WASF2_MOUSE
ID WASF2_MOUSE Reviewed; 497 AA.
AC Q8BH43;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Actin-binding protein WASF2 {ECO:0000305};
DE AltName: Full=Protein WAVE-2;
DE AltName: Full=Wiskott-Aldrich syndrome protein family member 2;
DE Short=WASP family protein member 2;
GN Name=Wasf2 {ECO:0000312|MGI:MGI:1098641};
GN Synonyms=Wave2 {ECO:0000312|MGI:MGI:1098641};
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 STRAIN=C57BL/6J; TISSUE=Kidney;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP COMPONENT OF WAVE2 COMPLEX.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=14765121; DOI=10.1038/sj.emboj.7600084;
RA Steffen A., Rottner K., Ehinger J., Innocenti M., Scita G., Wehland J.,
RA Stradal T.E.B.;
RT "Sra-1 and Nap1 link Rac to actin assembly driving lamellipodia
RT formation.";
RL EMBO J. 23:749-759(2004).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
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 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). {ECO:0000250|UniProtKB:Q9Y6W5}.
CC -!- SUBUNIT: Binds actin and the Arp2/3 complex. Interacts with BAIAP2.
CC Component of the WAVE2 complex composed of ABI1, CYFIP1/SRA1,
CC NCKAP1/NAP1 (NCKAP1l/HEM1 in hematopoietic cells) and WASF2/WAVE2.
CC Directly interacts with BRK1. Interacts with human cytomegalovirus
CC protein UL135. Interacts with FNBP1L (via the SH3 domain).
CC {ECO:0000250|UniProtKB:Q9Y6W5}.
CC -!- INTERACTION:
CC Q8BH43; Q8CBW3: Abi1; NbExp=2; IntAct=EBI-643162, EBI-375511;
CC Q8BH43; Q8CHG3: Gcc2; NbExp=6; IntAct=EBI-643162, EBI-643470;
CC Q8BH43; Q3URD3-4: Slmap; NbExp=3; IntAct=EBI-643162, EBI-3294998;
CC Q8BH43; Q8CG48: Smc2; NbExp=4; IntAct=EBI-643162, EBI-643436;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Cell
CC projection, lamellipodium {ECO:0000250}. Basolateral cell membrane
CC {ECO:0000250|UniProtKB:Q9Y6W5}. Note=At the interface between the
CC lamellipodial actin meshwork and the membrane. {ECO:0000250}.
CC -!- DOMAIN: Binds and activates the Arp2/3 complex via the C-terminal
CC domain. Interacts with actin via the WH2 domain (By similarity).
CC {ECO:0000250|UniProtKB:Q9Y6W5}.
CC -!- SIMILARITY: Belongs to the SCAR/WAVE family. {ECO:0000305}.
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DR EMBL; AY135643; AAN10152.1; -; mRNA.
DR EMBL; AK085458; BAC39451.1; -; mRNA.
DR CCDS; CCDS18742.1; -.
DR RefSeq; NP_700472.1; NM_153423.6.
DR RefSeq; XP_006538911.1; XM_006538848.3.
DR RefSeq; XP_006538912.1; XM_006538849.3.
DR RefSeq; XP_006538913.1; XM_006538850.3.
DR AlphaFoldDB; Q8BH43; -.
DR SMR; Q8BH43; -.
DR BioGRID; 232443; 13.
DR CORUM; Q8BH43; -.
DR DIP; DIP-29535N; -.
DR IntAct; Q8BH43; 17.
DR MINT; Q8BH43; -.
DR STRING; 10090.ENSMUSP00000081263; -.
DR iPTMnet; Q8BH43; -.
DR PhosphoSitePlus; Q8BH43; -.
DR EPD; Q8BH43; -.
DR jPOST; Q8BH43; -.
DR MaxQB; Q8BH43; -.
DR PaxDb; Q8BH43; -.
DR PeptideAtlas; Q8BH43; -.
DR PRIDE; Q8BH43; -.
DR ProteomicsDB; 299963; -.
DR Antibodypedia; 30784; 353 antibodies from 32 providers.
DR DNASU; 242687; -.
DR Ensembl; ENSMUST00000084241; ENSMUSP00000081263; ENSMUSG00000028868.
DR Ensembl; ENSMUST00000105912; ENSMUSP00000101532; ENSMUSG00000028868.
DR GeneID; 242687; -.
DR KEGG; mmu:242687; -.
DR UCSC; uc008vcf.1; mouse.
DR CTD; 10163; -.
DR MGI; MGI:1098641; Wasf2.
DR VEuPathDB; HostDB:ENSMUSG00000028868; -.
DR eggNOG; KOG1830; Eukaryota.
DR GeneTree; ENSGT00950000182962; -.
DR HOGENOM; CLU_036022_2_0_1; -.
DR InParanoid; Q8BH43; -.
DR OMA; PDMAYND; -.
DR OrthoDB; 1183697at2759; -.
DR PhylomeDB; Q8BH43; -.
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-9013404; RAC2 GTPase cycle.
DR Reactome; R-MMU-9013423; RAC3 GTPase cycle.
DR BioGRID-ORCS; 242687; 5 hits in 73 CRISPR screens.
DR ChiTaRS; Wasf2; mouse.
DR PRO; PR:Q8BH43; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q8BH43; protein.
DR Bgee; ENSMUSG00000028868; Expressed in animal zygote and 239 other tissues.
DR ExpressionAtlas; Q8BH43; baseline and differential.
DR Genevisible; Q8BH43; MM.
DR GO; GO:0016323; C:basolateral plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005911; C:cell-cell junction; IDA:MGI.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005769; C:early endosome; IDA:MGI.
DR GO; GO:0030027; C:lamellipodium; IDA:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0001726; C:ruffle; IDA:MGI.
DR GO; GO:0031209; C:SCAR complex; IDA:ARUK-UCL.
DR GO; GO:0045202; C:synapse; IDA:SynGO.
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:0017124; F:SH3 domain binding; ISO:MGI.
DR GO; GO:0030036; P:actin cytoskeleton organization; IMP:MGI.
DR GO; GO:0030048; P:actin filament-based movement; IMP:MGI.
DR GO; GO:0001667; P:ameboidal-type cell migration; IMP:MGI.
DR GO; GO:0001525; P:angiogenesis; IMP:MGI.
DR GO; GO:0006897; P:endocytosis; IDA:MGI.
DR GO; GO:0030032; P:lamellipodium assembly; IMP:MGI.
DR GO; GO:0072673; P:lamellipodium morphogenesis; IMP:MGI.
DR GO; GO:0035855; P:megakaryocyte development; IMP:MGI.
DR GO; GO:0051497; P:negative regulation of stress fiber assembly; ISO:MGI.
DR GO; GO:2000601; P:positive regulation of Arp2/3 complex-mediated actin nucleation; IBA:GO_Central.
DR GO; GO:0010592; P:positive regulation of lamellipodium assembly; ISO:MGI.
DR GO; GO:0098974; P:postsynaptic actin cytoskeleton organization; IDA:SynGO.
DR GO; GO:0016601; P:Rac protein signal transduction; IMP:MGI.
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 membrane; Cell projection; Cytoplasm; Cytoskeleton;
KW Membrane; Phosphoprotein; Reference proteome.
FT CHAIN 1..497
FT /note="Actin-binding protein WASF2"
FT /id="PRO_0000188995"
FT DOMAIN 435..452
FT /note="WH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00406"
FT REGION 173..203
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 239..436
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 184..203
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 295..424
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 473
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6W5"
SQ SEQUENCE 497 AA; 54074 MW; 4F970D0577792503 CRC64;
MPLVTRNIEP RHLCRQTLPS DTSELECRTN ITLANVIRQL GSLSKYAEDI FGEICTQASA
FASRVNSLAE RVDRVQVKVT QLDPKEEEVS LQGINTRKAF RSSTTQDQKL FDRNSLPVPV
LETYNSCDAP PPLNNLSPYR DDGKEALKFY TNPSYFFDLW KEKMLQDTKD IMKEKRKHRK
EKKDNPNRGN VNPRKIKTRK EEWEKMKMGQ EFVESKERLG PSGYSSTLVY QNGSIGSVEN
VDAASYPPPP QSDSASSPSP SFSEDNLPPP PAEFSYPADN QRGSVLAGPK RTSMVSPSHP
PPAPPLSSPP GPKPGFAPPP APPPPPPMSV PPPLPSMGFG SPGTPPPPSP PSFPPHPDFA
APPPPPPPPA ADYPMPPPPL SQPSGGAPPP PPPPPPPGPP PLPFSGADGQ PAAPPPPPPS
EATKPKSSLP AVSDARSDLL SAIRQGFQLR RVEEQREQEK RDVVGNDVAT ILSRRIAVEY
SDSEDDSSEF DEDDWSD
