ID   WASF1_HUMAN             Reviewed;         559 AA.
AC   Q92558; E1P5F2; Q5SZK7;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   27-MAR-2024, entry version 193.
DE   RecName: Full=Actin-binding protein WASF1 {ECO:0000305};
DE   AltName: Full=Protein WAVE-1;
DE   AltName: Full=Verprolin homology domain-containing protein 1;
DE   AltName: Full=Wiskott-Aldrich syndrome protein family member 1 {ECO:0000305};
DE            Short=WASP family protein member 1;
GN   Name=WASF1 {ECO:0000312|HGNC:HGNC:12732};
GN   Synonyms=KIAA0269, SCAR1, WAVE1;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=9732292; DOI=10.1083/jcb.142.5.1325;
RA   Bear J.E., Rawls J.F., Saxe C.L. III;
RT   "SCAR, a WASP-related protein, isolated as a suppressor of receptor defects
RT   in late Dictyostelium development.";
RL   J. Cell Biol. 142:1325-1335(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Bone marrow;
RX   PubMed=9039502; DOI=10.1093/dnares/3.5.321;
RA   Nagase T., Seki N., Ishikawa K., Ohira M., Kawarabayasi Y., Ohara O.,
RA   Tanaka A., Kotani H., Miyajima N., Nomura N.;
RT   "Prediction of the coding sequences of unidentified human genes. VI. The
RT   coding sequences of 80 new genes (KIAA0201-KIAA0280) deduced by analysis of
RT   cDNA clones from cell line KG-1 and brain.";
RL   DNA Res. 3:321-329(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=14574404; DOI=10.1038/nature02055;
RA   Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA   Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA   Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA   Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA   Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA   Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA   Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA   Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA   Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA   Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA   French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA   Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA   Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA   Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA   Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA   Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA   Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA   Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA   Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA   Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA   Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA   Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA   Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA   Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA   Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA   Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA   West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA   Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA   Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA   Rogers J., Beck S.;
RT   "The DNA sequence and analysis of human chromosome 6.";
RL   Nature 425:805-811(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
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   [6]
RP   CHARACTERIZATION, FUNCTION, SUBCELLULAR LOCATION, AND DOMAIN.
RX   PubMed=9889097; DOI=10.1016/s0960-9822(98)00015-3;
RA   Machesky L.M., Insall R.H.;
RT   "Scar1 and the related Wiskott-Aldrich syndrome protein, WASP, regulate the
RT   actin cytoskeleton through the Arp2/3 complex.";
RL   Curr. Biol. 8:1347-1356(1998).
RN   [7]
RP   INTERACTION WITH BAIAP2.
RX   PubMed=11130076; DOI=10.1038/35047107;
RA   Miki H., Yamaguchi H., Suetsugu S., Takenawa T.;
RT   "IRSp53 is an essential intermediate between Rac and WAVE in the regulation
RT   of membrane ruffling.";
RL   Nature 408:732-735(2000).
RN   [8]
RP   INTERACTION WITH SORBS2, SUBCELLULAR LOCATION, AND PHOSPHORYLATION.
RX   PubMed=18559503; DOI=10.1158/0008-5472.can-08-0958;
RA   Taieb D., Roignot J., Andre F., Garcia S., Masson B., Pierres A.,
RA   Iovanna J.L., Soubeyran P.;
RT   "ArgBP2-dependent signaling regulates pancreatic cell migration, adhesion,
RT   and tumorigenicity.";
RL   Cancer Res. 68:4588-4596(2008).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-489, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma, and Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [10]
RP   X-RAY CRYSTALLOGRAPHY (2.29 ANGSTROMS) OF WAVE1 COMPLEX, AND SUBUNIT.
RX   PubMed=21107423; DOI=10.1038/nature09623;
RA   Chen Z., Borek D., Padrick S.B., Gomez T.S., Metlagel Z., Ismail A.M.,
RA   Umetani J., Billadeau D.D., Otwinowski Z., Rosen M.K.;
RT   "Structure and control of the actin regulatory WAVE complex.";
RL   Nature 468:533-538(2010).
RN   [11]
RP   VARIANTS NEDALVS 506-ARG--GLU-559 DEL AND 520-GLN--GLU-559 DEL,
RP   CHARACTERIZATION OF VARIANT NEDALVS 506-ARG--GLU-559 DEL, AND FUNCTION.
RX   PubMed=29961568; DOI=10.1016/j.ajhg.2018.06.001;
RG   NIHR BioResource;
RG   Care4Rare Canada Consortium;
RA   Ito Y., Carss K.J., Duarte S.T., Hartley T., Keren B., Kurian M.A.,
RA   Marey I., Charles P., Mendonca C., Nava C., Pfundt R., Sanchis-Juan A.,
RA   van Bokhoven H., van Essen A., van Ravenswaaij-Arts C., Boycott K.M.,
RA   Kernohan K.D., Dyack S., Raymond F.L.;
RT   "De Novo Truncating Mutations in WASF1 Cause Intellectual Disability with
RT   Seizures.";
RL   Am. J. Hum. Genet. 103:144-153(2018).
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 (PubMed:29961568). The
CC       WAVE complex regulates actin filament reorganization via its
CC       interaction with the Arp2/3 complex (By similarity). As component of
CC       the WAVE1 complex, required for BDNF-NTRK2 endocytic trafficking and
CC       signaling from early endosomes (By similarity). Also involved in the
CC       regulation of mitochondrial dynamics (PubMed:29961568).
CC       {ECO:0000250|UniProtKB:Q8R5H6, ECO:0000269|PubMed:29961568,
CC       ECO:0000269|PubMed:9889097}.
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. {ECO:0000269|PubMed:11130076,
CC       ECO:0000269|PubMed:18559503, ECO:0000269|PubMed:21107423}.
CC   -!- INTERACTION:
CC       Q92558; Q9P2A4: ABI3; NbExp=3; IntAct=EBI-1548747, EBI-742038;
CC       Q92558; A0A1B0GWI1: CCDC196; NbExp=6; IntAct=EBI-1548747, EBI-10181422;
CC       Q92558; Q5JVL4: EFHC1; NbExp=3; IntAct=EBI-1548747, EBI-743105;
CC       Q92558; P62993: GRB2; NbExp=3; IntAct=EBI-1548747, EBI-401755;
CC       Q92558; O75031: HSF2BP; NbExp=3; IntAct=EBI-1548747, EBI-7116203;
CC       Q92558; Q8WYH8: ING5; NbExp=3; IntAct=EBI-1548747, EBI-488533;
CC       Q92558; P25791-3: LMO2; NbExp=3; IntAct=EBI-1548747, EBI-11959475;
CC       Q92558; O43639: NCK2; NbExp=4; IntAct=EBI-1548747, EBI-713635;
CC       Q92558; P07737: PFN1; NbExp=2; IntAct=EBI-1548747, EBI-713780;
CC       Q92558; Q12933: TRAF2; NbExp=3; IntAct=EBI-1548747, EBI-355744;
CC       Q92558; Q15642: TRIP10; NbExp=3; IntAct=EBI-1548747, EBI-739936;
CC       Q92558; Q15642-2: TRIP10; NbExp=3; IntAct=EBI-1548747, EBI-6550597;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC       {ECO:0000269|PubMed:9889097}. Synapse {ECO:0000250|UniProtKB:Q5BJU7}.
CC       Cell junction, focal adhesion {ECO:0000269|PubMed:18559503}. Note=Dot-
CC       like pattern in the cytoplasm. Concentrated in Rac-regulated membrane-
CC       ruffling areas (PubMed:9889097). Partial translocation to focal
CC       adhesion sites might be mediated by interaction with SORBS2
CC       (PubMed:18559503). In neurons, colocalizes with activated NTRK2 after
CC       BDNF addition in endocytic sites through the association with TMEM108
CC       (By similarity). {ECO:0000250|UniProtKB:Q8R5H6,
CC       ECO:0000269|PubMed:18559503, ECO:0000269|PubMed:9889097}.
CC   -!- TISSUE SPECIFICITY: Highly expressed in brain. Lowly expressed in
CC       testis, ovary, colon, kidney, pancreas, thymus, small intestine and
CC       peripheral blood.
CC   -!- DOMAIN: Binds the Arp2/3 complex through the C-terminal region and
CC       actin through verprolin homology (VPH) domain.
CC       {ECO:0000269|PubMed:9889097}.
CC   -!- PTM: Phosphorylated on tyrosine residues by ABL1 and dephosphorylated
CC       by PTPN12. {ECO:0000269|PubMed:18559503}.
CC   -!- DISEASE: Neurodevelopmental disorder with absent language and variable
CC       seizures (NEDALVS) [MIM:618707]: A disorder characterized by
CC       neurodevelopmental abnormalities, including moderate to profound
CC       intellectual disability, with autistic features, seizures, severe
CC       impairments in speech, and gross motor delay.
CC       {ECO:0000269|PubMed:29961568}. Note=The disease is caused by variants
CC       affecting the gene represented in this entry.
CC   -!- SIMILARITY: Belongs to the SCAR/WAVE family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA13399.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF134303; AAD33052.1; -; mRNA.
DR   EMBL; D87459; BAA13399.2; ALT_INIT; mRNA.
DR   EMBL; AL590009; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471051; EAW48325.1; -; Genomic_DNA.
DR   EMBL; CH471051; EAW48326.1; -; Genomic_DNA.
DR   EMBL; CH471051; EAW48327.1; -; Genomic_DNA.
DR   EMBL; CH471051; EAW48328.1; -; Genomic_DNA.
DR   EMBL; CH471051; EAW48329.1; -; Genomic_DNA.
DR   EMBL; BC044591; AAH44591.1; -; mRNA.
DR   CCDS; CCDS5080.1; -.
DR   RefSeq; NP_001020105.1; NM_001024934.1.
DR   RefSeq; NP_001020106.1; NM_001024935.1.
DR   RefSeq; NP_001020107.1; NM_001024936.1.
DR   RefSeq; NP_003922.1; NM_003931.2.
DR   RefSeq; XP_005267260.1; XM_005267203.3.
DR   RefSeq; XP_005267262.1; XM_005267205.2.
DR   RefSeq; XP_005267263.1; XM_005267206.2.
DR   RefSeq; XP_005267264.1; XM_005267207.2.
DR   RefSeq; XP_011534535.1; XM_011536233.1.
DR   RefSeq; XP_011534536.1; XM_011536234.1.
DR   RefSeq; XP_016866926.1; XM_017011437.1.
DR   RefSeq; XP_016866927.1; XM_017011438.1.
DR   PDB; 3P8C; X-ray; 2.29 A; D=1-186, D=485-559.
DR   PDB; 4N78; X-ray; 2.43 A; D=1-559.
DR   PDB; 7USC; EM; 3.00 A; C=1-230.
DR   PDB; 7USD; EM; 3.00 A; C=1-230.
DR   PDB; 7USE; EM; 3.00 A; C=1-230.
DR   PDBsum; 3P8C; -.
DR   PDBsum; 4N78; -.
DR   PDBsum; 7USC; -.
DR   PDBsum; 7USD; -.
DR   PDBsum; 7USE; -.
DR   AlphaFoldDB; Q92558; -.
DR   EMDB; EMD-26732; -.
DR   EMDB; EMD-26733; -.
DR   EMDB; EMD-26734; -.
DR   SMR; Q92558; -.
DR   BioGRID; 114449; 117.
DR   DIP; DIP-39391N; -.
DR   ELM; Q92558; -.
DR   IntAct; Q92558; 58.
DR   MINT; Q92558; -.
DR   STRING; 9606.ENSP00000376367; -.
DR   GlyGen; Q92558; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q92558; -.
DR   PhosphoSitePlus; Q92558; -.
DR   BioMuta; WASF1; -.
DR   DMDM; 2495730; -.
DR   EPD; Q92558; -.
DR   jPOST; Q92558; -.
DR   MassIVE; Q92558; -.
DR   MaxQB; Q92558; -.
DR   PaxDb; 9606-ENSP00000376368; -.
DR   PeptideAtlas; Q92558; -.
DR   ProteomicsDB; 75315; -.
DR   Pumba; Q92558; -.
DR   ABCD; Q92558; 1 sequenced antibody.
DR   Antibodypedia; 1180; 371 antibodies from 39 providers.
DR   DNASU; 8936; -.
DR   Ensembl; ENST00000359451.6; ENSP00000352425.2; ENSG00000112290.13.
DR   Ensembl; ENST00000392586.5; ENSP00000376365.1; ENSG00000112290.13.
DR   Ensembl; ENST00000392587.6; ENSP00000376366.2; ENSG00000112290.13.
DR   Ensembl; ENST00000392588.5; ENSP00000376367.1; ENSG00000112290.13.
DR   Ensembl; ENST00000392589.6; ENSP00000376368.1; ENSG00000112290.13.
DR   GeneID; 8936; -.
DR   KEGG; hsa:8936; -.
DR   MANE-Select; ENST00000392589.6; ENSP00000376368.1; NM_003931.3; NP_003922.1.
DR   UCSC; uc003ptv.1; human.
DR   AGR; HGNC:12732; -.
DR   CTD; 8936; -.
DR   DisGeNET; 8936; -.
DR   GeneCards; WASF1; -.
DR   HGNC; HGNC:12732; WASF1.
DR   HPA; ENSG00000112290; Tissue enhanced (brain, testis).
DR   MalaCards; WASF1; -.
DR   MIM; 605035; gene.
DR   MIM; 618707; phenotype.
DR   neXtProt; NX_Q92558; -.
DR   OpenTargets; ENSG00000112290; -.
DR   Orphanet; 528084; Non-specific syndromic intellectual disability.
DR   PharmGKB; PA37343; -.
DR   VEuPathDB; HostDB:ENSG00000112290; -.
DR   eggNOG; KOG1830; Eukaryota.
DR   GeneTree; ENSGT00950000182962; -.
DR   HOGENOM; CLU_036022_2_0_1; -.
DR   InParanoid; Q92558; -.
DR   OMA; NILTPYX; -.
DR   OrthoDB; 616448at2759; -.
DR   PhylomeDB; Q92558; -.
DR   TreeFam; TF315031; -.
DR   PathwayCommons; Q92558; -.
DR   Reactome; R-HSA-2029482; Regulation of actin dynamics for phagocytic cup formation.
DR   Reactome; R-HSA-4420097; VEGFA-VEGFR2 Pathway.
DR   Reactome; R-HSA-5663213; RHO GTPases Activate WASPs and WAVEs.
DR   Reactome; R-HSA-9013149; RAC1 GTPase cycle.
DR   Reactome; R-HSA-9013423; RAC3 GTPase cycle.
DR   Reactome; R-HSA-9664422; FCGR3A-mediated phagocytosis.
DR   SignaLink; Q92558; -.
DR   SIGNOR; Q92558; -.
DR   BioGRID-ORCS; 8936; 11 hits in 1155 CRISPR screens.
DR   ChiTaRS; WASF1; human.
DR   EvolutionaryTrace; Q92558; -.
DR   GeneWiki; WASF1; -.
DR   GenomeRNAi; 8936; -.
DR   Pharos; Q92558; Tbio.
DR   PRO; PR:Q92558; -.
DR   Proteomes; UP000005640; Chromosome 6.
DR   RNAct; Q92558; Protein.
DR   Bgee; ENSG00000112290; Expressed in cortical plate and 177 other cell types or tissues.
DR   ExpressionAtlas; Q92558; baseline and differential.
DR   GO; GO:0015629; C:actin cytoskeleton; TAS:ProtInc.
DR   GO; GO:0005856; C:cytoskeleton; TAS:ProtInc.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0005925; C:focal adhesion; IEA:UniProtKB-SubCell.
DR   GO; GO:0030027; C:lamellipodium; IBA:GO_Central.
DR   GO; GO:0005741; C:mitochondrial outer membrane; IEA:Ensembl.
DR   GO; GO:0098794; C:postsynapse; IEA:Ensembl.
DR   GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR   GO; GO:0031209; C:SCAR complex; IMP:UniProtKB.
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; IPI:UniProtKB.
DR   GO; GO:0034237; F:protein kinase A regulatory subunit binding; IBA:GO_Central.
DR   GO; GO:0030036; P:actin cytoskeleton organization; IMP:UniProtKB.
DR   GO; GO:0030041; P:actin filament polymerization; TAS:ProtInc.
DR   GO; GO:1990416; P:cellular response to brain-derived neurotrophic factor stimulus; ISS:UniProtKB.
DR   GO; GO:0097484; P:dendrite extension; IEA:Ensembl.
DR   GO; GO:0072673; P:lamellipodium morphogenesis; IMP:UniProtKB.
DR   GO; GO:0007005; P:mitochondrion organization; IMP:UniProtKB.
DR   GO; GO:0098885; P:modification of postsynaptic actin cytoskeleton; IEA:Ensembl.
DR   GO; GO:2000601; P:positive regulation of Arp2/3 complex-mediated actin nucleation; IMP:UniProtKB.
DR   GO; GO:0051388; P:positive regulation of neurotrophin TRK receptor signaling pathway; IEA:Ensembl.
DR   GO; GO:0065003; P:protein-containing complex assembly; NAS:ProtInc.
DR   GO; GO:0016601; P:Rac protein signal transduction; IMP:UniProtKB.
DR   GO; GO:0006898; P:receptor-mediated endocytosis; ISS:UniProtKB.
DR   CDD; cd22071; WH2_WAVE-1; 1.
DR   DisProt; DP02529; -.
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:SF8; WISKOTT-ALDRICH SYNDROME PROTEIN FAMILY MEMBER 1; 1.
DR   Pfam; PF02205; WH2; 1.
DR   SMART; SM00246; WH2; 1.
DR   PROSITE; PS51082; WH2; 1.
DR   Genevisible; Q92558; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Actin-binding; Cell junction; Cytoplasm; Cytoskeleton;
KW   Disease variant; Epilepsy; Intellectual disability; Methylation;
KW   Phosphoprotein; Reference proteome; Synapse.
FT   CHAIN           1..559
FT                   /note="Actin-binding protein WASF1"
FT                   /id="PRO_0000188992"
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          304..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:0000250|UniProtKB:Q8R5H6"
FT   MOD_RES         341
FT                   /note="Omega-N-methylarginine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8R5H6"
FT   MOD_RES         489
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   VARIANT         506..559
FT                   /note="Missing (in NEDALVS; expression of a truncated and
FT                   unstable protein; altered actin organization and longer
FT                   mitochondria)"
FT                   /evidence="ECO:0000269|PubMed:29961568"
FT                   /id="VAR_083471"
FT   VARIANT         520..559
FT                   /note="Missing (in NEDALVS)"
FT                   /evidence="ECO:0000269|PubMed:29961568"
FT                   /id="VAR_083472"
FT   HELIX           26..81
FT                   /evidence="ECO:0007829|PDB:3P8C"
FT   TURN            85..87
FT                   /evidence="ECO:0007829|PDB:3P8C"
FT   HELIX           93..96
FT                   /evidence="ECO:0007829|PDB:3P8C"
FT   HELIX           114..116
FT                   /evidence="ECO:0007829|PDB:3P8C"
FT   HELIX           119..127
FT                   /evidence="ECO:0007829|PDB:3P8C"
FT   HELIX           134..140
FT                   /evidence="ECO:0007829|PDB:3P8C"
FT   HELIX           147..150
FT                   /evidence="ECO:0007829|PDB:3P8C"
FT   HELIX           156..181
FT                   /evidence="ECO:0007829|PDB:3P8C"
FT   HELIX           500..509
FT                   /evidence="ECO:0007829|PDB:4N78"
FT   STRAND          512..514
FT                   /evidence="ECO:0007829|PDB:4N78"
FT   HELIX           531..540
FT                   /evidence="ECO:0007829|PDB:4N78"
SQ   SEQUENCE   559 AA;  61652 MW;  44B4527BDB77BC6E CRC64;
     MPLVKRNIDP RHLCHTALPR GIKNELECVT NISLANIIRQ LSSLSKYAED IFGELFNEAH
     SFSFRVNSLQ ERVDRLSVSV TQLDPKEEEL SLQDITMRKA FRSSTIQDQQ LFDRKTLPIP
     LQETYDVCEQ PPPLNILTPY RDDGKEGLKF YTNPSYFFDL WKEKMLQDTE DKRKEKRKQK
     QKNLDRPHEP EKVPRAPHDR RREWQKLAQG PELAEDDANL LHKHIEVANG PASHFETRPQ
     TYVDHMDGSY SLSALPFSQM SELLTRAEER VLVRPHEPPP PPPMHGAGDA KPIPTCISSA
     TGLIENRPQS PATGRTPVFV SPTPPPPPPP LPSALSTSSL RASMTSTPPP PVPPPPPPPA
     TALQAPAVPP PPAPLQIAPG VLHPAPPPIA PPLVQPSPPV ARAAPVCETV PVHPLPQGEV
     QGLPPPPPPP PLPPPGIRPS SPVTVTALAH PPSGLHPTPS TAPGPHVPLM PPSPPSQVIP
     ASEPKRHPST LPVISDARSV LLEAIRKGIQ LRKVEEQREQ EAKHERIEND VATILSRRIA
     VEYSDSEDDS EFDEVDWLE
//