WASF1_MOUSE
ID WASF1_MOUSE Reviewed; 559 AA.
AC Q8R5H6; Q91W51; Q9ERQ9;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 2.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Actin-binding protein WASF1 {ECO:0000305};
DE AltName: Full=Protein WAVE-1;
DE AltName: Full=Wiskott-Aldrich syndrome protein family member 1;
DE Short=WASP family protein member 1;
GN Name=Wasf1; Synonyms=Wave1;
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=10970852; DOI=10.1093/emboj/19.17.4589;
RA Westphal R.S., Soderling S.H., Alto N.M., Langeberg L.K., Scott J.D.;
RT "Scar/WAVE-1, a Wiskott-Aldrich syndrome protein, assembles an actin-
RT associated multi-kinase scaffold.";
RL EMBO J. 19:4589-4600(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=129/Sv;
RX PubMed=12062808; DOI=10.1016/s0378-1119(02)00560-7;
RA Benachenhou N., Massy I., Vacher J.;
RT "Characterization and expression analyses of the mouse Wiskott-Aldrich
RT syndrome protein (WASP) family member Wave1/Scar.";
RL Gene 290:131-140(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Kidney, and Limb;
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 [4]
RP PROTEIN SEQUENCE OF 499-507, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
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).
RN [6]
RP INTERACTION WITH SHANK3, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=24153177; DOI=10.1038/nature12630;
RA Han K., Holder J.L. Jr., Schaaf C.P., Lu H., Chen H., Kang H., Tang J.,
RA Wu Z., Hao S., Cheung S.W., Yu P., Sun H., Breman A.M., Patel A., Lu H.C.,
RA Zoghbi H.Y.;
RT "SHANK3 overexpression causes manic-like behaviour with unique
RT pharmacogenetic properties.";
RL Nature 503:72-77(2013).
RN [7]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-341, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [8]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=27605705; DOI=10.1091/mbc.e16-05-0326;
RA Xu C., Fu X., Zhu S., Liu J.J.;
RT "Retrolinkin recruits the WAVE1 protein complex to facilitate BDNF-induced
RT TrkB endocytosis and dendrite outgrowth.";
RL Mol. Biol. Cell 27:3342-3356(2016).
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 (By similarity). As component of the WAVE1 complex,
CC required for BDNF-NTRK2 endocytic trafficking and signaling from early
CC endosomes (PubMed:27605705). Also involved in the regulation of
CC mitochondrial dynamics (By similarity). {ECO:0000250|UniProtKB:Q92558,
CC ECO:0000269|PubMed:27605705}.
CC -!- SUBUNIT: Component of the WAVE1 complex composed of ABI2, CYFIP1 or
CC CYFIP2, BRK1, NCKAP1 and WASF1/WAVE1. Within the complex, a heterodimer
CC containing NCKAP1 and CYFIP1 interacts with a heterotrimer formed by
CC WAVE1, ABI2 and BRK1. CYFIP2 binds to activated RAC1 which causes the
CC complex to dissociate, releasing activated WASF1. The complex can also
CC be activated by NCK1. Binds actin and the Arp2/3 complex. Interacts
CC with BAIAP2. Interacts with SHANK3; the interaction mediates the
CC association of SHANK3 with the WAVE1 complex. Interacts with ABI1 (via
CC N-terminus). Interacts with SORBS2; this interaction greatly enhances
CC phosphorylation by ABL1 and dephosphorylation by PTPN12 and might
CC mediate partial to focal adhesion sites (By similarity).
CC {ECO:0000250|UniProtKB:Q92558, ECO:0000269|PubMed:24153177}.
CC -!- INTERACTION:
CC Q8R5H6; Q80TE2: Pcdh10; NbExp=3; IntAct=EBI-774719, EBI-6661550;
CC Q8R5H6; P26450: Pik3r1; NbExp=2; IntAct=EBI-774719, EBI-641764;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:Q92558}. Synapse {ECO:0000269|PubMed:24153177}.
CC Cell junction, focal adhesion {ECO:0000250|UniProtKB:Q92558}. Note=Dot-
CC like pattern in the cytoplasm. Concentrated in Rac-regulated membrane-
CC ruffling areas. Partial translocation to focal adhesion sites might be
CC mediated by interaction with SORBS2. In neurons, colocalizes with
CC activated NTRK2 after BDNF addition in endocytic sites through the
CC association with TMEM108 (PubMed:27605705).
CC {ECO:0000250|UniProtKB:Q92558, ECO:0000269|PubMed:27605705}.
CC -!- TISSUE SPECIFICITY: Highly expressed in brain.
CC {ECO:0000269|PubMed:12062808, ECO:0000269|PubMed:24153177}.
CC -!- DOMAIN: Binds the Arp2/3 complex through the C-terminal region and
CC actin through verprolin homology (VPH) domain.
CC {ECO:0000250|UniProtKB:Q92558}.
CC -!- SIMILARITY: Belongs to the SCAR/WAVE family. {ECO:0000305}.
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DR EMBL; AF290877; AAG02214.1; -; mRNA.
DR EMBL; AF467773; AAL75574.1; -; mRNA.
DR EMBL; BC016896; AAH16896.1; -; mRNA.
DR EMBL; BC053423; AAH53423.1; -; mRNA.
DR CCDS; CCDS23801.1; -.
DR RefSeq; NP_114083.1; NM_031877.3.
DR RefSeq; XP_006512995.1; XM_006512932.2.
DR AlphaFoldDB; Q8R5H6; -.
DR SMR; Q8R5H6; -.
DR BioGRID; 219971; 33.
DR CORUM; Q8R5H6; -.
DR ELM; Q8R5H6; -.
DR IntAct; Q8R5H6; 15.
DR MINT; Q8R5H6; -.
DR STRING; 10090.ENSMUSP00000019975; -.
DR iPTMnet; Q8R5H6; -.
DR PhosphoSitePlus; Q8R5H6; -.
DR SwissPalm; Q8R5H6; -.
DR MaxQB; Q8R5H6; -.
DR PaxDb; Q8R5H6; -.
DR PeptideAtlas; Q8R5H6; -.
DR PRIDE; Q8R5H6; -.
DR ProteomicsDB; 297621; -.
DR ABCD; Q8R5H6; 1 sequenced antibody.
DR Antibodypedia; 1180; 338 antibodies from 39 providers.
DR DNASU; 83767; -.
DR Ensembl; ENSMUST00000019975; ENSMUSP00000019975; ENSMUSG00000019831.
DR Ensembl; ENSMUST00000105509; ENSMUSP00000101148; ENSMUSG00000019831.
DR GeneID; 83767; -.
DR KEGG; mmu:83767; -.
DR UCSC; uc007exi.2; mouse.
DR CTD; 8936; -.
DR MGI; MGI:1890563; Wasf1.
DR VEuPathDB; HostDB:ENSMUSG00000019831; -.
DR eggNOG; KOG1830; Eukaryota.
DR GeneTree; ENSGT00950000182962; -.
DR HOGENOM; CLU_036022_2_0_1; -.
DR InParanoid; Q8R5H6; -.
DR OMA; DHIDGSY; -.
DR OrthoDB; 1183697at2759; -.
DR PhylomeDB; Q8R5H6; -.
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 Reactome; R-MMU-9013423; RAC3 GTPase cycle.
DR BioGRID-ORCS; 83767; 3 hits in 71 CRISPR screens.
DR ChiTaRS; Wasf1; mouse.
DR PRO; PR:Q8R5H6; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q8R5H6; protein.
DR Bgee; ENSMUSG00000019831; Expressed in piriform cortex and 229 other tissues.
DR Genevisible; Q8R5H6; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0032839; C:dendrite cytoplasm; IEA:GOC.
DR GO; GO:0005925; C:focal adhesion; IEA:UniProtKB-SubCell.
DR GO; GO:0030027; C:lamellipodium; IDA:MGI.
DR GO; GO:0005741; C:mitochondrial outer membrane; IDA:MGI.
DR GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR GO; GO:0098794; C:postsynapse; IDA:SynGO.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0031209; C:SCAR complex; ISO:MGI.
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:0051018; F:protein kinase A binding; ISO:MGI.
DR GO; GO:0034237; F:protein kinase A regulatory subunit binding; IBA:GO_Central.
DR GO; GO:0031267; F:small GTPase binding; ISO:MGI.
DR GO; GO:0030036; P:actin cytoskeleton organization; ISS:UniProtKB.
DR GO; GO:1990416; P:cellular response to brain-derived neurotrophic factor stimulus; IMP:UniProtKB.
DR GO; GO:0097484; P:dendrite extension; IMP:UniProtKB.
DR GO; GO:0098939; P:dendritic transport of mitochondrion; ISO:MGI.
DR GO; GO:0072673; P:lamellipodium morphogenesis; IMP:MGI.
DR GO; GO:0070584; P:mitochondrion morphogenesis; ISS:UniProtKB.
DR GO; GO:0098885; P:modification of postsynaptic actin cytoskeleton; IDA:SynGO.
DR GO; GO:0031175; P:neuron projection development; IMP:UniProtKB.
DR GO; GO:2000601; P:positive regulation of Arp2/3 complex-mediated actin nucleation; ISO:MGI.
DR GO; GO:0051388; P:positive regulation of neurotrophin TRK receptor signaling pathway; IMP:UniProtKB.
DR GO; GO:0016601; P:Rac protein signal transduction; ISO:MGI.
DR GO; GO:0006898; P:receptor-mediated endocytosis; IMP: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; Cell junction; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; Methylation; Phosphoprotein; Reference proteome;
KW Synapse.
FT CHAIN 1..559
FT /note="Actin-binding protein WASF1"
FT /id="PRO_0000188993"
FT DOMAIN 497..514
FT /note="WH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00406"
FT REGION 170..202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 273..400
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 412..491
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 318..334
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 346..399
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 418..440
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 456..481
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 341
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 341
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 489
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92558"
FT CONFLICT 2
FT /note="P -> L (in Ref. 2; AAL75574)"
FT /evidence="ECO:0000305"
FT CONFLICT 324
FT /note="P -> S (in Ref. 3; AAH16896)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 559 AA; 61509 MW; 8746910987D80D16 CRC64;
MPLVKRNIDP RHLCHTALPR GIKNELECVT NISLANIIRQ LSSLSKYAED IFGELFNEAH
SFSFRVNSLQ ERVDRLSVSV TQLDPKEEEL SLQDITMRKA FRSSTIQDQQ LFDRKTLPIP
LQETYDVCEQ PPPLNILTPY RDDGKEGLKF YTNPSYFFDL WKEKMLQDTE DKRKEKRKQK
QKNLDRPHEP EKVPRAPHDR RREWQKLAQG PELAEDDADL LHKHIEVANG PASHYETRPQ
TYVDHMDGSY SLSALPFSQM SELLTRAEER VLVRPHEPPP PPPMHGAGDA KPTPTCISSA
TGLIENRPQS PAAGRTPVFV SPTPPPPPPP LPSALSTSSL RASMTSTPPP PVPPPPPPPA
TALQAPAVPP PPAPLQIAPG VLHPAPPPIA PPLVQPSPPV ARAAPVCETV PVHPLPQGEV
QGLPPPPPPP PLPPPGIRPS SPVAVAALAH PPSGLHPAPS TAPGPHAPLM PPSPPSQVLP
ASEPKRHPST LPVISDARSV LLEAIRKGIQ LRKVEEQREQ EAKHERIEND VATILSRRIA
VEYSDSEDDS EFDEVDWLE
