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Database: UniProt
Entry: A0A3B4B6W4_9GOBI
LinkDB: A0A3B4B6W4_9GOBI
Original site: A0A3B4B6W4_9GOBI 
ID   A0A3B4B6W4_9GOBI        Unreviewed;       782 AA.
AC   A0A3B4B6W4;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   24-JAN-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};
OS   Periophthalmus magnuspinnatus.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Gobiaria; Gobiiformes; Gobioidei; Gobiidae; Oxudercinae; Periophthalmus.
OX   NCBI_TaxID=409849 {ECO:0000313|Ensembl:ENSPMGP00000024685.1, ECO:0000313|Proteomes:UP000261520};
RN   [1] {ECO:0000313|Ensembl:ENSPMGP00000024685.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-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   AlphaFoldDB; A0A3B4B6W4; -.
DR   STRING; 409849.ENSPMGP00000024685; -.
DR   Ensembl; ENSPMGT00000026305.1; ENSPMGP00000024685.1; ENSPMGG00000019977.1.
DR   Proteomes; UP000261520; Unplaced.
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: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; cd05100; PTKc_FGFR3; 1.
DR   Gene3D; 6.10.250.1740; -; 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:SF505; FIBROBLAST GROWTH FACTOR RECEPTOR 3; 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|PIRNR:PIRNR000628, ECO:0000256|PIRSR:PIRSR000628-
KW   2};
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   Repeat {ECO:0000256|ARBA:ARBA00022737};
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   TRANSMEM        346..366
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          9..101
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          126..219
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          228..330
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          442..721
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          104..126
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          746..782
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        587
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000628-1"
FT   BINDING         448..454
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000628-2"
FT   BINDING         478
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000628-2,
FT                   ECO:0000256|PROSITE-ProRule:PRU10141"
FT   BINDING         526..528
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000628-2"
FT   BINDING         532
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000628-2"
FT   BINDING         591
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000628-2"
FT   BINDING         605
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000628-2"
FT   DISULFID        38..84
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000628-3"
FT   DISULFID        151..203
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000628-3"
FT   DISULFID        250..314
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000628-3"
SQ   SEQUENCE   782 AA;  87285 MW;  C3275ED568ADD84D CRC64;
     MFSILIIPPS LVADPASSEA AFLEDFILGM GDTLDMSCDA ADPSKPVVWF KDGVSLVSHN
     RTRVGQRMLR IINVSYEDSG VYSCRTVHNN ALVSNYTIRV TDSLSSGDDE DYDEDPEDAG
     NANEAPYWTR PERMDKKLLA VPAANTVKFR CAAAGNPMPT IHWLKNGQVF KGEQRMGGIK
     LRHQQWSLVM ESAVPSDRGN YTCVVQNKYG TITHTYQLDV LERSPHRPIL QAGLPANQTV
     VVGSDVEFHC KVYSDAQPHI QWLKHIEVNG SRYAPDGAPY VNILKTAGIN TTDKELEVLF
     LTNVTFEDAG EYTCLAGNSI GFAHHSAWLT VLPAVSEGKD DYYADILIYV TGCVLVILTV
     IIIVLCRMRM TTQKTLPTPP VQKLSKFPLK RQVSLDSNSS MNSNTPLVRI ARLSSSDGPM
     LAHVSELELP SDPKWEFPRT RLTLGKPLGE GCFGQVVMAE AVGIDKEKPN KPLTVAAKML
     KDDATDKDLS DLVSEMEMMK MIGKHKNIIN LLGACTQDGP LYVLVEYASK GNLREYLRAR
     RPPGMDYSFD TCKIPDETLT FKDLVSCAYQ VARGMEYLAS QKCIHRDLAA RNVLVTEDNV
     MKIADFGLAR DVHNIDYYKK TTNGRLPVKW MAPEALFDRV YTHQSDVWSY GVLLWEIFTL
     GGSPYPGIPV EELFKLLKEG HRMDKPANCT HELYMIMREC WHAVPSQRPT FRQLVEDHDR
     ILSMTSTDEY LDLSVPFEQY SPTCPDSNST CSSGDDSVFA HDPLPDEPCL PKQLSSNGAI
     RT
//
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