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 03-AUG-2022, entry version 179.
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 investigating
RT 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, 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 -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; BX284606; CAA91991.2; -; Genomic_DNA.
DR RefSeq; NP_509835.2; NM_077434.2.
DR AlphaFoldDB; Q21041; -.
DR SMR; Q21041; -.
DR STRING; 6239.F59F3.5; -.
DR PaxDb; Q21041; -.
DR PeptideAtlas; Q21041; -.
DR PRIDE; 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 GeneTree; ENSGT00970000195899; -.
DR HOGENOM; CLU_260533_0_0_1; -.
DR InParanoid; Q21041; -.
DR OrthoDB; 236292at2759; -.
DR PhylomeDB; Q21041; -.
DR PRO; PR:Q21041; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00006897; Expressed in embryo and 2 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; -; 3.
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 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; Disulfide bond; Glycoprotein;
KW Immunoglobulin domain; Kinase; Membrane; Nucleotide-binding; Receptor;
KW Reference proteome; Repeat; Transferase; Transmembrane;
KW Transmembrane helix; Tyrosine-protein kinase.
FT CHAIN 1..1216
FT /note="Tyrosine-protein kinase receptor ver-4"
FT /evidence="ECO:0000305"
FT /id="PRO_0000434516"
FT TOPO_DOM 1..789
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 790..810
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 811..1216
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 596..691
FT /note="Ig-like C2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 697..783
FT /note="Ig-like C2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 870..1181
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 1042
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 876..884
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 908
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CARBOHYD 142
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 195
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 206
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 283
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 333
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 348
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 384
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 402
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 412
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 496
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 508
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 588
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 599
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 664
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 703
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 619..675
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 721..765
FT /evidence="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
