ID A0A1S3N342_SALSA Unreviewed; 731 AA.
AC A0A1S3N342;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=Fibroblast growth factor receptor {ECO:0000256|PIRNR:PIRNR000628};
DE EC=2.7.10.1 {ECO:0000256|PIRNR:PIRNR000628};
GN Name=fgfr2 {ECO:0000313|RefSeq:XP_014009903.1};
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_014009903.1};
RN [1] {ECO:0000313|RefSeq:XP_014009903.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_014009903.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1;
CC Evidence={ECO:0000256|ARBA:ARBA00001171,
CC ECO:0000256|PIRNR:PIRNR000628};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004251};
CC Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
CC Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane
CC protein {ECO:0000256|ARBA:ARBA00004479}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. Fibroblast growth factor receptor subfamily.
CC {ECO:0000256|PIRNR:PIRNR000628}.
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DR RefSeq; XP_014009903.1; XM_014154428.1.
DR AlphaFoldDB; A0A1S3N342; -.
DR PaxDb; 8030-ENSSSAP00000109654; -.
DR GeneID; 106576891; -.
DR OrthoDB; 1614410at2759; -.
DR Proteomes; UP000087266; Chromosome ssa18.
DR Bgee; ENSSSAG00000056070; Expressed in brain and 14 other cell types or tissues.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0005007; F:fibroblast growth factor receptor activity; IEA:InterPro.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IEA:InterPro.
DR CDD; cd05857; IgI_2_FGFR; 1.
DR CDD; cd05101; PTKc_FGFR2; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR016248; FGF_rcpt_fam.
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; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR020635; Tyr_kinase_cat_dom.
DR PANTHER; PTHR24416:SF505; FIBROBLAST GROWTH FACTOR RECEPTOR 3; 1.
DR PANTHER; PTHR24416; TYROSINE-PROTEIN KINASE RECEPTOR; 1.
DR Pfam; PF07679; I-set; 2.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PIRSF; PIRSF000628; FGFR; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00409; IG; 2.
DR SMART; SM00408; IGc2; 2.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF48726; Immunoglobulin; 2.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50835; IG_LIKE; 2.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRNR:PIRNR000628};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW ECO:0000256|PIRSR:PIRSR000628-3};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Immunoglobulin domain {ECO:0000256|ARBA:ARBA00023319};
KW Kinase {ECO:0000256|PIRNR:PIRNR000628};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR000628};
KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR000628, ECO:0000256|PROSITE-
KW ProRule:PRU10141};
KW Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|PIRNR:PIRNR000628};
KW Reference proteome {ECO:0000313|Proteomes:UP000087266};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|PIRNR:PIRNR000628};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius};
KW Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137,
KW ECO:0000256|PIRNR:PIRNR000628}.
FT SIGNAL 1..46
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 47..731
FT /note="Fibroblast growth factor receptor"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010186312"
FT TRANSMEM 291..311
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 66..159
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 168..270
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 391..680
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 536
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000628-1"
FT BINDING 397..403
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000628-2"
FT BINDING 427
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000628-2,
FT ECO:0000256|PROSITE-ProRule:PRU10141"
FT BINDING 475..477
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000628-2"
FT BINDING 481
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000628-2"
FT BINDING 540
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000628-2"
FT BINDING 554
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000628-2"
FT DISULFID 91..143
FT /evidence="ECO:0000256|PIRSR:PIRSR000628-3"
FT DISULFID 190..254
FT /evidence="ECO:0000256|PIRSR:PIRSR000628-3"
SQ SEQUENCE 731 AA; 82021 MW; 18F676051B685350 CRC64;
MGSVSRGRQS LRRGGWGTDS PSTNGMASWA WLLATILLSL ATATLARPPY TAAEEEEATL
EPEGAPYWTM LEKMEKRLHA VPAANTVKFR CAAGGNPRPK MRWLKNSRPF RQEDRMGGYK
VRHQHWTLIM ESVVPSDKGN YTCLVENAYG AINHTYTLDV VERSPHRPIL QAGLPANTSV
QVGEDARFVC KVYSDAQPHI QWLQHIQKNG SRTGPDGHSY VRVLKTAGVN TTDKEIEVLY
LPNVTYEDAG EYTCLAGNSI GISYHTAWLT VLPASNEETV TGLMSPDYVE IAIYCIGVFL
IACMVVIVVV CRMRNTAKKP DFGNQPAVHK LSKQIPLRRQ VTVSNDSSSS MNSSTPLVRI
TTRRSSAGHD DPIPEYDLPE DPRWEFSRDR LTLGKPLGEG CFGQVVMAEA LGIDKDKPKE
AITVAVKMLK DDATEKDLSD LVSEMEMMKM IGKHKNIINL LGACTQDGPL YVIVEYASKG
NLREYLRARR PPGMEYSYDI NRCSDEQLAF KDLVSCTYQV ARGMEYLASQ KCIHRDLAAR
NVLVTESNFM KIADFGLARD VHNIDYYKKT TNGRLPVKWM APEALFDRVY THQSDVWSFG
VLMWEIFTLG GSPYPGIPVE ELFKLLKEGH RMDKPGNCTN ELYMMMKDCW HAISSHRPTF
KQLVEDLDRI LTLVTNEEYL DLCAPAEQYS PSFQDTRSSC SSGDDSVFSH DPLPEEPCLP
KYQHINGGVK T
//
