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Database: UniProt
Entry: A0A2K5UD70_MACFA
LinkDB: A0A2K5UD70_MACFA
Original site: A0A2K5UD70_MACFA 
ID   A0A2K5UD70_MACFA        Unreviewed;       499 AA.
AC   A0A2K5UD70;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=Wiskott-Aldrich syndrome protein family member {ECO:0000256|RuleBase:RU367034};
DE            Short=WASP family protein member {ECO:0000256|RuleBase:RU367034};
GN   Name=WASF3 {ECO:0000313|Ensembl:ENSMFAP00000010297.1};
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541 {ECO:0000313|Ensembl:ENSMFAP00000010297.1, ECO:0000313|Proteomes:UP000233100};
RN   [1] {ECO:0000313|Ensembl:ENSMFAP00000010297.1, ECO:0000313|Proteomes:UP000233100}
RP   NUCLEOTIDE SEQUENCE.
RA   Warren W., Wilson R.K.;
RL   Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSMFAP00000010297.1}
RP   IDENTIFICATION.
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_005585579.1; XM_005585522.2.
DR   AlphaFoldDB; A0A2K5UD70; -.
DR   SMR; A0A2K5UD70; -.
DR   Ensembl; ENSMFAT00000040038.2; ENSMFAP00000010297.1; ENSMFAG00000006706.2.
DR   VEuPathDB; HostDB:ENSMFAG00000006706; -.
DR   GeneTree; ENSGT00950000182962; -.
DR   OrthoDB; 616448at2759; -.
DR   Proteomes; UP000233100; Chromosome 17.
DR   Bgee; ENSMFAG00000006706; Expressed in cerebellum and 11 other cell types or tissues.
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   CDD; cd22073; WH2_WAVE-3; 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:SF7; WISKOTT-ALDRICH SYNDROME PROTEIN FAMILY MEMBER 3; 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:UP000233100}.
FT   DOMAIN          437..454
FT                   /note="WH2"
FT                   /evidence="ECO:0000259|PROSITE:PS51082"
FT   REGION          171..204
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          217..441
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        228..259
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        297..312
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        335..352
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        385..409
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   499 AA;  55038 MW;  ACAB44CFCB218E49 CRC64;
     MPLVKRNIEP RHLCRGALPE GITSELECVT NSTLAAIIRQ LSSLSKHAED IFGELFNEAN
     NFYIRANSLQ DRIDRLAVKV TQLDSTVEEV SLQDINMKKA FKSSTVQDQQ VVSKNSIPNP
     VADIYNQSDK PPPLNILTPY RDDKKDGLKF YTDPSYFFDL WKEKMLQDTE DKRKEKRRQK
     REKHKLNPNR NQQVNVRKVR TRKEEWERRK MGIEFMSDAR KLEQAGSTTE DRVPSGSHAS
     DVTDYSYPAT PNHSLHPQPV TPSYAAGDVP PHGPASQAAE HEYRPPSASA RHMALNRPQQ
     PPPPPPPQAP EGSQASAPMA PADYGMLPAQ IIEYYNPSGP PPPPPPPVIP SAQTAFVSPL
     QMPMQPPFPA SAGSTHATPP HPPSTGLLVT APPPPGPPPP PPGPPGPGSS LSSSPMHGPP
     VAEAKRQEPA QPPISDARSD LLAAIRMGIQ LKKVQEQREQ EAKREPVGND VATILSRRIA
     VEYSDSDDDS EFDENDWSD
//
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