WASL_BOVIN
ID WASL_BOVIN Reviewed; 505 AA.
AC Q95107;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Actin nucleation-promoting factor WASL {ECO:0000305};
DE AltName: Full=Neural Wiskott-Aldrich syndrome protein;
DE Short=N-WASP;
GN Name=WASL;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=8895577; DOI=10.1002/j.1460-2075.1996.tb00917.x;
RA Miki H., Miura K., Takenawa T.;
RT "N-WASP, a novel actin-depolymerizing protein, regulates the cortical
RT cytoskeletal rearrangement in a PIP2-dependent manner downstream of
RT tyrosine kinases.";
RL EMBO J. 15:5326-5335(1996).
RN [2]
RP FUNCTION, AND INTERACTION WITH SNX9.
RX PubMed=17609109; DOI=10.1016/j.devcel.2007.04.014;
RA Yarar D., Waterman-Storer C.M., Schmid S.L.;
RT "SNX9 couples actin assembly to phosphoinositide signals and is required
RT for membrane remodeling during endocytosis.";
RL Dev. Cell 13:43-56(2007).
CC -!- FUNCTION: Regulates actin polymerization by stimulating the actin-
CC nucleating activity of the Arp2/3 complex (PubMed:17609109). Involved
CC in various processes, such as mitosis and cytokinesis, via its role in
CC the regulation of actin polymerization. Together with CDC42, involved
CC in the extension and maintenance of the formation of thin, actin-rich
CC surface projections called filopodia. In addition to its role in the
CC cytoplasm, also plays a role in the nucleus by regulating gene
CC transcription, probably by promoting nuclear actin polymerization (By
CC similarity). Binds to HSF1/HSTF1 and forms a complex on heat shock
CC promoter elements (HSE) that negatively regulates HSP90 expression.
CC Plays a role in dendrite spine morphogenesis (By similarity).
CC {ECO:0000250|UniProtKB:O00401, ECO:0000250|UniProtKB:Q91YD9,
CC ECO:0000269|PubMed:17609109}.
CC -!- SUBUNIT: Binds actin and the Arp2/3 complex. Interacts with CDC42 (By
CC similarity). Interacts with FCHSD1. Interacts with FCHSD2 (By
CC similarity). Binds to SH3 domains of GRB2. Interacts with the C-
CC terminal SH3 domain of DNMBP (By similarity). Interacts with SNX9
CC (PubMed:17609109). Interacts with the WW domains of PRPF40A/FBP11.
CC Interacts with PTK2/FAK1. Interacts with PACSIN1, PACSIN2 and PACSIN3
CC (By similarity). Interacts with NOSTRIN. Binds to TNK2. Interacts with
CC SNX33. Interacts with NONO (via second RRM domain); the interaction is
CC direct. Component of a multiprotein complex with NONO and SFPQ;
CC associates with the complex via direct interaction with NONO (By
CC similarity). {ECO:0000250|UniProtKB:O00401,
CC ECO:0000250|UniProtKB:Q91YD9, ECO:0000269|PubMed:17609109}.
CC -!- INTERACTION:
CC Q95107; A7MB62: ACTR2; NbExp=2; IntAct=EBI-6162776, EBI-6162748;
CC Q95107; Q95107: WASL; NbExp=3; IntAct=EBI-6162776, EBI-6162776;
CC Q95107; Q60598: Cttn; Xeno; NbExp=2; IntAct=EBI-6162776, EBI-397955;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:O00401}. Nucleus {ECO:0000250|UniProtKB:O00401}.
CC Cytoplasm {ECO:0000250|UniProtKB:Q91YD9}. Note=Preferentially localized
CC in the cytoplasm when phosphorylated and in the nucleus when
CC unphosphorylated. Exported from the nucleus by an nuclear export signal
CC (NES)-dependent mechanism to the cytoplasm.
CC {ECO:0000250|UniProtKB:Q91YD9}.
CC -!- PTM: Phosphorylation at Ser-242, Tyr-256, Ser-484 and Ser-485 enhances
CC actin polymerization activity. {ECO:0000250|UniProtKB:O00401}.
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DR EMBL; D67066; BAA11082.1; -; mRNA.
DR PIR; S72273; S72273.
DR RefSeq; NP_776644.1; NM_174219.2.
DR AlphaFoldDB; Q95107; -.
DR BMRB; Q95107; -.
DR SMR; Q95107; -.
DR CORUM; Q95107; -.
DR ELM; Q95107; -.
DR IntAct; Q95107; 5.
DR STRING; 9913.ENSBTAP00000006094; -.
DR iPTMnet; Q95107; -.
DR PaxDb; Q95107; -.
DR PeptideAtlas; Q95107; -.
DR PRIDE; Q95107; -.
DR Ensembl; ENSBTAT00000006094; ENSBTAP00000006094; ENSBTAG00000004643.
DR Ensembl; ENSBTAT00000074672; ENSBTAP00000074401; ENSBTAG00000004643.
DR GeneID; 281577; -.
DR KEGG; bta:281577; -.
DR CTD; 8976; -.
DR VEuPathDB; HostDB:ENSBTAG00000004643; -.
DR VGNC; VGNC:56336; WASL.
DR eggNOG; KOG3671; Eukaryota.
DR GeneTree; ENSGT00730000110895; -.
DR HOGENOM; CLU_015385_3_1_1; -.
DR InParanoid; Q95107; -.
DR OMA; LGRKCQT; -.
DR OrthoDB; 1407277at2759; -.
DR TreeFam; TF316736; -.
DR Proteomes; UP000009136; Chromosome 4.
DR Bgee; ENSBTAG00000004643; Expressed in occipital lobe and 103 other tissues.
DR ExpressionAtlas; Q95107; baseline and differential.
DR GO; GO:0030478; C:actin cap; IEA:Ensembl.
DR GO; GO:0005884; C:actin filament; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0030027; C:lamellipodium; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0030041; P:actin filament polymerization; ISS:UniProtKB.
DR GO; GO:0030048; P:actin filament-based movement; IBA:GO_Central.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0060997; P:dendritic spine morphogenesis; ISS:UniProtKB.
DR GO; GO:2000402; P:negative regulation of lymphocyte migration; IEA:Ensembl.
DR GO; GO:1903526; P:negative regulation of membrane tubulation; IEA:Ensembl.
DR GO; GO:2000601; P:positive regulation of Arp2/3 complex-mediated actin nucleation; IEA:InterPro.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0031503; P:protein-containing complex localization; IEA:Ensembl.
DR GO; GO:0032880; P:regulation of protein localization; IEA:Ensembl.
DR GO; GO:0009617; P:response to bacterium; IEA:Ensembl.
DR GO; GO:0051653; P:spindle localization; IEA:Ensembl.
DR CDD; cd01205; EVH1_WASP-like; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR Gene3D; 3.90.810.10; -; 2.
DR InterPro; IPR000095; CRIB_dom.
DR InterPro; IPR036936; CRIB_dom_sf.
DR InterPro; IPR030214; N-WASP.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR011026; WASP_C.
DR InterPro; IPR033927; WASPfam_EVH1.
DR InterPro; IPR000697; WH1/EVH1_dom.
DR InterPro; IPR003124; WH2_dom.
DR PANTHER; PTHR23202:SF39; PTHR23202:SF39; 1.
DR Pfam; PF00786; PBD; 1.
DR Pfam; PF00568; WH1; 1.
DR Pfam; PF02205; WH2; 2.
DR SMART; SM00285; PBD; 1.
DR SMART; SM00461; WH1; 1.
DR SMART; SM00246; WH2; 2.
DR SUPFAM; SSF47912; SSF47912; 2.
DR PROSITE; PS50108; CRIB; 1.
DR PROSITE; PS50229; WH1; 1.
DR PROSITE; PS51082; WH2; 2.
PE 1: Evidence at protein level;
KW Acetylation; Actin-binding; Cell cycle; Cell division; Cytoplasm;
KW Cytoskeleton; Methylation; Mitosis; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Transcription; Transcription regulation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:O00401"
FT CHAIN 2..505
FT /note="Actin nucleation-promoting factor WASL"
FT /id="PRO_0000188999"
FT DOMAIN 34..141
FT /note="WH1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00410"
FT DOMAIN 203..216
FT /note="CRIB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00057"
FT DOMAIN 405..422
FT /note="WH2 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00406"
FT DOMAIN 433..450
FT /note="WH2 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00406"
FT REGION 138..163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 185..205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 266..406
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 449..468
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 477..505
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 274..395
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 486..505
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:O00401"
FT MOD_RES 242
FT /note="Phosphoserine; by TNK2"
FT /evidence="ECO:0000250|UniProtKB:O00401"
FT MOD_RES 256
FT /note="Phosphotyrosine; by FAK1 and TNK2"
FT /evidence="ECO:0000250|UniProtKB:O00401"
FT MOD_RES 307
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:O00401"
FT MOD_RES 484
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00401"
FT MOD_RES 485
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00401"
SQ SEQUENCE 505 AA; 54672 MW; 54B83B48F1CDB3B8 CRC64;
MSSGQQQPPP PRRVTNVGSL LLTPQENESL FTFLGKKCVT MSSAVVQLYA ADRNCMWSKK
CSGVACLVKD NPQRSYFLRI FDIKDGKLLW EQELYNNFVY NSPRGYFHTF AGDTCQVALN
FANEEEAKKF RKAVTDLLGR RQRKSEKRRD PPNGPNLPMA TVDIKNPEIT TNRFYGPQIN
NISHTKEKKK GKAKKKRLTK ADIGTPSNFQ HIGHVGWDPN TGFDLNNLDP ELKNLFDMCG
ISEAQLKDRE TSKVIYDFIE KTGGVEAVKN ELRRQAPPPP PPSRGGPPPP PPPPHSSGPP
PPPARGRGAP PPPPSRAPTA APPPPPPSRP GVGAPPPPPN RMYPPPLPAL PSSAPSGPPP
PPPPLSVSGS VAPPPPPPPP PPPGPPPPPG LPSDGDHQVP TPAGSKAALL DQIREGAQLK
KVEQNSRPVS CSGRDALLDQ IRQGIQLKSV TDAPESTPPA PAPTSGIVGA LMEVMQKRSK
AIHSSDEDED EDDDEDFEDD DEWED
