VER1_CAEEL
ID VER1_CAEEL Reviewed; 1083 AA.
AC G5ED65;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Protein ver-1 {ECO:0000305};
DE AltName: Full=Vascular endothelial growth factor receptor related 1 {ECO:0000303|PubMed:10568743};
GN Name=ver-1 {ECO:0000312|WormBase:T17A3.1};
GN ORFNames=T17A3.1 {ECO:0000312|WormBase:T17A3.1};
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|EMBL:AAF00548.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Bristol N2 {ECO:0000312|EMBL:AAF00548.1};
RX PubMed=10568743; DOI=10.1101/gr.9.11.1026;
RA Popovici C., Roubin R., Coulier F., Pontarotti P., Birnbaum D.;
RT "The family of Caenorhabditis elegans tyrosine kinase receptors:
RT similarities and differences with mammalian receptors.";
RL Genome Res. 9:1026-1039(1999).
RN [2] {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 [3] {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 [4] {ECO:0000305}
RP FUNCTION, TISSUE SPECIFICITY, AND INDUCTION BY HIGH TEMPERATURES.
RX PubMed=21350017; DOI=10.1242/dev.058305;
RA Procko C., Lu Y., Shaham S.;
RT "Glia delimit shape changes of sensory neuron receptive endings in C.
RT elegans.";
RL Development 138:1371-1381(2011).
RN [5] {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: Involved in amphid glia remodeling during entry into dauer
CC stage by promoting the fusion of sheath amphid cells which encloses AWC
CC neuron sensory endings (PubMed:21350017). May be involved, downstream
CC of pvf-1, in the positioning of ray 1, the most anterior ray sensillum
CC in the male tail (PubMed:24004945). {ECO:0000269|PubMed:21350017,
CC ECO:0000269|PubMed:24004945}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in amphid and phasmid sheath cells, the
CC muscular intestinal cell and the first and last intestinal cells
CC (PubMed:12161275, PubMed:21350017). Expression in amphid and phasmid
CC sheath cells is increased in dauer animals (PubMed:21350017).
CC {ECO:0000269|PubMed:12161275, ECO:0000269|PubMed:21350017}.
CC -!- INDUCTION: By high temperatures. {ECO:0000269|PubMed:21350017}.
CC -!- DOMAIN: The protein kinase domain is predicted to be catalytically
CC inactive. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. {ECO:0000305}.
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DR EMBL; AF188751; AAF00548.1; -; mRNA.
DR EMBL; BX284603; CCD66075.1; -; Genomic_DNA.
DR PIR; T33434; T33434.
DR PIR; T33618; T33618.
DR RefSeq; NP_497162.2; NM_064761.2.
DR AlphaFoldDB; G5ED65; -.
DR STRING; 6239.T17A3.1; -.
DR PaxDb; G5ED65; -.
DR EnsemblMetazoa; T17A3.1.1; T17A3.1.1; WBGene00006894.
DR GeneID; 175182; -.
DR KEGG; cel:CELE_T17A3.1; -.
DR CTD; 175182; -.
DR WormBase; T17A3.1; CE31854; WBGene00006894; ver-1.
DR eggNOG; KOG0200; Eukaryota.
DR GeneTree; ENSGT00970000195899; -.
DR HOGENOM; CLU_260533_0_0_1; -.
DR InParanoid; G5ED65; -.
DR OMA; CKINDEN; -.
DR OrthoDB; 236292at2759; -.
DR PhylomeDB; G5ED65; -.
DR Reactome; R-CEL-109704; PI3K Cascade.
DR Reactome; R-CEL-1257604; PIP3 activates AKT signaling.
DR Reactome; R-CEL-186763; Downstream signal transduction.
DR Reactome; R-CEL-186797; Signaling by PDGF.
DR Reactome; R-CEL-210993; Tie2 Signaling.
DR Reactome; R-CEL-5673001; RAF/MAP kinase cascade.
DR Reactome; R-CEL-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
DR Reactome; R-CEL-9607240; FLT3 Signaling.
DR PRO; PR:G5ED65; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00006894; Expressed in embryo and 1 other tissue.
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 Pfam; PF13895; Ig_2; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00409; IG; 5.
DR SMART; SM00408; IGc2; 3.
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.
PE 2: Evidence at transcript level;
KW ATP-binding; Cell membrane; Disulfide bond; Glycoprotein;
KW Immunoglobulin domain; Membrane; Nucleotide-binding; Receptor;
KW Reference proteome; Repeat; Transmembrane; Transmembrane helix.
FT CHAIN 1..1083
FT /note="Protein ver-1"
FT /evidence="ECO:0000305"
FT /id="PRO_0000434513"
FT TOPO_DOM 1..735
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 736..756
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 757..1083
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 563..647
FT /note="Ig-like C2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 656..731
FT /note="Ig-like C2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 803..1076
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 809..817
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 832
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CARBOHYD 132
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 226
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 261
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 387
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 433
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 572
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 603
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 625
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 633
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 645
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 586..636
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 677..715
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 1083 AA; 123235 MW; 51485D8A61D905EA CRC64;
MTHRTPNFRR FHLFLPLFLK GMIFLLLHFK FLVIFALELP IISLRPKSDC FLFWKCTTDY
RIQKNQKIGK FVELTEGQTL SLQCAYRRGT PKFTYPNFLA ERVEQEFSEP LNTDYVRIED
IRESDTGSFS CNSTENPAQS DSIHVFVHKS KIFLPSKSVF SKKDLWNELT VPCKTTKLTE
SKEIELYADG KLVASQDFDP RHGFRITRKG YAAQPSFFEC KFNKKNKTQS VDFIISKNEP
IDNEYILFWE DSFPFPHVGY NFSLTCHLVY IEPNGNAPKL GELAFECPQC QSRLDNHLVI
EKHHNVGRKR LSSAIHIKNL QLRDAGKYRC IWKKTGKARQ EIEHSLHVSP TIAQVRILEQ
SPSFLKAKAG SGSVKLYAKF AVYPAGNYTV TWRRTYNSIE GPRDEIVEKG LSATFLENSE
SMEVLDITDL SCNKSGKYLL SINYQDTSET IFWEVAVESD YPDVQLIIRE PASFKVFGHQ
FYLLGTHLNI DCVSTSIPLV DALLEYRKEN FKIFTKVSRS FVADGTFERK ISYQVVLTEN
MMLKCRVGNR VALETVHVAD EIPNIKFKLA SNKSAIYEGD TVKLTCVVPK LAGRCSITWV
HRNLSILHST EVTEHSQLSF LYIRNATTSA SGNYTCVLEN QASENFSLST ILKVEPIIAP
YIVKTGFSAP TGSKLDCNID GRPPPEYQWF KDGTPYGTGR RLKFFEEDNS GIYQCLATNR
AGSATNSFEL KTAGRSYGIF VLLAILALGI LVILGWKIST KLGWKKNRDL KLLYKSLIGS
ENFLPNGKNQ FSNFNFEFHK DSLEILEPIG SGHFGVVRRG ILKGTKTVVA VKSSSYRSSI
GFQKVIVEEL KLMSAIPKHP NVLALVGAIT KNLRHGELYI LMEYIDGGNL RDFLQQRRNV
FIDELHDNFD ENIPLIRPDF NSLSTTDLVG IAHQIANGME WLGNVPCVHG NLCCRKVLIS
KTKTIRITDY GVGDRQRKSS SMRWMAPEAI EHQMFSSKSD VWSFGICLYE IFTLGGTPYP
TCVTENILKH IKNGSRNLQP EYCPSALYDL MQLCWRAPPQ DRPKFSLCSE LIEKQLKDLT
ISF
