WASF3_HUMAN
ID WASF3_HUMAN Reviewed; 502 AA.
AC Q9UPY6; O94974; Q86VQ2;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 2.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Actin-binding protein WASF3 {ECO:0000305};
DE AltName: Full=Protein WAVE-3;
DE AltName: Full=Verprolin homology domain-containing protein 3;
DE AltName: Full=Wiskott-Aldrich syndrome protein family member 3;
DE Short=WASP family protein member 3;
GN Name=WASF3; Synonyms=KIAA0900, SCAR3, WAVE3;
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] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=10381382; DOI=10.1006/bbrc.1999.0894;
RA Suetsugu S., Miki H., Takenawa T.;
RT "Identification of two human WAVE/SCAR homologues as general actin
RT regulatory molecules which associate with the Arp2/3 complex.";
RL Biochem. Biophys. Res. Commun. 260:296-302(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=10048485; DOI=10.1093/dnares/5.6.355;
RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 5:355-364(1998).
RN [4]
RP SEQUENCE REVISION.
RX PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT "Construction of expression-ready cDNA clones for KIAA genes: manual
RT curation of 330 KIAA cDNA clones.";
RL DNA Res. 9:99-106(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057823; DOI=10.1038/nature02379;
RA Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
RA Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S.,
RA Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L.,
RA Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C.,
RA Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P.,
RA Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L.,
RA Frankish A.G., Frankland J., French L., Garner P., Garnett J.,
RA Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M.,
RA Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D.,
RA Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D.,
RA Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
RA Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S.,
RA Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R.,
RA Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W.,
RA Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L.,
RA Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R.,
RA Rogers J., Ross M.T.;
RT "The DNA sequence and analysis of human chromosome 13.";
RL Nature 428:522-528(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
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 [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 48-502 (ISOFORM 1).
RA Machesky L.M., Insall R.H.;
RL Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP FUNCTION, AND PHOSPHORYLATION AT TYR-151; TYR-248; TYR-337 AND TYR-486.
RX PubMed=17623672; DOI=10.1074/jbc.m701484200;
RA Sossey-Alaoui K., Li X., Cowell J.K.;
RT "c-Abl-mediated phosphorylation of WAVE3 is required for lamellipodia
RT formation and cell migration.";
RL J. Biol. Chem. 282:26257-26265(2007).
RN [10]
RP FUNCTION.
RX PubMed=21834987; DOI=10.1186/1741-7007-9-54;
RA Bai S.W., Herrera-Abreu M.T., Rohn J.L., Racine V., Tajadura V.,
RA Suryavanshi N., Bechtel S., Wiemann S., Baum B., Ridley A.J.;
RT "Identification and characterization of a set of conserved and new
RT regulators of cytoskeletal organisation, cell morphology and migration.";
RL BMC Biol. 9:54-54(2011).
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.
CC {ECO:0000269|PubMed:17623672, ECO:0000269|PubMed:21834987}.
CC -!- SUBUNIT: Binds actin and the Arp2/3 complex.
CC -!- INTERACTION:
CC Q9UPY6-2; Q9NYB9-2: ABI2; NbExp=3; IntAct=EBI-12026286, EBI-11096309;
CC Q9UPY6-2; Q13895: BYSL; NbExp=3; IntAct=EBI-12026286, EBI-358049;
CC Q9UPY6-2; P61024: CKS1B; NbExp=3; IntAct=EBI-12026286, EBI-456371;
CC Q9UPY6-2; Q63ZY3: KANK2; NbExp=3; IntAct=EBI-12026286, EBI-2556193;
CC Q9UPY6-2; Q9BVG8-5: KIFC3; NbExp=3; IntAct=EBI-12026286, EBI-14069005;
CC Q9UPY6-2; Q86YV0: RASAL3; NbExp=3; IntAct=EBI-12026286, EBI-3437896;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9UPY6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UPY6-2; Sequence=VSP_054517;
CC -!- TISSUE SPECIFICITY: Expressed in ovary and brain.
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:0000269|PubMed:17623672}.
CC -!- SIMILARITY: Belongs to the SCAR/WAVE family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA74923.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB026543; BAA81796.1; -; mRNA.
DR EMBL; AF454702; AAL51032.1; -; mRNA.
DR EMBL; AB020707; BAA74923.2; ALT_INIT; mRNA.
DR EMBL; AL159978; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL163538; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL353789; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471075; EAX08388.1; -; Genomic_DNA.
DR EMBL; BC050283; AAH50283.1; -; mRNA.
DR EMBL; AF134305; AAD33054.1; -; mRNA.
DR CCDS; CCDS76626.1; -. [Q9UPY6-2]
DR CCDS; CCDS9318.1; -. [Q9UPY6-1]
DR RefSeq; NP_001278894.1; NM_001291965.1. [Q9UPY6-2]
DR RefSeq; NP_006637.2; NM_006646.5. [Q9UPY6-1]
DR RefSeq; XP_011533191.1; XM_011534889.1. [Q9UPY6-1]
DR RefSeq; XP_011533192.1; XM_011534890.1. [Q9UPY6-1]
DR AlphaFoldDB; Q9UPY6; -.
DR SMR; Q9UPY6; -.
DR BioGRID; 116024; 46.
DR CORUM; Q9UPY6; -.
DR DIP; DIP-61425N; -.
DR IntAct; Q9UPY6; 31.
DR STRING; 9606.ENSP00000335055; -.
DR iPTMnet; Q9UPY6; -.
DR PhosphoSitePlus; Q9UPY6; -.
DR BioMuta; WASF3; -.
DR DMDM; 59800455; -.
DR EPD; Q9UPY6; -.
DR jPOST; Q9UPY6; -.
DR MassIVE; Q9UPY6; -.
DR MaxQB; Q9UPY6; -.
DR PaxDb; Q9UPY6; -.
DR PeptideAtlas; Q9UPY6; -.
DR PRIDE; Q9UPY6; -.
DR ProteomicsDB; 70056; -.
DR ProteomicsDB; 85474; -. [Q9UPY6-1]
DR Antibodypedia; 22618; 220 antibodies from 28 providers.
DR DNASU; 10810; -.
DR Ensembl; ENST00000335327.6; ENSP00000335055.5; ENSG00000132970.14. [Q9UPY6-1]
DR Ensembl; ENST00000361042.8; ENSP00000354325.4; ENSG00000132970.14. [Q9UPY6-2]
DR GeneID; 10810; -.
DR KEGG; hsa:10810; -.
DR MANE-Select; ENST00000335327.6; ENSP00000335055.5; NM_006646.6; NP_006637.2.
DR UCSC; uc001uqv.5; human. [Q9UPY6-1]
DR CTD; 10810; -.
DR DisGeNET; 10810; -.
DR GeneCards; WASF3; -.
DR HGNC; HGNC:12734; WASF3.
DR HPA; ENSG00000132970; Tissue enhanced (brain, retina).
DR MIM; 605068; gene.
DR neXtProt; NX_Q9UPY6; -.
DR OpenTargets; ENSG00000132970; -.
DR PharmGKB; PA37345; -.
DR VEuPathDB; HostDB:ENSG00000132970; -.
DR eggNOG; KOG1830; Eukaryota.
DR GeneTree; ENSGT00950000182962; -.
DR HOGENOM; CLU_036022_2_0_1; -.
DR InParanoid; Q9UPY6; -.
DR OMA; QSVHHGA; -.
DR PhylomeDB; Q9UPY6; -.
DR TreeFam; TF315031; -.
DR PathwayCommons; Q9UPY6; -.
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-9664422; FCGR3A-mediated phagocytosis.
DR SignaLink; Q9UPY6; -.
DR SIGNOR; Q9UPY6; -.
DR BioGRID-ORCS; 10810; 8 hits in 1070 CRISPR screens.
DR ChiTaRS; WASF3; human.
DR GeneWiki; WASF3; -.
DR GenomeRNAi; 10810; -.
DR Pharos; Q9UPY6; Tbio.
DR PRO; PR:Q9UPY6; -.
DR Proteomes; UP000005640; Chromosome 13.
DR RNAct; Q9UPY6; protein.
DR Bgee; ENSG00000132970; Expressed in substantia nigra pars compacta and 193 other tissues.
DR ExpressionAtlas; Q9UPY6; baseline and differential.
DR Genevisible; Q9UPY6; HS.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
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; IBA:GO_Central.
DR GO; GO:0098794; C:postsynapse; IEA:Ensembl.
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:0030041; P:actin filament polymerization; TAS:ProtInc.
DR GO; GO:0007010; P:cytoskeleton organization; IMP:UniProtKB.
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:2000601; P:positive regulation of Arp2/3 complex-mediated actin nucleation; IBA:GO_Central.
DR GO; GO:0031643; P:positive regulation of myelination; IEA:Ensembl.
DR GO; GO:0065003; P:protein-containing complex assembly; TAS:ProtInc.
DR GO; GO:0008360; P:regulation of cell shape; 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; Alternative splicing; Coiled coil; Cytoplasm; Cytoskeleton;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..502
FT /note="Actin-binding protein WASF3"
FT /id="PRO_0000188996"
FT DOMAIN 440..457
FT /note="WH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00406"
FT REGION 169..210
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 223..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 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"
FT MOD_RES 151
FT /note="Phosphotyrosine; by ABL1"
FT /evidence="ECO:0000269|PubMed:17623672"
FT MOD_RES 248
FT /note="Phosphotyrosine; by ABL1"
FT /evidence="ECO:0000269|PubMed:17623672"
FT MOD_RES 337
FT /note="Phosphotyrosine; by ABL1"
FT /evidence="ECO:0000269|PubMed:17623672"
FT MOD_RES 486
FT /note="Phosphotyrosine; by ABL1"
FT /evidence="ECO:0000269|PubMed:17623672"
FT VAR_SEQ 181..239
FT /note="EQKRIDGTTREVKKVRKARNRRQEWNMMAYDKELRPDNRLSQSVYHGASSEG
FT SLSPDTR -> REKHKLNPNRNQQVNVRKVRTRKEEWERRKMGIEFMSDAKKLEQAGSA
FT KEDRVPSG (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_054517"
FT VARIANT 415
FT /note="S -> L (in dbSNP:rs17084492)"
FT /id="VAR_052953"
FT CONFLICT 307..308
FT /note="PP -> RR (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 502 AA; 55293 MW; C0655CE181BD3C57 CRC64;
MPLVKRNIEP RHLCRGALPE GITSELECVT NSTLAAIIRQ 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 FPASASSTHA APPHPPSTGL LVTAPPPPGP PPPPPGPPGP GSSLSSSPMH
GPPVAEAKRQ EPAQPPISDA RSDLLAAIRM GIQLKKVQEQ REQEAKREPV GNDVATILSR
RIAVEYSDSD DDSEFDENDW SD
