TP4A3_MOUSE
ID TP4A3_MOUSE Reviewed; 173 AA.
AC Q9D658; O70275; Q3T9Z5; Q9CTC8;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Protein tyrosine phosphatase type IVA 3;
DE EC=3.1.3.48;
DE AltName: Full=Protein-tyrosine phosphatase 4a3;
DE AltName: Full=Protein-tyrosine phosphatase of regenerating liver 3;
DE Short=PRL-3;
DE Flags: Precursor;
GN Name=Ptp4a3; Synonyms=Prl3;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=9514946; DOI=10.1006/bbrc.1998.8291;
RA Zeng Q., Hong W., Tan Y.H.;
RT "Mouse PRL-2 and PRL-3, two potentially prenylated protein tyrosine
RT phosphatases homologous to PRL-1.";
RL Biochem. Biophys. Res. Commun. 244:421-427(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, SUBCELLULAR LOCATION,
RP ACTIVITY REGULATION, MUTAGENESIS OF ASP-72 AND CYS-104, AND FUNCTION.
RC STRAIN=C57BL/6J; TISSUE=Heart;
RX PubMed=15161639; DOI=10.1016/s0002-9440(10)63763-7;
RA Wu X., Zeng H., Zhang X., Zhao Y., Sha H., Ge X., Zhang M., Gao X., Xu Q.;
RT "Phosphatase of regenerating liver-3 promotes motility and metastasis of
RT mouse melanoma cells.";
RL Am. J. Pathol. 164:2039-2054(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Embryo, Skin, and Spleen;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain, and Eye;
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 [5]
RP ISOPRENYLATION AT CYS-170, AND SUBCELLULAR LOCATION.
RX PubMed=10747914; DOI=10.1074/jbc.m000453200;
RA Zeng Q., Si X., Horstmann H., Xu Y., Hong W., Pallen C.J.;
RT "Prenylation-dependent association of protein-tyrosine phosphatases PRL-1,
RT -2, and -3 with the plasma membrane and the early endosome.";
RL J. Biol. Chem. 275:21444-21452(2000).
RN [6]
RP INDUCTION.
RX PubMed=15673457; DOI=10.1111/j.1460-9568.2005.03855.x;
RA Magnusson C., Svensson A., Christerson U., Taagerud S.;
RT "Denervation-induced alterations in gene expression in mouse skeletal
RT muscle.";
RL Eur. J. Neurosci. 21:577-580(2005).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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.
CC {ECO:0000269|PubMed:15161639}.
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.
CC {ECO:0000269|PubMed:15161639}.
CC -!- SUBUNIT: Interacts with tubulin. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane. Early endosome.
CC -!- TISSUE SPECIFICITY: Present in the small intestine, where it is located
CC in the differentiated epithelial cells of the villus but not in the
CC proliferating crypt cells (at protein level). Expressed in heart and
CC skeletal muscle, and at lower levels in lung, spleen and testis.
CC {ECO:0000269|PubMed:15161639, ECO:0000269|PubMed:9514946}.
CC -!- INDUCTION: Down-regulated upon skeletal muscle denervation.
CC {ECO:0000269|PubMed:15673457}.
CC -!- PTM: Farnesylated. Farnesylation is required for membrane targeting.
CC Unfarnesylated forms are shifted into the nucleus.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC {ECO:0000305}.
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DR EMBL; AF035645; AAC15875.1; -; mRNA.
DR EMBL; AK003954; BAB23091.1; -; mRNA.
DR EMBL; AK014601; BAB29456.1; -; mRNA.
DR EMBL; AK143702; BAE25506.1; -; mRNA.
DR EMBL; AK172192; BAE42875.1; -; mRNA.
DR EMBL; BC027445; AAH27445.1; -; mRNA.
DR EMBL; BC066043; AAH66043.1; -; mRNA.
DR CCDS; CCDS27519.1; -.
DR PIR; JC5982; JC5982.
DR RefSeq; NP_001159860.1; NM_001166388.1.
DR RefSeq; NP_001159861.1; NM_001166389.1.
DR RefSeq; NP_001159862.1; NM_001166390.1.
DR RefSeq; NP_033001.2; NM_008975.3.
DR RefSeq; XP_006520703.1; XM_006520640.3.
DR RefSeq; XP_006520705.1; XM_006520642.1.
DR RefSeq; XP_011243825.1; XM_011245523.1.
DR AlphaFoldDB; Q9D658; -.
DR SMR; Q9D658; -.
DR STRING; 10090.ENSMUSP00000131281; -.
DR ChEMBL; CHEMBL4523445; -.
DR iPTMnet; Q9D658; -.
DR PhosphoSitePlus; Q9D658; -.
DR SwissPalm; Q9D658; -.
DR MaxQB; Q9D658; -.
DR PaxDb; Q9D658; -.
DR PRIDE; Q9D658; -.
DR ProteomicsDB; 259160; -.
DR Antibodypedia; 27728; 350 antibodies from 35 providers.
DR DNASU; 19245; -.
DR Ensembl; ENSMUST00000053232; ENSMUSP00000060956; ENSMUSG00000059895.
DR Ensembl; ENSMUST00000163582; ENSMUSP00000131281; ENSMUSG00000059895.
DR Ensembl; ENSMUST00000165541; ENSMUSP00000132097; ENSMUSG00000059895.
DR Ensembl; ENSMUST00000230177; ENSMUSP00000154829; ENSMUSG00000059895.
DR GeneID; 19245; -.
DR KEGG; mmu:19245; -.
DR UCSC; uc007wcj.1; mouse.
DR CTD; 11156; -.
DR MGI; MGI:1277098; Ptp4a3.
DR VEuPathDB; HostDB:ENSMUSG00000059895; -.
DR eggNOG; KOG2836; Eukaryota.
DR GeneTree; ENSGT00940000159581; -.
DR HOGENOM; CLU_099263_1_0_1; -.
DR InParanoid; Q9D658; -.
DR OMA; KYRPRQR; -.
DR OrthoDB; 1398550at2759; -.
DR PhylomeDB; Q9D658; -.
DR TreeFam; TF313384; -.
DR BioGRID-ORCS; 19245; 1 hit in 73 CRISPR screens.
DR PRO; PR:Q9D658; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q9D658; protein.
DR Bgee; ENSMUSG00000059895; Expressed in hindlimb stylopod muscle and 266 other tissues.
DR ExpressionAtlas; Q9D658; baseline and differential.
DR Genevisible; Q9D658; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
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; IEP:MGI.
DR GO; GO:0043542; P:endothelial cell migration; IMP:MGI.
DR GO; GO:0007219; P:Notch signaling pathway; IDA:MGI.
DR GO; GO:1904951; P:positive regulation of establishment of protein localization; ISO:MGI.
DR GO; GO:1901224; P:positive regulation of NIK/NF-kappaB signaling; ISO:MGI.
DR GO; GO:0043117; P:positive regulation of vascular permeability; IMP:MGI.
DR GO; GO:0006470; P:protein dephosphorylation; IEA:InterPro.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:1900746; P:regulation of vascular endothelial growth factor signaling pathway; IMP:MGI.
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 1: Evidence at protein 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_0000094789"
FT PROPEP 171..173
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000396655"
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"
FT MUTAGEN 72
FT /note="D->A: Loss of enzymatic activity; reduced migration-
FT promoting activity."
FT /evidence="ECO:0000269|PubMed:15161639"
FT MUTAGEN 104
FT /note="C->S: Loss of enzymatic activity; reduced migration-
FT promoting activity."
FT /evidence="ECO:0000269|PubMed:15161639"
FT CONFLICT 101
FT /note="A -> L (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 173 AA; 19652 MW; 262718AA2040F126 CRC64;
MARMNRPAPV EVSYRHMRFL ITHNPSNATL STFIEDLKKY GATTVVRVCE VTYDKTPLEK
DGITVVDWPF DDGAPPPGKV VEDWLSLLKA KFYNDPGSCV AVHCVAGLGR APVLVALALI
ESGMKYEDAI QFIRQKRRGA INSKQLTYLE KYRPKQRLRF KDPHTHKTRC CVM
