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TYRP1_BOVIN
ID   TYRP1_BOVIN             Reviewed;         537 AA.
AC   Q8WN57;
DT   27-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 2.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=5,6-dihydroxyindole-2-carboxylic acid oxidase;
DE            Short=DHICA oxidase;
DE            EC=1.14.18.-;
DE   AltName: Full=Tyrosinase-related protein 1;
DE            Short=TRP-1;
DE            Short=TRP1;
DE   Flags: Precursor;
GN   Name=TYRP1;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Skin;
RA   Guibert S., Julien R., Oulmouden A.;
RT   "Transcriptional regulation of bovine TYRP1 gene.";
RL   Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Plays a role in melanin biosynthesis. Catalyzes the oxidation
CC       of 5,6-dihydroxyindole-2-carboxylic acid (DHICA) into indole-5,6-
CC       quinone-2-carboxylic acid. May regulate or influence the type of
CC       melanin synthesized. Also to a lower extent, capable of hydroxylating
CC       tyrosine and producing melanin. {ECO:0000250|UniProtKB:P07147}.
CC   -!- COFACTOR:
CC       Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
CC         Evidence={ECO:0000250|UniProtKB:P17643};
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000250|UniProtKB:P17643};
CC       Note=Contains bound zinc ions after heterologous expression in insect
CC       cells. {ECO:0000250|UniProtKB:P17643};
CC   -!- PATHWAY: Pigment biosynthesis; melanin biosynthesis.
CC       {ECO:0000250|UniProtKB:P17643}.
CC   -!- SUBUNIT: Monomer (By similarity). Interacts with ATP7A (By similarity).
CC       {ECO:0000250|UniProtKB:P07147, ECO:0000250|UniProtKB:P17643}.
CC   -!- SUBCELLULAR LOCATION: Melanosome membrane
CC       {ECO:0000250|UniProtKB:P07147}; Single-pass type I membrane protein
CC       {ECO:0000250|UniProtKB:P07147}. Melanosome
CC       {ECO:0000250|UniProtKB:P07147}. Note=Located to mature stage III and IV
CC       melanosomes and apposed endosomal tubular membranes. Transported to
CC       pigmented melanosomes by the BLOC-1 complex. Proper trafficking to
CC       melanosome is regulated by SGSM2, ANKRD27, RAB9A, RAB32 and RAB38.
CC       {ECO:0000250|UniProtKB:P07147}.
CC   -!- PTM: Glycosylated. {ECO:0000250|UniProtKB:P07147}.
CC   -!- SIMILARITY: Belongs to the tyrosinase family. {ECO:0000305}.
CC   -!- CAUTION: The precise function of this protein in melanin biosynthesis
CC       is still under debate. DHICA oxidase activity is controversial. The
CC       mouse protein has been shown to have DHICA oxidase activity (By
CC       similarity). In contrast, the human protein was shown lack DHICA
CC       oxidase activity, or to have DHICA oxidase activity only in the
CC       presence of Cu(2+), but not with Zn(2+) (By similarity).
CC       {ECO:0000250|UniProtKB:P07147, ECO:0000250|UniProtKB:P17643,
CC       ECO:0000305}.
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DR   EMBL; AF445638; AAL38167.2; -; mRNA.
DR   RefSeq; NP_776905.2; NM_174480.3.
DR   AlphaFoldDB; Q8WN57; -.
DR   SMR; Q8WN57; -.
DR   STRING; 9913.ENSBTAP00000027945; -.
DR   PaxDb; Q8WN57; -.
DR   PRIDE; Q8WN57; -.
DR   GeneID; 282105; -.
DR   KEGG; bta:282105; -.
DR   CTD; 7306; -.
DR   eggNOG; ENOG502QRNA; Eukaryota.
DR   InParanoid; Q8WN57; -.
DR   OrthoDB; 518234at2759; -.
DR   UniPathway; UPA00785; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0097708; C:intracellular vesicle; ISS:UniProtKB.
DR   GO; GO:0042470; C:melanosome; ISS:UniProtKB.
DR   GO; GO:0033162; C:melanosome membrane; ISS:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR   GO; GO:0004503; F:tyrosinase activity; ISS:UniProtKB.
DR   GO; GO:0042438; P:melanin biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 1.10.1280.10; -; 1.
DR   InterPro; IPR008922; Di-copper_centre_dom_sf.
DR   InterPro; IPR002227; Tyrosinase_Cu-bd.
DR   Pfam; PF00264; Tyrosinase; 1.
DR   PRINTS; PR00092; TYROSINASE.
DR   SUPFAM; SSF48056; SSF48056; 1.
DR   PROSITE; PS00497; TYROSINASE_1; 1.
DR   PROSITE; PS00498; TYROSINASE_2; 1.
PE   2: Evidence at transcript level;
KW   Albinism; Copper; Disulfide bond; Glycoprotein; Melanin biosynthesis;
KW   Membrane; Metal-binding; Monooxygenase; Oxidoreductase; Reference proteome;
KW   Signal; Transmembrane; Transmembrane helix; Zinc.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000250"
FT   CHAIN           25..537
FT                   /note="5,6-dihydroxyindole-2-carboxylic acid oxidase"
FT                   /id="PRO_0000035888"
FT   TOPO_DOM        25..477
FT                   /note="Lumenal, melanosome"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        478..501
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        502..537
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   BINDING         192
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="A"
FT                   /evidence="ECO:0000250|UniProtKB:P17643"
FT   BINDING         215
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="A"
FT                   /evidence="ECO:0000250|UniProtKB:P17643"
FT   BINDING         224
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="A"
FT                   /evidence="ECO:0000250|UniProtKB:P17643"
FT   BINDING         377
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="B"
FT                   /evidence="ECO:0000250|UniProtKB:P17643"
FT   BINDING         381
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="B"
FT                   /evidence="ECO:0000250|UniProtKB:P17643"
FT   BINDING         404
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="B"
FT                   /evidence="ECO:0000250|UniProtKB:P17643"
FT   CARBOHYD        96
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        104
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        181
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        304
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        350
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        385
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        30..41
FT                   /evidence="ECO:0000250|UniProtKB:P17643"
FT   DISULFID        42..65
FT                   /evidence="ECO:0000250|UniProtKB:P17643"
FT   DISULFID        56..99
FT                   /evidence="ECO:0000250|UniProtKB:P17643"
FT   DISULFID        101..110
FT                   /evidence="ECO:0000250|UniProtKB:P17643"
FT   DISULFID        113..122
FT                   /evidence="ECO:0000250|UniProtKB:P17643"
FT   DISULFID        258..261
FT                   /evidence="ECO:0000250|UniProtKB:P17643"
FT   DISULFID        290..303
FT                   /evidence="ECO:0000250|UniProtKB:P17643"
SQ   SEQUENCE   537 AA;  60617 MW;  2FAB599AE3FA217B CRC64;
     MKSPTLLSLG YMFLVLLFFQ QAWAQFPREC ATIEALRNGV CCPDLSPLSG PGSDRCGLSS
     GRGRCEVVIA DSRPHSHHYP HDGRDDREGW PTRSFNRTCH CNGNFSGHNC GTCRPGWGGA
     ACDQRVLTVR RNLLDLSTEE KNRFVRALDM AKRTTHPQFV IATRRSEEIL GPDGNTPQFE
     NISIYNYFVW THYYSVKKTF LGAGQESFGE VDFSHEGPAF LTWHRYHLLQ LERDMQEMLQ
     DPSFSLPYWN FATGKNTCDI CTDDLMGSRS NFDSTLISPN SVFSQWRVVC ESLEDYDTLG
     TLCNSTEGGP IKRNPAGNVA RPMVQRLPKP QDVAQCLEVG SYDTPPFYSN STNSFRNTVE
     GYSHPTGRYD PAVRSLHNLA HLFLNGTGGQ THLSPNDPIF VLLHTFTDAV FDEWLRRYNA
     DISTYPLENA PIGHNRQYNM VPFWPPVTNI EMFVTAPDNL GYTYEVQWPS RSFSISEIVT
     IAVVAALSLV AVIFAGASCL IRARSNMDEA NQPLLTDQYQ HYIEEYEKIH NPNQSVV
 
 
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