TP4A1_HUMAN
ID TP4A1_HUMAN Reviewed; 173 AA.
AC Q93096; B2R6C8; O00648; Q49A54;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 2.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Protein tyrosine phosphatase type IVA 1;
DE EC=3.1.3.48 {ECO:0000269|PubMed:9018080};
DE AltName: Full=PTP(CAAXI);
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, PTPCAAX1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, AND ISOPRENYLATION AT
RP CYS-170.
RC TISSUE=Mammary carcinoma;
RX PubMed=9018080; DOI=10.1016/s0304-3835(96)04459-x;
RA Cates C.A., Michael R.L., Stayrook K.R., Harvey K.A., Burke Y.D.,
RA Randall S.K., Crowell P.L., Crowell D.N.;
RT "Prenylation of oncogenic human PTP(CAAX) protein tyrosine phosphatases.";
RL Cancer Lett. 110:49-55(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Regenerating liver;
RX PubMed=9642300; DOI=10.1074/jbc.273.27.17286;
RA Peng Y., Genin A., Spinner N.B., Diamond R.H., Taub R.;
RT "The gene encoding human nuclear protein tyrosine phosphatase, PRL-1.
RT Cloning, chromosomal localization, and identification of an intron
RT enhancer.";
RL J. Biol. Chem. 273:17286-17295(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Thalamus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Fetal liver;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Muscle, and Testis;
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 [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 80-163.
RC TISSUE=Lung fibroblast;
RX PubMed=9633825;
RA Dayton M.A., Knobloch T.J.;
RT "Multiple phosphotyrosine phosphatase mRNAs are expressed in the human lung
RT fibroblast cell line WI-38.";
RL Recept. Signal Transduct. 7:241-256(1997).
RN [9]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=10940933;
RX DOI=10.1002/1521-4141(2000)30:8<2412::aid-immu2412>3.0.co;2-j;
RA Gjoerloff-Wingren A., Saxena M., Han S., Wang X., Alonso A., Renedo M.,
RA Oh P., Williams S., Schnitzer J., Mustelin T.;
RT "Subcellular localization of intracellular protein tyrosine phosphatases in
RT T cells.";
RL Eur. J. Immunol. 30:2412-2421(2000).
RN [10]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MUTAGENESIS OF ASP-71; ASP-72;
RP CYS-104; CYS-170 AND CYS-171, INTERACTION WITH TUBULIN, AND FUNCTION.
RX PubMed=12235145; DOI=10.1074/jbc.m206407200;
RA Wang J., Kirby C.E., Herbst R.;
RT "The tyrosine phosphatase PRL-1 localizes to the endoplasmic reticulum and
RT the mitotic spindle and is required for normal mitosis.";
RL J. Biol. Chem. 277:46659-46668(2002).
RN [11]
RP ACTIVITY REGULATION.
RX PubMed=12516958;
RA Pathak M.K., Dhawan D., Lindner D.J., Borden E.C., Farver C., Yi T.;
RT "Pentamidine is an inhibitor of PRL phosphatases with anticancer
RT activity.";
RL Mol. Cancer Ther. 1:1255-1264(2002).
RN [12]
RP FUNCTION.
RX PubMed=14643450; DOI=10.1016/s0304-3835(03)00517-2;
RA Werner S.R., Lee P.A., DeCamp M.W., Crowell D.N., Randall S.K.,
RA Crowell P.L.;
RT "Enhanced cell cycle progression and down regulation of p21(Cip1/Waf1) by
RT PRL tyrosine phosphatases.";
RL Cancer Lett. 202:201-211(2003).
RN [13]
RP FUNCTION.
RX PubMed=12782572;
RA Zeng Q., Dong J.-M., Guo K., Li J., Tan H.-X., Koh V., Pallen C.J.,
RA Manser E., Hong W.;
RT "PRL-3 and PRL-1 promote cell migration, invasion, and metastasis.";
RL Cancer Res. 63:2716-2722(2003).
RN [14]
RP INDUCTION.
RX PubMed=15501285; DOI=10.1016/j.toxicon.2004.07.018;
RA Raghavendra Prasad H.S., Qi Z., Srinivasan K.N., Gopalakrishnakone P.;
RT "Potential effects of tetrodotoxin exposure to human glial cells postulated
RT using microarray approach.";
RL Toxicon 44:597-608(2004).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF MUTANT SER-104, DISULFIDE BOND,
RP SUBCELLULAR LOCATION, SUBUNIT, MUTAGENESIS OF THR-13 AND GLN-131, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=15571731; DOI=10.1016/j.jmb.2004.10.061;
RA Jeong D.G., Kim S.J., Kim J.H., Son J.H., Park M.R., Lim S.M., Yoon T.-S.,
RA Ryu S.E.;
RT "Trimeric structure of PRL-1 phosphatase reveals an active enzyme
RT conformation and regulation mechanisms.";
RL J. Mol. Biol. 345:401-413(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. Enhances cell
CC proliferation, cell motility and invasive activity, and promotes cancer
CC metastasis. {ECO:0000269|PubMed:12235145, ECO:0000269|PubMed:12782572,
CC ECO:0000269|PubMed:14643450}.
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:9018080};
CC -!- ACTIVITY REGULATION: Inhibited by sodium orthovanadate and pentamidine.
CC {ECO:0000269|PubMed:12516958}.
CC -!- SUBUNIT: Homotrimer. Interacts with ATF5 (By similarity). Interacts
CC with tubulin. {ECO:0000250, ECO:0000269|PubMed:12235145,
CC ECO:0000269|PubMed:15571731}.
CC -!- INTERACTION:
CC Q93096; Q9NRU3: CNNM1; NbExp=6; IntAct=EBI-1058467, EBI-11986439;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10940933,
CC ECO:0000269|PubMed:15571731}; Lipid-anchor
CC {ECO:0000269|PubMed:10940933, ECO:0000269|PubMed:12235145,
CC ECO:0000269|PubMed:15571731}. Early endosome
CC {ECO:0000269|PubMed:12235145}. Endoplasmic reticulum
CC {ECO:0000269|PubMed:12235145}. Cytoplasm {ECO:0000269|PubMed:12235145}.
CC Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:12235145}. Nucleus
CC {ECO:0000250|UniProtKB:Q78EG7}. Note=And mitotic spindle.
CC {ECO:0000269|PubMed:12235145}.
CC -!- TISSUE SPECIFICITY: Expressed in bone marrow, lymph nodes, T
CC lymphocytes, spleen, thymus and tonsil. Overexpressed in tumor cell
CC lines. {ECO:0000269|PubMed:10940933, ECO:0000269|PubMed:12235145}.
CC -!- DEVELOPMENTAL STAGE: Expressed in fetal liver.
CC {ECO:0000269|PubMed:10940933}.
CC -!- INDUCTION: Strongly down-regulated upon tetrodotoxin treatment.
CC {ECO:0000269|PubMed:15501285}.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U48296; AAB40597.1; -; mRNA.
DR EMBL; AF051160; AAC39836.1; -; Genomic_DNA.
DR EMBL; AK312526; BAG35425.1; -; mRNA.
DR EMBL; CR749458; CAH18292.1; -; mRNA.
DR EMBL; AL135905; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471143; EAW88494.1; -; Genomic_DNA.
DR EMBL; BC023975; AAH23975.1; -; mRNA.
DR EMBL; BC045571; AAH45571.1; -; mRNA.
DR EMBL; U69701; AAB09080.1; -; mRNA.
DR CCDS; CCDS4965.1; -.
DR RefSeq; NP_003454.1; NM_003463.4.
DR RefSeq; XP_011534413.1; XM_011536111.1.
DR RefSeq; XP_011534414.1; XM_011536112.1.
DR RefSeq; XP_016866759.1; XM_017011270.1.
DR RefSeq; XP_016866760.1; XM_017011271.1.
DR PDB; 1RXD; X-ray; 1.90 A; A/B/C=2-160.
DR PDB; 1XM2; X-ray; 2.70 A; A/B/C/D/E/F=1-173.
DR PDB; 5BX1; X-ray; 1.90 A; A=4-160.
DR PDBsum; 1RXD; -.
DR PDBsum; 1XM2; -.
DR PDBsum; 5BX1; -.
DR AlphaFoldDB; Q93096; -.
DR BMRB; Q93096; -.
DR SMR; Q93096; -.
DR BioGRID; 113578; 109.
DR IntAct; Q93096; 27.
DR MINT; Q93096; -.
DR BindingDB; Q93096; -.
DR ChEMBL; CHEMBL1075169; -.
DR DEPOD; PTP4A1; -.
DR iPTMnet; Q93096; -.
DR PhosphoSitePlus; Q93096; -.
DR SwissPalm; Q93096; -.
DR BioMuta; PTP4A1; -.
DR DMDM; 68566217; -.
DR EPD; Q93096; -.
DR jPOST; Q93096; -.
DR MassIVE; Q93096; -.
DR MaxQB; Q93096; -.
DR PaxDb; Q93096; -.
DR PeptideAtlas; Q93096; -.
DR PRIDE; Q93096; -.
DR ProteomicsDB; 75721; -.
DR Antibodypedia; 1094; 287 antibodies from 34 providers.
DR DNASU; 7803; -.
DR Ensembl; ENST00000626021.3; ENSP00000485687.1; ENSG00000112245.13.
DR Ensembl; ENST00000648894.1; ENSP00000497588.1; ENSG00000112245.13.
DR Ensembl; ENST00000672924.1; ENSP00000500952.1; ENSG00000112245.13.
DR Ensembl; ENST00000673199.1; ENSP00000500859.1; ENSG00000112245.13.
DR GeneID; 7803; -.
DR KEGG; hsa:7803; -.
DR MANE-Select; ENST00000626021.3; ENSP00000485687.1; NM_003463.5; NP_003454.1.
DR UCSC; uc003pel.5; human.
DR CTD; 7803; -.
DR DisGeNET; 7803; -.
DR GeneCards; PTP4A1; -.
DR HGNC; HGNC:9634; PTP4A1.
DR HPA; ENSG00000112245; Tissue enhanced (liver).
DR MIM; 601585; gene.
DR neXtProt; NX_Q93096; -.
DR OpenTargets; ENSG00000112245; -.
DR PharmGKB; PA33977; -.
DR VEuPathDB; HostDB:ENSG00000112245; -.
DR eggNOG; KOG2836; Eukaryota.
DR GeneTree; ENSGT00940000154406; -.
DR HOGENOM; CLU_099263_1_0_1; -.
DR InParanoid; Q93096; -.
DR OMA; NGQKNSC; -.
DR OrthoDB; 1398550at2759; -.
DR PhylomeDB; Q93096; -.
DR TreeFam; TF313384; -.
DR BRENDA; 3.1.3.16; 2681.
DR PathwayCommons; Q93096; -.
DR SignaLink; Q93096; -.
DR SIGNOR; Q93096; -.
DR BioGRID-ORCS; 7803; 118 hits in 1048 CRISPR screens.
DR ChiTaRS; PTP4A1; human.
DR EvolutionaryTrace; Q93096; -.
DR GeneWiki; PTP4A1; -.
DR GenomeRNAi; 7803; -.
DR Pharos; Q93096; Tchem.
DR PRO; PR:Q93096; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q93096; protein.
DR Bgee; ENSG00000112245; Expressed in adrenal tissue and 101 other tissues.
DR ExpressionAtlas; Q93096; baseline and differential.
DR Genevisible; Q93096; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; IDA:UniProtKB.
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; IBA:GO_Central.
DR GO; GO:0005819; C:spindle; 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:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0030335; P:positive regulation of cell migration; IBA:GO_Central.
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_0000094780"
FT PROPEP 171..173
FT /note="Removed in mature form"
FT /evidence="ECO:0000305"
FT /id="PRO_0000396726"
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:0000305"
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 BINDING 110
FT /ligand="substrate"
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:9018080"
FT DISULFID 49..104
FT /evidence="ECO:0000269|PubMed:15571731"
FT MUTAGEN 13
FT /note="T->F: Reduces trimerization."
FT /evidence="ECO:0000269|PubMed:15571731"
FT MUTAGEN 71
FT /note="D->A: No effect on catalytic activity."
FT /evidence="ECO:0000269|PubMed:12235145"
FT MUTAGEN 72
FT /note="D->A: 80% loss of catalytic activity; delay in
FT progression through G2/M."
FT /evidence="ECO:0000269|PubMed:12235145"
FT MUTAGEN 104
FT /note="C->S: Abolishes enzymatic activity."
FT /evidence="ECO:0000269|PubMed:12235145"
FT MUTAGEN 131
FT /note="Q->A: Reduces trimerization."
FT /evidence="ECO:0000269|PubMed:15571731"
FT MUTAGEN 170
FT /note="C->S: Redistributes to the nucleus in resting cells,
FT but still locates to the mitotic spindle in dividing cells.
FT Induces defects in cytokinesis."
FT /evidence="ECO:0000269|PubMed:12235145"
FT MUTAGEN 171
FT /note="C->S: No effect on subcellular location."
FT /evidence="ECO:0000269|PubMed:12235145"
FT STRAND 10..14
FT /evidence="ECO:0007829|PDB:1RXD"
FT STRAND 17..21
FT /evidence="ECO:0007829|PDB:1RXD"
FT HELIX 27..29
FT /evidence="ECO:0007829|PDB:1RXD"
FT HELIX 30..39
FT /evidence="ECO:0007829|PDB:1RXD"
FT STRAND 42..47
FT /evidence="ECO:0007829|PDB:1RXD"
FT HELIX 56..60
FT /evidence="ECO:0007829|PDB:1RXD"
FT STRAND 64..67
FT /evidence="ECO:0007829|PDB:1RXD"
FT STRAND 72..74
FT /evidence="ECO:0007829|PDB:1XM2"
FT HELIX 78..94
FT /evidence="ECO:0007829|PDB:1RXD"
FT STRAND 99..103
FT /evidence="ECO:0007829|PDB:1RXD"
FT STRAND 105..108
FT /evidence="ECO:0007829|PDB:1RXD"
FT TURN 109..111
FT /evidence="ECO:0007829|PDB:1RXD"
FT HELIX 112..121
FT /evidence="ECO:0007829|PDB:1RXD"
FT HELIX 126..134
FT /evidence="ECO:0007829|PDB:1RXD"
FT HELIX 143..151
FT /evidence="ECO:0007829|PDB:1RXD"
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
