI.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0042470; C:melanosome; IDA:UniProtKB.
GO; GO:0033162; C:melanosome membrane; IDA:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
GO; GO:0046982; F:protein heterodimerization activity; IDA:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
GO; GO:0043438; P:acetoacetic acid metabolic process; IMP:MGI.
GO; GO:0006583; P:melanin biosynthetic process from tyrosine; TAS:UniProtKB.
GO; GO:0006582; P:melanin metabolic process; IMP:MGI.
GO; GO:0030318; P:melanocyte differentiation; IMP:MGI.
GO; GO:0032438; P:melanosome organization; IMP:MGI.
GO; GO:0043473; P:pigmentation; IMP:MGI.
GO; GO:0048023; P:positive regulation of melanin biosynthetic process; IGI:CACAO.
Gene3D; 1.10.1280.10; -; 1.
InterPro; IPR002227; Tyrosinase_Cu-bd.
InterPro; IPR008922; Unchr_di-copper_centre.
Pfam; PF00264; Tyrosinase; 1.
PRINTS; PR00092; TYROSINASE.
SUPFAM; SSF48056; SSF48056; 2.
PROSITE; PS00497; TYROSINASE_1; 1.
PROSITE; PS00498; TYROSINASE_2; 1.
1: Evidence at protein level;
Albinism; Complete proteome; Copper; Disease mutation; Disulfide bond;
Glycoprotein; Melanin biosynthesis; Membrane; Metal-binding;
Monooxygenase; Oxidoreductase; Reference proteome; Signal;
Transmembrane; Transmembrane helix.
SIGNAL 1 24
CHAIN 25 537 5,6-dihydroxyindole-2-carboxylic acid
oxidase.
/FTId=PRO_0000035890.
TOPO_DOM 25 477 Lumenal, melanosome. {ECO:0000255}.
TRANSMEM 478 501 Helical. {ECO:0000255}.
TOPO_DOM 502 537 Cytoplasmic. {ECO:0000255}.
METAL 192 192 Copper A. {ECO:0000250|UniProtKB:Q9ZP19}.
METAL 215 215 Copper A. {ECO:0000250|UniProtKB:Q9ZP19}.
METAL 224 224 Copper A. {ECO:0000250|UniProtKB:Q9ZP19}.
METAL 377 377 Copper B. {ECO:0000250|UniProtKB:Q9ZP19}.
METAL 381 381 Copper B. {ECO:0000250|UniProtKB:Q9ZP19}.
METAL 404 404 Copper B. {ECO:0000250|UniProtKB:Q9ZP19}.
CARBOHYD 96 96 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 104 104 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 181 181 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 304 304 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 350 350 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 385 385 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 30 41 {ECO:0000250|UniProtKB:P17643}.
DISULFID 42 65 {ECO:0000250|UniProtKB:P17643}.
DISULFID 56 99 {ECO:0000250|UniProtKB:P17643}.
DISULFID 101 110 {ECO:0000250|UniProtKB:P17643}.
DISULFID 113 122 {ECO:0000250|UniProtKB:P17643}.
DISULFID 258 261 {ECO:0000250|UniProtKB:P17643}.
DISULFID 290 303 {ECO:0000250|UniProtKB:P17643}.
VARIANT 110 110 C -> Y (in brown).
{ECO:0000269|PubMed:2245916}.
VARIANT 326 326 R -> H (in brown).
{ECO:0000269|PubMed:2245916}.
SEQUENCE 537 AA; 60761 MW; 86570998AA9EB0BC CRC64;
MKSYNVLPLA YISLFLMLFY QVWAQFPREC ANIEALRRGV CCPDLLPSSG PGTDPCGSSS
GRGRCVAVIA DSRPHSRHYP HDGKDDREAW PLRFFNRTCQ CNDNFSGHNC GTCRPGWRGA
ACNQKILTVR RNLLDLSPEE KSHFVRALDM AKRTTHPQFV IATRRLEDIL GPDGNTPQFE
NISVYNYFVW THYYSVKKTF LGTGQESFGD VDFSHEGPAF LTWHRYHLLQ LERDMQEMLQ
EPSFSLPYWN FATGKNVCDV CTDDLMGSRS NFDSTLISPN SVFSQWRVVC ESLEEYDTLG
TLCNSTEGGP IRRNPAGNVG RPAVQRLPEP QDVTQCLEVR VFDTPPFYSN STDSFRNTVE
GYSAPTGKYD PAVRSLHNLA HLFLNGTGGQ THLSPNDPIF VLLHTFTDAV FDEWLRRYNA
DISTFPLENA PIGHNRQYNM VPFWPPVTNT EMFVTAPDNL GYAYEVQWPG QEFTVSEIIT
IAVVAALLLV AAIFGVASCL IRSRSTKNEA NQPLLTDHYQ RYAEDYEELP NPNHSMV


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