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Database: UniProt
Entry: A0A091LAH1_CATAU
LinkDB: A0A091LAH1_CATAU
Original site: A0A091LAH1_CATAU 
ID   A0A091LAH1_CATAU        Unreviewed;       570 AA.
AC   A0A091LAH1;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   RecName: Full=Fibroblast growth factor receptor 2 {ECO:0000256|ARBA:ARBA00039656};
DE            EC=2.7.10.1 {ECO:0000256|ARBA:ARBA00011902};
DE   Flags: Fragment;
GN   ORFNames=N323_03241 {ECO:0000313|EMBL:KFP53359.1};
OS   Cathartes aura (Turkey vulture) (Vultur aura).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Accipitriformes; Cathartidae; Cathartes.
OX   NCBI_TaxID=43455 {ECO:0000313|EMBL:KFP53359.1, ECO:0000313|Proteomes:UP000053745};
RN   [1] {ECO:0000313|EMBL:KFP53359.1, ECO:0000313|Proteomes:UP000053745}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N323 {ECO:0000313|EMBL:KFP53359.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) 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: Golgi apparatus {ECO:0000256|ARBA:ARBA00004555}.
CC       Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane
CC       protein {ECO:0000256|ARBA:ARBA00004479}.
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DR   EMBL; KL312313; KFP53359.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A091LAH1; -.
DR   Proteomes; UP000053745; Unassembled WGS sequence.
DR   GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR   CDD; cd05858; IgI_3_FGFR2; 1.
DR   CDD; cd05101; PTKc_FGFR2; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
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; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   PRINTS; PR00109; TYRKINASE.
DR   SMART; SM00409; IG; 1.
DR   SMART; SM00408; IGc2; 1.
DR   SMART; SM00219; TyrKc; 1.
DR   SUPFAM; SSF48726; Immunoglobulin; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50835; IG_LIKE; 1.
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}; Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Golgi apparatus {ECO:0000256|ARBA:ARBA00023034};
KW   Immunoglobulin domain {ECO:0000256|ARBA:ARBA00023319};
KW   Kinase {ECO:0000256|ARBA:ARBA00023137};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW   Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000313|EMBL:KFP53359.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053745};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transferase {ECO:0000256|ARBA:ARBA00023137};
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}.
FT   TRANSMEM        129..149
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          7..109
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          230..519
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   BINDING         266
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFP53359.1"
FT   NON_TER         570
FT                   /evidence="ECO:0000313|EMBL:KFP53359.1"
SQ   SEQUENCE   570 AA;  64050 MW;  D4DB3AD2228EF938 CRC64;
     ERSPHRPILQ AGLPANASAV VGGDVEFVCK VYSDAQPHIQ WIKHVEKNGS KYGPDGLPYL
     QVLKAAGVNT TDKEIEVLYI RNVTFEDAGE YTCLAGNSIG ISFHTAWLTV LPAPEKEKEY
     PTSPDYLEIA IYCIGVFLIA CMVLTVILCR MKNTTKKPDF SSQPAVHKLT KRIPLRRQVS
     ADSSSSMNSN TPLVRITTRL SSTADAPMLA GVSEYELPED PKWEFPRDKL TLGKPLGEGC
     FGQVVMAEAV GIDKDRPKEA VTVAVKMLKD DATEKDLSDL VSEMEMMKMI GKHKNIINLL
     GACTQDGPLY VIVEYASKGN LREYLRARRP PGMEYSFDIN RVPEEQMTFK DLVSCTYQLA
     RGMEYLASQK CIHRDLAARN VLVTENNVMK IADFGLARDI NNIDYYKKTT NGRLPVKWMA
     PEALFDRVYT HQSDVWSFGV LMWEIFTLGG SPYPGIPVEE LFKLLKEGHR MDKPANCTNE
     LYMMMRDCWH AVPSQRPTFK QLVEDLDRIL TLTTNEEYLD LSGPLEQYSP SYPDTRSSCS
     SGDDSVFSPD PMPYEPCLPK YQHMNGSVKT
//
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