TP4A1_RAT
ID TP4A1_RAT Reviewed; 173 AA.
AC Q78EG7; Q4QRA5; Q8VH48;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Protein tyrosine phosphatase type IVA 1;
DE EC=3.1.3.48 {ECO:0000269|PubMed:8196618};
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, ACTIVITY REGULATION,
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION, AND MUTAGENESIS OF
RP CYS-104.
RC TISSUE=Regenerating liver;
RX PubMed=8196618; DOI=10.1128/mcb.14.6.3752-3762.1994;
RA Diamond R.H., Cressman D.E., Laz T.M., Abrams C.S., Taub R.;
RT "PRL-1, a unique nuclear protein tyrosine phosphatase, affects cell
RT growth.";
RL Mol. Cell. Biol. 14:3752-3762(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Wistar; TISSUE=Basophil;
RA Heneberg P., Draber P.;
RL Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung, and Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=8840018; DOI=10.1016/0169-328x(96)00035-6;
RA Takano S., Fukuyama H., Fukumoto M., Kimura J., Xue J.H., Ohashi H.,
RA Fujita J.;
RT "PRL-1, a protein tyrosine phosphatase, is expressed in neurons and
RT oligodendrocytes in the brain and induced in the cerebral cortex following
RT transient forebrain ischemia.";
RL Brain Res. Mol. Brain Res. 40:105-115(1996).
RN [5]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=10960362; DOI=10.1152/ajpgi.2000.279.3.g613;
RA Kong W., Swain G.P., Li S., Diamond R.H.;
RT "PRL-1 PTPase expression is developmentally regulated with tissue-specific
RT patterns in epithelial tissues.";
RL Am. J. Physiol. 279:G613-G621(2000).
RN [6]
RP DEVELOPMENTAL STAGE.
RX PubMed=10679780;
RX DOI=10.1002/(sici)1097-4547(20000201)59:3<430::aid-jnr18>3.0.co;2-7;
RA Scarlato M., Beesley J., Pleasure D.;
RT "Analysis of oligodendroglial differentiation using cDNA arrays.";
RL J. Neurosci. Res. 59:430-435(2000).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1-160.
RX PubMed=16142898; DOI=10.1021/bi0509191;
RA Sun J.-P., Wang W.-Q., Yang H., Liu S., Liang F., Fedorov A.A., Almo S.C.,
RA Zhang Z.-Y.;
RT "Structure and biochemical properties of PRL-1, a phosphatase implicated in
RT cell growth, differentiation, and tumor invasion.";
RL Biochemistry 44:12009-12021(2005).
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:0000269|PubMed:8196618};
CC -!- ACTIVITY REGULATION: Inhibited by sodium orthovanadate and pentamidine.
CC {ECO:0000269|PubMed:8196618}.
CC -!- SUBUNIT: Homotrimer. Interacts with ATF5 and tubulin (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q93096}.
CC Early endosome {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:0000269|PubMed:8196618}.
CC Note=And mitotic spindle. {ECO:0000250|UniProtKB:Q93096}.
CC -!- TISSUE SPECIFICITY: Brain (neurons and oligodendrocytes), skeletal
CC muscle, regenerating liver, tumor cell lines. Expressed in enterocytes
CC of the small intestine villi and colonic surface, zymogen cells of the
CC stomach, proximal tubule cells of the kidney, bronchiolar epithelium,
CC but not in esophagus and heart (at protein level).
CC {ECO:0000269|PubMed:10960362, ECO:0000269|PubMed:8196618,
CC ECO:0000269|PubMed:8840018}.
CC -!- DEVELOPMENTAL STAGE: Expressed in fetal brain. Up-regulated during
CC oligodendroglial differentiation. Expressed in the developing
CC intestine, esophagus, liver, kidney and lung (at protein level).
CC {ECO:0000269|PubMed:10679780, ECO:0000269|PubMed:10960362,
CC ECO:0000269|PubMed:8840018}.
CC -!- INDUCTION: By hepatectomy, mitogens, and ischemia-reperfusion.
CC {ECO:0000269|PubMed:8196618}.
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; L27843; AAA41935.1; -; mRNA.
DR EMBL; AY062269; AAL38661.1; -; mRNA.
DR EMBL; BC081772; AAH81772.1; -; mRNA.
DR EMBL; BC097307; AAH97307.1; -; mRNA.
DR RefSeq; NP_113767.1; NM_031579.3.
DR RefSeq; XP_002727244.1; XM_002727198.5.
DR RefSeq; XP_006244733.1; XM_006244671.3.
DR RefSeq; XP_008765001.1; XM_008766779.2.
DR PDB; 1X24; X-ray; 3.20 A; A/B=1-160.
DR PDB; 1ZCK; X-ray; 1.90 A; A/B/C=7-160.
DR PDB; 1ZCL; X-ray; 2.90 A; A/B=1-160.
DR PDB; 3RZ2; X-ray; 2.80 A; A/B=1-169.
DR PDBsum; 1X24; -.
DR PDBsum; 1ZCK; -.
DR PDBsum; 1ZCL; -.
DR PDBsum; 3RZ2; -.
DR AlphaFoldDB; Q78EG7; -.
DR BMRB; Q78EG7; -.
DR SMR; Q78EG7; -.
DR STRING; 10116.ENSRNOP00000016237; -.
DR jPOST; Q78EG7; -.
DR PaxDb; Q78EG7; -.
DR Ensembl; ENSRNOT00000016237; ENSRNOP00000016237; ENSRNOG00000011771.
DR GeneID; 29463; -.
DR KEGG; rno:29463; -.
DR UCSC; RGD:61970; rat.
DR CTD; 7803; -.
DR RGD; 61970; Ptp4a1.
DR eggNOG; KOG2836; Eukaryota.
DR GeneTree; ENSGT00940000154406; -.
DR HOGENOM; CLU_099263_1_0_1; -.
DR InParanoid; Q78EG7; -.
DR OMA; NGQKNSC; -.
DR OrthoDB; 1398550at2759; -.
DR PhylomeDB; Q78EG7; -.
DR TreeFam; TF313384; -.
DR EvolutionaryTrace; Q78EG7; -.
DR PRO; PR:Q78EG7; -.
DR Proteomes; UP000002494; Chromosome 9.
DR Bgee; ENSRNOG00000011771; Expressed in skeletal muscle tissue and 19 other tissues.
DR Genevisible; Q78EG7; RN.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; ISO:RGD.
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; IDA:RGD.
DR GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IDA:RGD.
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:0030335; P:positive regulation of cell migration; ISO:RGD.
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 3D-structure; Cell cycle; Cell membrane; Cytoplasm; Cytoskeleton;
KW Developmental protein; Disulfide bond; Endoplasmic reticulum; Endosome;
KW Hydrolase; Lipoprotein; Membrane; Methylation; Nucleus; Prenylation;
KW Protein phosphatase; Reference proteome.
FT CHAIN 1..170
FT /note="Protein tyrosine phosphatase type IVA 1"
FT /id="PRO_0000094784"
FT PROPEP 171..173
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000396730"
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"
FT MUTAGEN 104
FT /note="C->S: Abolishes enzymatic activity."
FT /evidence="ECO:0000269|PubMed:8196618"
FT CONFLICT 170
FT /note="C -> W (in Ref. 2; AAL38661)"
FT /evidence="ECO:0000305"
FT STRAND 10..13
FT /evidence="ECO:0007829|PDB:1ZCK"
FT STRAND 18..21
FT /evidence="ECO:0007829|PDB:1ZCK"
FT TURN 27..29
FT /evidence="ECO:0007829|PDB:1ZCK"
FT HELIX 30..39
FT /evidence="ECO:0007829|PDB:1ZCK"
FT STRAND 42..47
FT /evidence="ECO:0007829|PDB:1ZCK"
FT HELIX 56..60
FT /evidence="ECO:0007829|PDB:1ZCK"
FT STRAND 64..67
FT /evidence="ECO:0007829|PDB:1ZCK"
FT STRAND 72..74
FT /evidence="ECO:0007829|PDB:3RZ2"
FT HELIX 78..94
FT /evidence="ECO:0007829|PDB:1ZCK"
FT STRAND 99..103
FT /evidence="ECO:0007829|PDB:1ZCK"
FT STRAND 105..108
FT /evidence="ECO:0007829|PDB:1ZCK"
FT TURN 109..111
FT /evidence="ECO:0007829|PDB:1ZCK"
FT HELIX 112..121
FT /evidence="ECO:0007829|PDB:1ZCK"
FT HELIX 126..134
FT /evidence="ECO:0007829|PDB:1ZCK"
FT STRAND 137..139
FT /evidence="ECO:0007829|PDB:3RZ2"
FT HELIX 143..151
FT /evidence="ECO:0007829|PDB:1ZCK"
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
