ID A0A1S3MPX9_SALSA Unreviewed; 1926 AA.
AC A0A1S3MPX9;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=protein-tyrosine-phosphatase {ECO:0000256|ARBA:ARBA00013064};
DE EC=3.1.3.48 {ECO:0000256|ARBA:ARBA00013064};
GN Name=LOC106574153 {ECO:0000313|RefSeq:XP_014005278.1};
OS Salmo salar (Atlantic salmon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salmo.
OX NCBI_TaxID=8030 {ECO:0000313|Proteomes:UP000087266, ECO:0000313|RefSeq:XP_014005278.1};
RN [1] {ECO:0000313|RefSeq:XP_014005278.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_014005278.1};
RG RefSeq;
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 RefSeq; XP_014005278.1; XM_014149803.1.
DR OrthoDB; 2875525at2759; -.
DR Proteomes; UP000087266; Chromosome ssa16.
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 Receptor {ECO:0000313|RefSeq:XP_014005278.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000087266};
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..31
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 32..1926
FT /note="protein-tyrosine-phosphatase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010376984"
FT TRANSMEM 1275..1298
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 35..125
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 137..235
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 247..329
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 336..426
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 431..525
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 529..619
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 624..726
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 731..830
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 831..930
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 931..1026
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1030..1114
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1371..1626
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50055"
FT DOMAIN 1546..1617
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT DOMAIN 1658..1917
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50055"
FT DOMAIN 1835..1908
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT REGION 411..432
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1926 AA; 214649 MW; 3DA0906F797A2A5C CRC64;
MAAGGPPCLC LPALLPLSTL LLCMLLTGVH ALSPPRFTKV PVDQIGVSGG VVSFVCQATG
DPKPRVSWNK KGKKVNSQRI ETIEFDEGAG AVLRIQPLRA PRDENIYECV AENSEGEVNV
NAKLSIIRED LLPGGFPNID MGPQLKVVER TRTATMLCAA SGNPDPEITW FKDFLPIDPN
ASNGRIKQLR SEAFEGTPIR GALQIENSEE TDQGKYECVA SNVEGVRYSS PANLYVRELR
EVRRVPPRFS IPPTSHEMMP GGSVNITCVA VGSPMPYVKW MLNSEDLTPE DEMPVGRNVL
ELNSVRESAN YTCVAMSSLG IIEAVAQITV KSLPKPPGTP MVTETTATSV TITWDSGNPD
PVSYYIIQYR AKSPDSKFET MDGITTTRYS IGGLYPNTEY EIRVSAFNTI GQGPPSEPVE
TRTGEQAPAS PPRNIQARII SQNTMMVRWD EPEEPNGQIK GYRVYYTMDP SQPMSLWQIH
NVQDSIITTI QSLVASETYT IRVLAFTSVG DGPFSDPIHV KVLQGVPGQP TKFQVGAVSD
TSMELTWEPA FQKEGIISFE LRYKEGSFGS QVTKTFGPTA SYVVEGLRAN TEYYFSLAAI
SNKGIGAFTN EISQKTLQAK PSAPPQDVKC SSSSSTSLLV SWRPPPVESQ NGALAGYRVR
YQVVGASVEG GSAGEPMEEP AVLPSDGKVL LQKLEKWTQY SVTLAAFTEI GPGPESEPLL
CRTDEDVPGA PPRRVEVEVL NSTALKVMWR SLLPGRQHGQ IRGYQVHYVR VENGESRGPP
LIKDVMLADA QEMVIGGLQS DTTYSITVAA YTTKGDGARS KPKLVVTKGA VPGPPSLSVA
QDSETSAVVC WDAPDVMIPG MGLQGYRLQF GRKDVSPLAT LEFTPQERQY TVASVHRGAT
YLFKVQAKSR GGFGEEATAE LQVPEHTPQG YPQIRETSNV TCCSVELSWS PPMLAERNGD
ITEYTLAYQE TGLGDAPREL SLPASQSTYV LNSLKPNSAY DVKIRAHTSV GPGPYSPPIQ
YRTVAFETDV PKNFTVKWVT KTTVLLTWKF VERRFPFRCT IEYNRQKMDV DARLTKALVT
SLRPNTTYEF RVTCQENTEG GPRHRVVART TPPILVKKPK LDLYSEPDNI LTMGFAPVET
KDIKDFYVVA VPLKKGLGTA RHLKNPDEMD LEELLRDITP KRRTRRQLSQ ADGKKPYITA
CFKQLPTSFT LGTEHRHSSC ESKPLEPGQE YVFFLLAELN TTAGKMFAAS PYTDLVVTPE
LEADPLPMET GGDGLIWVVG PVLAVVFIIC IVIAILLYKN SKPDSRKRKE SEPRTKCLLN
NAEITPHHPT DPVEMRRINF QTTGMMSHPP IPIAELAEHT DLLKANDNLK LSQEYESIDP
GQQFTWEHSN LEVNKPKNRY ANVIAYDHSR VILAPIEGIT GSDYINANYI DGYRKQNAYM
ATQGPLPETF GDFWRMVWEQ RAATVVMMTR LEEKSRIKCD QYWPSRGTET YGMTQVTLLD
TIELATFCVR TFSLHKNGSS EKREVRQFQF TAWPDHGVPE YPTPFLAFLR RVKTCNPPDA
GPIIAHCSAG VGRTGCFIVI DAMLERIKHE KTVDIYGHVT LMRSQRNYMV QTEDQYSFNH
DALLEAVACG NTEVAARSLF SYIQKLAQVE TGEHVTGMEL EFKRLANSKA HTSRFISANL
PCNKFKNRLV NIMPYETTRV CLQPIRGLEG SDYINASFID GYRQQKAYIA TQGPLAETTE
DFWRMMWENN STIVVMLTKL REMGREKCHQ YWPAERSARY QYFVVDPMAE YNMPQYILRE
FKVTDARDGQ SRTVRQFQFT DWPEQGVPKS GEGFIDFIGQ VHKTKEQFGQ DGPISVHCSA
GVGRSGVFTT LSIVLERMRY EGVVDIFQTV KMLRTQRPAM VQTEDEYQFC YQAGLEYLGS
FDHYAT
//
