ID A0A099Z1B1_TINGU Unreviewed; 500 AA.
AC A0A099Z1B1;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 03-MAY-2023, 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 ORFNames=N309_09807 {ECO:0000313|EMBL:KGL75491.1};
OS Tinamus guttatus (White-throated tinamou).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Palaeognathae; Tinamiformes; Tinamidae; Tinamus.
OX NCBI_TaxID=94827 {ECO:0000313|EMBL:KGL75491.1, ECO:0000313|Proteomes:UP000053641};
RN [1] {ECO:0000313|EMBL:KGL75491.1, ECO:0000313|Proteomes:UP000053641}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N309 {ECO:0000313|EMBL:KGL75491.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
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; KL887975; KGL75491.1; -; Genomic_DNA.
DR RefSeq; XP_010210337.1; XM_010212035.1.
DR AlphaFoldDB; A0A099Z1B1; -.
DR STRING; 94827.A0A099Z1B1; -.
DR GeneID; 104565342; -.
DR KEGG; tgt:104565342; -.
DR CTD; 10810; -.
DR OrthoDB; 616448at2759; -.
DR Proteomes; UP000053641; Unassembled WGS sequence.
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:SF1; WISKOTT-ALDRICH SYNDROME PROTEIN FAMILY MEMBER; 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:UP000053641}.
FT DOMAIN 438..455
FT /note="WH2"
FT /evidence="ECO:0000259|PROSITE:PS51082"
FT REGION 169..210
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 223..256
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 280..440
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 169..193
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 300..318
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 337..354
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 364..411
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 500 AA; 55095 MW; 0840978186D5A92E CRC64;
MPLVKRNIEP RHLCRGALPE GITSELECVT NSTLAAIIRQ LSSLSKHAED IFGELFNEAN
SFYIRANSLQ DRIDRLAVKV TQLDSTVEEV SLQDINMKKA FKSSTIQDQQ VVSKNSIPNP
VADIYNQSDK PPPLNILSPY RDDKKDGLKF YTDPSYFFDL WKEKMLQDTE DKRKEKRRQK
EQKRIDGTTR EVKKVRKARN RRQEWNMMAY DKELRPDNRL SQSVYHGASS EGSLSPDTRS
HASDVTDYSY PATPNHSLHQ QMALPSYGAG DGPQYVAAAQ SHEHEYRAAS STARHATLNR
PQQPPPPPPQ PPDAQHGPVP VVPAEYGMLP AQMVDYYSPA GPPPPPPPPM IPSAQTAFVS
PLQLPGPPSH PGLVPGSTYT APHPPPPGGL VVTAPPPPGP PPPPPGPPAA ASSLSSSPLH
VGAEGKRHEP AQPPISDARS DLLAAIRMGI QLKKVQEQRE QEAKREPVGN DVATILSRRI
AVEYSDSDDD SEFDENDWSD
//
