ID A0A3Q2CL75_CYPVA Unreviewed; 556 AA.
AC A0A3Q2CL75;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
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:ENSCVAP00000006068.1};
OS Cyprinodon variegatus (Sheepshead minnow).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Cyprinodontidae;
OC Cyprinodon.
OX NCBI_TaxID=28743 {ECO:0000313|Ensembl:ENSCVAP00000006068.1, ECO:0000313|Proteomes:UP000265020};
RN [1] {ECO:0000313|Ensembl:ENSCVAP00000006068.1}
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}.
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DR RefSeq; XP_015232267.1; XM_015376781.1.
DR AlphaFoldDB; A0A3Q2CL75; -.
DR STRING; 28743.ENSCVAP00000006068; -.
DR Ensembl; ENSCVAT00000005618.1; ENSCVAP00000006068.1; ENSCVAG00000007577.1.
DR GeneID; 107086049; -.
DR CTD; 8936; -.
DR GeneTree; ENSGT00950000182962; -.
DR OrthoDB; 616448at2759; -.
DR Proteomes; UP000265020; 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 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:UP000265020};
KW Synapse {ECO:0000256|ARBA:ARBA00023018}.
FT DOMAIN 494..511
FT /note="WH2"
FT /evidence="ECO:0000259|PROSITE:PS51082"
FT REGION 198..221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 285..476
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 204..221
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 290..306
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 310..333
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 334..403
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 429..466
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 556 AA; 61722 MW; B58BE39881D3ADDC CRC64;
MPLVKRTIEP RHLCHTVLPR NIKNELECVT NISLASVIRQ LSSLSKYAED LFGELFNEAH
SFSFRVNSLQ ERVDRLSISV TQLDPKEEEL SLQDITMRKA FRSSTIQDQQ LFDRSSLPVP
LQESLQTCEE PPPLNILTPY RDDGKEGLKF YTDPSYFFDL WREKMLQDTE DKRKERRKQK
LQDPRMYDQV YRYLDLPGQL KAIDRPPEPE KVPRQPHDRK KEWQKLALGA ELAQDIPEDK
HREPNGSTGY HDSRAALYVE QLDGPFSLGA LPYTQMNELL NRTGDRMYSR PHDPPPPPPP
GHPLGEIKPP SVISSSSGFS DSRPQSPART AGLNSSTPPP PPPPLPPPPP PLPSSGLRGT
APPPIPPLPV QHQPPAIPPP PAPLQIAPGV LHPAPPPVAP PLHSLSPARL QHVHEKGQYS
GSGTQSDGTI LPPPPPPPPL PLPGVRSSSP CPSGPPPVPA FPSAGAMASP PPHAMHDVAT
KRHYSSNLPP ISDARSVLLE AIRKGIQLRK VEEQREQEAK HERVGNDVAT ILSRRIAVEY
SDSEDESEFD EGDWME
//
