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TP4A1_MACFA
ID   TP4A1_MACFA             Reviewed;         173 AA.
AC   Q9TSM6;
DT   05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Protein tyrosine phosphatase type IVA 1;
DE            EC=3.1.3.48 {ECO:0000250|UniProtKB:Q93096};
DE   AltName: Full=Protein-tyrosine phosphatase 4a1;
DE   AltName: Full=Protein-tyrosine phosphatase of regenerating liver 1;
DE            Short=PRL-1;
DE   Flags: Precursor;
GN   Name=PTP4A1; Synonyms=PRL1;
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC   TISSUE=Retina;
RX   PubMed=10814835; DOI=10.1016/s0169-328x(00)00045-0;
RA   Yarovinsky T.O., Rickman D.W., Diamond R.H., Taub R., Hageman G.S.,
RA   Bowes Rickman C.;
RT   "Expression of the protein tyrosine phosphatase, phosphatase of
RT   regenerating liver 1, in the outer segments of primate cone
RT   photoreceptors.";
RL   Brain Res. Mol. Brain Res. 77:95-103(2000).
CC   -!- FUNCTION: Protein tyrosine phosphatase which stimulates progression
CC       from G1 into S phase during mitosis. May play a role in the development
CC       and maintenance of differentiating epithelial tissues (By similarity).
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] +
CC         phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC         COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858,
CC         ChEBI:CHEBI:82620; EC=3.1.3.48;
CC         Evidence={ECO:0000250|UniProtKB:Q93096};
CC   -!- ACTIVITY REGULATION: Inhibited by sodium orthovanadate and pentamidine.
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Homotrimer. Interacts with ATF5 and tubulin (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10814835};
CC       Lipid-anchor {ECO:0000250|UniProtKB:Q93096}. Early endosome
CC       {ECO:0000269|PubMed:10814835}. Endoplasmic reticulum
CC       {ECO:0000269|PubMed:10814835}. Cytoplasm {ECO:0000269|PubMed:10814835}.
CC       Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:10814835}. Nucleus
CC       {ECO:0000250|UniProtKB:Q78EG7}. Note=And mitotic spindle.
CC       {ECO:0000269|PubMed:10814835}.
CC   -!- TISSUE SPECIFICITY: In the retina, expressed by red/green- but not
CC       blue-sensitive cone photoreceptor cells, and by rod bipolar cells (at
CC       protein level). {ECO:0000269|PubMed:10814835}.
CC   -!- PTM: Farnesylated. Farnesylation is required for membrane targeting (By
CC       similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC       {ECO:0000305}.
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DR   EMBL; AF190930; AAF05715.1; -; mRNA.
DR   RefSeq; XP_005552682.1; XM_005552625.2.
DR   RefSeq; XP_005552683.1; XM_005552626.2.
DR   AlphaFoldDB; Q9TSM6; -.
DR   BMRB; Q9TSM6; -.
DR   SMR; Q9TSM6; -.
DR   STRING; 9541.XP_005552682.1; -.
DR   Ensembl; ENSMFAT00000014519; ENSMFAP00000040252; ENSMFAG00000046284.
DR   GeneID; 107126363; -.
DR   KEGG; mcf:107126363; -.
DR   CTD; 7803; -.
DR   VEuPathDB; HostDB:ENSMFAG00000046284; -.
DR   eggNOG; KOG2836; Eukaryota.
DR   GeneTree; ENSGT00940000154406; -.
DR   OMA; NGQKNSC; -.
DR   OrthoDB; 1398550at2759; -.
DR   Proteomes; UP000233100; Chromosome 4.
DR   Bgee; ENSMFAG00000046284; Expressed in liver and 13 other tissues.
DR   GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; IEA:InterPro.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0006470; P:protein dephosphorylation; IEA:InterPro.
DR   Gene3D; 3.90.190.10; -; 1.
DR   InterPro; IPR000340; Dual-sp_phosphatase_cat-dom.
DR   InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR   InterPro; IPR003595; Tyr_Pase_cat.
DR   InterPro; IPR000387; Tyr_Pase_dom.
DR   InterPro; IPR020422; TYR_PHOSPHATASE_DUAL_dom.
DR   Pfam; PF00782; DSPc; 1.
DR   SMART; SM00404; PTPc_motif; 1.
DR   SUPFAM; SSF52799; SSF52799; 1.
DR   PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR   PROSITE; PS50054; TYR_PHOSPHATASE_DUAL; 1.
PE   1: Evidence at protein level;
KW   Cell cycle; Cell membrane; Cytoplasm; Cytoskeleton; Developmental protein;
KW   Disulfide bond; Endoplasmic reticulum; Endosome; Hydrolase; Lipoprotein;
KW   Membrane; Methylation; Nucleus; Prenylation; Protein phosphatase;
KW   Reference proteome.
FT   CHAIN           1..170
FT                   /note="Protein tyrosine phosphatase type IVA 1"
FT                   /id="PRO_0000094781"
FT   PROPEP          171..173
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000396727"
FT   DOMAIN          8..161
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT   REGION          97..132
FT                   /note="Interaction with ATF5"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        72
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        104
FT                   /note="Phosphocysteine intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT   BINDING         105..110
FT                   /ligand="phosphate"
FT                   /ligand_id="ChEBI:CHEBI:43474"
FT                   /evidence="ECO:0000250"
FT   BINDING         110
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         170
FT                   /note="Cysteine methyl ester"
FT                   /evidence="ECO:0000250"
FT   LIPID           170
FT                   /note="S-farnesyl cysteine"
FT                   /evidence="ECO:0000250|UniProtKB:Q93096"
FT   DISULFID        49..104
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   173 AA;  19815 MW;  702008013D3F3835 CRC64;
     MARMNRPAPV EVTYKNMRFL ITHNPTNATL NKFIEELKKY GVTTIVRVCE ATYDTTLVEK
     EGIHVLDWPF DDGAPPSNQI VDDWLSLVKI KFREEPGCCI AVHCVAGLGR APVLVALALI
     EGGMKYEDAV QFIRQKRRGA FNSKQLLYLE KYRPKMRLRF KDSNGHRNNC CIQ
 
 
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