TP4A1_MOUSE
ID TP4A1_MOUSE Reviewed; 173 AA.
AC Q63739; O09097; O09154; Q3UFU9;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 168.
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 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].
RA Oh B., Hwang S.-Y., Knowles B.B.;
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Bone marrow, and Head;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Colon, 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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-23, AND DEVELOPMENTAL STAGE.
RX PubMed=10194868;
RX DOI=10.1002/(sici)1097-010x(19990501)283:6<612::aid-jez14>3.3.co;2-o;
RA Rundle C.H., Kappen C.;
RT "Developmental expression of the murine Prl-1 protein tyrosine phosphatase
RT gene.";
RL J. Exp. Zool. 283:612-617(1999).
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 INTERACTION WITH ATF5, AND MUTAGENESIS OF CYS-104.
RX PubMed=11278933; DOI=10.1074/jbc.m011562200;
RA Peters C.S., Liang X., Li S., Kannan S., Peng Y., Taub R., Diamond R.H.;
RT "ATF-7, a novel bZIP protein, interacts with the PRL-1 protein-tyrosine
RT phosphatase.";
RL J. Biol. Chem. 276:13718-13726(2001).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Liver, Lung, Pancreas, Spleen,
RC and Testis;
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. 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 tubulin (By similarity). Interacts
CC with ATF5. {ECO:0000250, ECO:0000269|PubMed:11278933}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10747914};
CC Lipid-anchor {ECO:0000269|PubMed:10747914}. Early endosome
CC {ECO:0000269|PubMed:10747914}. Endoplasmic reticulum
CC {ECO:0000269|PubMed:10747914}. Cytoplasm {ECO:0000269|PubMed:10747914}.
CC Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:10747914}. Nucleus
CC {ECO:0000250|UniProtKB:Q78EG7}. Note=And mitotic spindle.
CC -!- DEVELOPMENTAL STAGE: Expressed in all tissues except heart and skeletal
CC muscle, from 10.5 dpc to 18.5 dpc. {ECO:0000269|PubMed:10194868}.
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; U84411; AAB58913.1; -; mRNA.
DR EMBL; AK081491; BAC38233.1; -; mRNA.
DR EMBL; AK148288; BAE28460.1; -; mRNA.
DR EMBL; AK150506; BAE29619.1; -; mRNA.
DR EMBL; AK151533; BAE30480.1; -; mRNA.
DR EMBL; BC055039; AAH55039.1; -; mRNA.
DR EMBL; BC086787; AAH86787.1; -; mRNA.
DR EMBL; BC094447; AAH94447.1; -; mRNA.
DR EMBL; AF064943; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS14858.1; -.
DR RefSeq; NP_035330.1; NM_011200.2.
DR RefSeq; XP_006495861.1; XM_006495798.3.
DR RefSeq; XP_006495862.1; XM_006495799.2.
DR PDB; 5LXQ; X-ray; 3.33 A; B/C=1-173.
DR PDB; 5MMZ; X-ray; 2.40 A; B=1-173.
DR PDB; 6WUS; X-ray; 2.76 A; B=7-160.
DR PDBsum; 5LXQ; -.
DR PDBsum; 5MMZ; -.
DR PDBsum; 6WUS; -.
DR AlphaFoldDB; Q63739; -.
DR BMRB; Q63739; -.
DR SASBDB; Q63739; -.
DR SMR; Q63739; -.
DR BioGRID; 202473; 2.
DR STRING; 10090.ENSMUSP00000027232; -.
DR iPTMnet; Q63739; -.
DR PhosphoSitePlus; Q63739; -.
DR EPD; Q63739; -.
DR MaxQB; Q63739; -.
DR PaxDb; Q63739; -.
DR PRIDE; Q63739; -.
DR ProteomicsDB; 258957; -.
DR DNASU; 19243; -.
DR Ensembl; ENSMUST00000027232; ENSMUSP00000027232; ENSMUSG00000117310.
DR Ensembl; ENSMUST00000232841; ENSMUSP00000156862; ENSMUSG00000026064.
DR GeneID; 19243; -.
DR KEGG; mmu:19243; -.
DR UCSC; uc007anh.1; mouse.
DR CTD; 7803; -.
DR MGI; MGI:1277096; Ptp4a1.
DR VEuPathDB; HostDB:ENSMUSG00000026064; -.
DR VEuPathDB; HostDB:ENSMUSG00000117310; -.
DR eggNOG; KOG2836; Eukaryota.
DR GeneTree; ENSGT00940000154406; -.
DR HOGENOM; CLU_099263_1_0_1; -.
DR InParanoid; Q63739; -.
DR OMA; TTVGVHC; -.
DR OrthoDB; 1398550at2759; -.
DR PhylomeDB; Q63739; -.
DR TreeFam; TF313384; -.
DR BioGRID-ORCS; 19243; 7 hits in 53 CRISPR screens.
DR ChiTaRS; Ptp4a1; mouse.
DR PRO; PR:Q63739; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q63739; protein.
DR Bgee; ENSMUSG00000026064; Expressed in granulocyte and 76 other tissues.
DR ExpressionAtlas; Q63739; baseline and differential.
DR Genevisible; Q63739; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; ISO:MGI.
DR GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0005768; C:endosome; TAS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; TAS:UniProtKB.
DR GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR GO; GO:0004727; F:prenylated protein tyrosine phosphatase activity; TAS:UniProtKB.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; ISO:MGI.
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; IDA:UniProtKB.
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_0000094782"
FT PROPEP 171..173
FT /note="Removed in mature form"
FT /evidence="ECO:0000305"
FT /id="PRO_0000396728"
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:0000269|PubMed:11278933"
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:0000305"
FT LIPID 170
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000269|PubMed:10747914"
FT DISULFID 49..104
FT /evidence="ECO:0000250"
FT MUTAGEN 104
FT /note="C->S: Abolishes activity."
FT /evidence="ECO:0000269|PubMed:11278933"
FT STRAND 10..14
FT /evidence="ECO:0007829|PDB:5MMZ"
FT STRAND 17..22
FT /evidence="ECO:0007829|PDB:5MMZ"
FT STRAND 27..29
FT /evidence="ECO:0007829|PDB:5MMZ"
FT HELIX 30..40
FT /evidence="ECO:0007829|PDB:5MMZ"
FT STRAND 42..47
FT /evidence="ECO:0007829|PDB:5MMZ"
FT HELIX 56..60
FT /evidence="ECO:0007829|PDB:5MMZ"
FT STRAND 64..67
FT /evidence="ECO:0007829|PDB:5MMZ"
FT HELIX 78..94
FT /evidence="ECO:0007829|PDB:5MMZ"
FT STRAND 99..103
FT /evidence="ECO:0007829|PDB:5MMZ"
FT STRAND 105..109
FT /evidence="ECO:0007829|PDB:6WUS"
FT HELIX 110..121
FT /evidence="ECO:0007829|PDB:5MMZ"
FT HELIX 126..136
FT /evidence="ECO:0007829|PDB:5MMZ"
FT STRAND 137..139
FT /evidence="ECO:0007829|PDB:5LXQ"
FT HELIX 143..151
FT /evidence="ECO:0007829|PDB:5MMZ"
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
