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Database: UniProt
Entry: A0A3Q1CKV0_AMPOC
LinkDB: A0A3Q1CKV0_AMPOC
Original site: A0A3Q1CKV0_AMPOC 
ID   A0A3Q1CKV0_AMPOC        Unreviewed;       833 AA.
AC   A0A3Q1CKV0;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=Fibroblast growth factor receptor {ECO:0000256|PIRNR:PIRNR000628};
DE            EC=2.7.10.1 {ECO:0000256|PIRNR:PIRNR000628};
OS   Amphiprion ocellaris (Clown anemonefish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Pomacentridae; Amphiprion.
OX   NCBI_TaxID=80972 {ECO:0000313|Ensembl:ENSAOCP00000027705.1, ECO:0000313|Proteomes:UP000257160};
RN   [1] {ECO:0000313|Ensembl:ENSAOCP00000027705.1}
RP   IDENTIFICATION.
RG   Ensembl;
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       Cytoplasm, cytosol {ECO:0000256|ARBA:ARBA00004514}. Cytoplasmic vesicle
CC       {ECO:0000256|ARBA:ARBA00004541}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein
CC       {ECO:0000256|ARBA:ARBA00004479}. Nucleus
CC       {ECO:0000256|ARBA:ARBA00004123}. Vesicle
CC       {ECO:0000256|ARBA:ARBA00004373}.
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; A0A3Q1CKV0; -.
DR   STRING; 80972.ENSAOCP00000027705; -.
DR   Ensembl; ENSAOCT00000020092.1; ENSAOCP00000027705.1; ENSAOCG00000016923.1.
DR   GeneTree; ENSGT00940000155860; -.
DR   Proteomes; UP000257160; Unplaced.
DR   GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; 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:Ensembl.
DR   GO; GO:0060249; P:anatomical structure homeostasis; IEA:Ensembl.
DR   GO; GO:0048738; P:cardiac muscle tissue development; IEA:Ensembl.
DR   GO; GO:0051216; P:cartilage development; IEA:Ensembl.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProt.
DR   GO; GO:0021535; P:cell migration in hindbrain; IEA:Ensembl.
DR   GO; GO:0009953; P:dorsal/ventral pattern formation; IEA:Ensembl.
DR   GO; GO:0031101; P:fin regeneration; IEA:Ensembl.
DR   GO; GO:0001889; P:liver development; IEA:Ensembl.
DR   GO; GO:0007498; P:mesoderm development; IEA:Ensembl.
DR   GO; GO:0042664; P:negative regulation of endodermal cell fate specification; IEA:Ensembl.
DR   GO; GO:0021628; P:olfactory nerve formation; IEA:Ensembl.
DR   GO; GO:0071699; P:olfactory placode morphogenesis; IEA:Ensembl.
DR   GO; GO:0033339; P:pectoral fin development; IEA:Ensembl.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; IEA:InterPro.
DR   GO; GO:0036342; P:post-anal tail morphogenesis; IEA:Ensembl.
DR   GO; GO:0048916; P:posterior lateral line development; IEA:Ensembl.
DR   GO; GO:0060255; P:regulation of macromolecule metabolic process; IEA:UniProt.
DR   GO; GO:0045471; P:response to ethanol; IEA:Ensembl.
DR   GO; GO:0043589; P:skin morphogenesis; IEA:Ensembl.
DR   CDD; cd05857; IgI_2_FGFR; 1.
DR   CDD; cd05098; PTKc_FGFR1; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 3.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR028174; FGF_rcpt_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; IPR013151; Immunoglobulin.
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:SF131; FIBROBLAST GROWTH FACTOR RECEPTOR 1; 1.
DR   PANTHER; PTHR24416; TYROSINE-PROTEIN KINASE RECEPTOR; 1.
DR   Pfam; PF07679; I-set; 2.
DR   Pfam; PF00047; ig; 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   Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00023329};
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}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|PIRNR:PIRNR000628};
KW   Reference proteome {ECO:0000313|Proteomes:UP000257160};
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};
KW   Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}.
FT   TRANSMEM        388..408
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          46..120
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          171..259
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          268..370
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          489..778
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          793..833
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        634
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000628-1"
FT   BINDING         495..501
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000628-2"
FT   BINDING         525
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000628-2,
FT                   ECO:0000256|PROSITE-ProRule:PRU10141"
FT   BINDING         573..575
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000628-2"
FT   BINDING         579
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000628-2"
FT   BINDING         638
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000628-2"
FT   BINDING         652
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000628-2"
FT   DISULFID        73..119
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000628-3"
FT   DISULFID        191..243
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000628-3"
FT   DISULFID        290..354
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000628-3"
SQ   SEQUENCE   833 AA;  93317 MW;  2F4634A2099508D8 CRC64;
     MPQRSEWSSS RRKANSCSSL SRMLMRPSKL LFLVLFAQVL RTQCRPASTD EVSVETQAEL
     FTLYLGDHLD LSCSAKDSPH AVNWTKDHVA VVDGEHTRIR SGQLEIEAVE LTDSGLYACT
     TFGNHSVFFN VTVDTLASSE DDDEDEESSS EEAKLLGSQK LLPMAPQWAH PEKMEKKLHA
     VPASKTVKFR CQASGNPTPT LKWYKNGKEF KRDHRIGGFK VRDHVWTIIM ESVVPSDKGN
     YTCVVENQYG SINHTYQLDV VERSPHRPIL QAGLPANRTA VVGSDVEFEC KVFSDPQPHI
     QWLKHIEVNG SRVGPDGLPY VRVLKTAGLN TTDKEMEVLQ LRNVSFDDAG EYTCLAGNSI
     GFSHHSAWLT VFEAVAHYPP ASHTYLEVVI YCVGFFFIAV MIAIAIIVKI RTSSKKSDFN
     SQLAVHKLAK SIPLRRQVTV SVDSSSSIHS GVMLVRPSRL SSSGSPMLSG VSEYELPQDP
     RWELPRDRLV LGKPLGEGCF GQVVMGEALG LDKEKPNRVT KVAVKMLKSD ATEKDLSDLI
     SEMEMMKIIG KHKNIINLLG ACTQDGPLYV IVEYASKGNL REYLRARRPP GMEYCYNPDQ
     VPVENMSIKD LVSCAYQVAR GMEYLASKKC IHRDLAARNV LVTEDNVMKI ADFGLARDIH
     HIDYYKKTTN GRLPVKWMAP EALFDRVYTH QSDVWSFGVL LWEIFTLGGS PYPGVPVEEL
     FKLLKEGHRM DKPSTCTHEL YMMMRDCWHA VPSQRPTFKQ LVEDLDRCLA MTSNQEYLEL
     SVPLDQYSPS YPDTRSSTCS SGEDSVFSHD AGAEEPCLPK FPPHSNGAAI KKR
//
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