ID PTN3_HUMAN Reviewed; 913 AA. AC P26045; A0AUW9; E7EN99; E9PGU7; DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot. DT 05-MAY-2009, sequence version 2. DT 24-JAN-2024, entry version 215. DE RecName: Full=Tyrosine-protein phosphatase non-receptor type 3; DE EC=3.1.3.48; DE AltName: Full=Protein-tyrosine phosphatase H1; DE Short=PTP-H1; GN Name=PTPN3; Synonyms=PTPH1; 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] (ISOFORM 1), AND VARIANT PRO-90. RX PubMed=1648725; DOI=10.1073/pnas.88.14.5949; RA Yang Q., Tonks N.K.; RT "Isolation of a cDNA clone encoding a human protein-tyrosine phosphatase RT with homology to the cytoskeletal-associated proteins band 4.1, ezrin, and RT talin."; RL Proc. Natl. Acad. Sci. U.S.A. 88:5949-5953(1991). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3). RC TISSUE=Fetal kidney, and Testis; 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15164053; DOI=10.1038/nature02465; RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., RA Dunham I.; RT "DNA sequence and analysis of human chromosome 9."; RL Nature 429:369-374(2004). RN [4] 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 [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Brain; 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 [6] RP NUCLEOTIDE SEQUENCE [MRNA] OF 194-896 (ISOFORM 1). RC TISSUE=Colon; RX PubMed=1626183; DOI=10.1159/000217763; RA Arimura Y., Hinoda Y., Itoh F., Takekawa M., Tsujisaki M., Adachi M., RA Imai K., Yachi A.; RT "cDNA cloning of new protein tyrosine phosphatases in the human colon."; RL Tumor Biol. 13:180-186(1992). RN [7] RP NUCLEOTIDE SEQUENCE [MRNA] OF 899-913 (ISOFORM 1). RX PubMed=7874267; DOI=10.1007/bf02349278; RA Ikuta S., Itoh F., Hinoda Y., Toyota M., Makiguchi Y., Imai K., Yachi A.; RT "Expression of cytoskeletal-associated protein tyrosine phosphatase PTPH1 RT mRNA in human hepatocellular carcinoma."; RL J. Gastroenterol. 29:727-732(1994). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-359; SER-367; THR-376 AND RP SER-381, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-357 AND SER-359, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-425, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [11] RP X-RAY CRYSTALLOGRAPHY (1.54 ANGSTROMS) OF 628-913. RX PubMed=19167335; DOI=10.1016/j.cell.2008.11.038; RA Barr A.J., Ugochukwu E., Lee W.H., King O.N.F., Filippakopoulos P., RA Alfano I., Savitsky P., Burgess-Brown N.A., Mueller S., Knapp S.; RT "Large-scale structural analysis of the classical human protein tyrosine RT phosphatome."; RL Cell 136:352-363(2009). CC -!- FUNCTION: May act at junctions between the membrane and the CC cytoskeleton. Possesses tyrosine phosphatase activity. 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; Evidence={ECO:0000255|PROSITE- CC ProRule:PRU10044}; CC -!- INTERACTION: CC P26045; Q04828: AKR1C1; NbExp=6; IntAct=EBI-1047946, EBI-2116455; CC P26045; Q14689-6: DIP2A; NbExp=3; IntAct=EBI-1047946, EBI-10233719; CC P26045; P42566-1: EPS15; NbExp=4; IntAct=EBI-1047946, EBI-15895294; CC P26045; P10912: GHR; NbExp=4; IntAct=EBI-1047946, EBI-286316; CC P26045; P25800: LMO1; NbExp=6; IntAct=EBI-1047946, EBI-8639312; CC P26045; P23508: MCC; NbExp=2; IntAct=EBI-1047946, EBI-307531; CC P26045; P40692: MLH1; NbExp=3; IntAct=EBI-1047946, EBI-744248; CC P26045; Q96QG7: MTMR9; NbExp=3; IntAct=EBI-1047946, EBI-744593; CC P26045; Q9NPJ8: NXT2; NbExp=3; IntAct=EBI-1047946, EBI-752122; CC P26045; Q9H8W4: PLEKHF2; NbExp=3; IntAct=EBI-1047946, EBI-742388; CC P26045; Q14524: SCN5A; NbExp=2; IntAct=EBI-1047946, EBI-726858; CC P26045; P31040: SDHA; NbExp=2; IntAct=EBI-1047946, EBI-1057265; CC P26045; Q6ZRS2-3: SRCAP; NbExp=3; IntAct=EBI-1047946, EBI-12029182; CC P26045; Q8NEK8: TENT5D; NbExp=3; IntAct=EBI-1047946, EBI-744726; CC P26045; Q01664: TFAP4; NbExp=3; IntAct=EBI-1047946, EBI-2514218; CC P26045; Q8WV44: TRIM41; NbExp=3; IntAct=EBI-1047946, EBI-725997; CC P26045; Q8TAA9: VANGL1; NbExp=4; IntAct=EBI-1047946, EBI-682393; CC P26045; Q9ULK5: VANGL2; NbExp=2; IntAct=EBI-1047946, EBI-1054279; CC P26045; P55072: VCP; NbExp=2; IntAct=EBI-1047946, EBI-355164; CC P26045; P11473: VDR; NbExp=4; IntAct=EBI-1047946, EBI-286357; CC P26045; Q5GFL6-3: VWA2; NbExp=3; IntAct=EBI-1047946, EBI-13451145; CC P26045; Q9NNW5: WDR6; NbExp=6; IntAct=EBI-1047946, EBI-1568315; CC P26045; P31946: YWHAB; NbExp=6; IntAct=EBI-1047946, EBI-359815; CC P26045; P61981: YWHAG; NbExp=6; IntAct=EBI-1047946, EBI-359832; CC P26045; P63104: YWHAZ; NbExp=5; IntAct=EBI-1047946, EBI-347088; CC P26045; Q8TBK6: ZCCHC10; NbExp=3; IntAct=EBI-1047946, EBI-597063; CC P26045; P06463: E6; Xeno; NbExp=4; IntAct=EBI-1047946, EBI-1186926; CC -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein; CC Cytoplasmic side. Cytoplasm, cytoskeleton. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=P26045-1; Sequence=Displayed; CC Name=2; CC IsoId=P26045-2; Sequence=VSP_046309; CC Name=3; CC IsoId=P26045-3; Sequence=VSP_046309, VSP_046310; CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non- CC receptor class subfamily. {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; M64572; AAA35647.1; -; mRNA. DR EMBL; BX648253; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; BX648735; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; AL359963; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL450025; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL162733; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471105; EAW59046.1; -; Genomic_DNA. DR EMBL; BC126117; AAI26118.1; -; mRNA. DR EMBL; S39392; AAB22439.2; -; mRNA. DR EMBL; S76309; AAB33583.1; -; mRNA. DR CCDS; CCDS48000.1; -. [P26045-3] DR CCDS; CCDS48001.1; -. [P26045-2] DR CCDS; CCDS6776.1; -. [P26045-1] DR PIR; A41109; A41109. DR RefSeq; NP_001138840.1; NM_001145368.1. DR RefSeq; NP_001138841.1; NM_001145369.1. [P26045-2] DR RefSeq; NP_001138842.1; NM_001145370.1. [P26045-3] DR RefSeq; NP_001138843.1; NM_001145371.1. DR RefSeq; NP_002820.3; NM_002829.3. [P26045-1] DR RefSeq; XP_006717262.1; XM_006717199.3. [P26045-1] DR RefSeq; XP_006717267.1; XM_006717204.3. DR RefSeq; XP_011517191.1; XM_011518889.2. DR RefSeq; XP_016870444.1; XM_017014955.1. [P26045-1] DR RefSeq; XP_016870446.1; XM_017014957.1. DR PDB; 2B49; X-ray; 1.54 A; A=628-913. DR PDB; 4QUM; X-ray; 2.52 A; A=628-909. DR PDB; 4QUN; X-ray; 1.86 A; A/B=628-909. DR PDB; 4RH5; X-ray; 1.60 A; A=628-909. DR PDB; 4RH9; X-ray; 1.60 A; A=628-909. DR PDB; 4RHG; X-ray; 1.58 A; A=628-909. DR PDB; 4RI4; X-ray; 1.60 A; A/B=628-909. DR PDB; 4RI5; X-ray; 1.26 A; A/B=628-909. DR PDB; 4S0G; X-ray; 1.72 A; A=628-909. DR PDB; 6HKS; X-ray; 2.19 A; A/B/C/D/E/F=489-597. DR PDB; 6T36; X-ray; 1.86 A; A=1-913. DR PDB; 8CQY; X-ray; 1.70 A; A=489-597. DR PDB; 8OEP; X-ray; 1.87 A; A/C=489-597. DR PDBsum; 2B49; -. DR PDBsum; 4QUM; -. DR PDBsum; 4QUN; -. DR PDBsum; 4RH5; -. DR PDBsum; 4RH9; -. DR PDBsum; 4RHG; -. DR PDBsum; 4RI4; -. DR PDBsum; 4RI5; -. DR PDBsum; 4S0G; -. DR PDBsum; 6HKS; -. DR PDBsum; 6T36; -. DR PDBsum; 8CQY; -. DR PDBsum; 8OEP; -. DR AlphaFoldDB; P26045; -. DR SMR; P26045; -. DR BioGRID; 111740; 93. DR DIP; DIP-38839N; -. DR IntAct; P26045; 57. DR MINT; P26045; -. DR STRING; 9606.ENSP00000363667; -. DR BindingDB; P26045; -. DR ChEMBL; CHEMBL2396509; -. DR DEPOD; PTPN3; -. DR iPTMnet; P26045; -. DR PhosphoSitePlus; P26045; -. DR BioMuta; PTPN3; -. DR DMDM; 229462761; -. DR EPD; P26045; -. DR jPOST; P26045; -. DR MassIVE; P26045; -. DR MaxQB; P26045; -. DR PaxDb; 9606-ENSP00000363667; -. DR PeptideAtlas; P26045; -. DR ProteomicsDB; 17113; -. DR ProteomicsDB; 20397; -. DR ProteomicsDB; 54312; -. [P26045-1] DR Pumba; P26045; -. DR Antibodypedia; 29434; 273 antibodies from 33 providers. DR DNASU; 5774; -. DR Ensembl; ENST00000374541.4; ENSP00000363667.1; ENSG00000070159.14. [P26045-1] DR Ensembl; ENST00000412145.5; ENSP00000416654.1; ENSG00000070159.14. [P26045-2] DR Ensembl; ENST00000446349.5; ENSP00000395384.1; ENSG00000070159.14. [P26045-3] DR GeneID; 5774; -. DR KEGG; hsa:5774; -. DR MANE-Select; ENST00000374541.4; ENSP00000363667.1; NM_002829.4; NP_002820.3. DR UCSC; uc004beb.2; human. [P26045-1] DR AGR; HGNC:9655; -. DR CTD; 5774; -. DR DisGeNET; 5774; -. DR GeneCards; PTPN3; -. DR HGNC; HGNC:9655; PTPN3. DR HPA; ENSG00000070159; Tissue enhanced (skeletal muscle, tongue). DR MalaCards; PTPN3; -. DR MIM; 176877; gene. DR neXtProt; NX_P26045; -. DR OpenTargets; ENSG00000070159; -. DR Orphanet; 70567; Cholangiocarcinoma. DR PharmGKB; PA33999; -. DR VEuPathDB; HostDB:ENSG00000070159; -. DR eggNOG; KOG0792; Eukaryota. DR GeneTree; ENSGT00940000157888; -. DR HOGENOM; CLU_001645_7_1_1; -. DR InParanoid; P26045; -. DR OMA; GIFHIRC; -. DR OrthoDB; 5345383at2759; -. DR PhylomeDB; P26045; -. DR TreeFam; TF315900; -. DR BRENDA; 3.1.3.48; 2681. DR PathwayCommons; P26045; -. DR Reactome; R-HSA-182971; EGFR downregulation. DR Reactome; R-HSA-5675221; Negative regulation of MAPK pathway. DR SignaLink; P26045; -. DR SIGNOR; P26045; -. DR BioGRID-ORCS; 5774; 18 hits in 1165 CRISPR screens. DR ChiTaRS; PTPN3; human. DR EvolutionaryTrace; P26045; -. DR GeneWiki; PTPN3; -. DR GenomeRNAi; 5774; -. DR Pharos; P26045; Tbio. DR PRO; PR:P26045; -. DR Proteomes; UP000005640; Chromosome 9. DR RNAct; P26045; Protein. DR Bgee; ENSG00000070159; Expressed in oocyte and 189 other cell types or tissues. DR ExpressionAtlas; P26045; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; IDA:UniProtKB. DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0051117; F:ATPase binding; IPI:BHF-UCL. DR GO; GO:0008092; F:cytoskeletal protein binding; IEA:InterPro. DR GO; GO:0001784; F:phosphotyrosine residue binding; IPI:BHF-UCL. DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IDA:UniProtKB. DR GO; GO:0017080; F:sodium channel regulator activity; IDA:BHF-UCL. DR GO; GO:0097421; P:liver regeneration; IEA:Ensembl. DR GO; GO:0000165; P:MAPK cascade; TAS:Reactome. DR GO; GO:0042059; P:negative regulation of epidermal growth factor receptor signaling pathway; TAS:Reactome. DR GO; GO:0051045; P:negative regulation of membrane protein ectodomain proteolysis; IMP:BHF-UCL. DR GO; GO:0045930; P:negative regulation of mitotic cell cycle; IDA:BHF-UCL. DR GO; GO:0006470; P:protein dephosphorylation; IDA:BHF-UCL. DR GO; GO:0098902; P:regulation of membrane depolarization during action potential; IDA:BHF-UCL. DR GO; GO:2000649; P:regulation of sodium ion transmembrane transporter activity; IDA:BHF-UCL. DR CDD; cd14473; FERM_B-lobe; 1. DR CDD; cd13189; FERM_C_PTPN4_PTPN3_like; 1. DR CDD; cd00992; PDZ_signaling; 1. DR CDD; cd14600; PTPc-N3; 1. DR Gene3D; 1.20.80.10; -; 1. DR Gene3D; 2.30.42.10; -; 1. DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1. DR Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 1. DR InterPro; IPR019749; Band_41_domain. DR InterPro; IPR014352; FERM/acyl-CoA-bd_prot_sf. DR InterPro; IPR035963; FERM_2. DR InterPro; IPR019748; FERM_central. DR InterPro; IPR019747; FERM_CS. DR InterPro; IPR000299; FERM_domain. DR InterPro; IPR018979; FERM_N. DR InterPro; IPR018980; FERM_PH-like_C. DR InterPro; IPR001478; PDZ. DR InterPro; IPR036034; PDZ_sf. DR InterPro; IPR011993; PH-like_dom_sf. DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like. DR InterPro; IPR000242; PTP_cat. DR InterPro; IPR041783; PTPN3/4_FERM_C. DR InterPro; IPR016130; Tyr_Pase_AS. DR InterPro; IPR003595; Tyr_Pase_cat. DR InterPro; IPR000387; Tyr_Pase_dom. DR InterPro; IPR012151; Tyr_Pase_non-rcpt_typ-3/4. DR InterPro; IPR029071; Ubiquitin-like_domsf. DR PANTHER; PTHR45706; TYROSINE-PROTEIN PHOSPHATASE; 1. DR PANTHER; PTHR45706:SF5; TYROSINE-PROTEIN PHOSPHATASE NON-RECEPTOR TYPE 3; 1. DR Pfam; PF09380; FERM_C; 1. DR Pfam; PF00373; FERM_M; 1. DR Pfam; PF09379; FERM_N; 1. DR Pfam; PF00595; PDZ; 1. DR Pfam; PF00102; Y_phosphatase; 1. DR PIRSF; PIRSF000927; Tyr-Ptase_nr3; 1. DR PRINTS; PR00935; BAND41. DR PRINTS; PR00700; PRTYPHPHTASE. DR SMART; SM00295; B41; 1. DR SMART; SM01196; FERM_C; 1. DR SMART; SM00228; PDZ; 1. DR SMART; SM00194; PTPc; 1. DR SMART; SM00404; PTPc_motif; 1. DR SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1. DR SUPFAM; SSF50156; PDZ domain-like; 1. DR SUPFAM; SSF50729; PH domain-like; 1. DR SUPFAM; SSF47031; Second domain of FERM; 1. DR SUPFAM; SSF54236; Ubiquitin-like; 1. DR PROSITE; PS00660; FERM_1; 1. DR PROSITE; PS00661; FERM_2; 1. DR PROSITE; PS50057; FERM_3; 1. DR PROSITE; PS50106; PDZ; 1. DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1. DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1. DR PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 1. DR Genevisible; P26045; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cell membrane; Cytoplasm; Cytoskeleton; KW Hydrolase; Membrane; Phosphoprotein; Protein phosphatase; KW Reference proteome. FT CHAIN 1..913 FT /note="Tyrosine-protein phosphatase non-receptor type 3" FT /id="PRO_0000219433" FT DOMAIN 29..312 FT /note="FERM" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00084" FT DOMAIN 510..582 FT /note="PDZ" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143" FT DOMAIN 646..901 FT /note="Tyrosine-protein phosphatase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160" FT REGION 363..400 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 420..475 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 420..470 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 842 FT /note="Phosphocysteine intermediate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160, FT ECO:0000255|PROSITE-ProRule:PRU10044" FT BINDING 811 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 842..848 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 886 FT /ligand="substrate" FT /evidence="ECO:0000250" FT MOD_RES 357 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 359 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163" FT MOD_RES 367 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 376 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 381 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 425 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT VAR_SEQ 1..131 FT /note="Missing (in isoform 2 and isoform 3)" FT /evidence="ECO:0000303|PubMed:17974005" FT /id="VSP_046309" FT VAR_SEQ 335..379 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:17974005" FT /id="VSP_046310" FT VARIANT 77 FT /note="D -> N (in dbSNP:rs35285139)" FT /id="VAR_055252" FT VARIANT 90 FT /note="A -> P (in dbSNP:rs3793524)" FT /evidence="ECO:0000269|PubMed:1648725" FT /id="VAR_055253" FT VARIANT 409 FT /note="T -> A (in dbSNP:rs10979858)" FT /id="VAR_055254" FT VARIANT 605 FT /note="F -> L (in dbSNP:rs7859962)" FT /id="VAR_055255" FT VARIANT 763 FT /note="D -> N (in dbSNP:rs10116806)" FT /id="VAR_055256" FT CONFLICT 814 FT /note="V -> I (in Ref. 1; AAA35647 and 6; AAB22439)" FT /evidence="ECO:0000305" FT STRAND 507..513 FT /evidence="ECO:0007829|PDB:8CQY" FT STRAND 522..528 FT /evidence="ECO:0007829|PDB:8CQY" FT HELIX 529..531 FT /evidence="ECO:0007829|PDB:8CQY" FT STRAND 533..540 FT /evidence="ECO:0007829|PDB:8CQY" FT HELIX 545..548 FT /evidence="ECO:0007829|PDB:8CQY" FT STRAND 549..551 FT /evidence="ECO:0007829|PDB:8CQY" FT STRAND 558..562 FT /evidence="ECO:0007829|PDB:8CQY" FT HELIX 572..581 FT /evidence="ECO:0007829|PDB:8CQY" FT STRAND 584..588 FT /evidence="ECO:0007829|PDB:8CQY" FT STRAND 590..596 FT /evidence="ECO:0007829|PDB:8CQY" FT HELIX 630..643 FT /evidence="ECO:0007829|PDB:4RI5" FT HELIX 645..652 FT /evidence="ECO:0007829|PDB:4RI5" FT HELIX 664..666 FT /evidence="ECO:0007829|PDB:4RI5" FT HELIX 668..673 FT /evidence="ECO:0007829|PDB:4RI5" FT STRAND 674..676 FT /evidence="ECO:0007829|PDB:4RH9" FT TURN 683..685 FT /evidence="ECO:0007829|PDB:4RI5" FT STRAND 686..688 FT /evidence="ECO:0007829|PDB:4RI5" FT STRAND 690..692 FT /evidence="ECO:0007829|PDB:4RI5" FT STRAND 695..705 FT /evidence="ECO:0007829|PDB:4RI5" FT TURN 706..709 FT /evidence="ECO:0007829|PDB:4RI5" FT STRAND 710..717 FT /evidence="ECO:0007829|PDB:4RI5" FT HELIX 722..724 FT /evidence="ECO:0007829|PDB:4RI5" FT HELIX 725..734 FT /evidence="ECO:0007829|PDB:4RI5" FT STRAND 739..742 FT /evidence="ECO:0007829|PDB:4RI5" FT STRAND 746..748 FT /evidence="ECO:0007829|PDB:4RI5" FT STRAND 751..754 FT /evidence="ECO:0007829|PDB:4RI5" FT STRAND 764..767 FT /evidence="ECO:0007829|PDB:4RI5" FT STRAND 770..779 FT /evidence="ECO:0007829|PDB:4RI5" FT STRAND 781..792 FT /evidence="ECO:0007829|PDB:4RI5" FT TURN 793..795 FT /evidence="ECO:0007829|PDB:4RI5" FT STRAND 798..806 FT /evidence="ECO:0007829|PDB:4RI5" FT STRAND 811..813 FT /evidence="ECO:0007829|PDB:2B49" FT HELIX 818..831 FT /evidence="ECO:0007829|PDB:4RI5" FT STRAND 838..841 FT /evidence="ECO:0007829|PDB:4RI5" FT STRAND 843..846 FT /evidence="ECO:0007829|PDB:4RI5" FT HELIX 847..863 FT /evidence="ECO:0007829|PDB:4RI5" FT HELIX 870..878 FT /evidence="ECO:0007829|PDB:4RI5" FT HELIX 888..907 FT /evidence="ECO:0007829|PDB:4RI5" SQ SEQUENCE 913 AA; 103990 MW; 44FBBFA35A5F2AFF CRC64; MTSRLRALGG RINNIRTSEL PKEKTRSEVI CSIHFLDGVV QTFKVTKQDT GQVLLDMVHN HLGVTEKEYF GLQHDDDSVD SPRWLEASKA IRKQLKGGFP CTLHFRVRFF IPDPNTLQQE QTRHLYFLQL KMDICEGRLT CPLNSAVVLA SYAVQSHFGD YNSSIHHPGY LSDSHFIPDQ NEDFLTKVES LHEQHSGLKQ SEAESCYINI ARTLDFYGVE LHSGRDLHNL DLMIGIASAG VAVYRKYICT SFYPWVNILK ISFKRKKFFI HQRQKQAESR EHIVAFNMLN YRSCKNLWKS CVEHHTFFQA KKLLPQEKNV LSQYWTMGSR NTKKSVNNQY CKKVIGGMVW NPAMRRSLSV EHLETKSLPS RSPPITPNWR SPRLRHEIRK PRHSSADNLA NEMTYITETE DVFYTYKGSL APQDSDSEVS QNRSPHQESL SENNPAQSYL TQKSSSSVSP SSNAPGSCSP DGVDQQLLDD FHRVTKGGST EDASQYYCDK NDNGDSYLVL IRITPDEDGK FGFNLKGGVD QKMPLVVSRI NPESPADTCI PKLNEGDQIV LINGRDISEH THDQVVMFIK ASRESHSREL ALVIRRRAVR SFADFKSEDE LNQLFPEAIF PMCPEGGDTL EGSMAQLKKG LESGTVLIQF EQLYRKKPGL AITFAKLPQN LDKNRYKDVL PYDTTRVLLQ GNEDYINASY VNMEIPAANL VNKYIATQGP LPHTCAQFWQ VVWDQKLSLI VMLTTLTERG RTKCHQYWPD PPDVMNHGGF HIQCQSEDCT IAYVSREMLV TNTQTGEEHT VTHLQYVAWP DHGVPDDSSD FLEFVNYVRS LRVDSEPVLV HCSAGIGRTG VLVTMETAMC LTERNLPIYP LDIVRKMRDQ RAMMVQTSSQ YKFVCEAILR VYEEGLVQML DPS //