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Database: UniProt
Entry: A0A3M0KJA6_HIRRU
LinkDB: A0A3M0KJA6_HIRRU
Original site: A0A3M0KJA6_HIRRU 
ID   A0A3M0KJA6_HIRRU        Unreviewed;       679 AA.
AC   A0A3M0KJA6;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 14.
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=DUI87_10656 {ECO:0000313|EMBL:RMC13125.1};
OS   Hirundo rustica rustica.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Passeriformes; Sylvioidea; Hirundinidae;
OC   Hirundo.
OX   NCBI_TaxID=333673 {ECO:0000313|EMBL:RMC13125.1, ECO:0000313|Proteomes:UP000269221};
RN   [1] {ECO:0000313|EMBL:RMC13125.1, ECO:0000313|Proteomes:UP000269221}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Chelidonia {ECO:0000313|EMBL:RMC13125.1};
RC   TISSUE=Blood {ECO:0000313|EMBL:RMC13125.1};
RA   Formenti G., Chiara M., Poveda L., Francoijs K.-J., Bonisoli-Alquati A.,
RA   Canova L., Gianfranceschi L., Horner D.S., Saino N.;
RT   "A high quality draft genome assembly of the barn swallow (H. rustica
RT   rustica).";
RL   Submitted (JUL-2018) 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: 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   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RMC13125.1}.
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DR   EMBL; QRBI01000106; RMC13125.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3M0KJA6; -.
DR   STRING; 333673.A0A3M0KJA6; -.
DR   Proteomes; UP000269221; 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; cd22071; WH2_WAVE-1; 1.
DR   Gene3D; 1.20.5.340; -; 2.
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   PRINTS; PR01217; PRICHEXTENSN.
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:UP000269221};
KW   Synapse {ECO:0000256|ARBA:ARBA00023018}.
FT   DOMAIN          617..634
FT                   /note="WH2"
FT                   /evidence="ECO:0000259|PROSITE:PS51082"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          287..319
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          392..610
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        420..434
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        435..452
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        464..516
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        536..559
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        570..607
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   679 AA;  75449 MW;  C28D6B58F48C33F7 CRC64;
     MGNAAVQRRS QGETPQPPSS YPAALLGSQE VQLQLGRNRQ DFLVVATNRK EYEVRSGQIT
     SRFAGPLIHF RMPLVKRNID PRHLCHTALP RGIKNELECV TNISLANIIR QLSSLTVAMW
     HCFVSIPNGH ERMSKRSLQQ EWKLCFILRI YLMLRTLINE LSKYAEDIFG ELFNEAHSFS
     FRVNSLQERV DRLSVSVTQL DPKEEELSLQ DITMRKAFRS STIQDQQLFD RKTLPIPLQE
     TYDICEQPPP LNILTPYRDD GKEGLKFYTN PSYFFDLWKE KMLQDTEDKR KEKRKQKQKN
     LDRPHEPEKV PRAPHDRRRE WQKLAQGPEL AEDDANLLHK HIEVANGPAS HFESRSQAYV
     DHIDGSYSLS ALPYSQMSEL LNRAEERVLV RPHEPPPPPP MHGAAEVKPV PPGVSSAPGL
     VENRPQSPAT GRTPVFVSPT PPPPPPPPLP SALSTSSLRA AMTSTPPPPV PPPPPPPTAA
     LQAPAVPPPP APLQIAPGVL HPAPPPVAPP LAQPSPPVTR AAQVCEAVPV HPVPPQAEAQ
     GLPPPPPPPP LPPPGIRPSS PVTVANISHP PPVLHPPPTT IVPSPHAPIM PPSPPSQVIP
     APEPKRHPST LPVISDARSV LLEAIRKGIQ LRKVEEQREQ EAKHERIEND VATILSRRIA
     VEYSDSEDDS EFDEVDWLE
//
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