WASF1_RAT
ID WASF1_RAT Reviewed; 559 AA.
AC Q5BJU7;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Actin-binding protein WASF1 {ECO:0000305};
DE AltName: Full=Protein WAVE-1;
DE AltName: Full=Wiskott-Aldrich syndrome protein family member 1;
DE Short=WASP family protein member 1;
GN Name=Wasf1; Synonyms=Wave1;
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 [LARGE SCALE MRNA].
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 [2]
RP INTERACTION WITH ABI1, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=17304222; DOI=10.1038/sj.emboj.7601569;
RA Proepper C., Johannsen S., Liebau S., Dahl J., Vaida B., Bockmann J.,
RA Kreutz M.R., Gundelfinger E.D., Boeckers T.M.;
RT "Abelson interacting protein 1 (Abi-1) is essential for dendrite
RT morphogenesis and synapse formation.";
RL EMBO J. 26:1397-1409(2007).
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). As component of the WAVE1 complex,
CC required for BDNF-NTRK2 endocytic trafficking and signaling from early
CC endosomes (By similarity). Also involved in the regulation of
CC mitochondrial dynamics (By similarity). {ECO:0000250|UniProtKB:Q8R5H6,
CC ECO:0000250|UniProtKB:Q92558}.
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 (By similarity).
CC {ECO:0000250|UniProtKB:Q92558, ECO:0000269|PubMed:17304222}.
CC -!- INTERACTION:
CC Q5BJU7; P60711: Actb; NbExp=2; IntAct=EBI-7269229, EBI-349272;
CC Q5BJU7; P08753: Gnai3; NbExp=2; IntAct=EBI-7269229, EBI-874897;
CC Q5BJU7; P54311: Gnb1; NbExp=2; IntAct=EBI-7269229, EBI-917779;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:Q92558}. Synapse {ECO:0000269|PubMed:17304222}.
CC Cell junction, focal adhesion {ECO:0000250|UniProtKB:Q92558}. Note=Dot-
CC like pattern in the cytoplasm. Concentrated in Rac-regulated membrane-
CC ruffling areas. Partial translocation to focal adhesion sites might be
CC mediated by interaction with SORBS2. In neurons, colocalizes with
CC activated NTRK2 after BDNF addition in endocytic sites through the
CC association with TMEM108 (By similarity).
CC {ECO:0000250|UniProtKB:Q8R5H6, ECO:0000250|UniProtKB:Q92558}.
CC -!- TISSUE SPECIFICITY: Expressed in hippocampal neurons (at protein
CC level). {ECO:0000269|PubMed:17304222}.
CC -!- DOMAIN: Binds the Arp2/3 complex through the C-terminal region and
CC actin through verprolin homology (VPH) domain.
CC {ECO:0000250|UniProtKB:Q92558}.
CC -!- SIMILARITY: Belongs to the SCAR/WAVE family. {ECO:0000305}.
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DR EMBL; BC091322; AAH91322.1; -; mRNA.
DR RefSeq; NP_001020285.1; NM_001025114.1.
DR RefSeq; XP_006256648.1; XM_006256586.3.
DR AlphaFoldDB; Q5BJU7; -.
DR SMR; Q5BJU7; -.
DR BioGRID; 254741; 4.
DR DIP; DIP-42570N; -.
DR IntAct; Q5BJU7; 8.
DR MINT; Q5BJU7; -.
DR STRING; 10116.ENSRNOP00000064342; -.
DR iPTMnet; Q5BJU7; -.
DR PhosphoSitePlus; Q5BJU7; -.
DR jPOST; Q5BJU7; -.
DR PaxDb; Q5BJU7; -.
DR PRIDE; Q5BJU7; -.
DR ABCD; Q5BJU7; 1 sequenced antibody.
DR GeneID; 294568; -.
DR KEGG; rno:294568; -.
DR CTD; 8936; -.
DR RGD; 1561954; Wasf1.
DR VEuPathDB; HostDB:ENSRNOG00000047476; -.
DR eggNOG; KOG1830; Eukaryota.
DR HOGENOM; CLU_036022_2_0_1; -.
DR InParanoid; Q5BJU7; -.
DR OMA; DHIDGSY; -.
DR OrthoDB; 1183697at2759; -.
DR PhylomeDB; Q5BJU7; -.
DR Reactome; R-RNO-2029482; Regulation of actin dynamics for phagocytic cup formation.
DR Reactome; R-RNO-4420097; VEGFA-VEGFR2 Pathway.
DR Reactome; R-RNO-5663213; RHO GTPases Activate WASPs and WAVEs.
DR Reactome; R-RNO-9013149; RAC1 GTPase cycle.
DR Reactome; R-RNO-9013423; RAC3 GTPase cycle.
DR PRO; PR:Q5BJU7; -.
DR Proteomes; UP000002494; Chromosome 20.
DR Bgee; ENSRNOG00000047476; Expressed in frontal cortex and 15 other tissues.
DR Genevisible; Q5BJU7; RN.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
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; ISO:RGD.
DR GO; GO:0005741; C:mitochondrial outer membrane; ISO:RGD.
DR GO; GO:0005739; C:mitochondrion; ISO:RGD.
DR GO; GO:0098794; C:postsynapse; ISO:RGD.
DR GO; GO:0032991; C:protein-containing complex; ISO:RGD.
DR GO; GO:0031209; C:SCAR complex; ISO:RGD.
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:RGD.
DR GO; GO:0034237; F:protein kinase A regulatory subunit binding; IBA:GO_Central.
DR GO; GO:0031267; F:small GTPase binding; IEA:Ensembl.
DR GO; GO:0030036; P:actin cytoskeleton organization; ISS:UniProtKB.
DR GO; GO:1990416; P:cellular response to brain-derived neurotrophic factor stimulus; ISS:UniProtKB.
DR GO; GO:0097484; P:dendrite extension; ISO:RGD.
DR GO; GO:0098939; P:dendritic transport of mitochondrion; IDA:SynGO.
DR GO; GO:0072673; P:lamellipodium morphogenesis; ISS:UniProtKB.
DR GO; GO:0070584; P:mitochondrion morphogenesis; ISS:UniProtKB.
DR GO; GO:0098885; P:modification of postsynaptic actin cytoskeleton; ISO:RGD.
DR GO; GO:0031175; P:neuron projection development; ISO:RGD.
DR GO; GO:2000601; P:positive regulation of Arp2/3 complex-mediated actin nucleation; ISO:RGD.
DR GO; GO:0051388; P:positive regulation of neurotrophin TRK receptor signaling pathway; ISO:RGD.
DR GO; GO:0016601; P:Rac protein signal transduction; ISO:RGD.
DR GO; GO:0006898; P:receptor-mediated endocytosis; ISS: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; Cell junction; Cytoplasm; Cytoskeleton; Methylation;
KW Phosphoprotein; Reference proteome; Synapse.
FT CHAIN 1..559
FT /note="Actin-binding protein WASF1"
FT /id="PRO_0000314291"
FT DOMAIN 497..514
FT /note="WH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00406"
FT REGION 169..202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 307..400
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 412..492
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 454..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:0000250|UniProtKB:Q92558"
SQ SEQUENCE 559 AA; 61515 MW; 5682117C6281D401 CRC64;
MPLVKRNIDP RHLCHTALPR GIKNELECVT NISLANIIRQ LSSLSKYAED IFGELFNEAH
SFSFRVNSLQ ERVDRLSVSV TQLDPKEEEL SLQDITMRKA FRSSTIQDQQ LFDRKTLPIP
LQETYDVCEQ PPPLNVLTPY RDDGKEGLKF YTNPSYFFDL WKEKMLQDTE DKRKEKRKQK
QKNLDRPHEP EKVPRAPHDR RREWQKLAQG PELAEDDADL LHKHIEVANG PASHFETRPQ
TYVDHMDGSY SLSALPFSQM SELLSRAEER VLVRPHEPPP PPPMHAAGDA RPTPTCVSSA
AGLIENRPQS PAAGRTPVFV SPTPPPPPPP LPSALSTSSL RASMTSTPPP PVPPPPPPPA
PALQAPAVPP PPAPLQIAPG VLHPAPPPIA PPLVQPSPPV ARAAPVCETV PVHPLPQGEV
QGLPPPPPPP PLPPPGIRPS SPVTVAALAH PPSGLHPTPS PAPGPHAPLM PPSPPSQVLP
ASEPKRHPST LPVISDARSV LLEAIRKGIQ LRKVEEQREQ EAKHERIEND VATILSRRIA
VEYSDSEDDS EFDEVDWLE
