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Protein

5,6-dihydroxyindole-2-carboxylic acid oxidase

Gene

Tyrp1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

Cofactori

Cu2+By similarityNote: Binds 2 copper ions per subunit.By similarity

Pathway: melanin biosynthesis

This protein is involved in the pathway melanin biosynthesis, which is part of Pigment biosynthesis.
View all proteins of this organism that are known to be involved in the pathway melanin biosynthesis and in Pigment biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi192 – 1921Copper ABy similarity
Metal bindingi215 – 2151Copper ABy similarity
Metal bindingi224 – 2241Copper ABy similarity
Metal bindingi377 – 3771Copper BBy similarity
Metal bindingi381 – 3811Copper BBy similarity
Metal bindingi404 – 4041Copper BBy similarity

GO - Molecular functioni

GO - Biological processi

  • acetoacetic acid metabolic process Source: MGI
  • melanin biosynthetic process from tyrosine Source: UniProtKB
  • melanin metabolic process Source: MGI
  • melanocyte differentiation Source: MGI
  • melanosome organization Source: MGI
  • pigmentation Source: MGI
  • positive regulation of melanin biosynthetic process Source: CACAO
Complete GO annotation...

Keywords - Molecular functioni

Monooxygenase, Oxidoreductase

Keywords - Biological processi

Melanin biosynthesis

Keywords - Ligandi

Copper, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-15620.
UniPathwayiUPA00785.

Names & Taxonomyi

Protein namesi
Recommended name:
5,6-dihydroxyindole-2-carboxylic acid oxidase (EC:1.14.18.-)
Short name:
DHICA oxidase
Alternative name(s):
Brown locus protein
Catalase B
Tyrosinase-related protein 1
Short name:
TRP
Short name:
TRP-1
Short name:
TRP1
Gene namesi
Name:Tyrp1
Synonyms:Tyrp-1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 4

Organism-specific databases

MGIiMGI:98881. Tyrp1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini25 – 477453Lumenal, melanosomeSequence AnalysisAdd
BLAST
Transmembranei478 – 50124HelicalSequence AnalysisAdd
BLAST
Topological domaini502 – 53736CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  • clathrin-coated endocytic vesicle membrane Source: MGI
  • endosome membrane Source: MGI
  • integral component of membrane Source: UniProtKB-KW
  • melanosome Source: UniProtKB
  • melanosome membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Involvement in diseasei

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

Keywords - Diseasei

Albinism, Disease mutation

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2424Add
BLAST
Chaini25 – 5375135,6-dihydroxyindole-2-carboxylic acid oxidasePRO_0000035890Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi96 – 961N-linked (GlcNAc...)Sequence Analysis
Glycosylationi104 – 1041N-linked (GlcNAc...)Sequence Analysis
Glycosylationi181 – 1811N-linked (GlcNAc...)Sequence Analysis
Glycosylationi304 – 3041N-linked (GlcNAc...)Sequence Analysis
Glycosylationi350 – 3501N-linked (GlcNAc...)Sequence Analysis
Glycosylationi385 – 3851N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQBiP07147.
PRIDEiP07147.

PTM databases

PhosphoSiteiP07147.

Expressioni

Tissue specificityi

Pigment cells.

Gene expression databases

BgeeiP07147.
CleanExiMM_TYRP1.
ExpressionAtlasiP07147. differential.
GenevisibleiP07147. MM.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
TyrP113442EBI-821614,EBI-821603

Protein-protein interaction databases

IntActiP07147. 1 interaction.
STRINGi10090.ENSMUSP00000006151.

Structurei

3D structure databases

ProteinModelPortaliP07147.
SMRiP07147. Positions 128-466.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the tyrosinase family.Curated

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG86242.
HOGENOMiHOG000118376.
HOVERGENiHBG003553.
InParanoidiP07147.
KOiK00506.
OMAiYYSVKKT.
PhylomeDBiP07147.
TreeFamiTF315865.

Family and domain databases

Gene3Di1.10.1280.10. 1 hit.
InterProiIPR015559. DiOHindole_carboxylic_A_Oxase.
IPR002227. Tyrosinase_Cu-bd.
IPR008922. Unchr_di-copper_centre.
[Graphical view]
PANTHERiPTHR11474:SF3. PTHR11474:SF3. 1 hit.
PfamiPF00264. Tyrosinase. 1 hit.
[Graphical view]
PRINTSiPR00092. TYROSINASE.
SUPFAMiSSF48056. SSF48056. 2 hits.
PROSITEiPS00497. TYROSINASE_1. 1 hit.
PS00498. TYROSINASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P07147-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKSYNVLPLA YISLFLMLFY QVWAQFPREC ANIEALRRGV CCPDLLPSSG
60 70 80 90 100
PGTDPCGSSS GRGRCVAVIA DSRPHSRHYP HDGKDDREAW PLRFFNRTCQ
110 120 130 140 150
CNDNFSGHNC GTCRPGWRGA ACNQKILTVR RNLLDLSPEE KSHFVRALDM
160 170 180 190 200
AKRTTHPQFV IATRRLEDIL GPDGNTPQFE NISVYNYFVW THYYSVKKTF
210 220 230 240 250
LGTGQESFGD VDFSHEGPAF LTWHRYHLLQ LERDMQEMLQ EPSFSLPYWN
260 270 280 290 300
FATGKNVCDV CTDDLMGSRS NFDSTLISPN SVFSQWRVVC ESLEEYDTLG
310 320 330 340 350
TLCNSTEGGP IRRNPAGNVG RPAVQRLPEP QDVTQCLEVR VFDTPPFYSN
360 370 380 390 400
STDSFRNTVE GYSAPTGKYD PAVRSLHNLA HLFLNGTGGQ THLSPNDPIF
410 420 430 440 450
VLLHTFTDAV FDEWLRRYNA DISTFPLENA PIGHNRQYNM VPFWPPVTNT
460 470 480 490 500
EMFVTAPDNL GYAYEVQWPG QEFTVSEIIT IAVVAALLLV AAIFGVASCL
510 520 530
IRSRSTKNEA NQPLLTDHYQ RYAEDYEELP NPNHSMV
Length:537
Mass (Da):60,761
Last modified:April 1, 1988 - v1
Checksum:i86570998AA9EB0BC
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti110 – 1101C → Y in brown. 1 Publication
Natural varianti326 – 3261R → H in brown. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X03687 mRNA. Translation: CAA27323.1.
BC076598 mRNA. Translation: AAH76598.1.
CCDSiCCDS18290.1.
PIRiA24933. YRMSB6.
RefSeqiNP_001268943.1. NM_001282014.1.
NP_001268944.1. NM_001282015.1.
NP_112479.1. NM_031202.3.
UniGeneiMm.30438.

Genome annotation databases

EnsembliENSMUST00000006151; ENSMUSP00000006151; ENSMUSG00000005994.
ENSMUST00000102831; ENSMUSP00000099895; ENSMUSG00000005994.
GeneIDi22178.
KEGGimmu:22178.
UCSCiuc008tjq.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X03687 mRNA. Translation: CAA27323.1.
BC076598 mRNA. Translation: AAH76598.1.
CCDSiCCDS18290.1.
PIRiA24933. YRMSB6.
RefSeqiNP_001268943.1. NM_001282014.1.
NP_001268944.1. NM_001282015.1.
NP_112479.1. NM_031202.3.
UniGeneiMm.30438.

3D structure databases

ProteinModelPortaliP07147.
SMRiP07147. Positions 128-466.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP07147. 1 interaction.
STRINGi10090.ENSMUSP00000006151.

PTM databases

PhosphoSiteiP07147.

Proteomic databases

MaxQBiP07147.
PRIDEiP07147.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000006151; ENSMUSP00000006151; ENSMUSG00000005994.
ENSMUST00000102831; ENSMUSP00000099895; ENSMUSG00000005994.
GeneIDi22178.
KEGGimmu:22178.
UCSCiuc008tjq.2. mouse.

Organism-specific databases

CTDi7306.
MGIiMGI:98881. Tyrp1.

Phylogenomic databases

eggNOGiNOG86242.
HOGENOMiHOG000118376.
HOVERGENiHBG003553.
InParanoidiP07147.
KOiK00506.
OMAiYYSVKKT.
PhylomeDBiP07147.
TreeFamiTF315865.

Enzyme and pathway databases

UniPathwayiUPA00785.
BioCyciMetaCyc:MONOMER-15620.

Miscellaneous databases

ChiTaRSiTyrp1. mouse.
NextBioi302135.
PROiP07147.
SOURCEiSearch...

Gene expression databases

BgeeiP07147.
CleanExiMM_TYRP1.
ExpressionAtlasiP07147. differential.
GenevisibleiP07147. MM.

Family and domain databases

Gene3Di1.10.1280.10. 1 hit.
InterProiIPR015559. DiOHindole_carboxylic_A_Oxase.
IPR002227. Tyrosinase_Cu-bd.
IPR008922. Unchr_di-copper_centre.
[Graphical view]
PANTHERiPTHR11474:SF3. PTHR11474:SF3. 1 hit.
PfamiPF00264. Tyrosinase. 1 hit.
[Graphical view]
PRINTSiPR00092. TYROSINASE.
SUPFAMiSSF48056. SSF48056. 2 hits.
PROSITEiPS00497. TYROSINASE_1. 1 hit.
PS00498. TYROSINASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. 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.

Entry informationi

Entry nameiTYRP1_MOUSE
AccessioniPrimary (citable) accession number: P07147
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: April 1, 1988
Last modified: June 24, 2015
This is version 145 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.