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Database: UniProt
Entry: A0A1S3M4F2_SALSA
LinkDB: A0A1S3M4F2_SALSA
Original site: A0A1S3M4F2_SALSA 
ID   A0A1S3M4F2_SALSA        Unreviewed;      1451 AA.
AC   A0A1S3M4F2;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   RecName: Full=protein-tyrosine-phosphatase {ECO:0000256|ARBA:ARBA00013064};
DE            EC=3.1.3.48 {ECO:0000256|ARBA:ARBA00013064};
GN   Name=LOC106570261 {ECO:0000313|RefSeq:XP_013997861.1};
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_013997861.1};
RN   [1] {ECO:0000313|RefSeq:XP_013997861.1}
RP   IDENTIFICATION.
RC   TISSUE=Muscle {ECO:0000313|RefSeq:XP_013997861.1};
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_013997861.1; XM_014142386.1.
DR   GeneID; 106570261; -.
DR   OrthoDB; 2875525at2759; -.
DR   Proteomes; UP000087266; Chromosome ssa14.
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; 3.
DR   CDD; cd06263; MAM; 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; 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; 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; 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, ECO:0000256|SAM:Phobius};
KW   Protein phosphatase {ECO:0000256|ARBA:ARBA00022912};
KW   Receptor {ECO:0000313|RefSeq:XP_013997861.1};
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|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           17..1451
FT                   /note="protein-tyrosine-phosphatase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5010208256"
FT   TRANSMEM        753..778
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          25..187
FT                   /note="MAM"
FT                   /evidence="ECO:0000259|PROSITE:PS50060"
FT   DOMAIN          189..273
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          286..381
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          384..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          910..1141
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS50055"
FT   DOMAIN          1061..1132
FT                   /note="Tyrosine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
FT   DOMAIN          1173..1438
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS50055"
FT   DOMAIN          1354..1429
FT                   /note="Tyrosine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
FT   REGION          832..867
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        832..849
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1451 AA;  163266 MW;  04E61DB6E9061720 CRC64;
     MYTGVFLLML LVGIYADTMD QGPTAGCTFD EDSDPGLCEY KQGQEDDFDW QLMRTYNWPH
     STPDLLRGSF MMVNSSQHAA GQRAHLLLRS LSENDTHCIQ FSYFLYSRDG HSPGDLQLYI
     RVNGGPRGSA VWNVSGSHGR QWHQVELAVS TFWPSEYQVV FEASVSAERR GYIAIDDILL
     LNYPCYKVPH FSRLGDVEVN AGQNATFQCV ATGKTTETEP FLLERRNGVV VAASSIQRLS
     HKRLMATFQV AAERGEQDLY RCVTESTRGA AVSNFAELIV RVPPTPIAPP QLLRAGPTYL
     IIQLNTNSIV GDGPVIRREI EYRASQSPWS ETHGVGSLTY KVWHLEPDTE YRISVLLTRP
     GEGGTGAPGP PLVSRTKCAE PMRALRGLTA TEIQPRQLTL QWEPMGYNLT RCHTYSVSLC
     YRYSTPAGGS AGNNATVREC LSVERNQSHF TLRDLPPFRS VHVRLALENP EGKKESREVT
     FQTEEDIPGG VAPESLTFTP LDDMIFLKWE EPVEPNGVIT QYEISYQGIE SSDPGINVPG
     PRRTVSKLRN ETYHMFSGLH PGTTYLVSVR ARTAKGFGQT ALTEITTNIS APVFDYEDVP
     APLSESESTI TVLLRPALGR GAPVSAYQVV VVEEDGSRRV RRSRRRRREL GSGSDCFPVP
     ASQVEAQSKS HYYTAELPPS SLPEATPFTV GDNHTYNGYW NTPLDPSKNY LVFFQAISNF
     RGETRMNCIR IARKGACKDH KRTLEVSQHA EDMGLILGAC AGGLVVLILL LGAIVIVVKK
     GRKKVALNKA AMSYRQEKTR KLGSLDCSMT EQSTLQQDER TANSFMDAHA CNTRNEQRSS
     VNESSSLLGG SPRRHCRRKS SPYHTGQLHP AVRVADLLQH INQMKTGEGY GFKQEYESFF
     DGWDVTKKKD KTKGRHDSLL GHDRHRVKLH SLLADPNSDY VNANYIDGYQ RSNHFIATQG
     PKQEMIYDFW RMVWQENCFS IVMITKLVEV GRMKCCKYWP EDSELYGDIK ITLLKTETLA
     EYTVRTFAME RRGYPAKHEV CQFHFTSWPE HGVPYHATGL LAFLRRVKAS TPPDAGPVVV
     HCSMGAGRTG CYIVLDVMLD MAECEGVVDI YNCVKTLCSR RINMIQTEEQ YVFIHDAILE
     ACLCGETAIP VIEFALTYKE MLRVDSQSNT SQLREEFQTL NSVTPHLDVE ECSVSLLPRN
     REKNRSMDVL PPDRALAFLV TTEGVAEGNS YINAALTDSF HRPAAFVVTP HPLPGTTADF
     WRLVYDYGCT SVVMLNQINQ SNSAWPCLQY WPEPGLQQFG PMTVELLSMM ADDDVIIRLF
     RVQNIMRLQE GQLVVRHFQF LRWSPYRDVP DSKKAFLSLL AQVHNWQREC GEGRTIVHCL
     NGGGRSGTFC ACTMLLEMIR HHSVVDVFYA AKTLRNSKPN MVETMEQYRF CYDLALEYLD
     ALDCLSEIEV R
//
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