TP4A1_PONAB
ID TP4A1_PONAB Reviewed; 173 AA.
AC Q5R7J8;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 87.
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 Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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:0000250|UniProtKB:Q93096};
CC Lipid-anchor {ECO:0000250|UniProtKB:Q93096}. Early endosome
CC {ECO:0000250|UniProtKB:Q93096}. Endoplasmic reticulum
CC {ECO:0000250|UniProtKB:Q93096}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q93096}. Cytoplasm, cytoskeleton, spindle
CC {ECO:0000250|UniProtKB:Q93096}. Nucleus {ECO:0000250|UniProtKB:Q78EG7}.
CC Note=And mitotic spindle. {ECO:0000250|UniProtKB:Q93096}.
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; CR860117; CAH92262.1; -; mRNA.
DR RefSeq; NP_001126324.1; NM_001132852.1.
DR AlphaFoldDB; Q5R7J8; -.
DR BMRB; Q5R7J8; -.
DR SMR; Q5R7J8; -.
DR STRING; 9601.ENSPPYP00000018734; -.
DR GeneID; 100173305; -.
DR KEGG; pon:100173305; -.
DR CTD; 7803; -.
DR eggNOG; KOG2836; Eukaryota.
DR InParanoid; Q5R7J8; -.
DR Proteomes; UP000001595; Unplaced.
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; 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 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_0000094783"
FT PROPEP 171..173
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000396729"
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"
FT DISULFID 49..104
FT /evidence="ECO:0000250"
SQ SEQUENCE 173 AA; 19727 MW; 5FF00B273E00A186 CRC64;
MARMNRPAPV EVTYKNMRFL ITHNPTNATL NKFIEELKKY GVTTIVRVCE ATYDTALVEK
EGIHVLDWPF DDGAPPSNQI VDGWLSLVKI KFREEPGCCI AVHCVAGLGR APVLVALALI
EGGMKYEDAV QFIRQKRRGA FNSKQLLYLE KYRPKMRLRF KDSNGHRNNC CIQ
