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Wiskott-Aldrich syndrome protein family member 1 (WASP family protein member 1) (Protein WAVE-1)

 WASF1_PONAB             Reviewed;         559 AA.
Q5NVG8;
15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
04-JAN-2005, sequence version 1.
10-MAY-2017, entry version 48.
RecName: Full=Wiskott-Aldrich syndrome protein family member 1;
Short=WASP family protein member 1;
AltName: Full=Protein WAVE-1;
Name=WASF1; Synonyms=WAVE1;
Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Pongo.
NCBI_TaxID=9601;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain cortex;
The German cDNA consortium;
Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Downstream effector molecule involved in the
transmission of signals from tyrosine kinase receptors and small
GTPases to the actin cytoskeleton. Promotes formation of actin
filaments. Part of the WAVE complex that regulates lamellipodia
formation. The WAVE complex regulates actin filament
reorganization via its interaction with the Arp2/3 complex (By
similarity). As component of the WAVE1 complex, required for BDNF-
NTRK2 endocytic trafficking and signaling from early endosomes (By
similarity). {ECO:0000250|UniProtKB:Q8R5H6,
ECO:0000250|UniProtKB:Q92558}.
-!- SUBUNIT: Component of the WAVE1 complex composed of ABI2, CYFIP1
or CYFIP2, BRK1, NCKAP1 and WASF1/WAVE1. Within the complex, a
heterodimer containing NCKAP1 and CYFIP1 interacts with a
heterotrimer formed by WAVE1, ABI2 and BRK1. CYFIP2 binds to
activated RAC1 which causes the complex to dissociate, releasing
activated WASF1. The complex can also be activated by NCK1. Binds
actin and the Arp2/3 complex. Interacts with BAIAP2. Interacts
with SHANK3; the interaction mediates the association of SHANK3
with the WAVE1 complex. Interacts with ABI1 (via N-terminus) (By
similarity). Interacts with SORBS2; this interaction greatly
enhances phosphorylation by ABL1 and dephosphorylation by PTPN12
and might mediate partial to focal adhesion sites.
{ECO:0000250|UniProtKB:Q8R5H6, ECO:0000250|UniProtKB:Q92558}.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
{ECO:0000250|UniProtKB:Q92558}. Cell junction, synapse
{ECO:0000250|UniProtKB:Q8R5H6}. Cell junction, focal adhesion
{ECO:0000250|UniProtKB:Q92558}. Note=Dot-like pattern in the
cytoplasm. Concentrated in Rac-regulated membrane-ruffling areas.
Partial translocation to focal adhesion sites might be mediated by
interaction with SORBS2 (By similarity). In neurons, colocalizes
with activated NTRK2 after BDNF addition in endocytic sites
through the association with TMEM108 (By similarity).
{ECO:0000250|UniProtKB:Q8R5H6, ECO:0000250|UniProtKB:Q92558}.
-!- DOMAIN: Binds the Arp2/3 complex through the C-terminal region and
actin through verprolin homology (VPH) domain.
{ECO:0000250|UniProtKB:Q92558}.
-!- SIMILARITY: Belongs to the SCAR/WAVE family. {ECO:0000305}.
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EMBL; CR926067; CAI29695.1; -; mRNA.
RefSeq; NP_001127108.1; NM_001133636.1.
UniGene; Pab.234; -.
GeneID; 100174148; -.
KEGG; pon:100174148; -.
CTD; 8936; -.
HOVERGEN; HBG058482; -.
InParanoid; Q5NVG8; -.
KO; K05753; -.
Proteomes; UP000001595; Unplaced.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
GO; GO:0005925; C:focal adhesion; IEA:UniProtKB-SubCell.
GO; GO:0045202; C:synapse; IEA:UniProtKB-SubCell.
GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
GO; GO:0030036; P:actin cytoskeleton organization; IEA:InterPro.
GO; GO:1990416; P:cellular response to brain-derived neurotrophic factor stimulus; ISS:UniProtKB.
GO; GO:0006898; P:receptor-mediated endocytosis; ISS:UniProtKB.
InterPro; IPR028288; SCAR/WAVE_fam.
InterPro; IPR003124; WH2_dom.
PANTHER; PTHR12902; PTHR12902; 1.
Pfam; PF02205; WH2; 1.
SMART; SM00246; WH2; 1.
PROSITE; PS51082; WH2; 1.
2: Evidence at transcript level;
Actin-binding; Cell junction; Complete proteome; Cytoplasm;
Cytoskeleton; Methylation; Phosphoprotein; Reference proteome;
Synapse.
CHAIN 1 559 Wiskott-Aldrich syndrome protein family
member 1.
/FTId=PRO_0000314290.
DOMAIN 497 514 WH2. {ECO:0000255|PROSITE-
ProRule:PRU00406}.
COMPBIAS 278 283 Poly-Pro.
COMPBIAS 322 332 Poly-Pro.
COMPBIAS 348 359 Poly-Pro.
COMPBIAS 369 374 Poly-Pro.
COMPBIAS 424 435 Poly-Pro.
MOD_RES 341 341 Asymmetric dimethylarginine; alternate.
{ECO:0000250|UniProtKB:Q8R5H6}.
MOD_RES 341 341 Omega-N-methylarginine; alternate.
{ECO:0000250|UniProtKB:Q8R5H6}.
MOD_RES 489 489 Phosphoserine.
{ECO:0000250|UniProtKB:Q92558}.
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


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