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P07147 (TYRP1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 137. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
5,6-dihydroxyindole-2-carboxylic acid oxidase

Short name=DHICA oxidase
EC=1.14.18.-
Alternative name(s):
Brown locus protein
Catalase B
Tyrosinase-related protein 1
Short name=TRP
Short name=TRP-1
Short name=TRP1
Gene names
Name:Tyrp1
Synonyms:Tyrp-1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length537 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Oxidation of 5,6-dihydroxyindole-2-carboxylic acid (DHICA) into indole-5,6-quinone-2-carboxylic acid. May regulate or influence the type of melanin synthesized. Ref.4 Ref.5 Ref.6

Cofactor

Binds 2 copper ions per subunit By similarity.

Pathway

Pigment biosynthesis; melanin biosynthesis.

Subcellular location

Melanosome membrane; Single-pass type I membrane protein. Note: Located to mature stage III and IV melanosomes and apposed endosomal tubular membranes. Transported to pigmented melanosomes by the BLOC-1 complex. Ref.7

Tissue specificity

Pigment cells.

Involvement in disease

Defects in Tyrp1 are the cause of the brown (b) phenotype. Brown mice have a brown or hypopigmented coat.

Sequence similarities

Belongs to the tyrosinase family.

Ontologies

Keywords
   Biological processMelanin biosynthesis
   Cellular componentMembrane
   DiseaseAlbinism
Disease mutation
   DomainSignal
Transmembrane
Transmembrane helix
   LigandCopper
Metal-binding
   Molecular functionMonooxygenase
Oxidoreductase
   PTMGlycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processacetoacetic acid metabolic process

Inferred from mutant phenotype PubMed 7665913. Source: MGI

melanin biosynthetic process from tyrosine

Traceable author statement PubMed 9918801. Source: UniProtKB

melanin metabolic process

Inferred from mutant phenotype PubMed 9548375. Source: MGI

melanocyte differentiation

Inferred from mutant phenotype PubMed 2379821. Source: MGI

melanosome organization

Inferred from mutant phenotype PubMed 9548375. Source: MGI

pigmentation

Inferred from mutant phenotype PubMed 13880466PubMed 17247639PubMed 2379821. Source: MGI

   Cellular_componentclathrin-coated endocytic vesicle membrane

Inferred from electronic annotation. Source: Ensembl

endosome membrane

Inferred from electronic annotation. Source: Ensembl

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

melanosome

Inferred from direct assay PubMed 9918801. Source: UniProtKB

melanosome membrane

Inferred from direct assay Ref.7. Source: UniProtKB

   Molecular_functioncopper ion binding

Inferred from electronic annotation. Source: InterPro

oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, another compound as one donor, and incorporation of one atom of oxygen

Inferred from electronic annotation. Source: InterPro

protein binding

Inferred from physical interaction PubMed 9918801. Source: UniProtKB

protein heterodimerization activity

Inferred from direct assay PubMed 9918801. Source: UniProtKB

protein homodimerization activity

Inferred from direct assay PubMed 9918801. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

TyrP113442EBI-821614,EBI-821603

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424
Chain25 – 5375135,6-dihydroxyindole-2-carboxylic acid oxidase
PRO_0000035890

Regions

Topological domain25 – 477453Lumenal, melanosome Potential
Transmembrane478 – 50124Helical; Potential
Topological domain502 – 53736Cytoplasmic Potential

Sites

Metal binding1921Copper A By similarity
Metal binding2151Copper A By similarity
Metal binding2241Copper A By similarity
Metal binding3771Copper B By similarity
Metal binding3811Copper B By similarity
Metal binding4041Copper B By similarity

Amino acid modifications

Glycosylation961N-linked (GlcNAc...) Potential
Glycosylation1041N-linked (GlcNAc...) Potential
Glycosylation1811N-linked (GlcNAc...) Potential
Glycosylation3041N-linked (GlcNAc...) Potential
Glycosylation3501N-linked (GlcNAc...) Potential
Glycosylation3851N-linked (GlcNAc...) Potential

Natural variations

Natural variant1101C → Y in brown. Ref.8
Natural variant3261R → H in brown. Ref.8

Sequences

Sequence LengthMass (Da)Tools
P07147 [UniParc].

Last modified April 1, 1988. Version 1.
Checksum: 86570998AA9EB0BC

FASTA53760,761
        10         20         30         40         50         60 
MKSYNVLPLA YISLFLMLFY QVWAQFPREC ANIEALRRGV CCPDLLPSSG PGTDPCGSSS 

        70         80         90        100        110        120 
GRGRCVAVIA DSRPHSRHYP HDGKDDREAW PLRFFNRTCQ CNDNFSGHNC GTCRPGWRGA 

       130        140        150        160        170        180 
ACNQKILTVR RNLLDLSPEE KSHFVRALDM AKRTTHPQFV IATRRLEDIL GPDGNTPQFE 

       190        200        210        220        230        240 
NISVYNYFVW THYYSVKKTF LGTGQESFGD VDFSHEGPAF LTWHRYHLLQ LERDMQEMLQ 

       250        260        270        280        290        300 
EPSFSLPYWN FATGKNVCDV CTDDLMGSRS NFDSTLISPN SVFSQWRVVC ESLEEYDTLG 

       310        320        330        340        350        360 
TLCNSTEGGP IRRNPAGNVG RPAVQRLPEP QDVTQCLEVR VFDTPPFYSN STDSFRNTVE 

       370        380        390        400        410        420 
GYSAPTGKYD PAVRSLHNLA HLFLNGTGGQ THLSPNDPIF VLLHTFTDAV FDEWLRRYNA 

       430        440        450        460        470        480 
DISTFPLENA PIGHNRQYNM VPFWPPVTNT EMFVTAPDNL GYAYEVQWPG QEFTVSEIIT 

       490        500        510        520        530 
IAVVAALLLV AAIFGVASCL IRSRSTKNEA NQPLLTDHYQ RYAEDYEELP NPNHSMV 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and expression of cDNA encoding mouse tyrosinase."
Shibahara S., Tomita Y., Sakakura T., Nager C., Chaudhuri B., Mueller R.
Nucleic Acids Res. 14:2413-2427(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Melanoma.
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6.
Tissue: Eye.
[3]"A cDNA encoding tyrosinase-related protein maps to the brown locus in mouse."
Jackson I.J.
Proc. Natl. Acad. Sci. U.S.A. 85:4392-4396(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION OF PROTEIN.
[4]"Murine and human b locus pigmentation genes encode a glycoprotein (gp75) with catalase activity."
Halaban R., Moellmann G.
Proc. Natl. Acad. Sci. U.S.A. 87:4809-4813(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: POSSIBLE FUNCTION.
[5]"The mouse brown (b) locus protein has dopachrome tautomerase activity and is located in lysosomes in transfected fibroblasts."
Winder A.J., Wittbjer A., Rosengren E., Rorsman H.
J. Cell Sci. 106:153-166(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: POSSIBLE FUNCTION.
[6]"Tyrosinase related protein 1 (TRP1) functions as a DHICA oxidase in melanin biosynthesis."
Kobayashi T., Urabe K., Winder A., Jimenez-Cervantes C., Imokawa G., Brewington T., Solano F., Garcia-Borron J.C., Hearing V.J.
EMBO J. 13:5818-5825(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[7]"BLOC-1 is required for cargo-specific sorting from vacuolar early endosomes toward lysosome-related organelles."
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.
Mol. Biol. Cell 18:768-780(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[8]"The molecular basis of brown, an old mouse mutation, and of an induced revertant to wild type."
Zdarsky E., Favor J., Jackson I.J.
Genetics 126:443-449(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS BROWN TYR-110 AND HIS-326.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X03687 mRNA. Translation: CAA27323.1.
BC076598 mRNA. Translation: AAH76598.1.
CCDSCCDS18290.1.
PIRYRMSB6. A24933.
RefSeqNP_001268943.1. NM_001282014.1.
NP_001268944.1. NM_001282015.1.
NP_112479.1. NM_031202.3.
UniGeneMm.30438.

3D structure databases

ProteinModelPortalP07147.
SMRP07147. Positions 128-466.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP07147. 1 interaction.

PTM databases

PhosphoSiteP07147.

Proteomic databases

MaxQBP07147.
PRIDEP07147.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000006151; ENSMUSP00000006151; ENSMUSG00000005994.
ENSMUST00000102831; ENSMUSP00000099895; ENSMUSG00000005994.
GeneID22178.
KEGGmmu:22178.
UCSCuc008tjq.2. mouse.

Organism-specific databases

CTD7306.
MGIMGI:98881. Tyrp1.

Phylogenomic databases

eggNOGNOG86242.
HOGENOMHOG000118376.
HOVERGENHBG003553.
InParanoidP07147.
KOK00506.
OMAVKKTFLG.
PhylomeDBP07147.
TreeFamTF315865.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-15620.
UniPathwayUPA00785.

Gene expression databases

BgeeP07147.
CleanExMM_TYRP1.
GenevestigatorP07147.

Family and domain databases

Gene3D1.10.1280.10. 1 hit.
InterProIPR015559. DiOHindole_carboxylic_A_Oxase.
IPR002227. Tyrosinase_Cu-bd.
IPR008922. Unchr_di-copper_centre.
[Graphical view]
PANTHERPTHR11474:SF3. PTHR11474:SF3. 1 hit.
PfamPF00264. Tyrosinase. 1 hit.
[Graphical view]
PRINTSPR00092. TYROSINASE.
SUPFAMSSF48056. SSF48056. 2 hits.
PROSITEPS00497. TYROSINASE_1. 1 hit.
PS00498. TYROSINASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSTYRP1. mouse.
NextBio302135.
PROP07147.
SOURCESearch...

Entry information

Entry nameTYRP1_MOUSE
AccessionPrimary (citable) accession number: P07147
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: April 1, 1988
Last modified: July 9, 2014
This is version 137 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot