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Database: UniProt
Entry: VER4_CAEEL
LinkDB: VER4_CAEEL
Original site: VER4_CAEEL 
ID   VER4_CAEEL              Reviewed;        1216 AA.
AC   Q21041;
DT   14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 2.
DT   08-MAY-2019, entry version 167.
DE   RecName: Full=Tyrosine-protein kinase receptor ver-4 {ECO:0000305};
DE            EC=2.7.10.1;
DE   AltName: Full=Vascular endothelial growth factor receptor related 4 {ECO:0000305};
GN   Name=ver-4 {ECO:0000312|WormBase:F59F3.5};
GN   ORFNames=F59F3.5 {ECO:0000312|WormBase:F59F3.5};
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
RT   investigating biology.";
RL   Science 282:2012-2018(1998).
RN   [2] {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,
CC       downstream of pvf-1, in the positioning of ray 1, the most
CC       anterior ray sensillum in the male tail.
CC       {ECO:0000269|PubMed:24004945}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-
CC         tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136,
CC         Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216;
CC         EC=2.7.10.1;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass
CC       type I membrane protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC       kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
DR   EMBL; BX284606; CAA91991.2; -; Genomic_DNA.
DR   RefSeq; NP_509835.2; NM_077434.2.
DR   STRING; 6239.F59F3.5; -.
DR   PaxDb; Q21041; -.
DR   PeptideAtlas; Q21041; -.
DR   EnsemblMetazoa; F59F3.5.1; F59F3.5.1; WBGene00006897.
DR   EnsemblMetazoa; F59F3.5.2; F59F3.5.2; WBGene00006897.
DR   GeneID; 186632; -.
DR   KEGG; cel:CELE_F59F3.5; -.
DR   UCSC; F59F3.5; c. elegans.
DR   CTD; 186632; -.
DR   WormBase; F59F3.5; CE43265; WBGene00006897; ver-4.
DR   eggNOG; KOG0200; Eukaryota.
DR   eggNOG; COG0515; LUCA.
DR   GeneTree; ENSGT00940000166704; -.
DR   HOGENOM; HOG000021122; -.
DR   InParanoid; Q21041; -.
DR   OrthoDB; 236292at2759; -.
DR   PhylomeDB; Q21041; -.
DR   Reactome; R-CEL-109704; PI3K Cascade.
DR   Reactome; R-CEL-1257604; PIP3 activates AKT signaling.
DR   Reactome; R-CEL-1433557; Signaling by SCF-KIT.
DR   Reactome; R-CEL-1433559; Regulation of KIT signaling.
DR   Reactome; R-CEL-186763; Downstream signal transduction.
DR   Reactome; R-CEL-186797; Signaling by PDGF.
DR   Reactome; R-CEL-5673001; RAF/MAP kinase cascade.
DR   Reactome; R-CEL-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
DR   PRO; PR:Q21041; -.
DR   Proteomes; UP000001940; Chromosome X.
DR   Bgee; WBGene00006897; Expressed in 3 organ(s), highest expression level in multi-cellular organism.
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:0008284; P:positive regulation of cell population proliferation; IBA:GO_Central.
DR   GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
DR   Gene3D; 2.60.40.10; -; 2.
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; Pkinase_Tyr; 1.
DR   PRINTS; PR00109; TYRKINASE.
DR   SMART; SM00409; IG; 4.
DR   SMART; SM00408; IGc2; 3.
DR   SMART; SM00219; TyrKc; 1.
DR   SUPFAM; SSF48726; SSF48726; 3.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS50835; IG_LIKE; 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   ATP-binding; Cell membrane; Complete proteome; Disulfide bond;
KW   Glycoprotein; Immunoglobulin domain; Kinase; Membrane;
KW   Nucleotide-binding; Receptor; Reference proteome; Repeat; Transferase;
KW   Transmembrane; Transmembrane helix; Tyrosine-protein kinase.
FT   CHAIN         1   1216       Tyrosine-protein kinase receptor ver-4.
FT                                {ECO:0000305}.
FT                                /FTId=PRO_0000434516.
FT   TOPO_DOM      1    789       Extracellular. {ECO:0000255}.
FT   TRANSMEM    790    810       Helical. {ECO:0000255}.
FT   TOPO_DOM    811   1216       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN      596    691       Ig-like C2-type 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00114}.
FT   DOMAIN      697    783       Ig-like C2-type 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00114}.
FT   DOMAIN      870   1181       Protein kinase. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159}.
FT   NP_BIND     876    884       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159}.
FT   ACT_SITE   1042   1042       Proton acceptor. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159}.
FT   BINDING     908    908       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159}.
FT   CARBOHYD    142    142       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00498}.
FT   CARBOHYD    195    195       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00498}.
FT   CARBOHYD    206    206       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00498}.
FT   CARBOHYD    245    245       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00498}.
FT   CARBOHYD    283    283       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00498}.
FT   CARBOHYD    333    333       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00498}.
FT   CARBOHYD    348    348       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00498}.
FT   CARBOHYD    384    384       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00498}.
FT   CARBOHYD    402    402       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00498}.
FT   CARBOHYD    412    412       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00498}.
FT   CARBOHYD    496    496       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00498}.
FT   CARBOHYD    508    508       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00498}.
FT   CARBOHYD    588    588       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00498}.
FT   CARBOHYD    599    599       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00498}.
FT   CARBOHYD    664    664       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00498}.
FT   CARBOHYD    703    703       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00498}.
FT   DISULFID    619    675       {ECO:0000255|PROSITE-ProRule:PRU00114}.
FT   DISULFID    721    765       {ECO:0000255|PROSITE-ProRule:PRU00114}.
SQ   SEQUENCE   1216 AA;  140906 MW;  67AFC63D918F177D CRC64;
     MRVSLTEFLV LAQVVTTLQP ITIKVDFHEV KHHESIGDYV ELVEGKNRDI SLTCYGQHKN
     LKIEPPKREE HAGFPEIGIR TSAEWKKNEY WFLLKNVRQC DTGSYYCVSD EFKESMLQNT
     VHIFVRKLDI FVPLKTIYHE HNGSEIIIPC KTTKFVDTKN VELYVNQVKL NSALQGYDQR
     YGFKLTKNMY TMKPNSTVFF ECKYTNDSNQ DLDYYISNSD PDATLIDQYF FYWEKSNDVP
     YVGNNYSITC HLVYIGSDSL RPLNHQEIVL ECPQNQCDGG YNNQSAHEIE KRSSGLRFGD
     PSSQDIVEKN TMLRYDRLSV YDRKTSRTVN FQNLTSEDSG IYRCTWRNRS KTNIVLDYDL
     NFNQKGTQIK IIETSKQRLK MRKNESTLLF VKFAVFPINK KNYTAKWSRL YNSTVEGGQQ
     VETIRNGFFR QITTKTSGRN VFLETLNLKS PKIEMSGIYV LSISNMDIVQ QVKWIIEVEN
     DEPNAQLTIR DPLTLNISNQ LFLPLNTNLS IFCLAVSSSP TDVIFEYRTD ENEWFRGFYK
     NKLRKIDDTF EKGFIYNFVL AKRTDFKCIN VKKKKTSTKF ITVTSNANKT FHEIEKSVNA
     TKTEPSDIIF EGDNVRLTCV VPYGAVEFDV FWKFENPKML KYTTFPAMHP VKDRYKRVIL
     NVRNITIDFT GTYYCIVKNK EFEHRFETSI SVEKVSPPFL LNNNSRSIIS ASNGQMFDIN
     CKVNGVPTPD YTWFKDGYPY TKGKVIGNAL HVSKAEKRDN GIFWCSATNR AGTTIDYIEV
     KVAGASSSSF FWLFITFFAF VVVGIVVSLL WKLFGQKDLK PSELSLNNLK RATDEYQKYT
     VSEKINNLPV EERIDYLTYN EDYEIDLENL EILETLGSGQ FGIVKKGYLN MASSKNFGFE
     SRLSVAIKSS TDSSNMELQK MFFEELKLMC AIPKHPNVLS LVGAVTKNME IGELFIVTEL
     IDGGNLREFL RERRDVFANE LVEKGYIFLT NVRENVPKRE VEKEQLLIDE FNSLCTSDLL
     SIGLQIANGM DWLANIPCVH RDLACRNVLI SKTKIIRIAD FGLAKKHTDK AYYRVRESLD
     TPLPVRWMPL ESITDLTFTQ KSDVWSYGIC LYEIFTLGGT PYPDCPNFSL VEYIKTGNIN
     KRPSNCHKDV YKIMKMCWQA SPDDRPTFAE CIKLFKNHIQ YFASKLLQQI EKDLECEKNN
     QQKFHYWVQK PTQLFF
//
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