ID A0A3B4ZFU4_9TELE Unreviewed; 834 AA.
AC A0A3B4ZFU4;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 29.
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_008296487.1};
OS Stegastes partitus (bicolor damselfish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Stegastes.
OX NCBI_TaxID=144197 {ECO:0000313|Ensembl:ENSSPAP00000007753.1, ECO:0000313|Proteomes:UP000261400};
RN [1] {ECO:0000313|Ensembl:ENSSPAP00000007753.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_008296487.1}
RP IDENTIFICATION.
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 Golgi apparatus {ECO:0000256|ARBA:ARBA00004555}. Membrane
CC {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein
CC {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_008296487.1; XM_008298265.1.
DR AlphaFoldDB; A0A3B4ZFU4; -.
DR Ensembl; ENSSPAT00000007902.1; ENSSPAP00000007753.1; ENSSPAG00000005860.1.
DR GeneID; 103369377; -.
DR CTD; 2263; -.
DR GeneTree; ENSGT00940000155447; -.
DR OrthoDB; 1614410at2759; -.
DR Proteomes; UP000261400; Unplaced.
DR Proteomes; UP000694891; Unplaced.
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; 3.
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:SF130; FIBROBLAST GROWTH FACTOR RECEPTOR 2; 1.
DR PANTHER; PTHR24416; TYROSINE-PROTEIN KINASE RECEPTOR; 1.
DR Pfam; PF07679; I-set; 2.
DR Pfam; PF13927; Ig_3; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PIRSF; PIRSF000628; FGFR; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00409; IG; 3.
DR SMART; SM00408; IGc2; 3.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF48726; Immunoglobulin; 3.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50835; IG_LIKE; 3.
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, ECO:0000256|PIRSR:PIRSR000628-
KW 4}; Golgi apparatus {ECO:0000256|ARBA:ARBA00023034};
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:UP000694891};
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..43
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 44..834
FT /note="Fibroblast growth factor receptor"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5041074212"
FT TRANSMEM 395..415
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 45..132
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 174..267
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 276..376
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 494..783
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 151..171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 446..482
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 446..466
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 467..482
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 639
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000628-1"
FT BINDING 500..506
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000628-2"
FT BINDING 530
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000628-2,
FT ECO:0000256|PROSITE-ProRule:PRU10141"
FT BINDING 578..580
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000628-2"
FT BINDING 584
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000628-2"
FT BINDING 643
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000628-2"
FT BINDING 657
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000628-2"
FT CARBOHYD 107
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000628-4"
FT CARBOHYD 144
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000628-4"
FT CARBOHYD 248
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000628-4"
FT CARBOHYD 261
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000628-4"
FT CARBOHYD 285
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000628-4"
FT CARBOHYD 317
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000628-4"
FT CARBOHYD 338
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000628-4"
FT CARBOHYD 349
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000628-4"
FT DISULFID 86..131
FT /evidence="ECO:0000256|PIRSR:PIRSR000628-3"
FT DISULFID 199..251
FT /evidence="ECO:0000256|PIRSR:PIRSR000628-3"
FT DISULFID 298..360
FT /evidence="ECO:0000256|PIRSR:PIRSR000628-3"
SQ SEQUENCE 834 AA; 92792 MW; 5D9A7E81282757A0 CRC64;
MGSVSRGRWR RGVWGALSPT NGMASWAWLL AAVLLSLLTV SVARPPLTAT KEEEATLEPE
EASNKYQISK PTVCSVHPGE VLKLSCPLPA TGTITWTKDG SSLGTNNRTV IEQEVLQIRD
ATPKDSGLYA CTSVGKDTVC FIVNVTDAIS SGDDEDDTER SEDTGADGEQ ISAPYWTSSA
KMEKKLHAVP AANTVKFRCA AGGNPRPKLR WLKNSRPFRQ EDRMGGYKVR SQHWTLIMES
VVPSDKGNYT CLVENEFGSI NHTYTLDVVE RSPHRPILQA GLPANTSVHV GEDARFVCKV
YSDAQPHIQW LKHITQNGSR YGPDGHPYVR VLKRSGINSS DLEMLTLTNV TEEDAGEYIC
KVSNYIGEES QSGWLTVIPA LEKSPGPLSP DYVEIAIYCA GVFLIACMVG IVVVCRMRNT
AKKPDFGGQP AVHKLSKQIP LRRQVTVSAD SSSSMNSSTP LVRITTRRSS AHDEPIPEYD
LPEDPRWEFS RDRLTLGKPL GEGCFGQVVM AEALGIDKDK PKEAVTVAVK MLKDDATEKD
LSDLVSEMEM MKMIGKHKNI INLLGACTQD GPLYVIVEYA SKGNLREYLR ARRPPGMEYS
YDIARVSDEQ LTFKDLVSCT YQVARGMEYL ASQKCIHRDL AARNVLVTES NVMKIADFGL
ARDVHNIDYY KKTTNGRLPV KWMAPEALFD RVYTHQSDVW SFGVLMWEIF TLGGSPYPGI
PVEELFKLLK EGHRMDKPGN CTNELYMMMK DCWHAISSQR PTFKQLVEDL DRILTLSTNE
EYLDLCAPTE QYSPSFPDTR SSCSSGDDSV FSHDPLPDEP CLPKYQHING NVKT
//
