WASL_RAT
ID WASL_RAT Reviewed; 501 AA.
AC O08816;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 2.
DT 03-AUG-2022, entry version 195.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9322739; DOI=10.1016/s0378-1119(97)00184-4;
RA Fukuoka M., Miki H., Takenawa T.;
RT "Identification of N-WASP homologs in human and rat brain.";
RL Gene 196:43-48(1997).
RN [2]
RP INTERACTION WITH PTK2/FAK1, SUBCELLULAR LOCATION, AND PHOSPHORYLATION AT
RP TYR-253.
RX PubMed=14676198; DOI=10.1074/jbc.m310739200;
RA Wu X., Suetsugu S., Cooper L.A., Takenawa T., Guan J.L.;
RT "Focal adhesion kinase regulation of N-WASP subcellular localization and
RT function.";
RL J. Biol. Chem. 279:9565-9576(2004).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-253, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [4]
RP STRUCTURE BY NMR OF 37-485.
RX PubMed=12437929; DOI=10.1016/s0092-8674(02)01076-0;
RA Volkman B.F., Prehoda K.E., Scott J.A., Peterson F.C., Lim W.A.;
RT "Structure of the N-WASP EVH1 domain-WIP complex: insight into the
RT molecular basis of Wiskott-Aldrich Syndrome.";
RL Cell 111:565-576(2002).
CC -!- FUNCTION: Regulates actin polymerization by stimulating the actin-
CC nucleating activity of the Arp2/3 complex. Involved in various
CC processes, such as mitosis and cytokinesis, via its role in the
CC regulation of actin polymerization. Together with CDC42, involved in
CC 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 -!- 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 (By
CC similarity). Interacts with the WW domains of PRPF40A/FBP11 (By
CC similarity). Interacts with PTK2/FAK1 (PubMed:14676198). Interacts with
CC PACSIN1, PACSIN2 and PACSIN3 (By similarity). Interacts with NOSTRIN.
CC Binds to TNK2. Interacts with SNX33. Interacts with NONO (via second
CC RRM domain); the interaction is direct. Component of a multiprotein
CC complex with NONO and SFPQ; associates with the complex via direct
CC interaction with NONO (By similarity). {ECO:0000250|UniProtKB:O00401,
CC ECO:0000250|UniProtKB:Q91YD9, ECO:0000250|UniProtKB:Q95107,
CC ECO:0000269|PubMed:14676198}.
CC -!- INTERACTION:
CC O08816; O08816: Wasl; NbExp=3; IntAct=EBI-6142604, EBI-6142604;
CC O08816; Q6IN36: Wipf1; NbExp=2; IntAct=EBI-6142604, EBI-6986245;
CC O08816; P60953: CDC42; Xeno; NbExp=2; IntAct=EBI-6142604, EBI-81752;
CC O08816; Q60598: Cttn; Xeno; NbExp=2; IntAct=EBI-6142604, EBI-397955;
CC O08816; P0DJ88: espF(U); Xeno; NbExp=4; IntAct=EBI-6142604, EBI-10039462;
CC O08816; Q8X482: espF(U); Xeno; NbExp=5; IntAct=EBI-6142604, EBI-22229752;
CC O08816; Q8IVI9: NOSTRIN; Xeno; NbExp=3; IntAct=EBI-6142604, EBI-1391643;
CC O08816; P07737: PFN1; Xeno; NbExp=4; IntAct=EBI-6142604, EBI-713780;
CC O08816; P35080: PFN2; Xeno; NbExp=3; IntAct=EBI-6142604, EBI-473138;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:14676198}. Nucleus {ECO:0000269|PubMed:14676198}.
CC Cytoplasm {ECO:0000250|UniProtKB:Q91YD9}. Note=Preferentially localized
CC in the cytoplasm when phosphorylated and in the nucleus when
CC unphosphorylated (By similarity). Exported from the nucleus by an
CC nuclear export signal (NES)-dependent mechanism to the cytoplasm (By
CC similarity). {ECO:0000250|UniProtKB:Q91YD9}.
CC -!- PTM: Phosphorylation at Ser-239, Tyr-253, Ser-480 and Ser-481 enhances
CC actin polymerization activity. {ECO:0000250|UniProtKB:O00401}.
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DR EMBL; D88461; BAA21534.1; -; mRNA.
DR PDB; 1MKE; NMR; -; A=26-147.
DR PDB; 2IFS; NMR; -; A=26-147.
DR PDBsum; 1MKE; -.
DR PDBsum; 2IFS; -.
DR AlphaFoldDB; O08816; -.
DR BMRB; O08816; -.
DR SMR; O08816; -.
DR DIP; DIP-17016N; -.
DR ELM; O08816; -.
DR IntAct; O08816; 19.
DR MINT; O08816; -.
DR STRING; 10116.ENSRNOP00000009261; -.
DR BindingDB; O08816; -.
DR ChEMBL; CHEMBL3774296; -.
DR iPTMnet; O08816; -.
DR jPOST; O08816; -.
DR PaxDb; O08816; -.
DR PRIDE; O08816; -.
DR UCSC; RGD:735144; rat.
DR RGD; 735144; Wasl.
DR eggNOG; KOG3671; Eukaryota.
DR PhylomeDB; O08816; -.
DR Reactome; R-RNO-2029482; Regulation of actin dynamics for phagocytic cup formation.
DR Reactome; R-RNO-203641; NOSTRIN mediated eNOS trafficking.
DR Reactome; R-RNO-373753; Nephrin family interactions.
DR Reactome; R-RNO-3928662; EPHB-mediated forward signaling.
DR Reactome; R-RNO-418885; DCC mediated attractive signaling.
DR Reactome; R-RNO-5663213; RHO GTPases Activate WASPs and WAVEs.
DR Reactome; R-RNO-8856828; Clathrin-mediated endocytosis.
DR Reactome; R-RNO-9013148; CDC42 GTPase cycle.
DR Reactome; R-RNO-9013149; RAC1 GTPase cycle.
DR Reactome; R-RNO-9013406; RHOQ GTPase cycle.
DR Reactome; R-RNO-9013409; RHOJ GTPase cycle.
DR Reactome; R-RNO-9013424; RHOV GTPase cycle.
DR EvolutionaryTrace; O08816; -.
DR PRO; PR:O08816; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0030478; C:actin cap; ISO:RGD.
DR GO; GO:0005884; C:actin filament; IBA:GO_Central.
DR GO; GO:0031252; C:cell leading edge; IDA:RGD.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:BHF-UCL.
DR GO; GO:0005829; C:cytosol; ISO:RGD.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0000139; C:Golgi membrane; IDA:RGD.
DR GO; GO:0030027; C:lamellipodium; ISO:RGD.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0098794; C:postsynapse; IDA:SynGO.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0008092; F:cytoskeletal protein binding; IPI:RGD.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0030036; P:actin cytoskeleton organization; ISO:RGD.
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:0010324; P:membrane invagination; IDA:BHF-UCL.
DR GO; GO:2000402; P:negative regulation of lymphocyte migration; ISO:RGD.
DR GO; GO:1903526; P:negative regulation of membrane tubulation; ISO:RGD.
DR GO; GO:0097320; P:plasma membrane tubulation; IDA:BHF-UCL.
DR GO; GO:2000601; P:positive regulation of Arp2/3 complex-mediated actin nucleation; IEA:InterPro.
DR GO; GO:0050921; P:positive regulation of chemotaxis; IMP:RGD.
DR GO; GO:2000370; P:positive regulation of clathrin-dependent endocytosis; IDA:BHF-UCL.
DR GO; GO:0051491; P:positive regulation of filopodium assembly; IDA:BHF-UCL.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0098974; P:postsynaptic actin cytoskeleton organization; IDA:SynGO.
DR GO; GO:0031503; P:protein-containing complex localization; ISO:RGD.
DR GO; GO:0060491; P:regulation of cell projection assembly; IMP:RGD.
DR GO; GO:0032880; P:regulation of protein localization; ISO:RGD.
DR GO; GO:0009617; P:response to bacterium; ISO:RGD.
DR GO; GO:0051653; P:spindle localization; ISO:RGD.
DR GO; GO:0006900; P:vesicle budding from membrane; IDA:BHF-UCL.
DR GO; GO:0016050; P:vesicle organization; IDA:BHF-UCL.
DR GO; GO:0030050; P:vesicle transport along actin filament; IDA:BHF-UCL.
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 3D-structure; Acetylation; Actin-binding; Cell cycle; Cell division;
KW Cytoplasm; 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..501
FT /note="Actin nucleation-promoting factor WASL"
FT /id="PRO_0000189002"
FT DOMAIN 31..138
FT /note="WH1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00410"
FT DOMAIN 200..213
FT /note="CRIB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00057"
FT DOMAIN 401..418
FT /note="WH2 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00406"
FT DOMAIN 429..446
FT /note="WH2 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00406"
FT REGION 135..159
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 180..202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 263..405
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 442..501
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 271..390
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 442..459
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 482..501
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 239
FT /note="Phosphoserine; by TNK2"
FT /evidence="ECO:0000250|UniProtKB:O00401"
FT MOD_RES 253
FT /note="Phosphotyrosine; by FAK1 and TNK2"
FT /evidence="ECO:0000269|PubMed:14676198,
FT ECO:0007744|PubMed:22673903"
FT MOD_RES 304
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:O00401"
FT MOD_RES 480
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00401"
FT MOD_RES 481
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00401"
FT TURN 8..11
FT /evidence="ECO:0007829|PDB:1MKE"
FT STRAND 13..16
FT /evidence="ECO:0007829|PDB:1MKE"
FT STRAND 19..21
FT /evidence="ECO:0007829|PDB:2IFS"
FT STRAND 36..49
FT /evidence="ECO:0007829|PDB:1MKE"
FT TURN 50..52
FT /evidence="ECO:0007829|PDB:1MKE"
FT STRAND 53..67
FT /evidence="ECO:0007829|PDB:1MKE"
FT TURN 68..71
FT /evidence="ECO:0007829|PDB:1MKE"
FT STRAND 72..78
FT /evidence="ECO:0007829|PDB:1MKE"
FT STRAND 80..82
FT /evidence="ECO:0007829|PDB:1MKE"
FT STRAND 84..90
FT /evidence="ECO:0007829|PDB:1MKE"
FT STRAND 100..108
FT /evidence="ECO:0007829|PDB:1MKE"
FT STRAND 110..120
FT /evidence="ECO:0007829|PDB:1MKE"
FT HELIX 121..137
FT /evidence="ECO:0007829|PDB:1MKE"
SQ SEQUENCE 501 AA; 54325 MW; 480E21F26F7FC77E CRC64;
MSSGQQPPRR VTNVGSLLLT PQENESLFSF LGKKCVTMSS AVVQLYAADR NCMWSKKCSG
VACLVKDNPQ RSYFLRIFDI KDGKLLWEQE LYNNFVYNSP RGYFHTFAGD TCQVALNFAN
EEEAKKFRKA VTDLLGRRQR KSEKRRDAPN GPNLPMATVD IKNPEITTNR FYSSQVNNIS
HTKEKKKGKA KKKRLTKADI GTPSNFQHIG HVGWDPNTGF DLNNLDPELK NLFDMCGISE
AQLKDRETSK VIYDFIEKTG GVEAVKNELR RQAPPPPPPS RGGPPPPPPP PHSSGPPPPP
ARGRGAPPPP PSRAPTAAPP PPPPSRPGVV VPPPPPNRMY PPPPPALPSS APSGPPPPPP
LSMAGSTAPP PPPPPPPPPG PPPPPGLPSD GDHQVPASSG NKAALLDQIR EGAQLKKVEQ
NSRPVSCSGR DALLDQIRQG IQLKSVSDGQ ESTPPTPAPT SGIVGALMEV MQKRSKAIHS
SDEDEDDDDE EDFQDDDEWE D
