ID A0A091PR11_HALAL Unreviewed; 847 AA.
AC A0A091PR11;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=receptor protein-tyrosine kinase {ECO:0000256|ARBA:ARBA00011902};
DE EC=2.7.10.1 {ECO:0000256|ARBA:ARBA00011902};
DE Flags: Fragment;
GN ORFNames=N329_08262 {ECO:0000313|EMBL:KFP98046.1};
OS Haliaeetus albicilla (White-tailed sea-eagle) (Falco albicilla).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Accipitriformes; Accipitridae;
OC Accipitrinae; Haliaeetus.
OX NCBI_TaxID=8969 {ECO:0000313|EMBL:KFP98046.1, ECO:0000313|Proteomes:UP000054379};
RN [1] {ECO:0000313|EMBL:KFP98046.1, ECO:0000313|Proteomes:UP000054379}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N329 {ECO:0000313|EMBL:KFP98046.1};
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: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. {ECO:0000256|ARBA:ARBA00006692}.
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DR EMBL; KK644580; KFP98046.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091PR11; -.
DR Proteomes; UP000054379; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00063; FN3; 2.
DR CDD; cd00096; Ig; 1.
DR CDD; cd05749; IgI_2_Axl_Tyro3_like; 1.
DR CDD; cd14204; PTKc_Mer; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 4.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
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:SF257; TYROSINE-PROTEIN KINASE MER; 1.
DR PANTHER; PTHR24416; TYROSINE-PROTEIN KINASE RECEPTOR; 1.
DR Pfam; PF00041; fn3; 1.
DR Pfam; PF00047; ig; 1.
DR Pfam; PF13927; Ig_3; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PIRSF; PIRSF000615; TyrPK_CSF1-R; 3.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00060; FN3; 2.
DR SMART; SM00409; IG; 2.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF49265; Fibronectin type III; 1.
DR SUPFAM; SSF48726; Immunoglobulin; 2.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50853; FN3; 2.
DR PROSITE; PS50835; IG_LIKE; 2.
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|PROSITE-
KW ProRule:PRU10141}; Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Immunoglobulin domain {ECO:0000256|ARBA:ARBA00023319};
KW Kinase {ECO:0000313|EMBL:KFP98046.1};
KW Magnesium {ECO:0000256|PIRSR:PIRSR000615-3};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR000615-3};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Receptor {ECO:0000256|ARBA:ARBA00023170};
KW Reference proteome {ECO:0000313|Proteomes:UP000054379};
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 432..455
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 29..116
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 127..209
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 216..311
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 316..413
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 517..788
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 805..835
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 807..822
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 653
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-1"
FT BINDING 549
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
FT BINDING 658
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT BINDING 671
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFP98046.1"
FT NON_TER 847
FT /evidence="ECO:0000313|EMBL:KFP98046.1"
SQ SEQUENCE 847 AA; 93544 MW; 9BE3A50CD63E0FEC CRC64;
TVGHWPHRSP EQPQDEPSTS SLGQIKFNPT VQHIVINEHK DVTFNCSIKV PQLLLRPETP
GISLWKDGRE LHVHHFEIAD EEEVTMTSTF SILAAQRSDN GSYVCKLNIS GTEVVSDPIS
VQLEGLPHFI RQPEKLNVTK NSPFNLTCQA VGPPEPVEIY WFRNNVQVNE KPHISPSVLT
VPGLNETTLF SCEAHNSKGL TASNPGQVNV KGIPSEPISM HVLNRTAHSI VISWVPGFDA
FSALNSCSVQ VKEAVPRSNV SLLLFNTSVP PHVYHIQQLG PMADYNIRVS CRNEVGWSAF
SPWITASTTE GAPTTPPLNV TVSFNESISS VEIRWVKPPL GKIHGELQGY HIWYRWQNSK
ELQNISTEAQ PNTSMAILPV VATNATCFVR VAAITKGGVG PFSSPVEVFI PGSGLITSAP
SSTPASGNAD SFIVALGFIC GTIAVGLILC LSVVIQKRCV ETKYGNAFSS NDLELAVNYT
AKKSYCRRAV ELTLGSLGVS SELQQKLQDV VVDRNALSLG KVLGEGEFGS VMEGHLSQPE
GTPQKVAVKT MKLDNFSQRE IEEFLSEAAC MKDFDHPNVI KLLGVCIELS NQQVPKPMVI
LPFMKYGDLH SFLLRSRLEM APQFVPLQTL VKFMVDIALG MEYLSSRHFL HRDLAARNCM
LRDDMTVCVA DFGLSKKIYS GDYYRQGRIA KMPVKWIAIE SLADRVYTTK SDVWAFGVTM
WEIVTRGMTP YPGVQNHEIY EYLFHGQRLK KPEDCLDELY EIMSACWRAN PTTRPTFSQL
KVHLEKLLEN LPTVRGSGDI IYINTSLPEE SPDSTQDSGF PQVDSDLDPG DVAEPCSPRA
AKALVAV
//
