WASF1_PONAB
ID WASF1_PONAB Reviewed; 559 AA.
AC Q5NVG8;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 03-AUG-2022, entry version 60.
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 Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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.
CC {ECO:0000250|UniProtKB:Q8R5H6, 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; CR926067; CAI29695.1; -; mRNA.
DR RefSeq; NP_001127108.1; NM_001133636.1.
DR AlphaFoldDB; Q5NVG8; -.
DR SMR; Q5NVG8; -.
DR STRING; 9601.ENSPPYP00000018938; -.
DR GeneID; 100174148; -.
DR KEGG; pon:100174148; -.
DR CTD; 8936; -.
DR eggNOG; KOG1830; Eukaryota.
DR InParanoid; Q5NVG8; -.
DR OrthoDB; 1183697at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005925; C:focal adhesion; IEA:UniProtKB-SubCell.
DR GO; GO:0045202; C:synapse; IEA:UniProtKB-SubCell.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
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: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_0000314290"
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..383
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 412..490
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..383
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; 61666 MW; 5E0452B0BA77BC3B 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 PPPMHGAGEA KPIPTCISSA
TGLIENRPQS PATGRTPVFV SPTPPPPPPP LPSALSTSSL RASMTSTPPP PVPPPPPPPA
TALQAPAVPP PPAPLQIAPG VLHPAPPPIA PPLVQPSPPV ARAAPVCETV PVHPLPQGEV
QGLPPPPPPP PLPPPGIRPS SPVTVTALAH PPSGLHPTPS TAPGPHVPLM PPSPPSQVIP
ASEPKRHPST LPVISDARSV LLEAIRKGIQ LRKVEEQREQ EAKHERIEND VATILSRRIA
VEYSDSEDDS EFDEVDWLE
