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   27-MAR-2024, entry version 97.
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   GlyGen; Q5BJU7; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q5BJU7; -.
DR   PhosphoSitePlus; Q5BJU7; -.
DR   jPOST; Q5BJU7; -.
DR   PaxDb; 10116-ENSRNOP00000064342; -.
DR   ABCD; Q5BJU7; 1 sequenced antibody.
DR   Ensembl; ENSRNOT00055001154; ENSRNOP00055000909; ENSRNOG00055000677.
DR   Ensembl; ENSRNOT00060011552; ENSRNOP00060008673; ENSRNOG00060007026.
DR   Ensembl; ENSRNOT00065014075; ENSRNOP00065010513; ENSRNOG00065008820.
DR   GeneID; 294568; -.
DR   KEGG; rno:294568; -.
DR   AGR; RGD:1561954; -.
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   OrthoDB; 616448at2759; -.
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 cell types or tissues.
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: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:0007005; P:mitochondrion organization; 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   CDD; cd22071; WH2_WAVE-1; 1.
DR   Gene3D; 1.20.5.340; -; 1.
DR   Gene3D; 6.10.280.150; -; 2.
DR   InterPro; IPR028288; SCAR/WAVE_fam.
DR   InterPro; IPR003124; WH2_dom.
DR   PANTHER; PTHR12902; WASP-1; 1.
DR   PANTHER; PTHR12902:SF8; WISKOTT-ALDRICH SYNDROME PROTEIN FAMILY MEMBER 1; 1.
DR   Pfam; PF02205; WH2; 1.
DR   SMART; SM00246; WH2; 1.
DR   PROSITE; PS51082; WH2; 1.
DR   Genevisible; Q5BJU7; RN.
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
//