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Database: UniProt
Entry: A0A091D668_FUKDA
LinkDB: A0A091D668_FUKDA
Original site: A0A091D668_FUKDA 
ID   A0A091D668_FUKDA        Unreviewed;       930 AA.
AC   A0A091D668;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 49.
DE   RecName: Full=Fibroblast growth factor receptor 3 {ECO:0000256|ARBA:ARBA00039657};
DE            EC=2.7.10.1 {ECO:0000256|ARBA:ARBA00011902};
GN   ORFNames=H920_12841 {ECO:0000313|EMBL:KFO25705.1};
OS   Fukomys damarensis (Damaraland mole rat) (Cryptomys damarensis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC   Fukomys.
OX   NCBI_TaxID=885580 {ECO:0000313|EMBL:KFO25705.1, ECO:0000313|Proteomes:UP000028990};
RN   [1] {ECO:0000313|EMBL:KFO25705.1, ECO:0000313|Proteomes:UP000028990}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Liver {ECO:0000313|EMBL:KFO25705.1};
RA   Gladyshev V.N., Fang X.;
RT   "The Damaraland mole rat (Fukomys damarensis) genome and evolution of
RT   African mole rats.";
RL   Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
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   -!- 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}.
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DR   EMBL; KN123337; KFO25705.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A091D668; -.
DR   STRING; 885580.ENSFDAP00000018359; -.
DR   eggNOG; KOG0200; Eukaryota.
DR   Proteomes; UP000028990; Unassembled WGS sequence.
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:0008284; P:positive regulation of cell population proliferation; IEA:InterPro.
DR   CDD; cd05857; IgI_2_FGFR; 1.
DR   Gene3D; 6.10.250.1740; -; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 4.
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; PF21165; FGFR3_TM; 1.
DR   Pfam; PF07679; I-set; 2.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   PIRSF; PIRSF000628; FGFR; 2.
DR   PRINTS; PR00109; TYRKINASE.
DR   SMART; SM00409; IG; 4.
DR   SMART; SM00408; IGc2; 4.
DR   SMART; SM00219; TyrKc; 1.
DR   SUPFAM; SSF48726; Immunoglobulin; 4.
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   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Cell membrane {ECO:0000256|ARBA:ARBA00022475};
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|ARBA:ARBA00023137};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000313|EMBL:KFO25705.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000028990};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Transferase {ECO:0000256|ARBA:ARBA00023137};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989};
KW   Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137}.
FT   DOMAIN          56..111
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          148..242
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          251..340
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          558..847
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          129..153
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          853..881
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        856..873
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         594
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
FT   DISULFID        63..111
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000628-3"
FT   DISULFID        174..226
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000628-3"
SQ   SEQUENCE   930 AA;  102481 MW;  73E436A10200F3F3 CRC64;
     MSIVPRFCAD GKFPLLVPRS PGRFVVSVSP SEWRDRRMEA LGSELGQQEP MVFGSGDTVE
     LSCHPPRGNP GGPTVWVKDG EGLVSSDRIL VEPQRLQVLN ASHEDAGAYS CWQQLMQRVL
     CRFSVHVTDA PSSGDDEDGE DVAEDTGPPY WTRPERMDKK LLAVPAANTV RFRCPAAGNP
     TPSISWLKNG KEFRGEHRIG GIKLRHQQWS LVMESVVPSD RGNYTCVVEN KFGSIQQTYT
     LDVLERSPHR PILQAGLPAN QTVVLGSDVE FHCKVYSDAQ PHIQWLKHVE VNGSKVGPDG
     TPYVTVLKSW ISENVEADAR LRLANVSERD GGEYLCRATN FIGVAEKAFW LRVHGPRAGS
     LCLRPLCQTR MAPTAAVATC FELPRPAVAL PTLPCTAGAN TTDKELEVLS LRNVTFEDAG
     EYTCLAGNSI GFSHHSAWLV VLPAEEELVE ADTAGSVYAG ILSSGVGFFL FTLVVAAVTL
     CRLRSPPKKG LGSPTVHKVS RFPLKRQQVS LESNSSMSSN TPLVRIARLS SGEGPTLANV
     SELELPADPK WELSRSRLTL GKPLGEGCFG QVVMAEAIGI DKDRAAKPVT VAVKMLKDDA
     TDKDLSDLVS EMEMMKMIGK HKNIINLLGA CTQGGPLYVL VEYAAKGNLR EYLRARRPPG
     LDYSFDTCKL PEEQLTFKDL VSCAYQVARG MEYLASQKCI HRDLAARNVL VTEDNVMKIA
     DFGLARDVHN LDYYKKTTNG RLPVKWMAPE ALFDRVYTHQ SDVWSFGVLL WEIFTLGGSP
     YPGIPVEELF KLLKEGHRMD KPANCTQDLY MIMRECWHAV PSQRPTFKQL VEDLDRILTV
     TSTDEYLDLS VPFEQYSPGG QDTPSSSSSG GPMPKPSADG HRQMLHLCEG EVSRPRHKVP
     GASALLYKAL LSDWHQEAKG PCSGDARLRM
//
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