ID A0A091IEX0_CALAN Unreviewed; 419 AA.
AC A0A091IEX0;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 03-MAY-2023, entry version 24.
DE RecName: Full=Wiskott-Aldrich syndrome protein family member {ECO:0000256|RuleBase:RU367034};
DE Short=WASP family protein member {ECO:0000256|RuleBase:RU367034};
DE Flags: Fragment;
GN ORFNames=N300_05816 {ECO:0000313|EMBL:KFP06807.1};
OS Calypte anna (Anna's hummingbird) (Archilochus anna).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Caprimulgimorphae; Apodiformes;
OC Trochilidae; Calypte.
OX NCBI_TaxID=9244 {ECO:0000313|EMBL:KFP06807.1, ECO:0000313|Proteomes:UP000054308};
RN [1] {ECO:0000313|EMBL:KFP06807.1, ECO:0000313|Proteomes:UP000054308}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N300 {ECO:0000313|EMBL:KFP06807.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-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; KL218597; KFP06807.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091IEX0; -.
DR STRING; 9244.A0A091IEX0; -.
DR Proteomes; UP000054308; 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 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:UP000054308}.
FT DOMAIN 357..374
FT /note="WH2"
FT /evidence="ECO:0000259|PROSITE:PS51082"
FT REGION 177..359
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 188..222
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 231..251
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 254..279
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 283..300
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 301..343
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFP06807.1"
FT NON_TER 419
FT /evidence="ECO:0000313|EMBL:KFP06807.1"
SQ SEQUENCE 419 AA; 46558 MW; 3A0D990A80BD2B5D CRC64;
SRSTMPLVTR NIEPRHLCRQ TLPSVPSELE CMTNITLANV IRQLGSLSKF AEDIFGELFT
QAKTFASRVS VLVERVDRLQ VKVTQLDPKE EEVSLQGINT RKAFKSSTTQ DQKLFDRDSL
PVPVLETYKT CNTPPPLNIL SPYRDDGKEA LKFYTDPSYF FDLWKEKMLQ DTKDIMKEKR
KHRKEKKENP NRGNVNPRKI KTRKEEWEKL KMGQEFVESK DKHGPGGYPS NMVYQNGSIG
SNESMDGNCY PPPPQTDSIV PPPPSFPDDS LPPPPVEFSY PVDNQRGSGS GGTKRSSLVS
PSHPPPAPPI GSPSAARPAP GPPPLSSGGL DGAPPPPPPS DTSTSKPKSS LPAVSDARSD
LLSAIRQGFQ LRKVEEQREQ EKRDVVGNDV ATILSRRIAV EYSDSEDDSS EFDEDEWSD
//
