ID PTN1_CHICK Reviewed; 434 AA. AC O13016; Q90704; DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1997, sequence version 1. DT 24-JAN-2024, entry version 152. DE RecName: Full=Tyrosine-protein phosphatase non-receptor type 1; DE EC=3.1.3.48; DE AltName: Full=CPTP1; DE AltName: Full=Protein-tyrosine phosphatase 1B; DE Short=PTP-1B; GN Name=PTPN1; Synonyms=PTP1B; OS Gallus gallus (Chicken). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae; OC Phasianinae; Gallus. OX NCBI_TaxID=9031; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Retina; RX PubMed=8707857; DOI=10.1083/jcb.134.3.801; RA Balsamo J., Leung T., Ernst H., Zanin M.K., Hoffman S., Lilien J.; RT "Regulated binding of PTP1B-like phosphatase to N-cadherin: control of RT cadherin-mediated adhesion by dephosphorylation of beta-catenin."; RL J. Cell Biol. 134:801-813(1996). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=9600099; DOI=10.1006/bbrc.1998.8605; RA Jung E.J., Kang Y.-S., Kim C.W.; RT "Multiple phosphorylation of chicken protein tyrosine phosphatase 1 and RT human protein tyrosine phosphatase 1B by casein kinase II and p60c-src in RT vitro."; RL Biochem. Biophys. Res. Commun. 246:238-242(1998). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] OF 14-369. RC TISSUE=Intestine; RA Kim C.W., Jung E.J., Kang Y.-S.; RT "Cloning and characterization of a chicken protein tyrosine phosphatase, RT CPTP1."; RL Exp. Mol. Med. 28:207-213(1996). CC -!- FUNCTION: May play an important role in CKII- and p60c-src-induced CC signal transduction cascades. May regulate the EFNA5-EPHA3 signaling CC pathway which modulates cell reorganization and cell-cell repulsion. CC May also regulate the hepatocyte growth factor receptor signaling CC pathway through dephosphorylation of MET (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; Evidence={ECO:0000255|PROSITE- CC ProRule:PRU10044}; CC -!- SUBUNIT: Interacts with EPHA3 (phosphorylated); dephosphorylates EPHA3 CC and may regulate its trafficking and function. Interacts with MET. CC Interacts with NCK1. {ECO:0000250|UniProtKB:P18031}. CC -!- INTERACTION: CC O13016; P10288: CDH2; NbExp=10; IntAct=EBI-6938259, EBI-985728; CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; CC Peripheral membrane protein {ECO:0000250}; Cytoplasmic side CC {ECO:0000250}. CC -!- PTM: Phosphorylated on serine and threonine residues near the N- CC terminus by casein kinase II (CK2). CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non- CC receptor class 1 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; U86410; AAB53270.1; -; mRNA. DR EMBL; U46662; AAA91186.1; -; mRNA. DR PIR; JW0049; JW0049. DR RefSeq; NP_990206.1; NM_204875.1. DR AlphaFoldDB; O13016; -. DR SMR; O13016; -. DR BioGRID; 675966; 3. DR IntAct; O13016; 7. DR MINT; O13016; -. DR STRING; 9031.ENSGALP00000012986; -. DR iPTMnet; O13016; -. DR PaxDb; 9031-ENSGALP00000032803; -. DR GeneID; 395688; -. DR KEGG; gga:395688; -. DR CTD; 5770; -. DR VEuPathDB; HostDB:geneid_395688; -. DR eggNOG; KOG0789; Eukaryota. DR HOGENOM; CLU_001645_9_0_1; -. DR InParanoid; O13016; -. DR PhylomeDB; O13016; -. DR TreeFam; TF315897; -. DR PRO; PR:O13016; -. DR Proteomes; UP000000539; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005769; C:early endosome; ISS:UniProtKB. DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0004726; F:non-membrane spanning protein tyrosine phosphatase activity; IBA:GO_Central. DR GO; GO:0019901; F:protein kinase binding; IBA:GO_Central. DR GO; GO:0004725; F:protein tyrosine phosphatase activity; ISS:UniProtKB. DR GO; GO:0030036; P:actin cytoskeleton organization; ISS:UniProtKB. DR GO; GO:0030968; P:endoplasmic reticulum unfolded protein response; ISS:UniProtKB. DR GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; IBA:GO_Central. DR GO; GO:1903898; P:negative regulation of PERK-mediated unfolded protein response; IBA:GO_Central. DR GO; GO:0035335; P:peptidyl-tyrosine dephosphorylation; ISS:UniProtKB. DR GO; GO:0030100; P:regulation of endocytosis; ISS:UniProtKB. DR GO; GO:0009966; P:regulation of signal transduction; ISS:UniProtKB. DR CDD; cd14608; PTPc-N1; 1. DR Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 1. DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like. DR InterPro; IPR000242; PTP_cat. DR InterPro; IPR012265; Ptpn1/Ptpn2. DR InterPro; IPR016130; Tyr_Pase_AS. DR InterPro; IPR003595; Tyr_Pase_cat. DR InterPro; IPR000387; Tyr_Pase_dom. DR PANTHER; PTHR46047:SF2; TYROSINE-PROTEIN PHOSPHATASE NON-RECEPTOR TYPE 1; 1. DR PANTHER; PTHR46047; TYROSINE-PROTEIN PHOSPHATASE NON-RECEPTOR TYPE 61F; 1. DR Pfam; PF00102; Y_phosphatase; 1. DR PIRSF; PIRSF000926; Tyr-Ptase_nr1; 1. DR PRINTS; PR00700; PRTYPHPHTASE. DR SMART; SM00194; PTPc; 1. DR SMART; SM00404; PTPc_motif; 1. DR SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1. DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1. DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1. DR PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 1. PE 1: Evidence at protein level; KW Endoplasmic reticulum; Hydrolase; Membrane; Phosphoprotein; KW Protein phosphatase; Reference proteome. FT CHAIN 1..434 FT /note="Tyrosine-protein phosphatase non-receptor type 1" FT /id="PRO_0000094751" FT DOMAIN 3..277 FT /note="Tyrosine-protein phosphatase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160" FT REGION 291..319 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 301..315 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 215 FT /note="Phosphocysteine intermediate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160, FT ECO:0000255|PROSITE-ProRule:PRU10044" FT BINDING 181 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 215..221 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 262 FT /ligand="substrate" FT /evidence="ECO:0000250" FT MOD_RES 50 FT /note="Phosphoserine" FT /evidence="ECO:0000250" FT CONFLICT 14 FT /note="A -> R (in Ref. 3; AAA91186)" FT /evidence="ECO:0000305" FT CONFLICT 62..63 FT /note="GD -> RC (in Ref. 3; AAA91186)" FT /evidence="ECO:0000305" SQ SEQUENCE 434 AA; 50334 MW; 0FF340B2333CC311 CRC64; MEIEKEFHRL DQAASWAAIY QDIRHEASDF PCKVAKHPRN KNRNRYRDVS PFDHSRIKLN QGDNDYINAS LIKMEEAQRS YILTQGPLPN TCGHFWEMVW EQKSRGVVML NRVMEKGSIK CAQYWPRKEE KEMFFEDTNL KLTLISEDIK SYYTVRQLEL ENLTTQETRE ILHFHYTTWP DFGVPESPAS FLNFLFKVRE SGSLNPEYGP VVVHCSAGIG RSGTFCLVDT CLLLMDKRKD PSSVDVKQVL LEMRKYRMGL IQTADQLRFS YLAVIEGAKF IMGDASVQEQ WKELSNEDLD PPPEHTPPPP RPPKRTSEMH NGRMHEHAEF FPKHQVVEEE IRCSVSTAEE TVSDGRVFSS VPLITDSTSQ DTEIRRRTVG ENLHVTAHKE ESKSESVEED DENMMTTWKP FLVNICMFTF LTAGAYLCYR VCFH //