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   27-MAR-2024, entry version 170.
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.2; -.
DR   iPTMnet; P28191; -.
DR   EPD; P28191; -.
DR   PaxDb; 6239-C48D5-2a; -.
DR   PeptideAtlas; 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   AGR; WB:WBGene00004213; -.
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; 2874613at2759; -.
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 cell types or 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:0016311; P:dephosphorylation; IEA:InterPro.
DR   CDD; cd14473; FERM_B-lobe; 1.
DR   CDD; cd13189; FERM_C_PTPN4_PTPN3_like; 1.
DR   CDD; cd17100; FERM_F1_PTPN3_like; 1.
DR   CDD; cd00992; PDZ_signaling; 1.
DR   CDD; cd14541; PTPc-N3_4; 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; IPR014847; FA.
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:SF4; TYROSINE-PROTEIN PHOSPHATASE; 1.
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; 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.
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
//