ID A0A0D9RZG6_CHLSB Unreviewed; 502 AA.
AC A0A0D9RZG6;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=Wiskott-Aldrich syndrome protein family member {ECO:0000256|RuleBase:RU367034};
DE Short=WASP family protein member {ECO:0000256|RuleBase:RU367034};
GN Name=WASF3 {ECO:0000313|Ensembl:ENSCSAP00000014005.1};
OS Chlorocebus sabaeus (Green monkey) (Cercopithecus sabaeus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Chlorocebus.
OX NCBI_TaxID=60711 {ECO:0000313|Ensembl:ENSCSAP00000014005.1, ECO:0000313|Proteomes:UP000029965};
RN [1] {ECO:0000313|Ensembl:ENSCSAP00000014005.1, ECO:0000313|Proteomes:UP000029965}
RP NUCLEOTIDE SEQUENCE.
RA Warren W., Wilson R.K.;
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCSAP00000014005.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Downstream effector molecule involved in the transmission of
CC signals from tyrosine kinase receptors and small GTPases to the actin
CC cytoskeleton. Promotes formation of actin filaments. Part of the WAVE
CC complex that regulates lamellipodia formation. The WAVE complex
CC regulates actin filament reorganization via its interaction with the
CC Arp2/3 complex. {ECO:0000256|RuleBase:RU367034}.
CC -!- SUBUNIT: Binds actin and the Arp2/3 complex.
CC {ECO:0000256|RuleBase:RU367034}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000256|ARBA:ARBA00004245, ECO:0000256|RuleBase:RU367034}.
CC -!- SIMILARITY: Belongs to the SCAR/WAVE family.
CC {ECO:0000256|ARBA:ARBA00006993, ECO:0000256|RuleBase:RU367034}.
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DR EMBL; AQIB01113839; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_008019972.1; XM_008021781.1.
DR RefSeq; XP_008019973.1; XM_008021782.1.
DR RefSeq; XP_008019974.1; XM_008021783.1.
DR RefSeq; XP_008019975.1; XM_008021784.1.
DR AlphaFoldDB; A0A0D9RZG6; -.
DR STRING; 60711.ENSCSAP00000014005; -.
DR Ensembl; ENSCSAT00000016083.1; ENSCSAP00000014005.1; ENSCSAG00000017987.1.
DR GeneID; 103249043; -.
DR KEGG; csab:103249043; -.
DR CTD; 10810; -.
DR eggNOG; KOG1830; Eukaryota.
DR GeneTree; ENSGT00950000182962; -.
DR OMA; QSVHHGA; -.
DR OrthoDB; 616448at2759; -.
DR BioGRID-ORCS; 103249043; 0 hits in 16 CRISPR screens.
DR Proteomes; UP000029965; Chromosome 3.
DR Bgee; ENSCSAG00000017987; Expressed in prefrontal cortex and 7 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0097386; C:glial cell projection; IEA:Ensembl.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR GO; GO:0030027; C:lamellipodium; IEA:Ensembl.
DR GO; GO:0098794; C:postsynapse; IEA:Ensembl.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-UniRule.
DR GO; GO:0030036; P:actin cytoskeleton organization; IEA:UniProtKB-UniRule.
DR GO; GO:0030032; P:lamellipodium assembly; IEA:Ensembl.
DR GO; GO:0098885; P:modification of postsynaptic actin cytoskeleton; IEA:Ensembl.
DR GO; GO:0014003; P:oligodendrocyte development; IEA:Ensembl.
DR GO; GO:0031643; P:positive regulation of myelination; IEA:Ensembl.
DR GO; GO:0008360; P:regulation of cell shape; IEA:Ensembl.
DR CDD; cd22073; WH2_WAVE-3; 1.
DR Gene3D; 1.20.5.340; -; 1.
DR Gene3D; 6.10.280.150; -; 2.
DR InterPro; IPR028288; SCAR/WAVE_fam.
DR InterPro; IPR003124; WH2_dom.
DR PANTHER; PTHR12902; WASP-1; 1.
DR PANTHER; PTHR12902:SF7; WISKOTT-ALDRICH SYNDROME PROTEIN FAMILY MEMBER 3; 1.
DR Pfam; PF02205; WH2; 1.
DR SMART; SM00246; WH2; 1.
DR PROSITE; PS51082; WH2; 1.
PE 3: Inferred from homology;
KW Actin-binding {ECO:0000256|RuleBase:RU367034};
KW Cytoplasm {ECO:0000256|RuleBase:RU367034};
KW Cytoskeleton {ECO:0000256|RuleBase:RU367034};
KW Reference proteome {ECO:0000313|Proteomes:UP000029965}.
FT DOMAIN 440..457
FT /note="WH2"
FT /evidence="ECO:0000259|PROSITE:PS51082"
FT REGION 169..210
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 223..444
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 169..193
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 223..262
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 300..315
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 338..355
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 388..412
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 502 AA; 55279 MW; 0D07CE75214C7B95 CRC64;
MPLVKRNIEP RHLCRGALPE GITSELECVT NSTLAAVIRQ LSSLSKHAED IFGELFNEAN
NFYIRANSLQ DRIDRLAVKV TQLDSTVEEV SLQDINMKKA FKSSTVQDQQ VVSKNSIPNP
VADIYNQSDK PPPLNILTPY RDDKKDGLKF YTDPSYFFDL WKEKMLQDTE DKRKEKRRQK
EQKRIDGTTR EVKKVRKARN RRQEWNMMAY DKELRPDNRL SQSVYHGASS EGSLSPDTRS
HASDVTDYSY PATPNHSLHP QPVTPSYAAG DVPPHGPASQ AAEHEYRPPS ASARHMALNR
PQQPPPPPPP QAPEGSQASA PMAPADYGML PAQIIEYYNP SGPPPPPPPP VIPSAQTAFV
SPLQMPMQPP FPASAGSTHT APPHPPSTGL LVTAPPPPGP PPPPPGPPGP GSSLSSSPMH
GPPVAEAKRQ EPAQPPISDA RSDLLAAIRM GIQLKKVQEQ REQEAKREPV GNDVATILSR
RIAVEYSDSD DDSEFDENDW SD
//
