ID A0A7K8H6G8_9CORV Unreviewed; 597 AA.
AC A0A7K8H6G8;
DT 07-APR-2021, integrated into UniProtKB/TrEMBL.
DT 07-APR-2021, sequence version 1.
DT 28-JAN-2026, entry version 20.
DE SubName: Full=CSF1R factor {ECO:0000313|EMBL:NXC51726.1};
DE Flags: Fragment;
GN Name=Csf1r {ECO:0000313|EMBL:NXC51726.1};
GN ORFNames=ALERUF_R13246 {ECO:0000313|EMBL:NXC51726.1};
OS Aleadryas rufinucha (rufous-naped whistler).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Neoaves; Telluraves; Australaves;
OC Passeriformes; Corvoidea; Pachycephalidae; Aleadryas.
OX NCBI_TaxID=461220 {ECO:0000313|EMBL:NXC51726.1, ECO:0000313|Proteomes:UP000557196};
RN [1] {ECO:0000313|EMBL:NXC51726.1, ECO:0000313|Proteomes:UP000557196}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B10K-DU-029-36 {ECO:0000313|EMBL:NXC51726.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:NXC51726.1};
RA Zhang G.;
RT "Bird 10,000 Genomes (B10K) Project - Family phase.";
RL Submitted (SEP-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] +
CC ADP + H(+); Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:20101, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:61978, ChEBI:CHEBI:456216; EC=2.7.10.1;
CC Evidence={ECO:0000256|ARBA:ARBA00051243};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:NXC51726.1}.
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DR EMBL; VZTH01000284; NXC51726.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A7K8H6G8; -.
DR Proteomes; UP000557196; Unassembled WGS sequence.
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 FunFam; 2.60.40.10:FF:001169; Macrophage colony-stimulating factor 1 receptor; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 5.
DR Gene3D; 3.30.200.20; Phosphorylase Kinase, domain 1; 1.
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; IPR003598; Ig_sub2.
DR InterPro; IPR013151; Immunoglobulin_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR PANTHER; PTHR10075; BASIGIN RELATED; 1.
DR PANTHER; PTHR10075:SF14; CELL ADHESION MOLECULE DSCAM2-RELATED; 1.
DR Pfam; PF00047; ig; 1.
DR Pfam; PF25305; Ig_PDGFR_d4; 1.
DR PIRSF; PIRSF000615; TyrPK_CSF1-R; 1.
DR PRINTS; PR01832; VEGFRECEPTOR.
DR SMART; SM00409; IG; 4.
DR SMART; SM00408; IGc2; 3.
DR SUPFAM; SSF48726; Immunoglobulin; 5.
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.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|PIRSR:PIRSR000615-2, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Immunoglobulin domain {ECO:0000256|ARBA:ARBA00023319};
KW Magnesium {ECO:0000256|PIRSR:PIRSR000615-3};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR000615-3};
KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000615-2, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Receptor {ECO:0000256|ARBA:ARBA00023170};
KW Reference proteome {ECO:0000313|Proteomes:UP000557196};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 492..516
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 5..75
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 182..274
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 381..482
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 560..597
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT BINDING 539
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT BINDING 567..574
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT BINDING 594
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-2,
FT ECO:0000256|PROSITE-ProRule:PRU10141"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:NXC51726.1"
FT NON_TER 597
FT /evidence="ECO:0000313|EMBL:NXC51726.1"
SQ SEQUENCE 597 AA; 66644 MW; 58668E0037C9A3BF CRC64;
GSASPVISPD LPALVVDTGD PILLHCSGES EVAWSSKKNT FSNHTTSTLS IPKATYRNTG
TYSCGYVNSS DQGIAAIHVF VRDPSNVWYS PSFRVGVTEG GNVDLPCLIT APEYGSNVIL
IMDDASPLPP GTNYSFSAEK GIRLYNVQSK HKGYYRCQAQ INGKIKNSSR IRLVVEEVVK
RPVSVMMDPA DHVRIVGEPF KVTCRVISPS HKYVIRWVTA AKTVMRTKKT DFENENYIID
DTLSIAAVTM EDSGKYICIA NNSVGFRNAS TMLQVVERGY VHLIPGQATS QEVALGESLE
LQVHIKAYPK LLQWVWEHTN PLKNSKTTIF KSQMISGNNW YNNTLFLNRL KEGEGGFYTF
HALNNVTNES VTFSISLKSS PRVCKIKVPA NDSSILQCTA VGYPAPRIEW YQCPVHSDRY
SEDYRLIWND SRPQVVNMLP FQEVEVESTI LFQELGDNFT FCCVAINGEG NTSDMLHSLT
ITRSVMVLPN KLFSPVLSTC IGALVLLLLL LLFLLYKYNQ KPKYQVRWKI IEACEGNNYI
FIDPTQLPYN EKWEFPRNNL QFGKTLGAGA FGKVVEATAF GLGKEDSVLK VAVKMLK
//
