ID C5H7S0_APIME Unreviewed; 1238 AA.
AC C5H7S0;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 2.
DT 24-JAN-2024, entry version 80.
DE SubName: Full=Venus kinase receptor {ECO:0000313|EMBL:ACF34409.1};
DE Flags: Fragment;
GN Name=VKR {ECO:0000313|EMBL:ACF34409.1};
OS Apis mellifera (Honeybee).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea;
OC Anthophila; Apidae; Apis.
OX NCBI_TaxID=7460 {ECO:0000313|EMBL:ACF34409.1};
RN [1] {ECO:0000313|EMBL:ACF34409.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=19461966; DOI=10.1371/journal.pone.0005651;
RA Ahier A., Rondard P., Gouignard N., Khayath N., Huang S., Trolet J.,
RA Donoghue D.J., Gauthier M., Pin J.P., Dissous C.;
RT "A new family of receptor tyrosine kinases with a venus flytrap binding
RT domain in insects and other invertebrates activated by aminoacids.";
RL PLoS ONE 4:E5651-E5651(2009).
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};
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DR EMBL; EU878396; ACF34409.1; -; mRNA.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004383; F:guanylate cyclase activity; IEA:UniProtKB-EC.
DR GO; GO:0004713; F:protein tyrosine kinase activity; IEA:InterPro.
DR GO; GO:0007154; P:cell communication; IEA:UniProt.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd06366; PBP1_GABAb_receptor; 1.
DR CDD; cd00192; PTKc; 1.
DR Gene3D; 3.40.50.2300; -; 2.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR001828; ANF_lig-bd_rcpt.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR028082; Peripla_BP_I.
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:SF489; PROTEIN KINASE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR24416; TYROSINE-PROTEIN KINASE RECEPTOR; 1.
DR Pfam; PF01094; ANF_receptor; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF53822; Periplasmic binding protein-like I; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PE 2: Evidence at transcript level;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Kinase {ECO:0000313|EMBL:ACF34409.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Receptor {ECO:0000313|EMBL:ACF34409.1};
KW Transferase {ECO:0000313|EMBL:ACF34409.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 813..837
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 877..1150
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1214..1238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 909
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
FT UNSURE 1101
FT /note="D or N"
FT /evidence="ECO:0000313|EMBL:ACF34409.1"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ACF34409.1"
FT NON_TER 1238
FT /evidence="ECO:0000313|EMBL:ACF34409.1"
SQ SEQUENCE 1238 AA; 142279 MW; 6A51354948716F1A CRC64;
KIVISNRCLT MLEDVNPKRV IHLDGQPLNI NFEVSRRVTQ RLATIIMKIF LTEVLGYSKV
SIYEKEDEFR AEETFSRLSD DIMFSSKLPM VNMEVWIPPH LDTMPLLNSH EVKECGSIAP
PGRFGWFVPT ALSRRNDNWI IFTELEKASR FEMDESTLDS IRNFTIDPKT STYYCQESYC
QQGMYIPEWC QGKPCALLLT SYIDVTNLVK DRIDQMKLYV NVIWFGPNLK HVIKLAEELM
FDRNSSTSID RSLVFLHWTP STVIPNERDF VSIDFPRCGA TSSEIGCKYE SNRLTKLVWA
RLEYAAKLAY EAINRAKFTR EMYEDLIDRR NRDSSMNEEE IACDWLRENL NYTLDAWMPN
TADKNILYVG GIFPMSETFY SGKAILVAAM MAKEAINVNN TILRDYNFTL LVNDGQCKSD
MVMRSFINYI VHNQYEKLVG VLGPACSETV EPLVGVSKHY KTVVISYSAE GSSFNDRTKY
PYFFRTIGEN KQYKHVYLQL LKKLGWKRVA SLTEDGQKYT EYISYMQDLF RDNGIVFVAN
AKFPREREPI VMTKYLQDFK QKKAKIIIAD VYDQAARQVM CNAYKLEMTA VQGYVWFLPL
WLRPEWYDTD RYNQEGEQVP CTTAEMSKAI NGYLGLSHAY FAPDNDIMQE GITVRQWRDR
YELQCQNKEQ PPSNYAGYAY DAMWTYAYAM DRLLRENQSY VFDLHSNHTI NRLTDIIGET
DFYGVSGRIK FFGGPSRYSV INIVQHVNNE TRLVGNFYPN VSEKQHEVAG GKLDLNVSSL
VWLSKSMPDD GSEPPQRCVI GGFADFINVS CEVAFVIVNI IGFTLLGIFL IIGFLIIKQR
YERKVREQRE YLKSMGISYA CDDSSDLDKW EIPRHRVVIN RKLGEGAFGT VYGGEAFFPE
KGWLAVAVKT LKIGSSTEEK LDFLSEVEVM KQFEHKNIIK LLGVCIKSEP VLTVMEFMLY
GDLKTYLLAR RHLVNDNSYE DSDEISNKKL TAMALDVARA LSYLAQSKYV HRDIASRNCL
VNAQRVVKLG DFGMTRLMYE NDYYKFNRRR MLPVRWMAPE SLGLGIFSPA SDVWSYGVLL
YEIITFGSFP FQGMSNIEVL DHVKSGNSLM VPKGVKIQLE NLMYSCWRLD HIKRPTAPEI
VEFLATNPRI LSPCLDVPLA SVQXEHTGQL DIELPENLRK FSLSWSPQNS TTRPASTSSP
FGVPYPSLLD INDHDDKPIQ NSIMGNGIAD TESSRPLL
//
