GenomeNet

Database: UniProt
Entry: A0A3Q1GUZ4_9TELE
LinkDB: A0A3Q1GUZ4_9TELE
Original site: A0A3Q1GUZ4_9TELE 
ID   A0A3Q1GUZ4_9TELE        Unreviewed;       585 AA.
AC   A0A3Q1GUZ4;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 21.
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=WASF1 {ECO:0000313|Ensembl:ENSAPOP00000034601.1};
OS   Acanthochromis polyacanthus (spiny chromis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Pomacentridae; Acanthochromis.
OX   NCBI_TaxID=80966 {ECO:0000313|Ensembl:ENSAPOP00000034601.1, ECO:0000313|Proteomes:UP000257200};
RN   [1] {ECO:0000313|Ensembl:ENSAPOP00000034601.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-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: Cell junction, focal adhesion
CC       {ECO:0000256|ARBA:ARBA00004246}. Cytoplasm, cytoskeleton
CC       {ECO:0000256|ARBA:ARBA00004245, ECO:0000256|RuleBase:RU367034}. Synapse
CC       {ECO:0000256|ARBA:ARBA00034103}.
CC   -!- SIMILARITY: Belongs to the SCAR/WAVE family.
CC       {ECO:0000256|ARBA:ARBA00006993, ECO:0000256|RuleBase:RU367034}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   AlphaFoldDB; A0A3Q1GUZ4; -.
DR   STRING; 80966.ENSAPOP00000034601; -.
DR   Ensembl; ENSAPOT00000030533.1; ENSAPOP00000034601.1; ENSAPOG00000000679.1.
DR   GeneTree; ENSGT00950000182962; -.
DR   InParanoid; A0A3Q1GUZ4; -.
DR   OrthoDB; 616448at2759; -.
DR   Proteomes; UP000257200; Unplaced.
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; cd22071; WH2_WAVE-1; 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:SF8; WISKOTT-ALDRICH SYNDROME PROTEIN FAMILY MEMBER 1; 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   Cell junction {ECO:0000256|ARBA:ARBA00022949};
KW   Cytoplasm {ECO:0000256|RuleBase:RU367034};
KW   Cytoskeleton {ECO:0000256|RuleBase:RU367034};
KW   Methylation {ECO:0000256|ARBA:ARBA00022481};
KW   Reference proteome {ECO:0000313|Proteomes:UP000257200};
KW   Synapse {ECO:0000256|ARBA:ARBA00023018}.
FT   DOMAIN          523..540
FT                   /note="WH2"
FT                   /evidence="ECO:0000259|PROSITE:PS51082"
FT   REGION          229..248
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          313..519
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        232..248
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        318..334
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        338..361
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        362..431
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        458..495
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   585 AA;  65074 MW;  D7A6A7AEF556BC3D CRC64;
     MPLVKRTIEP RHLCHTVLPR NIKNELECVT NISLANVIRQ LSSLSKYAED LFGELFNEAH
     SFSFRVNSLQ ERVDRLSISV TQLDPKEEEL SLQDITMRKA FRSSTIQDQQ LFDRTSLPVP
     LQETFHTCEQ PPPLNILTPY RDDGKEGLKF YTNPSYFFDL WREKMLQDTE DKRKERRKQK
     LEMPYLVYPK SLIRALSETP PPFFTPPELQ DPRMYDQVYR YLDLPGQLKA IDRPPEPEKV
     PRAPHDRKKE WQKLALGAEL AQDIPEDKHR EANGSAGYHD NRTQLYMEHL DGPFSLAALP
     YSQMNELLNR TGDRMYSRPH DPPPPPPPMH PLGEIKPPSV ISSSSGFSDS RPQSPARTAG
     LNSNTPPPPP PPLPPPPPPL PSSGLRGTPP PPIPPLPVQQ HPPAIPPPPA PLQIAPGVLH
     PAPPPVAPPL HSSSPARLQQ VLDRGPCMGG SGTQSDGSIL PPPPPPPPLP LPGARSSSPC
     PSGPPPVPAF PSAGAMASPP PHSLHDVGPK RHHPANLPPI SDARSVLLEA IRKGIQLRKV
     EEQREQEAKH ERVGNDVATI LSRRIAVEYS DSEDESEFDE GDWME
//
DBGET integrated database retrieval system