PTP1_CAEEL
ID PTP1_CAEEL Reviewed; 1026 AA.
AC P28191; P45449; Q8MM81; Q9U3N7;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 3.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Tyrosine-protein phosphatase 1;
DE EC=3.1.3.48;
DE AltName: Full=Protein-tyrosine phosphatase 1;
GN Name=ptp-1; ORFNames=C48D5.2;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 844-950.
RX PubMed=1704870; DOI=10.1007/bf00211693;
RA Matthews R.J., Flores E., Thomas M.L.;
RT "Protein tyrosine phosphatase domains from the protochordate Styela
RT plicata.";
RL Immunogenetics 33:33-41(1991).
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 -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=a;
CC IsoId=P28191-1; Sequence=Displayed;
CC Name=b;
CC IsoId=P28191-2; Sequence=VSP_020641, VSP_020644;
CC Name=c;
CC IsoId=P28191-3; Sequence=VSP_020642, VSP_020643;
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class subfamily. {ECO:0000305}.
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DR EMBL; Z36237; CAA85272.1; -; Genomic_DNA.
DR EMBL; Z48241; CAA85272.1; JOINED; Genomic_DNA.
DR EMBL; Z36237; CAD44107.1; -; Genomic_DNA.
DR EMBL; Z48241; CAD44107.1; JOINED; Genomic_DNA.
DR EMBL; Z48241; CAB54194.1; -; Genomic_DNA.
DR EMBL; M38013; AAA28127.1; -; mRNA.
DR PIR; T19630; T19630.
DR PIR; T19631; T19631.
DR RefSeq; NP_497732.1; NM_065331.3. [P28191-1]
DR RefSeq; NP_497733.1; NM_065332.3. [P28191-2]
DR RefSeq; NP_741112.1; NM_171099.3. [P28191-3]
DR AlphaFoldDB; P28191; -.
DR SMR; P28191; -.
DR BioGRID; 40703; 3.
DR STRING; 6239.C48D5.2a; -.
DR iPTMnet; P28191; -.
DR EPD; P28191; -.
DR PaxDb; P28191; -.
DR PeptideAtlas; P28191; -.
DR PRIDE; P28191; -.
DR EnsemblMetazoa; C48D5.2a.1; C48D5.2a.1; WBGene00004213. [P28191-1]
DR EnsemblMetazoa; C48D5.2b.1; C48D5.2b.1; WBGene00004213. [P28191-2]
DR EnsemblMetazoa; C48D5.2c.1; C48D5.2c.1; WBGene00004213. [P28191-3]
DR GeneID; 175463; -.
DR KEGG; cel:CELE_C48D5.2; -.
DR UCSC; C48D5.2a; c. elegans. [P28191-1]
DR CTD; 175463; -.
DR WormBase; C48D5.2a; CE17578; WBGene00004213; ptp-1. [P28191-1]
DR WormBase; C48D5.2b; CE23603; WBGene00004213; ptp-1. [P28191-2]
DR WormBase; C48D5.2c; CE31450; WBGene00004213; ptp-1. [P28191-3]
DR eggNOG; KOG0792; Eukaryota.
DR GeneTree; ENSGT00940000166146; -.
DR HOGENOM; CLU_001645_7_0_1; -.
DR InParanoid; P28191; -.
DR OMA; MRWLDPS; -.
DR OrthoDB; 96595at2759; -.
DR PhylomeDB; P28191; -.
DR Reactome; R-CEL-182971; EGFR downregulation.
DR Reactome; R-CEL-5675221; Negative regulation of MAPK pathway.
DR PRO; PR:P28191; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00004213; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0016529; C:sarcoplasmic reticulum; HDA:WormBase.
DR GO; GO:0008092; F:cytoskeletal protein binding; IEA:InterPro.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IBA:GO_Central.
DR GO; GO:0006470; P:protein dephosphorylation; IEA:InterPro.
DR CDD; cd14473; FERM_B-lobe; 1.
DR CDD; cd13189; FERM_C_PTPN4_PTPN3_like; 1.
DR Gene3D; 1.20.80.10; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 3.90.190.10; -; 1.
DR InterPro; IPR019749; Band_41_domain.
DR InterPro; IPR014847; FERM-adjacent.
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 Pfam; PF08736; FA; 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; SM01195; FA; 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; SSF47031; SSF47031; 1.
DR SUPFAM; SSF50156; SSF50156; 1.
DR SUPFAM; SSF52799; SSF52799; 1.
DR SUPFAM; SSF54236; SSF54236; 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.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cytoplasm; Cytoskeleton; Hydrolase;
KW Protein phosphatase; Reference proteome.
FT CHAIN 1..1026
FT /note="Tyrosine-protein phosphatase 1"
FT /id="PRO_0000219442"
FT DOMAIN 29..315
FT /note="FERM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00084"
FT DOMAIN 617..689
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 753..1011
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT REGION 376..396
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 430..456
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 489..515
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 584..616
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 376..395
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 584..613
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 952
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160,
FT ECO:0000255|PROSITE-ProRule:PRU10044"
FT BINDING 920
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 952..958
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 996
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..45
FT /note="MRLGSNSYDVQRTEAIGQTPVKTPPPNQIRCTVTFLDSTSYHFEI -> MEV
FT PAFVGKACLKLKGLCVNVWTATVATCQENAEIDEKLPPRAFR (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_020641"
FT VAR_SEQ 3..9
FT /note="LGSNSYD -> RRRTART (in isoform c)"
FT /evidence="ECO:0000305"
FT /id="VSP_020642"
FT VAR_SEQ 10..446
FT /note="Missing (in isoform c)"
FT /evidence="ECO:0000305"
FT /id="VSP_020643"
FT VAR_SEQ 46..447
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_020644"
SQ SEQUENCE 1026 AA; 115094 MW; 2F43F7A614EDBC59 CRC64;
MRLGSNSYDV QRTEAIGQTP VKTPPPNQIR CTVTFLDSTS YHFEIEKNSL GIVLLEKVFN
YLEIIEKDYF GLVFIAVDNS SAQQKKWLDP SKNLRKQMIC PPYHLFFRVK FYVRDPNRLR
DEFTRFQFYQ QVRQNLEEGR LPCNEGSLAL LASYVVQAEV GDFEEKTHGM SRTCLCYKIQ
FATLPDDFSD RVAELHQLHI GQTPDVAEQN FLDHARRLEM YGMDVYDGVD ANHLPIEIGV
GAVGIKVFHE GIKMNEYAWV RIRKLSFKKK QFQVLVANED GVSETIMIFN IMSAKICKLL
WKCCIEQHTF FRLKTPPKTP QRKVFNFGSK FRYSGRTEYQ TLEENEHRKS AGHRNFHRSL
SKSSFLRSTF SGNTQSIDSS RYTNTTTTDS PELPSSGQLL ARRLLSAARH DTDSSDALGY
ASDGAVVCAP LTTPLSPRRT RDYATDSESS APSLRQQRLS KEAIYYGTQE SCDEKSWTPS
MACTSTSPGI HASTASVRPV SSGSTPNGAS RKSANSGYSG YGYATQTQQP TSTTNASYSP
YLNGTISRSS GAAVAKAAAR GLPPTNQQAY NTSSPRNSVA SYSSFASAGI GGSPPRSKRS
PQSNKSSSPV GEDQVVTIKM RPDRHGRFGF NVKGGADQNY PVIVSRVAPG SSADKCQPRL
NEGDQVLFID GRDVSTMSHD HVVQFIRSAR SGLNGGELHL TIRPNVYRLG EEVDEPDSTM
VPEPARVADS VPNSDKLSKS LQLLADSLNS GKVVDHFEML YRKKPGMSMN ICRLTANLAK
NRYRDVCPYD DTRVTLQASP SGDYINANYV NMEIPSSGIV NRYIACQGPL AHTSSDFWVM
VWEQHCTTIV MLTTITERGR VKCHQYWPRV FETQEYGRLM IKCIKDKQTT NCCYREFSIR
DRNSSEERRV TQMQYIAWPD HGVPDDPKHF IQFVDEVRKA RQGSVDPIVV HCSAGIGRTG
VLILMETAAC LVESNEPVYP LDIVRTMRDQ RAMLIQTPGQ YTFVCESILR AYHDGTIKPL
AEYSKR
