ID A0A3M0K9Q8_HIRRU Unreviewed; 1052 AA.
AC A0A3M0K9Q8;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Receptor protein-tyrosine kinase {ECO:0008006|Google:ProtNLM};
GN ORFNames=DUI87_15259 {ECO:0000313|EMBL:RMC07790.1};
OS Hirundo rustica rustica.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Sylvioidea; Hirundinidae;
OC Hirundo.
OX NCBI_TaxID=333673 {ECO:0000313|EMBL:RMC07790.1, ECO:0000313|Proteomes:UP000269221};
RN [1] {ECO:0000313|EMBL:RMC07790.1, ECO:0000313|Proteomes:UP000269221}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Chelidonia {ECO:0000313|EMBL:RMC07790.1};
RC TISSUE=Blood {ECO:0000313|EMBL:RMC07790.1};
RA Formenti G., Chiara M., Poveda L., Francoijs K.-J., Bonisoli-Alquati A.,
RA Canova L., Gianfranceschi L., Horner D.S., Saino N.;
RT "A high quality draft genome assembly of the barn swallow (H. rustica
RT rustica).";
RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
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:RMC07790.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; QRBI01000119; RMC07790.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3M0K9Q8; -.
DR STRING; 333673.A0A3M0K9Q8; -.
DR Proteomes; UP000269221; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004713; F:protein tyrosine kinase activity; IEA:InterPro.
DR CDD; cd00096; Ig; 2.
DR CDD; cd05046; PTK_CCK4; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 7.
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; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR020635; Tyr_kinase_cat_dom.
DR PANTHER; PTHR45080; CONTACTIN 5; 1.
DR PANTHER; PTHR45080:SF21; INACTIVE TYROSINE-PROTEIN KINASE 7; 1.
DR Pfam; PF07679; I-set; 4.
DR Pfam; PF13927; Ig_3; 2.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PIRSF; PIRSF000615; TyrPK_CSF1-R; 7.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00409; IG; 7.
DR SMART; SM00408; IGc2; 7.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF48726; Immunoglobulin; 7.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50835; IG_LIKE; 7.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|PIRSR:PIRSR000615-2};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Immunoglobulin domain {ECO:0000256|ARBA:ARBA00023319};
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|PIRSR:PIRSR000615-2};
KW Receptor {ECO:0000256|ARBA:ARBA00023170};
KW Reference proteome {ECO:0000313|Proteomes:UP000269221};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..1052
FT /note="Receptor protein-tyrosine kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018332462"
FT TRANSMEM 690..711
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 38..112
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 120..208
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 217..286
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 312..392
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 397..476
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 491..572
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 577..665
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 784..1049
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1028..1052
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1035..1052
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 912
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-1"
FT BINDING 791..798
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT BINDING 818
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT BINDING 864..870
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT BINDING 916
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT BINDING 917
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
SQ SEQUENCE 1052 AA; 116435 MW; 179BEC534951DF58 CRC64;
MAAARRMAAV RALLVLAVGT QASILFTKEP YSQDALHGRG AILRCEVKEP ADVEFQWLQN
GLPVQDTEQR FKEGSNLQFA AVDRHRDAGV FQCLARNVLS GEEARSANAS FNIKWIETGS
VVLKQPASVA EIQPSSTVVL RCHIDGHPRP TWQWFRDGSP LPEGRGTYSV SSKERTLTLQ
SAGPDDNGLY YCCARSAVGF VCSHNNFTLN VVDESFPQAV IVPQDLIVTK NEEAMFDCQF
AAVPPPTQEW LFEDNPISNR SKITVFANGS LLITQVRARS TGVYKCVGRG QRGKTLVLKA
TLRLAEIEDM APFSPKVLTA NQGHRVSCPA PQGVPTPQVW WERNQERVPT AGRVYQEAEQ
LIFTSITETD AGIYTCHAAN KAGEKKQELS VTVATVPKWV EMPKDSQLEE SKPGYLHCLS
KASLKPTVTW YRNGVSISED SRFEISENGT LRINNVEVYD GTMYKCVSST PAGSIEGYAR
VHVLEKLKFT PPPQPLQCME FDKEVTVSCS ATGREKPTIQ WTKTDGSSLP SHVSHNAGIL
SFHKVSRSDS GNYTCIASNR PQGEIRATVQ LVVAVFVTFK LEPEPTTVYQ GHTAMFQCQA
EGDPVPHIQW KGKDKILDPG KLLPRIQIMP NGSLVIYDVT TEDSGKYTCI AGNSCNIKHR
EAFLYVVDKP AAEEDEGPGS HTPYKMIQTI GLSVGAAVAY IIIVLGLMFY CKKRRKAKRL
KKHPEGEEPE MECLNGEAGG ALLQNGQMTA EIQEEVALTN LGGSSGASKR HSATDKMHFP
RSNLQTITTL GRGEFGEVFL AKAKGAEDGE GEVLVLVKSL QTRDEQLQLD FRREAEMFGK
LNHANVVRLL GLCREAEPHY MVLEYVDLGD LKQFLRISKS KDESLKPQPL TTKHKVALGM
EHLSNGRFVH RDLAARNCLV SAQRQVKVSS LSLSKDVYNS EYYHFRQAWI PLRWMPPEAV
LEDEFSTKSD VWSFGVLMWE VFTHGEMPYA PLADDEVLAG LQSGKTKLPQ PEGCPSRLAK
LMQRCWAPSP KDRPSFSELA TTLGDSPAES KA
//
