GenomeNet

Database: UniProt
Entry: A0A452FV80_CAPHI
LinkDB: A0A452FV80_CAPHI
Original site: A0A452FV80_CAPHI 
ID   A0A452FV80_CAPHI        Unreviewed;       506 AA.
AC   A0A452FV80;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 19.
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=WASF2 {ECO:0000313|Ensembl:ENSCHIP00000028037.1};
OS   Capra hircus (Goat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Caprinae; Capra.
OX   NCBI_TaxID=9925 {ECO:0000313|Ensembl:ENSCHIP00000028037.1, ECO:0000313|Proteomes:UP000291000};
RN   [1] {ECO:0000313|Ensembl:ENSCHIP00000028037.1, ECO:0000313|Proteomes:UP000291000}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Bickhart D.M., Koren S., Rosen B., Hastie A., Liachko I., Sullivan S.T.,
RA   Burton J., Sayre B.L., Huson H.J., Lee J., Lam E., Kelley C.M.,
RA   Hutchison J.L., Zhou Y., Sun J., Crisa A., Schwartz J.C., Hammond J.A.,
RA   Schroeder S.G., Liu G.E., Dunham M., Shendure J., Sonstegard T.S.,
RA   Phillippy A.M., Van Tassell C.P., Smith T.P.;
RT   "Polished mammalian reference genomes with single-molecule sequencing and
RT   chromosome conformation capture applied to the Capra hircus genome.";
RL   Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSCHIP00000028037.1}
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   EMBL; LWLT01000002; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; A0A452FV80; -.
DR   STRING; 9925.ENSCHIP00000028037; -.
DR   Ensembl; ENSCHIT00000035906.1; ENSCHIP00000028037.1; ENSCHIG00000023712.1.
DR   GeneTree; ENSGT00950000182962; -.
DR   Proteomes; UP000291000; Chromosome 2.
DR   Bgee; ENSCHIG00000023712; Expressed in thymus and 17 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   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   PRINTS; PR01217; PRICHEXTENSN.
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:UP000291000}.
FT   DOMAIN          444..461
FT                   /note="WH2"
FT                   /evidence="ECO:0000259|PROSITE:PS51082"
FT   REGION          173..200
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          247..446
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        184..200
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        257..282
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        305..420
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   506 AA;  55187 MW;  706C896692B3FFF9 CRC64;
     MPLVTRNIEP RHLCRQTLPS VRSELECMTN ITLANVIRQL GSLSKYAEDI FGELFTQANT
     FASRVSSLAE RVDRLQVKVT QLDPKEEEVS LQGINTRKAF RSSTVQDQKL FDRNSLPIPV
     LETYNTCDTP PPLNNLTPYR DDGKEALKFY TDPSYFFDLW KEKMLQDTKD IMKEKRKHRK
     EKKDNPNRGN VNPRKIKTRK EEWEKMKMGQ EFVESKENIT QALNNNFGIG YPPTLVYQNG
     SIGSVENVDA GNYPPPPQSD SISPPSPSFS EDNLPPPPAE FSYPADGNQR GAGVAGLKRS
     SVVSPSHPPP APPLGSAPGP KPGFAPPPAP PPPPPMINTP PPPPPGGFGS PATPPPPSPP
     SFPPHPDFAA PPPPPPPPAV DYSTLPPPPL SQPTGGAPPP PPPPPPPGPP PPPFSGADGQ
     LAAPPPPLSD TTKPKSSLPP VSDARSDLLS AIRQGFQLRR VEEQREQEKR DVVGNDVATI
     LSRRIAVEYS DSEDDSSEFD EDEWSD
//
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