TP4A2_RAT
ID TP4A2_RAT Reviewed; 167 AA.
AC Q6P9X4; O88765;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Protein tyrosine phosphatase type IVA 2;
DE EC=3.1.3.48;
DE AltName: Full=Protein-tyrosine phosphatase 4a2;
DE AltName: Full=Protein-tyrosine phosphatase of regenerating liver 2;
DE Short=PRL-2;
DE Flags: Precursor;
GN Name=Ptp4a2; Synonyms=Prl2;
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], AND TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley; TISSUE=Pituitary anterior lobe;
RX PubMed=9805001; DOI=10.1016/s0167-4781(98)00173-0;
RA Carter D.A.;
RT "Expression of a novel rat protein tyrosine phosphatase gene.";
RL Biochim. Biophys. Acta 1442:405-408(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pituitary;
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).
CC -!- FUNCTION: Protein tyrosine phosphatase which stimulates progression
CC from G1 into S phase during mitosis. Inhibits geranylgeranyl
CC transferase type II activity by blocking the association between
CC RABGGTA and RABGGTB (By 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 pentamidine.
CC {ECO:0000250}.
CC -!- SUBUNIT: In contrast to PTP4A1 and PTP4A3, does not interact with
CC tubulin. Interacts with RABGGTB (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}. Early endosome
CC {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Anterior pituitary, liver, brain, adrenal gland,
CC kidney, testis and heart. Expression in the anterior pituitary is 3
CC fold higher in male as compared to female.
CC {ECO:0000269|PubMed:9805001}.
CC -!- PTM: Farnesylated. Farnesylation is required for membrane targeting and
CC for interaction with RABGGTB (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC {ECO:0000305}.
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DR EMBL; AJ007016; CAA07417.1; -; mRNA.
DR EMBL; BC060549; AAH60549.1; -; mRNA.
DR RefSeq; NP_445927.1; NM_053475.1.
DR RefSeq; XP_017449153.1; XM_017593664.1.
DR RefSeq; XP_017449154.1; XM_017593665.1.
DR AlphaFoldDB; Q6P9X4; -.
DR BMRB; Q6P9X4; -.
DR SMR; Q6P9X4; -.
DR IntAct; Q6P9X4; 1.
DR STRING; 10116.ENSRNOP00000064832; -.
DR iPTMnet; Q6P9X4; -.
DR PhosphoSitePlus; Q6P9X4; -.
DR jPOST; Q6P9X4; -.
DR PaxDb; Q6P9X4; -.
DR Ensembl; ENSRNOT00000074415; ENSRNOP00000064832; ENSRNOG00000050044.
DR GeneID; 85237; -.
DR KEGG; rno:85237; -.
DR CTD; 8073; -.
DR RGD; 619786; Ptp4a2.
DR eggNOG; KOG2836; Eukaryota.
DR GeneTree; ENSGT00940000154383; -.
DR HOGENOM; CLU_099263_2_0_1; -.
DR InParanoid; Q6P9X4; -.
DR OMA; IQVHGWT; -.
DR OrthoDB; 1398550at2759; -.
DR PhylomeDB; Q6P9X4; -.
DR Reactome; R-RNO-8873719; RAB geranylgeranylation.
DR PRO; PR:Q6P9X4; -.
DR Proteomes; UP000002494; Chromosome 5.
DR Bgee; ENSRNOG00000050044; Expressed in quadriceps femoris and 19 other tissues.
DR Genevisible; Q6P9X4; RN.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
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: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 membrane; Cytoplasm; Disulfide bond; Endosome; Hydrolase; Lipoprotein;
KW Membrane; Methylation; Prenylation; Protein phosphatase;
KW Reference proteome.
FT CHAIN 1..164
FT /note="Protein tyrosine phosphatase type IVA 2"
FT /id="PRO_0000094787"
FT PROPEP 165..167
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000396733"
FT DOMAIN 5..158
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT ACT_SITE 69
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 101
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT BINDING 102..107
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000250"
FT BINDING 107
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 164
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250"
FT LIPID 164
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000250"
FT DISULFID 46..101
FT /evidence="ECO:0000250"
FT CONFLICT 23
FT /note="T -> A (in Ref. 1; CAA07417)"
FT /evidence="ECO:0000305"
FT CONFLICT 157
FT /note="F -> S (in Ref. 1; CAA07417)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 167 AA; 19127 MW; E97B88BF87B87943 CRC64;
MNRPAPVEIS YENMRFLITH NPTNATLNKF TEELKKYGVT TLVRVCDATY DKAPVEKEGI
HVLDWPFDDG APPPNQIVDD WLNLLKTKFR EEPGCCVAVH CVAGLGRAPV LVALALIECG
MKYEDAVQFI RQKRRGAFNS KQLLYLEKYR PKMRLRFRDT NGHCCVQ
