VASP_DICDI
ID VASP_DICDI Reviewed; 380 AA.
AC Q5TJ65; Q54HE2;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Protein VASP homolog;
DE AltName: Full=DdVASP;
GN Name=vasp; ORFNames=DDB_G0289541;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH FORH, SUBCELLULAR
RP LOCATION, AND MUTAGENESIS OF 264-GLY--GLU-285 AND 275-LYS--LYS-280.
RC STRAIN=AX2;
RX PubMed=16675552; DOI=10.1073/pnas.0511243103;
RA Schirenbeck A., Arasada R., Bretschneider T., Stradal T.E.B.,
RA Schleicher M., Faix J.;
RT "The bundling activity of vasodilator-stimulated phosphoprotein is required
RT for filopodium formation.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:7694-7699(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=12388544; DOI=10.1074/jbc.m209107200;
RA Han Y.-H., Chung C.Y., Wessels D., Stephens S., Titus M.A., Soll D.R.,
RA Firtel R.A.;
RT "Requirement of a vasodilator-stimulated phosphoprotein family member for
RT cell adhesion, the formation of filopodia, and chemotaxis in
RT dictyostelium.";
RL J. Biol. Chem. 277:49877-49887(2002).
CC -!- FUNCTION: Ena/VASP proteins are actin-associated proteins involved in a
CC range of processes dependent on cytoskeleton remodeling and cell
CC polarity such as lamellipodial and filopodial dynamics in migrating
CC cells. Plays a crucial role in filopodia formation, cell-substratum
CC adhesion, and proper chemotaxis. Nucleates and bundles actin filaments.
CC When complexed with fotH in filopodial tips, may support formin-
CC mediated filament elongation by bundling nascent actin filaments.
CC {ECO:0000269|PubMed:12388544, ECO:0000269|PubMed:16675552}.
CC -!- SUBUNIT: May self-associate (By similarity). Binds F-actin and G-actin
CC (By similarity). Binds to the FH2 domain of forH. {ECO:0000250}.
CC -!- INTERACTION:
CC Q5TJ65; Q54N00: forH; NbExp=2; IntAct=EBI-1808546, EBI-1808560;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cell cortex. Cell projection,
CC filopodium. Cytoplasm, cytoskeleton. Note=Localizes to the leading edge
CC of migrating cells and to the tips of filipodia. Translocates to the
CC cell cortex in response to cAMP chemoattractant stimulation.
CC -!- DEVELOPMENTAL STAGE: Expressed in vegatatively growing cells.
CC Expression increases upon starvation from and remains high until
CC fruiting body formation. {ECO:0000269|PubMed:12388544}.
CC -!- DOMAIN: The EVH2 domain is comprised of 3 regions. Block A is a
CC thymosin-like domain required for G-actin binding and actin
CC polymerization. Block B is required for F-actin binding and subcellular
CC location, and Block C for self-association (By similarity).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the Ena/VASP family. {ECO:0000305}.
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DR EMBL; AJ786025; CAH05068.1; -; mRNA.
DR EMBL; AAFI02000141; EAL62702.1; -; Genomic_DNA.
DR RefSeq; XP_636196.1; XM_631104.1.
DR AlphaFoldDB; Q5TJ65; -.
DR SMR; Q5TJ65; -.
DR DIP; DIP-46562N; -.
DR IntAct; Q5TJ65; 1.
DR STRING; 44689.DDB0229340; -.
DR PaxDb; Q5TJ65; -.
DR EnsemblProtists; EAL62702; EAL62702; DDB_G0289541.
DR GeneID; 8627183; -.
DR KEGG; ddi:DDB_G0289541; -.
DR dictyBase; DDB_G0289541; vasP.
DR eggNOG; KOG4590; Eukaryota.
DR HOGENOM; CLU_728481_0_0_1; -.
DR InParanoid; Q5TJ65; -.
DR OMA; RTHYGIN; -.
DR Reactome; R-DDI-5658442; Regulation of RAS by GAPs.
DR PRO; PR:Q5TJ65; -.
DR Proteomes; UP000002195; Chromosome 5.
DR GO; GO:0005938; C:cell cortex; IDA:dictyBase.
DR GO; GO:0031252; C:cell leading edge; IDA:dictyBase.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IDA:dictyBase.
DR GO; GO:0030175; C:filopodium; IDA:dictyBase.
DR GO; GO:0032433; C:filopodium tip; IDA:dictyBase.
DR GO; GO:0044354; C:macropinosome; IDA:dictyBase.
DR GO; GO:0097203; C:phagocytic cup lip; IDA:dictyBase.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0017124; F:SH3 domain binding; IEA:InterPro.
DR GO; GO:0051017; P:actin filament bundle assembly; IDA:dictyBase.
DR GO; GO:0007015; P:actin filament organization; IMP:dictyBase.
DR GO; GO:0030041; P:actin filament polymerization; IDA:dictyBase.
DR GO; GO:0045010; P:actin nucleation; IDA:dictyBase.
DR GO; GO:0031589; P:cell-substrate adhesion; IMP:dictyBase.
DR GO; GO:0043327; P:chemotaxis to cAMP; IDA:dictyBase.
DR GO; GO:0046847; P:filopodium assembly; IMP:dictyBase.
DR GO; GO:0006972; P:hyperosmotic response; IDA:dictyBase.
DR GO; GO:0044351; P:macropinocytosis; IMP:dictyBase.
DR GO; GO:0050922; P:negative regulation of chemotaxis; IMP:dictyBase.
DR GO; GO:0006911; P:phagocytosis, engulfment; IMP:dictyBase.
DR GO; GO:0051289; P:protein homotetramerization; IEA:InterPro.
DR GO; GO:0072697; P:protein localization to cell cortex; IMP:dictyBase.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR017354; VASP/EVL.
DR InterPro; IPR038023; VASP_sf.
DR InterPro; IPR014885; VASP_tetra.
DR InterPro; IPR000697; WH1/EVH1_dom.
DR InterPro; IPR003124; WH2_dom.
DR Pfam; PF08776; VASP_tetra; 1.
DR Pfam; PF00568; WH1; 1.
DR Pfam; PF02205; WH2; 1.
DR PIRSF; PIRSF038010; Vasodilator_Phospo; 1.
DR SMART; SM00461; WH1; 1.
DR SUPFAM; SSF118370; SSF118370; 1.
DR PROSITE; PS50229; WH1; 1.
DR PROSITE; PS51082; WH2; 1.
PE 1: Evidence at protein level;
KW Actin-binding; Cell adhesion; Cell projection; Chemotaxis; Coiled coil;
KW Cytoplasm; Cytoskeleton; Reference proteome; Repeat.
FT CHAIN 1..380
FT /note="Protein VASP homolog"
FT /id="PRO_0000327694"
FT DOMAIN 1..110
FT /note="WH1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00410"
FT DOMAIN 199..218
FT /note="WH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00406"
FT REPEAT 349..363
FT /note="1"
FT REPEAT 364..378
FT /note="2"
FT REGION 94..346
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 229..380
FT /note="EVH2"
FT REGION 229..249
FT /note="EVH2 block A"
FT REGION 263..280
FT /note="EVH2 block B"
FT REGION 348..380
FT /note="EVH2 block C"
FT REGION 349..378
FT /note="2 X 15 AA tandem repeats of [LI]-Q-[SK]-[AL]-K-[DE]-
FT E-I-L-[ET]-[AE]-[IV]-[KR]-[ES]"
FT COILED 350..380
FT /evidence="ECO:0000255"
FT COMPBIAS 115..143
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 150..193
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 224..255
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 292..310
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 311..332
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 264..285
FT /note="Missing: Impairs actin bundling and filopodia
FT formation without affecting actin nucleation."
FT /evidence="ECO:0000269|PubMed:16675552"
FT MUTAGEN 275..280
FT /note="KRAKMK->AAAAMA: Impairs actin bundling and filopodia
FT formation without affecting actin nucleation."
FT /evidence="ECO:0000269|PubMed:16675552"
SQ SEQUENCE 380 AA; 39107 MW; 31983D07B4DFEA9D CRC64;
MSETAIFNAT GQVFTYSPQT RNWVPSSNVP ATLQMYFNSG ANTYRVIGRA GDDPNNFLIN
FAVKSEVVYS RASEIFHQFT DQRTHFGINF TSKQDADTFG GGFENVLRSL KGGPQQPPPQ
VPKPQPQQPP QPQQPPQRPP STVIAKPVAP QAPVAPPQAP AAAPQAPAPP AAPPAPPKPP
GPPPPPPAPK PPAAGGGTGR NALLGSIENF SKGGLKKTVT VDKSAGVPTK TTPSANSAAS
NAGSEPSSGG STPAPAPKSS GGGGGGDLMA EVMAKRAKMK AAASQPKEES SAPTPAPTPA
PTPAPTPSST SFKPPQSFSK PATKTAAANK PPSPSLSAPL PSTVANEDLQ SLKEEILTEV
RKEIQKAKDE ILEAIRASQH
