ID A0A091I9E1_CALAN Unreviewed; 1231 AA.
AC A0A091I9E1;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 48.
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=N300_09956 {ECO:0000313|EMBL:KFP04842.1};
OS Calypte anna (Anna's hummingbird) (Archilochus anna).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Caprimulgimorphae; Apodiformes;
OC Trochilidae; Calypte.
OX NCBI_TaxID=9244 {ECO:0000313|EMBL:KFP04842.1, ECO:0000313|Proteomes:UP000054308};
RN [1] {ECO:0000313|EMBL:KFP04842.1, ECO:0000313|Proteomes:UP000054308}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N300 {ECO:0000313|EMBL:KFP04842.1};
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 plexin family.
CC {ECO:0000256|ARBA:ARBA00010297}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00352}.
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DR EMBL; KL218426; KFP04842.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091I9E1; -.
DR STRING; 9244.A0A091I9E1; -.
DR Proteomes; UP000054308; 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:0004714; F:transmembrane receptor protein tyrosine kinase activity; IEA:UniProtKB-EC.
DR CDD; cd00102; IPT; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR Gene3D; 3.30.1680.10; ligand-binding face of the semaphorins, domain 2; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR002909; IPT_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR002165; Plexin_repeat.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR016201; PSI.
DR InterPro; IPR001627; Semap_dom.
DR InterPro; IPR036352; Semap_dom_sf.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR020635; Tyr_kinase_cat_dom.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR PANTHER; PTHR24416:SF113; MACROPHAGE-STIMULATING PROTEIN RECEPTOR; 1.
DR PANTHER; PTHR24416; TYROSINE-PROTEIN KINASE RECEPTOR; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF01437; PSI; 1.
DR Pfam; PF01833; TIG; 2.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00429; IPT; 3.
DR SMART; SM00423; PSI; 1.
DR SMART; SM00630; Sema; 1.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF81296; E set domains; 2.
DR SUPFAM; SSF103575; Plexin repeat; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF101912; Sema domain; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR PROSITE; PS51004; SEMA; 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 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:KFP04842.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000054308};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
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};
KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..1231
FT /note="receptor protein-tyrosine kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001875047"
FT TRANSMEM 780..805
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 23..289
FT /note="Sema"
FT /evidence="ECO:0000259|PROSITE:PS51004"
FT DOMAIN 912..1177
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1203..1231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1217..1231
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 944
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:KFP04842.1"
FT NON_TER 1231
FT /evidence="ECO:0000313|EMBL:KFP04842.1"
SQ SEQUENCE 1231 AA; 135756 MW; 9C50753F587A3751 CRC64;
CCGCLLLLFT LTPLGAGTWQ CPRIPYSSTR NFSVPYVLPS LDAHSPVQNV AVFTDSALPA
AIFVAVRNRI LVASPELHLH SVLITGPVGS TECEICHLCP VTTDSPEDMD NVLLLLDPLE
PWLYSCGTAR HGLCYQHQLE VWDGKVTITT TRCLYTATGN RPTSCPDCVA SPLGTSATVV
ATSYASYFYL GSTINSSVAA QYSPQSVSVR RLKGTLDGFS DDFQWLTVLP QYRDNYTIHY
IHSFADGDYV YFLTVQLEPP GSAVYHTSLA RLSAHERNLR HYRELVLDCR FDSYLLTLAN
FSLGEPGPVQ GAMGLQSHSL YFTAGTKVWQ LNVTGPGCRH FSTCQRCLRA ERFMGCGWCR
DGCRRQHECH GPWVQDSCPP LLTDFHPRSA PLRGQTRVTL CGMTFRSHLE PDPQRIPSGT
YRVAVGQRGC FVLLEESRSH RPLPTSRHKE FVDVLVCELE LGSLTVMRGP AEVVLTVEEP
NRSSGFHVNG SSSLGGFFFV EPRISALHPP FGPQGGGTQL SLHGMHLSSG SSWQVMVNGS
ECPLSRQPSQ GDGVIWCTVP AAGGLGTVQV SLRIDQEEFL APLSFQYRPD PSISAILPSC
SYEGSVLTII GTHLNSVYRT KIYFEANGVK TEATECQDPQ TPEQLLCPSP AFPFESKVET
ALGNLSVLLD GAAGHRHFRL RYYPKPEVFP LEQEGRRLHL KPGDDEIEVH QLGLDAVATC
MNITMTVGGR DCHPNVLKNE ELTCRLPREL RLPPAGAPVE ICVNGACEAL GWVLPAASSL
GMAASLALGT GITFLVCCVL AAVLLHWRWR KTAGTENLEL LVHPGRGDIP TTTQRPGVDY
REVLVLPTAG SPGPMVPRAR FTSAGASAAG SVAGDGSPIP LLRATSCCLE DLRPELLEEV
KDILIPEERL VTHRHQVIGK GHFGSVYHGT YTDPVLGDLH CAVKSLHRIT DLEEVEEFLR
EGILMKSFHH PQVLSLLGIC LPRHGLPLVV LPYMRHGDLR HFIRAQERSP TVKDLVGFGL
QVALGMEYLA QKKFVHRDLA ARNCMLDETL TVKVADFGLA RDVFGKEYYS IRQHRHAKLP
VKWMALESLQ TQKFTTKSDV WSFGVLMWEL LTRGASPYPG VDPYDMTSYL LRGRRLPQPC
HCPDTLSRYG VMLSCWAPAP EERPSFTGLV GELERVLATL EGKHYVNLAV TYVNLECGPL
FPPAPSEHLP EGEDENRDNA KEEEEEEEDM D
//
