WASF1_BOVIN
ID WASF1_BOVIN Reviewed; 559 AA.
AC Q0IIJ3;
DT 06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 96.
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 {ECO:0000312|EMBL:AAI22613.1};
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] {ECO:0000312|EMBL:AAI22613.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford {ECO:0000312|EMBL:AAI22613.1};
RC TISSUE=Basal ganglia {ECO:0000312|EMBL:AAI22613.1};
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000305}
RP COMPONENT OF WAVE1 COMPLEX.
RX PubMed=12181570; DOI=10.1038/nature00859;
RA Eden S., Rohatgi R., Podtelejnikov A.V., Mann M., Kirschner M.W.;
RT "Mechanism of regulation of WAVE1-induced actin nucleation by Rac1 and
RT Nck.";
RL Nature 418:790-793(2002).
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) (By similarity). Interacts with SORBS2; this interaction
CC greatly enhances phosphorylation by ABL1 and dephosphorylation by
CC PTPN12 and might mediate partial to focal adhesion sites (By
CC similarity). {ECO:0000250|UniProtKB:Q8R5H6,
CC ECO:0000250|UniProtKB:Q92558}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:Q92558}. Synapse {ECO:0000250|UniProtKB:Q8R5H6}.
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 (By similarity). In neurons,
CC colocalizes with activated NTRK2 after BDNF addition in endocytic sites
CC through the association with TMEM108 (By similarity).
CC {ECO:0000250|UniProtKB:Q8R5H6, ECO:0000250|UniProtKB:Q92558}.
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; BC122612; AAI22613.1; -; mRNA.
DR RefSeq; NP_001029189.2; NM_001034017.3.
DR AlphaFoldDB; Q0IIJ3; -.
DR SMR; Q0IIJ3; -.
DR CORUM; Q0IIJ3; -.
DR IntAct; Q0IIJ3; 3.
DR STRING; 9913.ENSBTAP00000022116; -.
DR PaxDb; Q0IIJ3; -.
DR PRIDE; Q0IIJ3; -.
DR Ensembl; ENSBTAT00000022116; ENSBTAP00000022116; ENSBTAG00000016627.
DR GeneID; 531488; -.
DR KEGG; bta:531488; -.
DR CTD; 8936; -.
DR VEuPathDB; HostDB:ENSBTAG00000016627; -.
DR VGNC; VGNC:36865; WASF1.
DR eggNOG; KOG1830; Eukaryota.
DR GeneTree; ENSGT00950000182962; -.
DR HOGENOM; CLU_036022_2_0_1; -.
DR InParanoid; Q0IIJ3; -.
DR OMA; DHIDGSY; -.
DR OrthoDB; 1183697at2759; -.
DR TreeFam; TF315031; -.
DR Proteomes; UP000009136; Chromosome 9.
DR Bgee; ENSBTAG00000016627; Expressed in occipital lobe and 91 other tissues.
DR ExpressionAtlas; Q0IIJ3; baseline and differential.
DR GO; GO:0005938; C:cell cortex; IDA:AgBase.
DR GO; GO:0032154; C:cleavage furrow; IDA:AgBase.
DR GO; GO:0005737; C:cytoplasm; IDA:AgBase.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005925; C:focal adhesion; IEA:UniProtKB-SubCell.
DR GO; GO:0030027; C:lamellipodium; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:AgBase.
DR GO; GO:0045120; C:pronucleus; IDA:AgBase.
DR GO; GO:0031209; C:SCAR complex; IBA:GO_Central.
DR GO; GO:0045202; C:synapse; IEA:UniProtKB-SubCell.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0071933; F:Arp2/3 complex binding; IPI:AgBase.
DR GO; GO:0034237; F:protein kinase A regulatory subunit binding; IDA:AgBase.
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:0072673; P:lamellipodium morphogenesis; ISS:UniProtKB.
DR GO; GO:0070584; P:mitochondrion morphogenesis; ISS:UniProtKB.
DR GO; GO:2000601; P:positive regulation of Arp2/3 complex-mediated actin nucleation; IMP:CAFA.
DR GO; GO:0035046; P:pronuclear migration; IMP:AgBase.
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 2: Evidence at transcript 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_0000279721"
FT DOMAIN 497..514
FT /note="WH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00406"
FT REGION 170..202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 304..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 456..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; 61640 MW; E1CE0954B42C9C79 CRC64;
MPLVKRNIDP RHLCHTALPR GIKNELECVT NISLANIIRQ LSSLSKYAED IFGELFNEAH
SFSFRVNSLQ ERVDRLSVSV TQLDPKEEEL SLQDITMRKA FRSSTIQDQQ LFDRKTLPIP
LQETYDVCEQ PPPLNILTPY RDDGKEGLKF YTNPSYFFDL WKEKMLQDTE DKRKEKRKQK
QKNLDRPHEP EKVPRAPHDR RREWQKLAQG PELAEDDANL LHKHIEVANG PASHFETRPQ
TYVDHMDGSY SLSALPFSQM SELLTRAEER VLVRPHEPPP PPPMHGAGDA KPIPTCISSA
TGLIENRPQS PATGRTPVFV SPTPPPPPPP LPSALSTSSL RASMTSTPPP PVPPPPPPPT
TALQAPAVPP PPAPLQIAPG VLHPAPPPIA PPLVQPSPPV ARAAPVCETV PVHPLPQGEV
QGLPPPPPPP PLPPPGIRPS SPVTVAALAH PPSGLHPTPS TAPGPHVPLM PPSPPSQVTP
ASEPKRHPST LPVISDARSV LLEAIRKGIQ LRKVEEQREQ EAKHERIEND VATILSRRIA
VEYSDSEDDS EFDEVDWLE
