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TP4A3_BOVIN
ID   TP4A3_BOVIN             Reviewed;         173 AA.
AC   A2VDT1;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-MAR-2007, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Protein tyrosine phosphatase type IVA 3;
DE            EC=3.1.3.48;
DE   AltName: Full=Protein-tyrosine phosphatase 4a3;
DE   Flags: Precursor;
GN   Name=PTP4A3;
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 [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Fetal muscle;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Protein tyrosine phosphatase which stimulates progression
CC       from G1 into S phase during mitosis. Enhances cell proliferation, cell
CC       motility and invasive activity, and promotes cancer metastasis. May be
CC       involved in the progression of cardiac hypertrophy by inhibiting
CC       intracellular calcium mobilization in response to angiotensin II (By
CC       similarity). {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   -!- ACTIVITY REGULATION: Inhibited by sodium orthovanadate and
CC       peroxovanadium compounds, and by pentamidine. {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with tubulin. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane. Early endosome {ECO:0000250}.
CC   -!- PTM: Farnesylated. Farnesylation is required for membrane targeting.
CC       Unfarnesylated forms are shifted into the nucleus (By similarity).
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC       {ECO:0000305}.
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DR   EMBL; BC133386; AAI33387.1; -; mRNA.
DR   RefSeq; NP_001077235.1; NM_001083766.1.
DR   RefSeq; XP_005215180.1; XM_005215123.3.
DR   RefSeq; XP_005215181.1; XM_005215124.3.
DR   RefSeq; XP_010810118.1; XM_010811816.2.
DR   RefSeq; XP_015329814.1; XM_015474328.1.
DR   AlphaFoldDB; A2VDT1; -.
DR   SMR; A2VDT1; -.
DR   STRING; 9913.ENSBTAP00000056281; -.
DR   PaxDb; A2VDT1; -.
DR   PRIDE; A2VDT1; -.
DR   Ensembl; ENSBTAT00000064455; ENSBTAP00000056281; ENSBTAG00000046467.
DR   Ensembl; ENSBTAT00000086143; ENSBTAP00000056717; ENSBTAG00000046467.
DR   GeneID; 100137722; -.
DR   KEGG; bta:100137722; -.
DR   CTD; 11156; -.
DR   VEuPathDB; HostDB:ENSBTAG00000046467; -.
DR   VGNC; VGNC:33525; PTP4A3.
DR   eggNOG; KOG2836; Eukaryota.
DR   GeneTree; ENSGT00940000159581; -.
DR   HOGENOM; CLU_099263_1_0_1; -.
DR   InParanoid; A2VDT1; -.
DR   OMA; KYRPRQR; -.
DR   OrthoDB; 1398550at2759; -.
DR   TreeFam; TF313384; -.
DR   Proteomes; UP000009136; Chromosome 14.
DR   Bgee; ENSBTAG00000046467; Expressed in infraspinatus muscle and 103 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IBA:GO_Central.
DR   GO; GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; IEA:InterPro.
DR   GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEA:Ensembl.
DR   GO; GO:0043542; P:endothelial cell migration; IBA:GO_Central.
DR   GO; GO:0007219; P:Notch signaling pathway; IEA:Ensembl.
DR   GO; GO:1904951; P:positive regulation of establishment of protein localization; IEA:Ensembl.
DR   GO; GO:1901224; P:positive regulation of NIK/NF-kappaB signaling; IEA:Ensembl.
DR   GO; GO:0043117; P:positive regulation of vascular permeability; IEA:Ensembl.
DR   GO; GO:0006470; P:protein dephosphorylation; IEA:InterPro.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:Ensembl.
DR   GO; GO:1900746; P:regulation of vascular endothelial growth factor signaling pathway; IEA:Ensembl.
DR   Gene3D; 3.90.190.10; -; 1.
DR   InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR   InterPro; IPR000242; PTP_cat.
DR   InterPro; IPR003595; Tyr_Pase_cat.
DR   InterPro; IPR000387; Tyr_Pase_dom.
DR   InterPro; IPR020422; TYR_PHOSPHATASE_DUAL_dom.
DR   Pfam; PF00102; Y_phosphatase; 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   2: Evidence at transcript level;
KW   Cell membrane; Disulfide bond; Endosome; Hydrolase; Lipoprotein; Membrane;
KW   Methylation; Prenylation; Protein phosphatase; Proto-oncogene;
KW   Reference proteome.
FT   CHAIN           1..170
FT                   /note="Protein tyrosine phosphatase type IVA 3"
FT                   /id="PRO_0000329024"
FT   PROPEP          171..173
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000396734"
FT   DOMAIN          8..161
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
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         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"
FT   DISULFID        49..104
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   173 AA;  19511 MW;  439BEBE1BCC16B94 CRC64;
     MARMNRPAPV EVSYKNMRFL ITHNPTNATL SSFIEDLKKY GATTVVRVCE VTYDKAPLEK
     DGITVVDWPF DDGAPPPGKV VEDWLSLLKN KFCDDPGSCV AVHCVAGLGR APVLVALALI
     ESGMKYEDAI QFIRQKRRGA INSKQLTYLE KYRPKQRLRF KDPHAHKTKC CIM
 
 
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