ID A0A2K6MN27_RHIBE Unreviewed; 491 AA.
AC A0A2K6MN27;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
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:ENSRBIP00000037166.1};
OS Rhinopithecus bieti (Black snub-nosed monkey) (Pygathrix bieti).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Colobinae; Rhinopithecus.
OX NCBI_TaxID=61621 {ECO:0000313|Ensembl:ENSRBIP00000037166.1, ECO:0000313|Proteomes:UP000233180};
RN [1] {ECO:0000313|Ensembl:ENSRBIP00000037166.1, ECO:0000313|Proteomes:UP000233180}
RP NUCLEOTIDE SEQUENCE.
RA Wu, C.-I. and Zhang, Y.;
RT "Genome of Rhinopithecus bieti.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSRBIP00000037166.1}
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 AlphaFoldDB; A0A2K6MN27; -.
DR Ensembl; ENSRBIT00000061177.1; ENSRBIP00000037166.1; ENSRBIG00000042169.1.
DR GeneTree; ENSGT00950000182962; -.
DR Proteomes; UP000233180; 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: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:UP000233180}.
FT DOMAIN 429..446
FT /note="WH2"
FT /evidence="ECO:0000259|PROSITE:PS51082"
FT REGION 173..203
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 240..428
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 184..203
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 240..262
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 290..405
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 491 AA; 53870 MW; 3BA00EF75311D400 CRC64;
MPLVTRNIEP RHLCRQTLPS VRSELECVTN ITLANVIRQL GSLSKYAEDI FGELFTQANT
FASRVSSLAE RVDRLQVKVT QLDPKEEEVS LQGINTRKAF RSSTIQDQKL FDRNSLPVPV
LETYNTCDTP PPLNNLTPYR DDGKEALKFY TDPSYFFDLW KEKMLQDTKD IMKEKRKHRK
EKKDNPNRGN VNPRKIKTRK EEWEKMKMGQ EFVESKEKLG PSGYPPTLVY QNGSIGCVEN
VDASSYPPPP QSDSASSPSP SFSEDNLPPP PAEFSGYTLN NKRMDQEQCP SHPPPAPPLG
SPPGPKPGFA PPPAPPPPPP PMIGIPSPPP PVGFVSPGTP PPPSPPSFPP HPDFAAPPPP
PPPPATDYPT LPPPPLSQPT GGAPPPPPPP PPPGPPPPPF TGADGQPAVP PLLSDTTKPK
SSLPAVSDAR SDLLSAIRQG FQLRRVEEQR EQEKRDVVGN DVATILSRRI AVEYSDSEDD
SSEFDEDDWS D
//
