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 24-JAN-2024, entry version 108.
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 RefSeq; XP_005570475.1; XM_005570418.2.
DR AlphaFoldDB; Q9TSM6; -.
DR BMRB; Q9TSM6; -.
DR SMR; Q9TSM6; -.
DR STRING; 9541.ENSMFAP00000040252; -.
DR Ensembl; ENSMFAT00000014519.2; ENSMFAP00000040252.1; ENSMFAG00000046284.2.
DR GeneID; 102134176; -.
DR GeneID; 107126363; -.
DR KEGG; mcf:102134176; -.
DR KEGG; mcf:107126363; -.
DR CTD; 7803; -.
DR VEuPathDB; HostDB:ENSMFAG00000046284; -.
DR eggNOG; KOG2836; Eukaryota.
DR GeneTree; ENSGT00940000154406; -.
DR OMA; GQKNSCC; -.
DR OrthoDB; 117411at2759; -.
DR Proteomes; UP000233100; Chromosome 4.
DR Bgee; ENSMFAG00000046284; Expressed in liver and 13 other cell types or 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:0016311; P:dephosphorylation; IEA:InterPro.
DR CDD; cd18537; PTP-IVa1; 1.
DR Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 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 PANTHER; PTHR23339:SF55; PROTEIN TYROSINE PHOSPHATASE TYPE IVA 1; 1.
DR PANTHER; PTHR23339; TYROSINE SPECIFIC PROTEIN PHOSPHATASE AND DUAL SPECIFICITY PROTEIN PHOSPHATASE; 1.
DR Pfam; PF00782; DSPc; 1.
DR SMART; SM00404; PTPc_motif; 1.
DR SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 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
//
