VER3_CAEEL
ID VER3_CAEEL Reviewed; 1227 AA.
AC Q21038;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Tyrosine-protein kinase receptor ver-3 {ECO:0000305};
DE EC=2.7.10.1;
DE AltName: Full=Vascular endothelial growth factor receptor related 3 {ECO:0000303|PubMed:12161275};
DE Flags: Precursor;
GN Name=ver-3 {ECO:0000312|WormBase:F59F3.1};
GN ORFNames=F59F3.1 {ECO:0000312|WormBase:F59F3.1};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2] {ECO:0000305}
RP TISSUE SPECIFICITY.
RX PubMed=12161275; DOI=10.1016/s0304-3940(02)00595-5;
RA Popovici C., Isnardon D., Birnbaum D., Roubin R.;
RT "Caenorhabditis elegans receptors related to mammalian vascular endothelial
RT growth factor receptors are expressed in neural cells.";
RL Neurosci. Lett. 329:116-120(2002).
RN [3] {ECO:0000305}
RP FUNCTION.
RX PubMed=24004945; DOI=10.1242/dev.095190;
RA Dalpe G., Tarsitano M., Persico M.G., Zheng H., Culotti J.;
RT "C. elegans PVF-1 inhibits permissive UNC-40 signalling through CED-10
RT GTPase to position the male ray 1 sensillum.";
RL Development 140:4020-4030(2013).
CC -!- FUNCTION: Receptor tyrosine kinase which may be involved, downstream of
CC pvf-1, in the positioning of ray 1, the most anterior ray sensillum in
CC the male tail. {ECO:0000269|PubMed:24004945}.
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 -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in the ALA neuron.
CC {ECO:0000269|PubMed:12161275}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; BX284606; CAA91990.1; -; Genomic_DNA.
DR PIR; T23004; T23004.
DR RefSeq; NP_509836.1; NM_077435.4.
DR AlphaFoldDB; Q21038; -.
DR SMR; Q21038; -.
DR DIP; DIP-26190N; -.
DR STRING; 6239.F59F3.1; -.
DR EPD; Q21038; -.
DR PaxDb; Q21038; -.
DR PeptideAtlas; Q21038; -.
DR EnsemblMetazoa; F59F3.1.1; F59F3.1.1; WBGene00006896.
DR GeneID; 181289; -.
DR KEGG; cel:CELE_F59F3.1; -.
DR UCSC; F59F3.1; c. elegans.
DR CTD; 181289; -.
DR WormBase; F59F3.1; CE03437; WBGene00006896; ver-3.
DR eggNOG; KOG0200; Eukaryota.
DR GeneTree; ENSGT00970000195899; -.
DR HOGENOM; CLU_260533_0_0_1; -.
DR InParanoid; Q21038; -.
DR OMA; KIMCAIG; -.
DR OrthoDB; 236292at2759; -.
DR PhylomeDB; Q21038; -.
DR PRO; PR:Q21038; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00006896; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0043235; C:receptor complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IBA:GO_Central.
DR GO; GO:0045138; P:nematode male tail tip morphogenesis; IGI:WormBase.
DR GO; GO:0033674; P:positive regulation of kinase activity; IBA:GO_Central.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
DR Gene3D; 2.60.40.10; -; 5.
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; 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 InterPro; IPR020635; Tyr_kinase_cat_dom.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR SMART; SM00409; IG; 4.
DR SMART; SM00408; IGc2; 4.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF48726; SSF48726; 4.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50835; IG_LIKE; 3.
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; Cell membrane; Disulfide bond; Glycoprotein;
KW Immunoglobulin domain; Kinase; Membrane; Nucleotide-binding; Receptor;
KW Reference proteome; Repeat; Signal; Transferase; Transmembrane;
KW Transmembrane helix; Tyrosine-protein kinase.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..1227
FT /note="Tyrosine-protein kinase receptor ver-3"
FT /evidence="ECO:0000305"
FT /id="PRO_0000434515"
FT TOPO_DOM 18..764
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 765..785
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 786..1227
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 20..110
FT /note="Ig-like C2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 200..325
FT /note="Ig-like C2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 565..666
FT /note="Ig-like C2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 673..758
FT /note="Ig-like C2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 847..1175
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1194..1227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1211..1227
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1030
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 853..861
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 886
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CARBOHYD 119
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 211
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 245
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 255
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 381
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 425
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 528
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 697
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 52..110
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 204..313
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 592..650
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 696..740
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 1227 AA; 140549 MW; 46397D60FD6FC2DB CRC64;
MKLKLTVLLI LVHASASYKP PAIEVEDYQV QEHDSIGKFV ELEEHTRLIL KCSAHHNGDL
KYNFPSMEGN VGYDENNFKK RMEEYYDDAF GDKVLTLNDV RESDTGTYSC SSMEHSSLND
TIYVFVHRKK VFLPLKSVMI IYKQGEVMVP CKTTKFVDKS DIELYASNVL VKEASKYNYD
QRYGFKITKK LYSEKQIVDV NFECRYKKEE NQTATYIITE KEASSDDGYH FSWEKGFQWP
HVGYNFSLTC NLNYNGSKIF HGYTNKLSIE CPQCSHDPGS HVHVDRHRII GNKISTTVRI
QHLELEDSGK YTCIWEHENK ETKYTDYHLY VAPKKAQIKV IETSPTIMRI KENRATSLTA
KFAIYPFEKE SYTAKWSRIY NSSIHEGPQS ETIINDDFRK IAATSFGDGA FSENLDIKAF
AVSTNMSGTY VLSISHMDTV QVVQWEVAIE NDEPDVQITV REPSSFFISN QEYYKPDTNL
HIECISISIP PADVVFEYKT KNSEQFQEIE PNKLVSVGGT FDRGLIYNVT FTEGMDLKCS
SIRKGNRAIT VNKLIKIGEG FEVRPHHEKS SKATESEPSK IIYEGDNVKL TCVFPLDSDD
WSVSWRFENS KSSDISSIPT TTETEIKQYS KHLILNLRDV TTSFTGTYTC VVKNEDSEKL
LETSIDVKAI SKPSITGGNS NAVVIVDYDQ YFEINCNMTG TPPPVYQWFK DGNPYTHGDV
DGSILRVSRA RGEDDGEFHC LATNRAGDKL NSIEVQVNNA PKGSLFFYWF LALLLLISII
AVFLLTCKLR ASNRLTKQKD IALNTLYETM IKHQAGPLPE EMKDLPVEER TYYLPYNNDY
EIDPVNLEIL NPIGSGHFGV VKKGLLGMAY PKSKIESKTR LPVAVKSSTN PFNVELQKMM
AEELKVMCAI PKNPNVLALI GAVTKNMRQG QLYIVTEFID GGNLREFLQA HRNTFINELV
EDEHVPVDDS YLVPNSVKKK IYKFDEKLGE GTRLLVEDPD ALCTSDLLSI GLQIAKGMAW
LADVPCVHRD LACRNVLITK TKIVRIADFG LSKKHTNKTY YRTKKSKDTP LPVRWMPLEC
IEEFKFTQKS DVWSFGICLY EIFTLGGTPY PNCDTFNVIE FIRNGNRNKQ PEYCHDEIYE
LMKVCWQFNP KDRPTFNDCI TFFENHMRDS SSQFLERVEN MLHTEMQEQS KLDDWIQDSR
PDVPNVSFQK SPKKQKEERY LIVESHA
