ID A0A1D2MUQ1_ORCCI Unreviewed; 629 AA.
AC A0A1D2MUQ1;
DT 30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Vascular endothelial growth factor receptor 3 {ECO:0000313|EMBL:ODM96773.1};
GN ORFNames=Ocin01_09910 {ECO:0000313|EMBL:ODM96773.1};
OS Orchesella cincta (Springtail) (Podura cincta).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Collembola;
OC Entomobryomorpha; Entomobryoidea; Orchesellidae; Orchesellinae; Orchesella.
OX NCBI_TaxID=48709 {ECO:0000313|EMBL:ODM96773.1, ECO:0000313|Proteomes:UP000094527};
RN [1] {ECO:0000313|EMBL:ODM96773.1, ECO:0000313|Proteomes:UP000094527}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Mixed pool {ECO:0000313|EMBL:ODM96773.1};
RX PubMed=27289101; DOI=10.1093/gbe/evw134;
RA Faddeeva-Vakhrusheva A., Derks M.F., Anvar S.Y., Agamennone V., Suring W.,
RA Smit S., van Straalen N.M., Roelofs D.;
RT "Gene Family Evolution Reflects Adaptation to Soil Environmental Stressors
RT in the Genome of the Collembolan Orchesella cincta.";
RL Genome Biol. Evol. 8:2106-2117(2016).
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: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the AMP family. {ECO:0000256|ARBA:ARBA00007887}.
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:ODM96773.1}.
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DR EMBL; LJIJ01000505; ODM96773.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1D2MUQ1; -.
DR STRING; 48709.A0A1D2MUQ1; -.
DR OMA; CHWNGSL; -.
DR OrthoDB; 1701853at2759; -.
DR Proteomes; UP000094527; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR CDD; cd00192; PTKc; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR013006; Antimicrobial_C6_CS.
DR InterPro; IPR009101; Gurmarin/antifun_pep.
DR InterPro; IPR024206; Gurmarin/antimicrobial_peptd.
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 PANTHER; PTHR24416:SF600; PDGF-AND VEGF-RECEPTOR RELATED, ISOFORM J; 1.
DR PANTHER; PTHR24416; TYROSINE-PROTEIN KINASE RECEPTOR; 1.
DR Pfam; PF11410; Antifungal_pept; 4.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SUPFAM; SSF57048; Gurmarin-like; 5.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS60011; PLANT_C6_AMP; 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 Antimicrobial {ECO:0000256|ARBA:ARBA00022529};
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Fungicide {ECO:0000256|ARBA:ARBA00022577};
KW Knottin {ECO:0000256|ARBA:ARBA00022854};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Receptor {ECO:0000313|EMBL:ODM96773.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000094527};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 248..272
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 325..619
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT BINDING 352
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 629 AA; 69429 MW; C3EF59EBB94EC915 CRC64;
MSSCIKDHNP CHYDGSLGYC CSSNCLQFEG QNFGTCMPKP TSQPSSTTPT SSSSSNPSCI
KDNERCHYDG SLGYCCSGNC LHIAGQAFGA CVAKPTTQPP TTSSTSSSLS CIEDNGRCHW
NGSLGYCCST NCLQLEGQPF GKCEPKATSR PSTSSSSSSC LGDKEQCKSD GSMGSCCSFN
CQQLEGDAFG QCVGSSPPTV PAKCLNDGAD CKSDGSFGFC CSKICDVIAP HTEGTCRIRP
NQSSNNSWII YVSVSMSVVV ILAVLGFVWL YYRQRKLESK LSKDETEHFF KGNPEAISIN
GYAHEMVEDL PYNTDLEIAV SDFWINKDLQ LGSGCFGLVL AGKVKGTDVA AKTIRNKTDS
GSHLRSLLSE IKILQYIGKF DNIVSLVGCN TADLTNGNVY MFLEFCKLGS LENYLRTNKY
HFSDSLKSET TSRTANERQY ENSPGQKDEV ALTHTDLLTW SLQITNAMRY LAGKKVIHAD
LATRNVLLLT KTCAKVTDFG LSRRLYDYSN YVKKQQEPLP WRWMAIESLQ HLTFSHQSDV
WSLGVTMWEV YSLGDIPYPG LSWTADFVSN LENNLRPNKP ARASHELYDI MLDCWKPIAD
TRPTFEMIYK RLQTQMEALS NITAYTDVT
//
