VAV_CAEEL
ID VAV_CAEEL Reviewed; 1007 AA.
AC Q45FX5; Q18479;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Protein vav-1;
GN Name=vav-1 {ECO:0000312|WormBase:C35B8.2a};
GN ORFNames=C35B8.2 {ECO:0000312|WormBase:C35B8.2a};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION, TISSUE SPECIFICITY, AND
RP MUTAGENESIS OF TYR-183; TYR-200 AND TYR-217.
RX PubMed=16213217; DOI=10.1016/j.cell.2005.08.001;
RA Norman K.R., Fazzio R.T., Mellem J.E., Espelt M.V., Strange K.,
RA Beckerle M.C., Maricq A.V.;
RT "The Rho/Rac family guanine nucleotide exchange factor VAV-1 regulates
RT rhythmic behaviors in Caenorhabditis elegans.";
RL Cell 123:119-132(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
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]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=21408209; DOI=10.1371/journal.pgen.1002010;
RA Nelson M.D., Zhou E., Kiontke K., Fradin H., Maldonado G., Martin D.,
RA Shah K., Fitch D.H.;
RT "A bow-tie genetic architecture for morphogenesis suggested by a genome-
RT wide RNAi screen in Caenorhabditis elegans.";
RL PLoS Genet. 7:E1002010-E1002010(2011).
CC -!- FUNCTION: Acts as guanine nucleotide exchange factor (GEF) for Rho
CC GTPase. Has a critical roles in the generation of rhythmic behaviors:
CC feeding, defecation and ovulation by dynamically regulating the
CC concentration of intracellular calcium. Plays a role in male tail tip
CC morphogenesis (PubMed:21408209). {ECO:0000269|PubMed:16213217,
CC ECO:0000269|PubMed:21408209}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a {ECO:0000312|WormBase:C35B8.2a};
CC IsoId=Q45FX5-1; Sequence=Displayed;
CC Name=b {ECO:0000312|WormBase:C35B8.2b};
CC IsoId=Q45FX5-2; Sequence=VSP_018992;
CC -!- TISSUE SPECIFICITY: Strong expression in the pharynx, proximal gonad,
CC spermatheca, intestine and rectal epithelia.
CC {ECO:0000269|PubMed:16213217}.
CC -!- DOMAIN: An acidic domain (AC) contains three highly conserved tyrosines
CC that are involved in the autoinhibition of GEF activity. {ECO:0000250}.
CC -!- PTM: GEF activity is regulated by phosphorylation on tyrosine residues.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown results in male tail tip
CC defects. {ECO:0000269|PubMed:21408209}.
CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=Nematode tempo - Issue 71 of
CC June 2006;
CC URL="https://web.expasy.org/spotlight/back_issues/071";
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DR EMBL; DQ136172; AAZ66767.1; -; mRNA.
DR EMBL; BX284606; CCD66769.1; -; Genomic_DNA.
DR EMBL; BX284606; CCD66770.1; -; Genomic_DNA.
DR PIR; T15778; T15778.
DR RefSeq; NP_001041222.1; NM_001047757.2. [Q45FX5-2]
DR RefSeq; NP_001041223.1; NM_001047758.1.
DR AlphaFoldDB; Q45FX5; -.
DR SMR; Q45FX5; -.
DR BioGRID; 46070; 34.
DR DIP; DIP-25959N; -.
DR IntAct; Q45FX5; 27.
DR STRING; 6239.C35B8.2b; -.
DR iPTMnet; Q45FX5; -.
DR EPD; Q45FX5; -.
DR PaxDb; Q45FX5; -.
DR PeptideAtlas; Q45FX5; -.
DR PRIDE; Q45FX5; -.
DR EnsemblMetazoa; C35B8.2a.1; C35B8.2a.1; WBGene00006887. [Q45FX5-2]
DR EnsemblMetazoa; C35B8.2b.1; C35B8.2b.1; WBGene00006887. [Q45FX5-1]
DR GeneID; 181153; -.
DR UCSC; C35B8.2a.1; c. elegans. [Q45FX5-1]
DR CTD; 181153; -.
DR WormBase; C35B8.2a; CE38040; WBGene00006887; vav-1. [Q45FX5-2]
DR WormBase; C35B8.2b; CE39333; WBGene00006887; vav-1. [Q45FX5-1]
DR eggNOG; KOG2996; Eukaryota.
DR GeneTree; ENSGT00940000168738; -.
DR HOGENOM; CLU_013787_0_0_1; -.
DR InParanoid; Q45FX5; -.
DR OMA; NEDPVGE; -.
DR OrthoDB; 710582at2759; -.
DR PhylomeDB; Q45FX5; -.
DR Reactome; R-CEL-114604; GPVI-mediated activation cascade.
DR Reactome; R-CEL-1257604; PIP3 activates AKT signaling.
DR Reactome; R-CEL-1433557; Signaling by SCF-KIT.
DR Reactome; R-CEL-193648; NRAGE signals death through JNK.
DR Reactome; R-CEL-3928665; EPH-ephrin mediated repulsion of cells.
DR Reactome; R-CEL-416482; G alpha (12/13) signalling events.
DR Reactome; R-CEL-4420097; VEGFA-VEGFR2 Pathway.
DR Reactome; R-CEL-445144; Signal transduction by L1.
DR Reactome; R-CEL-5218920; VEGFR2 mediated vascular permeability.
DR Reactome; R-CEL-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
DR Reactome; R-CEL-8980692; RHOA GTPase cycle.
DR Reactome; R-CEL-9013026; RHOB GTPase cycle.
DR Reactome; R-CEL-9013106; RHOC GTPase cycle.
DR Reactome; R-CEL-9013148; CDC42 GTPase cycle.
DR Reactome; R-CEL-9013149; RAC1 GTPase cycle.
DR Reactome; R-CEL-912631; Regulation of signaling by CBL.
DR Reactome; R-CEL-9748787; Azathioprine ADME.
DR Reactome; R-CEL-983695; Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
DR SignaLink; Q45FX5; -.
DR PRO; PR:Q45FX5; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00006887; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR ExpressionAtlas; Q45FX5; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0045746; P:negative regulation of Notch signaling pathway; IGI:WormBase.
DR GO; GO:0040017; P:positive regulation of locomotion; IMP:UniProtKB.
DR GO; GO:0110039; P:positive regulation of nematode male tail tip morphogenesis; IMP:UniProtKB.
DR GO; GO:0043087; P:regulation of GTPase activity; IBA:GO_Central.
DR GO; GO:0040028; P:regulation of vulval development; IGI:WormBase.
DR CDD; cd00029; C1; 1.
DR CDD; cd00014; CH; 1.
DR CDD; cd01223; PH_Vav; 1.
DR CDD; cd00160; RhoGEF; 1.
DR CDD; cd09940; SH2_Vav_family; 1.
DR Gene3D; 1.10.418.10; -; 1.
DR Gene3D; 1.20.900.10; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR Gene3D; 3.30.505.10; -; 1.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR001715; CH-domain.
DR InterPro; IPR036872; CH_dom_sf.
DR InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR000219; DH-domain.
DR InterPro; IPR001331; GDS_CDC24_CS.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR037832; PH_Vav.
DR InterPro; IPR000980; SH2.
DR InterPro; IPR036860; SH2_dom_sf.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR035031; Vav_SH2_invertebrate.
DR Pfam; PF00130; C1_1; 1.
DR Pfam; PF00307; CH; 1.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF00621; RhoGEF; 1.
DR Pfam; PF00017; SH2; 1.
DR Pfam; PF07653; SH3_2; 1.
DR PRINTS; PR00401; SH2DOMAIN.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00109; C1; 1.
DR SMART; SM00033; CH; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00325; RhoGEF; 1.
DR SMART; SM00252; SH2; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF47576; SSF47576; 1.
DR SUPFAM; SSF48065; SSF48065; 1.
DR SUPFAM; SSF50044; SSF50044; 2.
DR SUPFAM; SSF55550; SSF55550; 1.
DR SUPFAM; SSF57889; SSF57889; 1.
DR PROSITE; PS50021; CH; 1.
DR PROSITE; PS00741; DH_1; 1.
DR PROSITE; PS50010; DH_2; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50001; SH2; 1.
DR PROSITE; PS50002; SH3; 2.
DR PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Guanine-nucleotide releasing factor; Metal-binding;
KW Phosphoprotein; Reference proteome; Repeat; SH2 domain; SH3 domain; Zinc;
KW Zinc-finger.
FT CHAIN 1..1007
FT /note="Protein vav-1"
FT /id="PRO_0000238786"
FT DOMAIN 37..151
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 240..437
FT /note="DH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00062"
FT DOMAIN 470..598
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 688..750
FT /note="SH3 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 831..925
FT /note="SH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT DOMAIN 926..991
FT /note="SH3 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT ZN_FING 610..664
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT REGION 151..239
FT /note="AC"
FT REGION 153..176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 778..817
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 159..173
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 183
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250"
FT MOD_RES 200
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250"
FT MOD_RES 217
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..32
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_018992"
FT MUTAGEN 183
FT /note="Y->F: Leads to a dominant hypercontracted and
FT uncoordinated phenotype; when associated with Y-200 and Y-
FT 217."
FT /evidence="ECO:0000269|PubMed:16213217"
FT MUTAGEN 200
FT /note="Y->F: Leads to a dominant hypercontracted and
FT uncoordinated phenotype; when associated with Y-183 and Y-
FT 217."
FT /evidence="ECO:0000269|PubMed:16213217"
FT MUTAGEN 217
FT /note="Y->F: Leads to a dominant hypercontracted and
FT uncoordinated phenotype. Leads to a dominant
FT hypercontracted and uncoordinated phenotype; when
FT associated with Y-183 and Y-200."
FT /evidence="ECO:0000269|PubMed:16213217"
SQ SEQUENCE 1007 AA; 113554 MW; 4B0E7A79C7BB2DFD CRC64;
MSRRSTTTST NFGLSWSLVD VISSSTAVFK VPMNGGCDLW IGCARWLRDM KVLTTDKNGT
MLEFASVLRD GILLCRLANT LVPNGIDQKK IMRTNQPSPF LCCNNINYFA MFCKTYFNLE
DADLFTAEDL YYMNGFQKVL KTLSFLSHTK ESLSRGVDPF PDTDNNQEGT SNGSEFEDDV
EIYQSLHDNI ENVDPNRTIY GPITSADPEE QQSEQLYDRI VTNRKPSMNE NDLQNTPTLK
RNRCIRELYD TEKNYVAQAL VTIIKTFYEP LKGIIPTSDY NIIFGNIEEI NVLHTALLAD
LEYPVKVALG LSDATPPRPI SLNECVPQTI GEVFIKYRDQ FLAYGKYCSN LPDSRKLSNE
LLKTNEFISR NINELTAQGN CKFGMNDLLC VPFQRLTKYP LLLKELQKKT DLASPDRKSL
EEAVEVMEDV CNYINEESRD TNAIKVIDEI EQSITDLSMP LNVKLHDYGR VNLDGEVKMA
ESTLTQAGKP KQRYIFLFDK VIVVCKAANK VMAAKTTGAS ARTNTFTYKN AYVMSELTID
KNASLDVKSG GTITRRTQYV IIMTRDRNEN NEITQLTFYF KNEATRNNWM TALLLSKSNV
SPTDYLRDTN HKVAFHSFRV DVKNPATCDV CDKLMKGLQY QGYKCESCNM SMHKECLGLK
KCEAVRKSTH ETRSSQSFNC NRPRFHIHEG DIVVANSNST PSDLSYLQFA KGDRIEVIKM
QGHNRFTGCL INNRNRTGLV HLDHVSQSRT TSMIGLSPID SPAGSIAPRV VRNESTVLPN
KLLSDGSSRS LSGPHGSRSS RNSSSSTING SMDSVPRQQD YVNTEISEFL WYMGEMERAK
AESTLKGTPN GTFLVRYSKN RKQTAISLSY KNDVKHMIIE QNSDGKVYLD EDYIFNSTVE
LVQYYRSNNL IEIFAALDTC LKNPYSQCKV FKAVHDYDAP SPNNEGKFLS FKTGDIVVLL
DTVGEDRGWW KGQVNNKSGF FPLSYVKPYD PATEGSSSPV TPTSSSS
