ID A0A3P9NCD1_POERE Unreviewed; 481 AA.
AC A0A3P9NCD1;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Wiskott-Aldrich syndrome protein family member {ECO:0000256|RuleBase:RU367034};
DE Short=WASP family protein member {ECO:0000256|RuleBase:RU367034};
OS Poecilia reticulata (Guppy) (Acanthophacelus reticulatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=8081 {ECO:0000313|Ensembl:ENSPREP00000007225.1, ECO:0000313|Proteomes:UP000242638};
RN [1] {ECO:0000313|Proteomes:UP000242638}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Guanapo {ECO:0000313|Proteomes:UP000242638};
RA Kuenstner A., Dreyer C.;
RT "The genomic landscape of the Guanapo guppy.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPREP00000007225.1}
RP IDENTIFICATION.
RC STRAIN=Guanapo {ECO:0000313|Ensembl:ENSPREP00000007225.1};
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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. {ECO:0000256|RuleBase:RU367034}.
CC -!- SUBUNIT: Binds actin and the Arp2/3 complex.
CC {ECO:0000256|RuleBase:RU367034}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000256|ARBA:ARBA00004245, ECO:0000256|RuleBase:RU367034}.
CC -!- SIMILARITY: Belongs to the SCAR/WAVE family.
CC {ECO:0000256|ARBA:ARBA00006993, ECO:0000256|RuleBase:RU367034}.
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DR RefSeq; XP_008420049.1; XM_008421827.2.
DR AlphaFoldDB; A0A3P9NCD1; -.
DR Ensembl; ENSPRET00000007316.1; ENSPREP00000007225.1; ENSPREG00000004977.1.
DR GeneID; 103472306; -.
DR KEGG; pret:103472306; -.
DR CTD; 10163; -.
DR GeneTree; ENSGT00950000182962; -.
DR OrthoDB; 616448at2759; -.
DR Proteomes; UP000242638; Unassembled WGS sequence.
DR Bgee; ENSPREG00000004977; Expressed in caudal fin and 1 other cell type or tissue.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-UniRule.
DR GO; GO:0030036; P:actin cytoskeleton organization; IEA:UniProtKB-UniRule.
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:SF6; WISKOTT-ALDRICH SYNDROME PROTEIN FAMILY MEMBER 2; 1.
DR Pfam; PF02205; WH2; 1.
DR SMART; SM00246; WH2; 1.
DR PROSITE; PS51082; WH2; 1.
PE 3: Inferred from homology;
KW Actin-binding {ECO:0000256|RuleBase:RU367034};
KW Cytoplasm {ECO:0000256|RuleBase:RU367034};
KW Cytoskeleton {ECO:0000256|RuleBase:RU367034};
KW Reference proteome {ECO:0000313|Proteomes:UP000242638}.
FT DOMAIN 419..436
FT /note="WH2"
FT /evidence="ECO:0000259|PROSITE:PS51082"
FT REGION 174..424
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 185..213
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 222..250
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 251..273
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 289..402
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 481 AA; 52494 MW; D8F54CFAFE7A7466 CRC64;
MPLVTRNIEP RHVSRQTIPS NIRSELECVT NISLANIIRQ LGSLSKYAED VFGELFIQAG
AFATRVNTLG ERVDRLQVKV TQLDPKEEEV SLQAITTRKA FRSSLTQDQQ LFTRPSLPVP
VQDTYTTCNP PPPLNQLSQY REDGKEALKF YTDPSYFFDL WKEKMLQDTK DIMKEKRKHR
REKKDNVNPR TLHPRKIKTR KDEWERLKMG QEFVVPKNER NPSDGLNGSI GSGEDFNSDI
LEQSTDSYHF EPGSPPPPPG PDDNLPPPPP DMEFNDGTAA QHRVSMLSPT HPPPAPPSMS
PPPNSRPNLS PPPAPPPPPP PSGFAPPPPP TGFDGSPSPP PPSFPSPPAP PPPPNMPMAP
PPPPISTGGG PPPPPPPPPP PGPPPPPSAY SAPPPPPPSG GGLASSSAPK PQPAPASDGR
SDLLQAIRQG FNLRKVEAQR EQEKSDHFGN DVAAILSRRI AVECSDSEDD SSEFDDDEWS
E
//
