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Database: UniProt
Entry: A0A3P8YBX9_ESOLU
LinkDB: A0A3P8YBX9_ESOLU
Original site: A0A3P8YBX9_ESOLU 
ID   A0A3P8YBX9_ESOLU        Unreviewed;      1923 AA.
AC   A0A3P8YBX9;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   02-DEC-2020, sequence version 2.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=protein-tyrosine-phosphatase {ECO:0000256|ARBA:ARBA00013064};
DE            EC=3.1.3.48 {ECO:0000256|ARBA:ARBA00013064};
GN   Name=PTPRS {ECO:0000313|Ensembl:ENSELUP00000013611.2};
OS   Esox lucius (Northern pike).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Esociformes;
OC   Esocidae; Esox.
OX   NCBI_TaxID=8010 {ECO:0000313|Ensembl:ENSELUP00000013611.2, ECO:0000313|Proteomes:UP000265140};
RN   [1] {ECO:0000313|Ensembl:ENSELUP00000013611.2, ECO:0000313|Proteomes:UP000265140}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=25069045;
RA   Rondeau E.B., Minkley D.R., Leong J.S., Messmer A.M., Jantzen J.R.,
RA   von Schalburg K.R., Lemon C., Bird N.H., Koop B.F.;
RT   "The genome and linkage map of the northern pike (Esox lucius): conserved
RT   synteny revealed between the salmonid sister group and the Neoteleostei.";
RL   PLoS ONE 9:e102089-e102089(2014).
RN   [2] {ECO:0000313|Ensembl:ENSELUP00000013611.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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;
CC         Evidence={ECO:0000256|ARBA:ARBA00001490};
CC   -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC       Receptor class 2A subfamily. {ECO:0000256|ARBA:ARBA00010504}.
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DR   Ensembl; ENSELUT00000022206.2; ENSELUP00000013611.2; ENSELUG00000013946.2.
DR   GeneTree; ENSGT00940000153617; -.
DR   Proteomes; UP000265140; LG08.
DR   Bgee; ENSELUG00000013946; Expressed in embryo and 13 other cell types or tissues.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016043; P:cellular component organization; IEA:UniProt.
DR   GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR   CDD; cd00063; FN3; 8.
DR   CDD; cd05738; IgI_2_RPTP_IIa_LAR_like; 1.
DR   CDD; cd05739; IgI_3_RPTP_IIa_LAR_like; 1.
DR   CDD; cd14627; R-PTP-S-2; 1.
DR   CDD; cd14625; R-PTPc-S-1; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 11.
DR   Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 2.
DR   InterPro; IPR003961; FN3_dom.
DR   InterPro; IPR036116; FN3_sf.
DR   InterPro; IPR007110; Ig-like_dom.
DR   InterPro; IPR036179; Ig-like_dom_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR013098; Ig_I-set.
DR   InterPro; IPR003599; Ig_sub.
DR   InterPro; IPR003598; Ig_sub2.
DR   InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR   InterPro; IPR000242; PTP_cat.
DR   InterPro; IPR016130; Tyr_Pase_AS.
DR   InterPro; IPR003595; Tyr_Pase_cat.
DR   InterPro; IPR000387; Tyr_Pase_dom.
DR   PANTHER; PTHR46957; CYTOKINE RECEPTOR; 1.
DR   PANTHER; PTHR46957:SF8; PROTEIN TYROSINE PHOSPHATASE RECEPTOR TYPE S; 1.
DR   Pfam; PF00041; fn3; 7.
DR   Pfam; PF07679; I-set; 1.
DR   Pfam; PF13927; Ig_3; 2.
DR   Pfam; PF00102; Y_phosphatase; 2.
DR   PRINTS; PR00700; PRTYPHPHTASE.
DR   SMART; SM00060; FN3; 8.
DR   SMART; SM00409; IG; 3.
DR   SMART; SM00408; IGc2; 3.
DR   SMART; SM00194; PTPc; 2.
DR   SMART; SM00404; PTPc_motif; 2.
DR   SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 2.
DR   SUPFAM; SSF49265; Fibronectin type III; 5.
DR   SUPFAM; SSF48726; Immunoglobulin; 3.
DR   PROSITE; PS50853; FN3; 8.
DR   PROSITE; PS50835; IG_LIKE; 3.
DR   PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR   PROSITE; PS50056; TYR_PHOSPHATASE_2; 2.
DR   PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 2.
PE   3: Inferred from homology;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Immunoglobulin domain {ECO:0000256|ARBA:ARBA00023319};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Protein phosphatase {ECO:0000256|ARBA:ARBA00022912};
KW   Reference proteome {ECO:0000313|Proteomes:UP000265140};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           27..1923
FT                   /note="protein-tyrosine-phosphatase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5027805688"
FT   TRANSMEM        1261..1284
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          30..120
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          132..221
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          233..315
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          322..412
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          417..511
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          515..605
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          610..712
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          717..816
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          817..916
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          917..1012
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          1016..1099
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          1368..1623
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS50055"
FT   DOMAIN          1543..1614
FT                   /note="Tyrosine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
FT   DOMAIN          1655..1914
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS50055"
FT   DOMAIN          1832..1905
FT                   /note="Tyrosine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
FT   REGION          397..419
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1923 AA;  213865 MW;  A0F08DEC5418A7F6 CRC64;
     MAAEGPPCLS LPSLLLLSLL LTCCHALSPP RFTKVPVDQI GVSGGVVSFV CQATGDPKPR
     VGWNKKGKKV NSQRIETIEF DEGAGAVLRI QPLRAPRDEN IYECVAENSE GEVNVNAKLS
     IIREDLLPAG FPNIDMGPQL KVVERTRTAT MLCAASGNPD PEITWFKDFL PIDPNSSNGR
     IKQLRSGALQ IENSEETDQG KYECVASNVE GVRYSSPANL YVRELREVRR VPPRFSIPPT
     SHEIMPGGSV NITCVAVGSP MPYVKWMINS EDLTPEDEMP VGRNVLELNS VRESANYTCV
     AMSSLGIIEA VAQITVKSLP KPPGAPLVTE TTATSVTITW DSGNPDPVSH YIIQYRAKSP
     DSKFETVDGI TTTRYSIGGL YPNTEYEIRV SAFNTIGQGP PSDPVEARTG EQAPASPPRN
     VQVRIISQTT MMVRWDEPEE PNGQIRGYRV YYTMDPSQPM NMWQISNVQD SIITTIKSLV
     ASETYSVRVL AFTSVGDGPF SDPVHVKVLQ GVPGQPTKFQ VGAVSDTSIE LTWEPAYDKE
     GIVSYELRYK EGNSGSQVTK TFNPTSAYVV EGLRANTEYH FSLAAISNKG IGAFTNDISQ
     KTLQAKPSAP PQDIKCSSSS STALLVSWSP PPVESQNGAL AGYLVRYQVV GASVEGGGVG
     EPMEEPAVPP SEGRLLLQKL EKWTQYRITL AAFTEIGPGP ESEPLLCRTD EDVPGAPPRR
     VEVEVLNSTA IKVMWRSLLP GGQHGQIRGY QVHYVRVENG ESRGLPLIKD VMLADAQEMV
     IGGLQPDTTY SITVAAYTTK GDGARSKPKL VVTKGAVPGP PYLSVAQDSE TSAMVRWDPP
     DVLIQGVGLQ GYRLQFGRKD ISPLATLEFT PQERQYTVAN VHRGATYLFK VQAKSRGGFG
     EEATAELQVP EHTPQGYPQI SESSNVTCCS VELAWSPPVL AERNGDITEY TLAYQEAGTT
     GAPRELSLPA SQSSYVLSSL KPNSAYDVKI RAHTSVGPGP FSPPVQYRTV AYDTDVPKNF
     TVKWVTKTTV LLTWKFAERR FPFRCTIEYN RQKMDVDARL TKALVTGLRP NTTYEFRISC
     QDNTEGAPRH RVVARTAPPI LVKKPRLDLY SEPDNILTMG FAPVDGKDIK IFYVVVVPIK
     KGSGTVRHLK NPDEMDLEEL LRDVTPKRRT RRQLGPADSR KPYITACFKQ LPASFTLGTD
     HRQSSCENKP LEPGQEYVFF LLAELNTTAG KTFAASPYTD SVVTPETEGD PTPADNGGDG
     LIWVVGPVLA VVFIICIVIA ILLYKNRKRK ESEPRTKCLL NNAEIAPPHP TDPVEMRRIN
     FQTPDSGLSS PLSEADFDYE SMMNHPPIPI AELPEHTDLL KANDNLKLSQ EYESIDPGQQ
     FTWEHSNLEV NKPKNRYANV IAYDHSRVIL TPIEGITGSD YINANYIDGY RKQNAYIATQ
     GPLPETFGDF WRMVWEQRAA TVVMMTRLEE KSRIKCDQYW PSRGTETYGM TQVTLLDTIE
     LATFCVRTFS LHKNGSSEKR EVRQFQFTAW PDHGVPEYPT PFLAFLRRVK TCNPPDAGPI
     IAHCSAGVGR TGCFIVIDAM LERIKHEKTV DIYGHVTLMR SQRNYMVQTE DQYSFIHDAL
     LEAVACGNTE VAARSLYSYI QKLAQVETGE HVTGMELEFK RLANSKAHTS RFISANLPCN
     KFKNRLVNIM PYETTRVCLQ PIRGLEGSDY INASFIDGYR QQKAYIATQG PLAETTEDFW
     RMLWENNSTI IVMLTKLREM GREKCHQYWP AERSARYQYF VVDPMAEYNM PQYILREFKV
     TDARDGQSRT VRQFQFTDWP EQGVPKSGEG FIDFIGQVHK TKEQFGQDGP ISVHCSAGVG
     RTGVFITLSI VLERMRYEGV VDIFQTVKML RTQRPAMVQT EDEYQFCYQA GLEYLGSFDH
     YAT
//
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