WASH1_DICDI
ID WASH1_DICDI Reviewed; 472 AA.
AC Q54CK9;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 25-MAY-2022, entry version 69.
DE RecName: Full=WAS protein family homolog DDB_G0292878;
GN ORFNames=DDB_G0292878;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
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 [2]
RP PROTEIN SEQUENCE OF 1-45; 51-208 AND 210-231, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=AX2;
RA Bienvenut W.V., Sumpton D., Ura S., Insall R.H.;
RL Submitted (OCT-2008) to UniProtKB.
CC -!- FUNCTION: Acts as a nucleation-promoting factor by activating the
CC Arp2/3 complex to induce actin polymerization. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the WASH1 family. {ECO:0000305}.
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DR EMBL; AAFI02000197; EAL60988.1; -; Genomic_DNA.
DR RefSeq; XP_629407.1; XM_629405.1.
DR AlphaFoldDB; Q54CK9; -.
DR SMR; Q54CK9; -.
DR STRING; 44689.DDB0191666; -.
DR PaxDb; Q54CK9; -.
DR EnsemblProtists; EAL60988; EAL60988; DDB_G0292878.
DR GeneID; 8628926; -.
DR KEGG; ddi:DDB_G0292878; -.
DR dictyBase; DDB_G0292878; wshA.
DR eggNOG; ENOG502QSX3; Eukaryota.
DR HOGENOM; CLU_029156_1_0_1; -.
DR InParanoid; Q54CK9; -.
DR OMA; MYSAAKY; -.
DR PhylomeDB; Q54CK9; -.
DR PRO; PR:Q54CK9; -.
DR Proteomes; UP000002195; Chromosome 6.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0005769; C:early endosome; IBA:GO_Central.
DR GO; GO:0032009; C:early phagosome; IDA:dictyBase.
DR GO; GO:0140220; C:pathogen-containing vacuole; IDA:dictyBase.
DR GO; GO:0032010; C:phagolysosome; IDA:dictyBase.
DR GO; GO:0055037; C:recycling endosome; IBA:GO_Central.
DR GO; GO:0071203; C:WASH complex; IDA:dictyBase.
DR GO; GO:0003779; F:actin binding; IC:dictyBase.
DR GO; GO:0043014; F:alpha-tubulin binding; IBA:GO_Central.
DR GO; GO:0043015; F:gamma-tubulin binding; IBA:GO_Central.
DR GO; GO:0030041; P:actin filament polymerization; IMP:dictyBase.
DR GO; GO:0045010; P:actin nucleation; IMP:dictyBase.
DR GO; GO:0034314; P:Arp2/3 complex-mediated actin nucleation; IBA:GO_Central.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; IMP:dictyBase.
DR GO; GO:0032456; P:endocytic recycling; IMP:dictyBase.
DR GO; GO:0006887; P:exocytosis; IMP:dictyBase.
DR GO; GO:0007041; P:lysosomal transport; IMP:dictyBase.
DR GO; GO:0044655; P:phagosome reneutralization; IMP:dictyBase.
DR GO; GO:2001137; P:positive regulation of endocytic recycling; IMP:dictyBase.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; IBA:GO_Central.
DR GO; GO:0033299; P:secretion of lysosomal enzymes; IMP:dictyBase.
DR InterPro; IPR028290; WASH1.
DR InterPro; IPR021854; WASH1_WAHD.
DR InterPro; IPR003124; WH2_dom.
DR PANTHER; PTHR23331; PTHR23331; 1.
DR Pfam; PF11945; WASH_WAHD; 1.
DR PROSITE; PS51082; WH2; 1.
PE 1: Evidence at protein level;
KW Actin-binding; Direct protein sequencing; Reference proteome.
FT CHAIN 1..472
FT /note="WAS protein family homolog DDB_G0292878"
FT /id="PRO_0000388366"
FT DOMAIN 382..401
FT /note="WH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00406"
FT REGION 279..472
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 279..320
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 321..358
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 388..409
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 472 AA; 50922 MW; 46336D02070F89B8 CRC64;
MTTQIYQVPV VSNGLRETES ILQIVDSLEK LEKVFNDMYS TISARVSHEK SRIDNVANRL
NNAQHKVNQI VGSKQAITVF SSAKYPADKK WGDYVPIYSG KHKLPFKPSH YHGLNSEDSP
IKKRPEDSYL DVNDLVFIEK SIDTTSKEVE VKEGLGRIPA QIPSVSNLLL FNTQENPYKK
YSNTLDNLSG GDGGEDDYTI FGDQLSKKKR LGDAPVTVKD GDSRIDAENV KIGYEPGTFE
IPVYNFPSIL PLPNVAENIT WAAESQSIAP SQKATLNLLP TYDNSNSGSA PVNQSSGGDN
NVNNNNNNNN SNNSTGIMQP PQPTNAPPPP PPPPQSANAP PPPPPPPVSA PPPFNPPSVN
SNNDDDDDDD DDNGGGGGPG GAIGDLLADI RRGHKNRLKK ADVGGDNGDG EDNKPPPVSD
GGGGLMGDLF KKLALRRQSI ATTKSTKKQS KSKKEDTDDQ DGESDTDSSE WE
