WASF1_HUMAN
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 03-AUG-2022, entry version 184.
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}; 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};
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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 PDBsum; 3P8C; -.
DR PDBsum; 4N78; -.
DR AlphaFoldDB; Q92558; -.
DR SMR; Q92558; -.
DR BioGRID; 114449; 105.
DR DIP; DIP-39391N; -.
DR ELM; Q92558; -.
DR IntAct; Q92558; 52.
DR MINT; Q92558; -.
DR STRING; 9606.ENSP00000376368; -.
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; Q92558; -.
DR PeptideAtlas; Q92558; -.
DR PRIDE; Q92558; -.
DR ProteomicsDB; 75315; -.
DR ABCD; Q92558; 1 sequenced antibody.
DR Antibodypedia; 1180; 338 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 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; XPQTYVD; -.
DR OrthoDB; 1183697at2759; -.
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; 10 hits in 1079 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 175 other tissues.
DR ExpressionAtlas; Q92558; baseline and differential.
DR Genevisible; Q92558; HS.
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:0032839; C:dendrite cytoplasm; IEA:GOC.
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:0098939; P:dendritic transport of mitochondrion; IEA:Ensembl.
DR GO; GO:0072673; P:lamellipodium morphogenesis; IMP:UniProtKB.
DR GO; GO:0070584; P:mitochondrion morphogenesis; 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 DisProt; DP02529; -.
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 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
