PTN1_CHICK
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 03-AUG-2022, entry version 147.
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 -!- 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}.
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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.ENSGALP00000032803; -.
DR iPTMnet; O13016; -.
DR PaxDb; O13016; -.
DR PRIDE; O13016; -.
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 OrthoDB; 411281at2759; -.
DR PhylomeDB; O13016; -.
DR TreeFam; TF315897; -.
DR PRO; PR:O13016; -.
DR Proteomes; UP000000539; Unplaced.
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:0031532; P:actin cytoskeleton reorganization; 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 Gene3D; 3.90.190.10; -; 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 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; SSF52799; 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
