WASF3_MOUSE
ID WASF3_MOUSE Reviewed; 501 AA.
AC Q8VHI6;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Actin-binding protein WASF3 {ECO:0000305};
DE AltName: Full=Protein WAVE-3;
DE AltName: Full=Wiskott-Aldrich syndrome protein family member 3;
DE Short=WASP family protein member 3;
GN Name=Wasf3; Synonyms=Wave3;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=12856283; DOI=10.1007/s00335-002-2247-7;
RA Sossey-Alaoui K., Head K., Nowak N., Cowell J.K.;
RT "Genomic organization and expression profile of the human and mouse WAVE
RT gene family.";
RL Mamm. Genome 14:314-322(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Liver;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Downstream effector molecules involved in the transmission of
CC signals from tyrosine kinase receptors and small GTPases to the actin
CC cytoskeleton. Plays a role in the regulation of cell morphology and
CC cytoskeletal organization. Required in the control of cell shape (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Binds actin and the Arp2/3 complex. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}.
CC -!- DOMAIN: Binds the Arp2/3 complex through the C-terminal region and
CC actin through verprolin homology (VPH) domain.
CC -!- PTM: Phosphorylation by ABL1 promotes lamellipodia formation and cell
CC migration. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the SCAR/WAVE family. {ECO:0000305}.
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DR EMBL; AF454703; AAL51033.1; -; mRNA.
DR EMBL; BC027038; AAH27038.1; -; mRNA.
DR CCDS; CCDS19870.1; -.
DR RefSeq; NP_660137.1; NM_145155.3.
DR RefSeq; XP_006504896.1; XM_006504833.3.
DR AlphaFoldDB; Q8VHI6; -.
DR SMR; Q8VHI6; -.
DR BioGRID; 232846; 4.
DR STRING; 10090.ENSMUSP00000016143; -.
DR iPTMnet; Q8VHI6; -.
DR PhosphoSitePlus; Q8VHI6; -.
DR MaxQB; Q8VHI6; -.
DR PaxDb; Q8VHI6; -.
DR PRIDE; Q8VHI6; -.
DR ProteomicsDB; 297622; -.
DR Antibodypedia; 22618; 220 antibodies from 28 providers.
DR DNASU; 245880; -.
DR Ensembl; ENSMUST00000016143; ENSMUSP00000016143; ENSMUSG00000029636.
DR GeneID; 245880; -.
DR KEGG; mmu:245880; -.
DR UCSC; uc009anf.1; mouse.
DR CTD; 10810; -.
DR MGI; MGI:2658986; Wasf3.
DR VEuPathDB; HostDB:ENSMUSG00000029636; -.
DR eggNOG; KOG1830; Eukaryota.
DR GeneTree; ENSGT00950000182962; -.
DR HOGENOM; CLU_036022_2_0_1; -.
DR InParanoid; Q8VHI6; -.
DR OMA; QSVHHGA; -.
DR OrthoDB; 1183697at2759; -.
DR PhylomeDB; Q8VHI6; -.
DR TreeFam; TF315031; -.
DR Reactome; R-MMU-2029482; Regulation of actin dynamics for phagocytic cup formation.
DR Reactome; R-MMU-4420097; VEGFA-VEGFR2 Pathway.
DR Reactome; R-MMU-5663213; RHO GTPases Activate WASPs and WAVEs.
DR Reactome; R-MMU-9013149; RAC1 GTPase cycle.
DR BioGRID-ORCS; 245880; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Wasf3; mouse.
DR PRO; PR:Q8VHI6; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q8VHI6; protein.
DR Bgee; ENSMUSG00000029636; Expressed in ventral tegmental area and 206 other tissues.
DR ExpressionAtlas; Q8VHI6; baseline and differential.
DR Genevisible; Q8VHI6; MM.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0097386; C:glial cell projection; IDA:MGI.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0030027; C:lamellipodium; IDA:MGI.
DR GO; GO:0098794; C:postsynapse; IDA:SynGO.
DR GO; GO:0031209; C:SCAR complex; IBA:GO_Central.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0071933; F:Arp2/3 complex binding; IBA:GO_Central.
DR GO; GO:0034237; F:protein kinase A regulatory subunit binding; IBA:GO_Central.
DR GO; GO:0030036; P:actin cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0007010; P:cytoskeleton organization; ISS:UniProtKB.
DR GO; GO:0030032; P:lamellipodium assembly; IMP:MGI.
DR GO; GO:0098885; P:modification of postsynaptic actin cytoskeleton; IDA:SynGO.
DR GO; GO:0014003; P:oligodendrocyte development; IMP:MGI.
DR GO; GO:2000601; P:positive regulation of Arp2/3 complex-mediated actin nucleation; IBA:GO_Central.
DR GO; GO:0031643; P:positive regulation of myelination; IDA:MGI.
DR GO; GO:0008360; P:regulation of cell shape; ISS:UniProtKB.
DR InterPro; IPR028288; SCAR/WAVE_fam.
DR InterPro; IPR003124; WH2_dom.
DR PANTHER; PTHR12902; PTHR12902; 1.
DR Pfam; PF02205; WH2; 1.
DR SMART; SM00246; WH2; 1.
DR PROSITE; PS51082; WH2; 1.
PE 1: Evidence at protein level;
KW Actin-binding; Coiled coil; Cytoplasm; Cytoskeleton; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..501
FT /note="Actin-binding protein WASF3"
FT /id="PRO_0000188997"
FT DOMAIN 439..456
FT /note="WH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00406"
FT REGION 170..443
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 57..93
FT /evidence="ECO:0000255"
FT COILED 162..206
FT /evidence="ECO:0000255"
FT COMPBIAS 170..193
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 201..220
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 222..275
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 300..314
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 365..379
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 389..415
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 151
FT /note="Phosphotyrosine; by ABL1"
FT /evidence="ECO:0000250|UniProtKB:Q9UPY6"
FT MOD_RES 248
FT /note="Phosphotyrosine; by ABL1"
FT /evidence="ECO:0000250|UniProtKB:Q9UPY6"
FT MOD_RES 337
FT /note="Phosphotyrosine; by ABL1"
FT /evidence="ECO:0000250|UniProtKB:Q9UPY6"
FT MOD_RES 485
FT /note="Phosphotyrosine; by ABL1"
FT /evidence="ECO:0000250|UniProtKB:Q9UPY6"
SQ SEQUENCE 501 AA; 55204 MW; FD30EEC6867D4AF1 CRC64;
MPLVKRNIEP RHLCRGALPE GVTSELECVT NSTLAAIIRQ LSSLSKHAED IFGELFNEAN
NFYIRANSLQ DRIDRLAVKV TQLDSTVEEV SLQDINMKKA FKSSTIQDQQ VVSKNSIPNP
VADIYNQSDK PPPLSILTPY RDDKKDGLKF YTDPSYFFDL WKEKMLQDTE DKRKEKRRQK
EQKRVDGTTR EVKKVRKARN RRQEWNMMAY DKELRPDNRL SQSVHHGASS EGSLSPDTRS
HTSDVTDYSY PATPNHALQA QPATPSYTAG DAPLHGTTNQ GAEHEYRPSS ASARHMALNR
PQQPPPPPPP QAPEGSQAST SVAPADYGML PAQIIEYYSP SGPPPPPPPP MIPSAQTAFV
SPLQMPTQPP FPASAVSTYP TPPHQPSTGL LATAPPPPGP PPPPPGPPGP SSLSSSPMHG
PPVAEAKRPE PAQPPISDAR SDLLAAIRMG IQLKKVQEQR EQEAKREPVG NDVATILSRR
IAVEYSDSDD DSEFDENDWS D
