ID A0A1S3KJ85_SALSA Unreviewed; 1907 AA.
AC A0A1S3KJ85;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Receptor-type tyrosine-protein phosphatase F {ECO:0000256|ARBA:ARBA00044158};
DE EC=3.1.3.48 {ECO:0000256|ARBA:ARBA00013064};
GN Name=ptprf {ECO:0000313|RefSeq:XP_013978642.1};
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_013978642.1};
RN [1] {ECO:0000313|RefSeq:XP_013978642.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_013978642.1};
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; XP_013978642.1; XM_014123167.1.
DR Ensembl; ENSSSAT00000147429; ENSSSAP00000112423; ENSSSAG00000050060.
DR OrthoDB; 2875525at2759; -.
DR Proteomes; UP000087266; Chromosome ssa10.
DR Bgee; ENSSSAG00000050060; Expressed in pharyngeal gill and 12 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 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:SF7; PROTEIN-TYROSINE-PHOSPHATASE; 1.
DR Pfam; PF00041; fn3; 7.
DR Pfam; PF07679; I-set; 2.
DR Pfam; PF13927; Ig_3; 1.
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; 1.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 2.
DR PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 2.
PE 3: Inferred from homology;
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_013978642.1};
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..33
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 34..1907
FT /note="Receptor-type tyrosine-protein phosphatase F"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010178865"
FT TRANSMEM 1262..1285
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 37..127
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 139..228
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 236..318
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 325..416
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 420..514
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 518..607
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 612..709
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 714..822
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 823..916
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 921..1013
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1018..1102
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1352..1607
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50055"
FT DOMAIN 1527..1598
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT DOMAIN 1639..1898
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50055"
FT DOMAIN 1816..1889
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
SQ SEQUENCE 1907 AA; 213345 MW; 8A98ECEA4313D258 CRC64;
MALSHRWAQS PLARGATLIL LLGSLALPSP SHADSMPNFI KSPDDQTGIS GGVASFVCQA
VGDPKPRITW MKKGKKVSSQ RFEVIEFDDG SGSVLRIQPL RTHRDEAIYE CTATNSVGEI
NTSAKLTVLE EDQIPHGFPT IDMGPQLKVV EKTRTATMLC AASGNPDPEI SWFKDFLPVD
INSSNGRIKQ LRSGALQIEN SEESDQGKYE CVAVNSAGTR YSAPANLYVR VRRVPPRFSI
PPTNHEVMPG GSVNLTCVAV GAPMPYVKWM MGVEELTKEE EMPIGRNVLE VTNILQSANY
SCVAISSLGM IETTAQITVK ALPKPPTSLI VTETTATSVT LTWDSGNPEP VSYYVIQYRA
KVSDNSFQEV DGVATTRYSI GGLSPYSEYE FHVMAVNNIG RGPPSSLVDT RTSEQAPSSP
PLAVQARMLS ASTMLVQWEP PEEPNGQIRG YRVYYSSDLR APLSGWQKHN TDDSRLTTIS
GLTTDITYSL RVLGFTSVGD GPPSDVLQVK TQQGVPAQPS SFDAEAELDT RIMLSWLWPV
QDQITKYELM YWEANSGNKL HVTFPPAGSY AVEGLKPDTL YMFSLAARSE MGLGVYTQPI
EARTAQSTPS APPQEVHLLS LSSTSIKVSW VAPPAASRHG DIVRYSLAYQ AATGEDLEHH
KVSGIRADVS SYILEGLEKW TEYQVWVRAH TDVGPGPESP AVRIRTKEDV PGAPPRKVEA
DVLNSTALRV TWKPPLQVKQ HGQIRGYQVV YSRLENGEPR GQPNIMDVSL PEAQWNVEDT
MDYEAVITGL LPETTYSVTV AAYTTKGDGA RSKAKVVTTT GAVPGRPTMM ISTTIGNTAL
IQWQPPKEMV GEHVGYQLQY KRMEEESFTV KDFKKTDDHF TVTGLHKGAT YVFKLCAKNR
AGTGEEYVKE ITTPDDVPSS YPQNLSVVGL TTTTTKLAWE PPALAERNGR IVQYVVVYRD
INSQQNHTNS TIETQMTIMG LQPDTTYDIR VRAFTSKGAG PNSPSIQSRT MSTSMPEFTK
NFGVKAVMKT SVLLTWEVPE TYKSQVPFKI LYNQQSVEVQ GNLKRKLITR LQPDTDYSFV
LMSRGNSAGG LQQQVSIRTA PDLLKTKPIQ YQHHPEEGGK LTITLPRVPT TAPVRWYYIV
VVPVTPATLR RWEDPEDMDL DELLEASSDD SLRRRRQTQE FLRPYIAAKM DTLPDTFTLG
DEKKYNGFYN KPLPGQQQYL CFVLAALKDH ESQNTFAASP YSDPITVKLH SGMSLHAEDP
EMLWVMGPVL AVVLIIIIVI VILLFKRKRA SPSAKDEHSA GVKDSLLAHS SDPVEMRRLN
YQTQGMREHP LISTTDLANH IERLKANDGL RFSQEYESVD PGQQFTWEHS NLEVNKPKNR
YANVIAYDHS RVILASVDGV PGSDYINANY IDSYRKQNAC IATQGPLPET LSDFWRMVWE
QRTNTIVMMT RLEEKSRVKC DQYWPSRGTE TYGMIQVTML DTVELATYSV RTFALYKNGS
SEKREVRQFQ FMAWPDHGVP EYPTPTLAFL RRVKACNPTD AGPMVVHCSA GVGRTGCFIV
IEAMLERMKH EKSVDIYGHV TCMRAQRNYM VQTEDQYIFI HEALLEAATC GNTEVPARNL
YAHIQKLTQV TPGDTVTAME LEFKKLANSK AHTSRFISAN LPCNKFKNRL VNIMPFESTR
VSLQPIRGVE GSDYINASFI DGYRQQKAYM ATQGPLAETT EDFWRMLWEH NSTIVVMLTK
LREMGREKCH QYWPAERSAR YQYFVVDPMA EYNMPQYILR EFKVTDARDG QSRTIRQFQF
TDWPEQGVPK TGEGFIDFIG QVHKTKEQFG QDGPISAHCS AGVGRTGVFI TLSIVLERMR
YEGVVDLFQT VKTLRTQRPA MVQTEDQYQL CYRAALEYLG SFDHYAT
//