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5,6-dihydroxyindole-2-carboxylic acid oxidase (DHICA oxidase) (EC 1.14.18.-) (Catalase B) (Glycoprotein 75) (Melanoma antigen gp75) (Tyrosinase-related protein 1) (TRP) (TRP-1) (TRP1)

 TYRP1_HUMAN             Reviewed;         537 AA.
P17643; P78468; P78469; Q13721; Q15679;
01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
11-JAN-2001, sequence version 2.
12-SEP-2018, entry version 183.
RecName: Full=5,6-dihydroxyindole-2-carboxylic acid oxidase;
Short=DHICA oxidase;
EC=1.14.18.- {ECO:0000269|PubMed:28661582};
AltName: Full=Catalase B;
AltName: Full=Glycoprotein 75 {ECO:0000303|PubMed:1693779};
AltName: Full=Melanoma antigen gp75 {ECO:0000303|PubMed:2324688};
AltName: Full=Tyrosinase-related protein 1 {ECO:0000303|PubMed:9434945};
Short=TRP {ECO:0000303|PubMed:2111010};
Short=TRP-1;
Short=TRP1;
Flags: Precursor;
Name=TYRP1; Synonyms=CAS2 {ECO:0000303|PubMed:1906272}, TYRP, TYRRP;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Melanoma;
PubMed=2111010; DOI=10.1093/nar/18.9.2807;
Cohen T., Muller R.M., Tomita Y., Shibahara S.;
"Nucleotide sequence of the cDNA encoding human tyrosinase-related
protein.";
Nucleic Acids Res. 18:2807-2807(1990).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1906272; DOI=10.1016/0006-291X(91)91803-K;
Chintamaneni C.D., Ramsay M., Colman M.-A., Fox M.F., Pickard R.T.,
Kwon B.S.;
"Mapping the human CAS2 gene, the homologue of the mouse brown (b)
locus, to human chromosome 9p22-pter.";
Biochem. Biophys. Res. Commun. 178:227-235(1991).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=9434945; DOI=10.1007/s003359900678;
Box N.F., Wyeth J.R., Mayne C.J., O'Gorman L.E., Martin N.G.,
Sturm R.A.;
"Complete sequence and polymorphism study of the human TYRP1 gene
encoding tyrosinase-related protein 1.";
Mamm. Genome 9:50-53(1998).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Skin;
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).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-128.
TISSUE=Liver;
PubMed=8530077; DOI=10.1006/geno.1995.1211;
Sturm R.A., O'Sullivan B.J., Box N.F., Smith A.G., Smit S.E.,
Puttick E.R.J., Parsons P.G., Dunn I.S.;
"Chromosomal structure of the human TYRP1 and TYRP2 loci and
comparison of the tyrosinase-related protein gene family.";
Genomics 29:24-34(1995).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-17.
PubMed=1575733; DOI=10.1016/0006-291X(92)90627-W;
Shibata K., Takeda K., Tomita Y., Tagami H., Shibahara S.;
"Downstream region of the human tyrosinase-related protein gene
enhances its promoter activity.";
Biochem. Biophys. Res. Commun. 184:568-575(1992).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 218-465, AND PARTIAL PROTEIN SEQUENCE.
TISSUE=Melanoma;
PubMed=2324688; DOI=10.1084/jem.171.4.1375;
Vijayasaradhi S., Bouchard B., Houghton A.N.;
"The melanoma antigen gp75 is the human homologue of the mouse b
(brown) locus gene product.";
J. Exp. Med. 171:1375-1380(1990).
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 481-537.
TISSUE=Blood, and Hair root;
PubMed=1945866; DOI=10.1093/nar/19.20.5803;
Urquhart A.J.;
"Human tyrosinase-like protein (TYRL) carboxy terminus: closer
homology with the mouse protein than previously reported.";
Nucleic Acids Res. 19:5803-5803(1991).
[9]
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).
[10]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
TISSUE=Melanoma;
PubMed=12643545; DOI=10.1021/pr025562r;
Basrur V., Yang F., Kushimoto T., Higashimoto Y., Yasumoto K.,
Valencia J., Muller J., Vieira W.D., Watabe H., Shabanowitz J.,
Hearing V.J., Hunt D.F., Appella E.;
"Proteomic analysis of early melanosomes: identification of novel
melanosomal proteins.";
J. Proteome Res. 2:69-79(2003).
[11]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
TISSUE=Melanoma;
PubMed=17081065; DOI=10.1021/pr060363j;
Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H.,
Mangini N.J., Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R.,
Yamagishi S., Shabanowitz J., Hearing V.J., Wu C., Appella E.,
Hunt D.F.;
"Proteomic and bioinformatic characterization of the biogenesis and
function of melanosomes.";
J. Proteome Res. 5:3135-3144(2006).
[12] {ECO:0000244|PDB:5M8L, ECO:0000244|PDB:5M8M, ECO:0000244|PDB:5M8N, ECO:0000244|PDB:5M8O, ECO:0000244|PDB:5M8P, ECO:0000244|PDB:5M8Q, ECO:0000244|PDB:5M8R, ECO:0000244|PDB:5M8T}
X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 25-470 IN COMPLEX WITH ZINC
IONS AND SYNTHETIC INHIBITORS, FUNCTION, COFACTOR, CATALYTIC ACTIVITY,
ACTIVITY REGULATION, GLYCOSYLATION AT ASN-96; ASN-104; ASN-181;
ASN-304; ASN-350 AND ASN-385, DISULFIDE BONDS, AND MUTAGENESIS OF
TYR-362; ARG-374 AND THR-391.
PubMed=28661582; DOI=10.1002/anie.201704616;
Lai X., Wichers H.J., Soler-Lopez M., Dijkstra B.W.;
"Structure of Human Tyrosinase Related Protein1 Reveals a Binuclear
Zinc Active Site Important for Melanogenesis.";
Angew. Chem. Int. Ed. Engl. 56:9812-9815(2017).
[13]
INVOLVEMENT IN SHEP11, VARIANT CYS-93, ASSOCIATION OF VARIANT CYS-93
WITH BLOND HAIR, FUNCTION, AND PATHWAY.
PubMed=22556244; DOI=10.1126/science.1217849;
Kenny E.E., Timpson N.J., Sikora M., Yee M.C., Moreno-Estrada A.,
Eng C., Huntsman S., Burchard E.G., Stoneking M., Bustamante C.D.,
Myles S.;
"Melanesian blond hair is caused by an amino acid change in TYRP1.";
Science 336:554-554(2012).
[14]
VARIANT OCA3 GLN-356, PATHWAY, AND FUNCTION.
PubMed=16704458; DOI=10.1111/j.1600-0749.2006.00298.x;
Rooryck C., Roudaut C., Robine E., Muesebeck J., Arveiler B.;
"Oculocutaneous albinism with TYRP1 gene mutations in a Caucasian
patient.";
Pigment Cell Res. 19:239-242(2006).
[15]
VARIANT OCA3 THR-24, PATHWAY, AND FUNCTION.
PubMed=23504663; DOI=10.1002/humu.22315;
Simeonov D.R., Wang X., Wang C., Sergeev Y., Dolinska M., Bower M.,
Fischer R., Winer D., Dubrovsky G., Balog J.Z., Huizing M., Hart R.,
Zein W.M., Gahl W.A., Brooks B.P., Adams D.R.;
"DNA variations in oculocutaneous albinism: an updated mutation list
and current outstanding issues in molecular diagnostics.";
Hum. Mutat. 34:827-835(2013).
-!- FUNCTION: Catalyzes the oxidation of 5,6-dihydroxyindole-2-
carboxylic acid (DHICA) into indole-5,6-quinone-2-carboxylic acid
in the presence of bound Cu(2+) ions (PubMed:28661582). May
regulate or influence the type of melanin synthesized
(PubMed:22556244, PubMed:16704458). Also to a lower extent,
capable of hydroxylating tyrosine and producing melanin (By
similarity). {ECO:0000250|UniProtKB:P07147,
ECO:0000269|PubMed:28661582, ECO:0000305|PubMed:16704458,
ECO:0000305|PubMed:22556244, ECO:0000305|PubMed:23504663}.
-!- COFACTOR:
Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
Evidence={ECO:0000269|PubMed:28661582};
Note=Binds 2 copper ions per subunit (By similarity). Contains
bound zinc ions after heterologous expression in insect cells,
giving rise to a protein that lacks DHICA oxidase activity
(PubMed:28661582). {ECO:0000250|UniProtKB:Q9ZP19,
ECO:0000269|PubMed:28661582};
-!- ACTIVITY REGULATION: The activity depends critically on the nature
of the bound metal ion. Catalyzes the oxidation of 5,6-
dihydroxyindole-2-carboxylic acid (DHICA) in the presence of bound
Cu(2+) ions, but lacks activity in the presence of bound Zn(2+)
ions. {ECO:0000269|PubMed:28661582}.
-!- PATHWAY: Pigment biosynthesis; melanin biosynthesis.
{ECO:0000269|PubMed:16704458, ECO:0000269|PubMed:22556244,
ECO:0000269|PubMed:23504663}.
-!- SUBUNIT: Monomer. {ECO:0000269|PubMed:28661582}.
-!- INTERACTION:
O14908:GIPC1; NbExp=3; IntAct=EBI-7900408, EBI-373132;
-!- SUBCELLULAR LOCATION: Melanosome membrane
{ECO:0000250|UniProtKB:P07147}; Single-pass type I membrane
protein {ECO:0000250|UniProtKB:P07147}. Melanosome
{ECO:0000250|UniProtKB:P07147}. 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:0000250|UniProtKB:P07147}.
-!- TISSUE SPECIFICITY: Pigment cells.
-!- PTM: Glycosylated. {ECO:0000250|UniProtKB:P07147}.
-!- POLYMORPHISM: Genetic variants in TYRP1 define the skin/hair/eye
pigmentation variation locus 11 (SHEP11) [MIM:612271] and are
responsible for variability in hair color linked to chromosome
9p23 in Melanesians. Hair, eye and skin pigmentation are among the
most visible examples of human phenotypic variation, with a broad
normal range that is subject to substantial geographic
stratification. {ECO:0000269|PubMed:22556244}.
-!- DISEASE: Albinism, oculocutaneous, 3 (OCA3) [MIM:203290]: An
autosomal recessive disorder in which the biosynthesis of melanin
pigment is reduced in skin, hair, and eyes. Tyrosinase activity is
normal and patients have only moderate reduction of pigment. The
eyes present red reflex on transillumination of the iris, dilution
of color of iris, nystagmus and strabismus. Darker-skinned
individuals have bright copper-red coloration of the skin and
hair. {ECO:0000269|PubMed:16704458, ECO:0000269|PubMed:23504663}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- SIMILARITY: Belongs to the tyrosinase family. {ECO:0000305}.
-!- CAUTION: The precise function of this protein in melanin
biosynthesis is still under debate. {ECO:0000305|PubMed:28661582}.
-!- WEB RESOURCE: Name=Mutations of the TYRP1 gene; Note=Retina
International's Scientific Newsletter;
URL="http://www.retina-international.org/files/sci-news/trp1mut.htm";
-!- WEB RESOURCE: Name=Albinism database (ADB); Note=TYRP1 mutations;
URL="http://www.ifpcs.org/albinism/oca3mut.html";
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EMBL; X51420; CAA35785.1; -; mRNA.
EMBL; AF001295; AAC15468.1; -; Genomic_DNA.
EMBL; L38952; AAC41924.1; -; Genomic_DNA.
EMBL; D83059; BAA11759.1; -; Genomic_DNA.
EMBL; BC052608; AAH52608.1; -; mRNA.
EMBL; X51455; CAA35820.1; -; mRNA.
EMBL; X60955; CAA43288.1; -; Genomic_DNA.
CCDS; CCDS34990.1; -.
PIR; S09999; YRHUB6.
RefSeq; NP_000541.1; NM_000550.2.
UniGene; Hs.270279; -.
PDB; 5M8L; X-ray; 2.35 A; A/B/C/D=25-470.
PDB; 5M8M; X-ray; 2.65 A; A/B/C/D=25-470.
PDB; 5M8N; X-ray; 2.60 A; A/B/C/D=25-470.
PDB; 5M8O; X-ray; 2.50 A; A/B/C/D=25-470.
PDB; 5M8P; X-ray; 2.80 A; A/B/C/D=25-470.
PDB; 5M8Q; X-ray; 2.85 A; A/B/C/D=25-470.
PDB; 5M8R; X-ray; 2.40 A; A/B/C/D=25-470.
PDB; 5M8S; X-ray; 2.20 A; A/B/C/D=25-470.
PDB; 5M8T; X-ray; 2.35 A; A/B/C/D=25-470.
PDBsum; 5M8L; -.
PDBsum; 5M8M; -.
PDBsum; 5M8N; -.
PDBsum; 5M8O; -.
PDBsum; 5M8P; -.
PDBsum; 5M8Q; -.
PDBsum; 5M8R; -.
PDBsum; 5M8S; -.
PDBsum; 5M8T; -.
ProteinModelPortal; P17643; -.
SMR; P17643; -.
BioGrid; 113156; 7.
IntAct; P17643; 2.
MINT; P17643; -.
STRING; 9606.ENSP00000373570; -.
ChEMBL; CHEMBL3712886; -.
iPTMnet; P17643; -.
PhosphoSitePlus; P17643; -.
BioMuta; TYRP1; -.
DMDM; 12644141; -.
PaxDb; P17643; -.
PeptideAtlas; P17643; -.
PRIDE; P17643; -.
ProteomicsDB; 53498; -.
Ensembl; ENST00000388918; ENSP00000373570; ENSG00000107165.
GeneID; 7306; -.
KEGG; hsa:7306; -.
UCSC; uc003zkv.5; human.
CTD; 7306; -.
DisGeNET; 7306; -.
EuPathDB; HostDB:ENSG00000107165.12; -.
GeneCards; TYRP1; -.
HGNC; HGNC:12450; TYRP1.
HPA; CAB002520; -.
HPA; HPA000937; -.
MalaCards; TYRP1; -.
MIM; 115501; gene.
MIM; 203290; phenotype.
MIM; 612271; phenotype.
neXtProt; NX_P17643; -.
OpenTargets; ENSG00000107165; -.
Orphanet; 79433; Oculocutaneous albinism type 3.
PharmGKB; PA37101; -.
eggNOG; ENOG410IEEB; Eukaryota.
eggNOG; ENOG410XSJD; LUCA.
GeneTree; ENSGT00500000044790; -.
HOGENOM; HOG000118376; -.
HOVERGEN; HBG003553; -.
InParanoid; P17643; -.
KO; K00506; -.
OMA; TCHCNGN; -.
OrthoDB; EOG091G03YR; -.
PhylomeDB; P17643; -.
TreeFam; TF315865; -.
Reactome; R-HSA-5662702; Melanin biosynthesis.
SIGNOR; P17643; -.
UniPathway; UPA00785; -.
GeneWiki; TYRP1; -.
GenomeRNAi; 7306; -.
PRO; PR:P17643; -.
Proteomes; UP000005640; Chromosome 9.
Bgee; ENSG00000107165; Expressed in 144 organ(s), highest expression level in pigmented layer of retina.
CleanEx; HS_TYRP1; -.
ExpressionAtlas; P17643; baseline and differential.
Genevisible; P17643; HS.
GO; GO:0030669; C:clathrin-coated endocytic vesicle membrane; IDA:UniProtKB.
GO; GO:0010008; C:endosome membrane; IDA:UniProtKB.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0042470; C:melanosome; ISS:UniProtKB.
GO; GO:0033162; C:melanosome membrane; ISS:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
GO; GO:0016491; F:oxidoreductase activity; TAS:Reactome.
GO; GO:0046982; F:protein heterodimerization activity; ISS:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
GO; GO:0043438; P:acetoacetic acid metabolic process; IEA:Ensembl.
GO; GO:0042438; P:melanin biosynthetic process; TAS:Reactome.
GO; GO:0030318; P:melanocyte differentiation; IEA:Ensembl.
GO; GO:0032438; P:melanosome organization; IEA:Ensembl.
GO; GO:0048023; P:positive regulation of melanin biosynthetic process; IMP: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;
3D-structure; Albinism; Complete proteome; Copper;
Direct protein sequencing; Disease mutation; Disulfide bond;
Glycoprotein; Melanin biosynthesis; Membrane; Metal-binding;
Monooxygenase; Oxidoreductase; Polymorphism; Reference proteome;
Signal; Transmembrane; Transmembrane helix; Zinc.
SIGNAL 1 24
CHAIN 25 537 5,6-dihydroxyindole-2-carboxylic acid
oxidase.
/FTId=PRO_0000035889.
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:0000305|PubMed:28661582}.
METAL 215 215 Copper A. {ECO:0000305|PubMed:28661582}.
METAL 224 224 Copper A. {ECO:0000305|PubMed:28661582}.
METAL 377 377 Copper B. {ECO:0000305|PubMed:28661582}.
METAL 381 381 Copper B. {ECO:0000305|PubMed:28661582}.
METAL 404 404 Copper B. {ECO:0000305|PubMed:28661582}.
CARBOHYD 96 96 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:5M8L,
ECO:0000269|PubMed:28661582}.
CARBOHYD 104 104 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:5M8L,
ECO:0000269|PubMed:28661582}.
CARBOHYD 181 181 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:5M8L,
ECO:0000269|PubMed:28661582}.
CARBOHYD 304 304 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:5M8L,
ECO:0000269|PubMed:28661582}.
CARBOHYD 350 350 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:5M8L,
ECO:0000269|PubMed:28661582}.
CARBOHYD 385 385 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:5M8L,
ECO:0000269|PubMed:28661582}.
DISULFID 30 41 {ECO:0000244|PDB:5M8L,
ECO:0000244|PDB:5M8M,
ECO:0000244|PDB:5M8N,
ECO:0000244|PDB:5M8O,
ECO:0000244|PDB:5M8P,
ECO:0000244|PDB:5M8Q,
ECO:0000244|PDB:5M8R,
ECO:0000244|PDB:5M8T,
ECO:0000269|PubMed:28661582}.
DISULFID 42 65 {ECO:0000244|PDB:5M8L,
ECO:0000244|PDB:5M8M,
ECO:0000244|PDB:5M8N,
ECO:0000244|PDB:5M8O,
ECO:0000244|PDB:5M8P,
ECO:0000244|PDB:5M8Q,
ECO:0000244|PDB:5M8R,
ECO:0000244|PDB:5M8T,
ECO:0000269|PubMed:28661582}.
DISULFID 56 99 {ECO:0000244|PDB:5M8L,
ECO:0000244|PDB:5M8M,
ECO:0000244|PDB:5M8N,
ECO:0000244|PDB:5M8O,
ECO:0000244|PDB:5M8P,
ECO:0000244|PDB:5M8Q,
ECO:0000244|PDB:5M8R,
ECO:0000244|PDB:5M8T,
ECO:0000269|PubMed:28661582}.
DISULFID 101 110 {ECO:0000244|PDB:5M8L,
ECO:0000244|PDB:5M8M,
ECO:0000244|PDB:5M8N,
ECO:0000244|PDB:5M8O,
ECO:0000244|PDB:5M8P,
ECO:0000244|PDB:5M8Q,
ECO:0000244|PDB:5M8R,
ECO:0000244|PDB:5M8T,
ECO:0000269|PubMed:28661582}.
DISULFID 113 122 {ECO:0000244|PDB:5M8L,
ECO:0000244|PDB:5M8M,
ECO:0000244|PDB:5M8N,
ECO:0000244|PDB:5M8O,
ECO:0000244|PDB:5M8P,
ECO:0000244|PDB:5M8Q,
ECO:0000244|PDB:5M8R,
ECO:0000244|PDB:5M8T,
ECO:0000269|PubMed:28661582}.
DISULFID 258 261 {ECO:0000244|PDB:5M8L,
ECO:0000244|PDB:5M8M,
ECO:0000244|PDB:5M8N,
ECO:0000244|PDB:5M8O,
ECO:0000244|PDB:5M8P,
ECO:0000244|PDB:5M8Q,
ECO:0000244|PDB:5M8R,
ECO:0000244|PDB:5M8T,
ECO:0000269|PubMed:28661582}.
DISULFID 290 303 {ECO:0000244|PDB:5M8L,
ECO:0000244|PDB:5M8M,
ECO:0000244|PDB:5M8N,
ECO:0000244|PDB:5M8O,
ECO:0000244|PDB:5M8P,
ECO:0000244|PDB:5M8Q,
ECO:0000244|PDB:5M8R,
ECO:0000244|PDB:5M8T,
ECO:0000269|PubMed:28661582}.
VARIANT 24 24 A -> T (in OCA3; dbSNP:rs61758405).
{ECO:0000269|PubMed:23504663}.
/FTId=VAR_072599.
VARIANT 93 93 R -> C (polymorphism associated with
blond hair in individuals from the
Solomon Islands; rare or absent outside
of Oceania; dbSNP:rs387907171).
{ECO:0000269|PubMed:22556244}.
/FTId=VAR_068176.
VARIANT 326 326 R -> H (in dbSNP:rs16929374).
/FTId=VAR_026827.
VARIANT 356 356 R -> Q (in OCA3; dbSNP:rs281865424).
{ECO:0000269|PubMed:16704458}.
/FTId=VAR_026828.
MUTAGEN 362 362 Y->F: No effect; when associated with S-
374 and V-391.
{ECO:0000269|PubMed:28661582}.
MUTAGEN 374 374 R->S: No effect; when associated with F-
362 and V-391.
{ECO:0000269|PubMed:28661582}.
MUTAGEN 391 391 T->V: No effect; when associated with F-
362 and S-374.
{ECO:0000269|PubMed:28661582}.
CONFLICT 395 396 PN -> SQ (in Ref. 7; CAA35820).
{ECO:0000305}.
CONFLICT 526 537 YEKLQNPNQSVV -> RI (in Ref. 1; CAA35785
and 2). {ECO:0000305}.
TURN 28 30 {ECO:0000244|PDB:5M8S}.
HELIX 33 38 {ECO:0000244|PDB:5M8S}.
STRAND 44 46 {ECO:0000244|PDB:5M8S}.
STRAND 48 50 {ECO:0000244|PDB:5M8S}.
STRAND 53 55 {ECO:0000244|PDB:5M8S}.
TURN 56 61 {ECO:0000244|PDB:5M8S}.
STRAND 62 67 {ECO:0000244|PDB:5M8S}.
TURN 86 94 {ECO:0000244|PDB:5M8S}.
STRAND 96 101 {ECO:0000244|PDB:5M8S}.
STRAND 105 107 {ECO:0000244|PDB:5M8S}.
TURN 119 122 {ECO:0000244|PDB:5M8S}.
STRAND 128 130 {ECO:0000244|PDB:5M8S}.
HELIX 133 135 {ECO:0000244|PDB:5M8S}.
HELIX 138 153 {ECO:0000244|PDB:5M8S}.
STRAND 157 164 {ECO:0000244|PDB:5M8S}.
HELIX 166 168 {ECO:0000244|PDB:5M8S}.
STRAND 174 176 {ECO:0000244|PDB:5M8S}.
STRAND 179 183 {ECO:0000244|PDB:5M8Q}.
HELIX 184 196 {ECO:0000244|PDB:5M8S}.
STRAND 203 205 {ECO:0000244|PDB:5M8Q}.
STRAND 213 217 {ECO:0000244|PDB:5M8S}.
HELIX 220 239 {ECO:0000244|PDB:5M8S}.
TURN 263 266 {ECO:0000244|PDB:5M8L}.
STRAND 271 273 {ECO:0000244|PDB:5M8N}.
HELIX 282 285 {ECO:0000244|PDB:5M8S}.
HELIX 293 299 {ECO:0000244|PDB:5M8S}.
HELIX 322 324 {ECO:0000244|PDB:5M8S}.
HELIX 330 336 {ECO:0000244|PDB:5M8S}.
HELIX 355 360 {ECO:0000244|PDB:5M8S}.
HELIX 376 383 {ECO:0000244|PDB:5M8S}.
HELIX 387 389 {ECO:0000244|PDB:5M8S}.
TURN 391 393 {ECO:0000244|PDB:5M8S}.
HELIX 394 396 {ECO:0000244|PDB:5M8S}.
HELIX 399 417 {ECO:0000244|PDB:5M8S}.
TURN 418 420 {ECO:0000244|PDB:5M8S}.
HELIX 422 424 {ECO:0000244|PDB:5M8L}.
STRAND 427 431 {ECO:0000244|PDB:5M8S}.
HELIX 449 452 {ECO:0000244|PDB:5M8S}.
HELIX 456 459 {ECO:0000244|PDB:5M8S}.
STRAND 461 464 {ECO:0000244|PDB:5M8S}.
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


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