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Database: UniProt
Entry: A0A1S3PBG5_SALSA
LinkDB: A0A1S3PBG5_SALSA
Original site: A0A1S3PBG5_SALSA 
ID   A0A1S3PBG5_SALSA        Unreviewed;      1455 AA.
AC   A0A1S3PBG5;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   RecName: Full=protein-tyrosine-phosphatase {ECO:0000256|ARBA:ARBA00013064};
DE            EC=3.1.3.48 {ECO:0000256|ARBA:ARBA00013064};
GN   Name=ptpru {ECO:0000313|RefSeq:XP_014024912.1};
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_014024912.1};
RN   [1] {ECO:0000313|RefSeq:XP_014024912.1}
RP   IDENTIFICATION.
RC   TISSUE=Muscle {ECO:0000313|RefSeq:XP_014024912.1};
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   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC       pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
CC   -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC       Receptor class 2B subfamily. {ECO:0000256|ARBA:ARBA00006396}.
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DR   RefSeq; XP_014024912.1; XM_014169437.1.
DR   GeneID; 106584293; -.
DR   CTD; 335096; -.
DR   OrthoDB; 2875525at2759; -.
DR   Proteomes; UP000087266; Chromosome ssa02.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR   CDD; cd00063; FN3; 2.
DR   CDD; cd06263; MAM; 1.
DR   CDD; cd14632; R-PTPc-U-1; 1.
DR   Gene3D; 2.60.120.200; -; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 4.
DR   Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 2.
DR   InterPro; IPR013320; ConA-like_dom_sf.
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; IPR003599; Ig_sub.
DR   InterPro; IPR013151; Immunoglobulin.
DR   InterPro; IPR000998; MAM_dom.
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; PTHR24051:SF10; PROTEIN-TYROSINE-PHOSPHATASE-RELATED; 1.
DR   PANTHER; PTHR24051; SUSHI DOMAIN-CONTAINING PROTEIN 1; 1.
DR   Pfam; PF00041; fn3; 2.
DR   Pfam; PF00047; ig; 1.
DR   Pfam; PF00629; MAM; 1.
DR   Pfam; PF00102; Y_phosphatase; 2.
DR   PRINTS; PR00020; MAMDOMAIN.
DR   PRINTS; PR00700; PRTYPHPHTASE.
DR   SMART; SM00060; FN3; 3.
DR   SMART; SM00409; IG; 1.
DR   SMART; SM00137; MAM; 1.
DR   SMART; SM00194; PTPc; 2.
DR   SMART; SM00404; PTPc_motif; 2.
DR   SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 2.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR   SUPFAM; SSF49265; Fibronectin type III; 2.
DR   SUPFAM; SSF48726; Immunoglobulin; 1.
DR   PROSITE; PS50853; FN3; 3.
DR   PROSITE; PS50835; IG_LIKE; 1.
DR   PROSITE; PS00740; MAM_1; 1.
DR   PROSITE; PS50060; MAM_2; 1.
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};
KW   Protein phosphatase {ECO:0000256|ARBA:ARBA00022912};
KW   Receptor {ECO:0000313|RefSeq:XP_014024912.1};
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};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..1455
FT                   /note="protein-tyrosine-phosphatase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5010328178"
FT   DOMAIN          25..187
FT                   /note="MAM"
FT                   /evidence="ECO:0000259|PROSITE:PS50060"
FT   DOMAIN          189..274
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          287..382
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          385..486
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          492..592
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          903..1151
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS50055"
FT   DOMAIN          1071..1142
FT                   /note="Tyrosine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
FT   DOMAIN          1183..1446
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS50055"
FT   DOMAIN          1362..1437
FT                   /note="Tyrosine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
FT   REGION          818..858
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        821..844
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1455 AA;  163553 MW;  40DEEA347C21922A CRC64;
     MNTCAFLLLL AVQIYAEGIE GPTAAGCTFD EDSEPSLCDF TQGEEDDFDW QLFRTHNSPY
     ASSDLLCGSY MLVNSSQHAA GHRAQLLLQT LSENDTHCVQ FSYFLYSRDG HSPGALRAYV
     RVNGGPLGSP VWNTSGSHGR QWHQVELAVS TFWPNEYQVL IEATVSRERR GYIAMDDILL
     LTYPCYKAPH FSRLGDEEVN AGQNATFQCV ASGRASEAEK FLLERHSGDV TSTALVKHLS
     HRRFVASFQV DSVQRNDQDL YRCVTQSSRG SGVSNFAELI VKVPPSPIAP PQLLRAGSTY
     LIIQLNTNSI LGDGPIIRKE IEYRASQSPW SEVHGVNMVT YKLWHLDPDT EYHISVLLTR
     PGEGGTGPPG PPLISRTKCA EPTRALRGLT ASEIQSRQLT LQWETLAYNL TRCHTYSVSL
     CYRYATVGGG GGHNTTVREC LAVEHNASRF TLRDLPAYHS IRVRLALANP EGKKEGREVT
     FQTEEDIPGG IAPESLTFTP LEDMIFLKWE EPVEPNGLIT QYEISYQSIE SSDPGINVPG
     PRRTVSKLRN ETYHMFSNLH PGTTYLISVR ARTTKGFGQT ALTEITTNIS APMFDYGDMP
     SPLSETESTI TVLLRPALGR GAPVSTYQVV VEEESGRKVK RELGVQDCYP LPMSHGEAQA
     RGTPHYYTAE LPPSSLPEAS PFTVGDNHTY NGYWNTPLDP RKSYLVYFQA MSNFRGETRM
     NCIRIARKAA CKDHRRALEV SQHSEEMGLI LGVCAGGLVV LILLLGAIII IIRKGKPVNI
     NKTPITYRQE KSHMGSMERS FTDQSTLQED ERMALSAARM AHTCSTRSEQ RSSVNESSSL
     LGGSPRRQCG HKGSPYHTGQ LHPAVRVADL LQHINQMKTA EGYGFKQEYE SFFDGWDCTK
     KKDKTKGRHD TLMGCKSSWT CQPSCDESTD HHDRHRVKLH PLLGDPNSDY INANYIDGYH
     RSNHFIATQG PKQETVYDFW RMVWQENCFS IVMITKLVEV GRVKCCKYWP DDSEMYGDIK
     ITLLKTETLS EYTVRTFAME RRGYSAKHEV RQFHFTSWPE HGVPYHATGL LAFIRRVKAS
     TPPDAGPVVV HCSVGAGRTG CYIVLDVMLD MAECEGVVDI YNCVKTLCSR RINMIQTEEQ
     YIFIHDAILE ACLCGETAIL VNEFALTYKD MLRVDSQSNS SQLREEFQTL NSVTPHLDVE
     ECSIALLPRN REKNRSMDVL PPDRALAFLV TTEGESNNYI NAALTDSFHQ PAAFIVTPHP
     LPGTTADFWR LVFDYGCTSV VMLNQLNQSN SAWPCVQYWP EPGLQQYGPM EVEFLSTSAD
     DDVITRLFRV KNVTRLQEGQ LVVCQFQFLR WSAYRDVPDS KKAFLSLLAH VHKWQRECGD
     GRTVVHCLSG GGRSGTFCAS TILLEMIQYQ NMVDIFYSVK TLRNSKPNMV ESLDQYRFCY
     DLILEYLDCI EDSMR
//
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