ID G1N2S0_MELGA Unreviewed; 1924 AA.
AC G1N2S0;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 29-SEP-2021, sequence version 3.
DT 27-MAR-2024, entry version 75.
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:ENSMGAP00000005955.3};
OS Meleagris gallopavo (Wild turkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Meleagridinae; Meleagris.
OX NCBI_TaxID=9103 {ECO:0000313|Ensembl:ENSMGAP00000005955.3, ECO:0000313|Proteomes:UP000001645};
RN [1] {ECO:0000313|Ensembl:ENSMGAP00000005955.3, ECO:0000313|Proteomes:UP000001645}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20838655; DOI=10.1371/journal.pbio.1000475;
RA Dalloul R.A., Long J.A., Zimin A.V., Aslam L., Beal K., Blomberg L.A.,
RA Bouffard P., Burt D.W., Crasta O., Crooijmans R.P., Cooper K.,
RA Coulombe R.A., De S., Delany M.E., Dodgson J.B., Dong J.J., Evans C.,
RA Frederickson K.M., Flicek P., Florea L., Folkerts O., Groenen M.A.,
RA Harkins T.T., Herrero J., Hoffmann S., Megens H.J., Jiang A., de Jong P.,
RA Kaiser P., Kim H., Kim K.W., Kim S., Langenberger D., Lee M.K., Lee T.,
RA Mane S., Marcais G., Marz M., McElroy A.P., Modise T., Nefedov M.,
RA Notredame C., Paton I.R., Payne W.S., Pertea G., Prickett D., Puiu D.,
RA Qioa D., Raineri E., Ruffier M., Salzberg S.L., Schatz M.C., Scheuring C.,
RA Schmidt C.J., Schroeder S., Searle S.M., Smith E.J., Smith J.,
RA Sonstegard T.S., Stadler P.F., Tafer H., Tu Z.J., Van Tassell C.P.,
RA Vilella A.J., Williams K.P., Yorke J.A., Zhang L., Zhang H.B., Zhang X.,
RA Zhang Y., Reed K.M.;
RT "Multi-platform next-generation sequencing of the domestic turkey
RT (Meleagris gallopavo): genome assembly and analysis.";
RL PLoS Biol. 8:E1000475-E1000475(2010).
RN [2] {ECO:0000313|Ensembl:ENSMGAP00000005955.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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; ENSMGAT00000006700.3; ENSMGAP00000005955.3; ENSMGAG00000005856.3.
DR GeneTree; ENSGT00940000153617; -.
DR HOGENOM; CLU_001645_4_1_1; -.
DR Proteomes; UP000001645; Chromosome 30.
DR Bgee; ENSMGAG00000005856; Expressed in testis and 17 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; PR00014; FNTYPEIII.
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; 2.
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:UP000001645};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 7..25
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1263..1286
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 29..119
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 131..220
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 228..310
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 317..407
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 412..506
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 510..611
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 616..713
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 718..817
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 818..911
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 916..1012
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1016..1100
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1369..1624
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50055"
FT DOMAIN 1544..1615
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT DOMAIN 1656..1915
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50055"
FT DOMAIN 1833..1906
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT REGION 549..572
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 555..572
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1924 AA; 215711 MW; 4A3BE2EE01D83B17 CRC64;
LSPAWKQILS VLVPIMIFFL FLFILKGPPV FIKKPVDQIG VSGGVASFVC QATGDPKPRV
TWNKKGKKVN SQRFETIEFD ESAGAVLRIQ PLRTPRDENI YECVAQNPHG EVTVHAKLTV
LREDQLPPGF PNIDMGPQLK VVERTRTATM LCAASGNPDP EITWFKDFLP VDPSTSNGRI
KQLRSGGLQI ESSEETDQGK YECVASNSAG VRYSSPANLY VRVRRVAPRF SILPVSHEIM
PGGNVNITCV AVGSPMPYVK WMQGAEDLTP EDDMPVGRNV LELTDVKDSA NYTCVAMSSL
GVIEAVAQIT VKCKGVLLGR PVVTETTATS ITITWDSGNP DPVSYYVIEY KSKSQDGPYQ
IKEDITTTRY SIGGLSPNSE YEIWVSAVNS IGQGPPSESV VTRTGEQAPA SAPRNVQGRM
LSSTTMIIQW EEPVEPNGQI RGYRVYYTME PDQPVSNWQK HNVDDSLLTT VGSLLEDETY
TVRVLAFTSV GDGPLSDPIQ VKTQQGVPGQ PMNFRAEAKT ETSIMLSWSP PRQEIIVKYE
LLFKEGDHGR EVSPERSSTT GWGPEENFEP TTSFTVEGLK PNTEYVFRLA ARSALGLGAF
TPEVRERTLQ SKPSAPPQDI KCVSTRSTAI LVSWRPPPAE SQNGVLAGYS VYYRALDSED
TELKEVNDIP PTTSQILLES LEKWTEYRIT VVAHTEVGPG PESSPVIVRT DEDVPSAPPR
KVEVEVLNST AIQVFWRSPV QNRQHGQIRG YQVHYVRMEN GEARGLPQIK DIMLADAQEM
VIAGLQPETA YSITVAAYTM KGDGARSKPK VVTTKGAVPG KPILSVHQTE ENTLLVKWEP
PLDAEGQVMG YRLQFGRKDV DPLATLEFSA LEDKYTAPSI HKGATYVFKL AVKSRAGFGE
EAVQELTTPE DIPKGYPQIL EASNITSMSV QFGWLPPVLA ERNGAIVKYT VAYREAGSPG
NPLEKDLPPS PENSYTLNGL KPNTAYDVKI RAHTSKGPGP YSPTVQYRTF QLDQVLPKNF
KVKMVTKTSV LLSWEFPENY NSPTPYKIQY NGLNVDVDGR TTKKLITNLK PHTFYNFVLM
NRGNSMGGLQ QNVAAWTAAN MLSRKPEVTH KPDADGNVVV ILPDVKSSVA VQAYYIVVVP
LRKSRGGQFL NPLGSPEEMD LEELVQDIAR LRRRSLRHSR QLDFPKPYIA ARFRSLPNHF
VLGDMKHYDN FENRALEPGQ RYVIFILAVL QEPEATFAAS PFSDPIQLDN PDPQPIIDGE
EGLIWVIGPV LAVVFIICIV IAILLYKNKR KDSEPRTKCL LNNAEITPHH PKDPVEMRRI
NFQTPDSGLS SPLSDPEFDF ESMLSHPPIP VSELAEHTEH LKANDNLKLS QEYESIDPGQ
QFTWEHSNLE VNKPKNRYAN VIAYDHSRVI LLPIEGIVGS DYINANYIDG YRKQNAYIAT
QGPLPETFGD FWRMVWEQRS ATIVMMTKLE EKSRIKCDQY WPGRGTDTYG MIQVTLLDTI
ELATFCVRTF SLHKNGSSEK REVRQFQFTA WPDHGVPEYP TPFLAFLRRV KTCNPPDAGP
IVVHCSAGVG RTGCFIVIDA MLERIKHEKT VDIYGHVTLM RSQRNYMVQT EDQYSFIHDA
LLEAVACGNT EVPARNLYTY IQKLAQIEVG EHVTGMELEF KRLANSKAHT SRFISANLPC
NKFKNRLVNI MPYETTRVCL QPIRGVEGSD YINASFIDGY RQQKAYIATQ GPLAETTEDF
WRMLWENNST IVVMLTKLRE MGREKCHQYW PAERSARYQY FVVDPMAEYN MPQYILREFK
VTDARDGQSR TVRQFQFTDW PEQGVPKSGE GFIDFIGQVH KTKEQFGQDG PISVHCSAGV
GRTGVFITLS IVLERMRYEG VVDIFQTVKM LRTQRPAMVQ TEDEYQFCYQ AALEYLGSFD
HYAT
//
