ID   A0A1A9V626_GLOAU        Unreviewed;       286 AA.
AC   A0A1A9V626;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=F-actin-capping protein subunit alpha {ECO:0000256|ARBA:ARBA00014038, ECO:0000256|RuleBase:RU365077};
OS   Glossina austeni (Savannah tsetse fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Hippoboscoidea;
OC   Glossinidae; Glossina.
OX   NCBI_TaxID=7395 {ECO:0000313|EnsemblMetazoa:GAUT027157-PA, ECO:0000313|Proteomes:UP000078200};
RN   [1] {ECO:0000313|Proteomes:UP000078200}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TTRI {ECO:0000313|Proteomes:UP000078200};
RA   Aksoy S., Warren W., Wilson R.K.;
RL   Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblMetazoa:GAUT027157-PA}
RP   IDENTIFICATION.
RC   STRAIN=TTRI {ECO:0000313|EnsemblMetazoa:GAUT027157-PA};
RG   EnsemblMetazoa;
RL   Submitted (MAY-2020) to UniProtKB.
CC   -!- FUNCTION: F-actin-capping proteins bind in a Ca(2+)-independent manner
CC       to the fast growing ends of actin filaments (barbed end) thereby
CC       blocking the exchange of subunits at these ends. Unlike other capping
CC       proteins (such as gelsolin and severin), these proteins do not sever
CC       actin filaments. {ECO:0000256|RuleBase:RU365077}.
CC   -!- SUBUNIT: Heterodimer of an alpha and a beta subunit.
CC       {ECO:0000256|ARBA:ARBA00011355, ECO:0000256|RuleBase:RU365077}.
CC   -!- SIMILARITY: Belongs to the F-actin-capping protein alpha subunit
CC       family. {ECO:0000256|ARBA:ARBA00010479, ECO:0000256|RuleBase:RU365077}.
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DR   AlphaFoldDB; A0A1A9V626; -.
DR   STRING; 7395.A0A1A9V626; -.
DR   EnsemblMetazoa; GAUT027157-RA; GAUT027157-PA; GAUT027157.
DR   VEuPathDB; VectorBase:GAUT027157; -.
DR   OrthoDB; 179910at2759; -.
DR   Proteomes; UP000078200; Unassembled WGS sequence.
DR   GO; GO:0008290; C:F-actin capping protein complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   GO; GO:0051016; P:barbed-end actin filament capping; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.1140.60; F-actin capping protein, alpha subunit; 1.
DR   Gene3D; 3.90.1150.210; F-actin capping protein, beta subunit; 1.
DR   InterPro; IPR002189; CapZ_alpha.
DR   InterPro; IPR037282; CapZ_alpha/beta.
DR   InterPro; IPR042276; CapZ_alpha/beta_2.
DR   InterPro; IPR042489; CapZ_alpha_1.
DR   InterPro; IPR017865; F-actin_cap_asu_CS.
DR   PANTHER; PTHR10653; F-ACTIN-CAPPING PROTEIN SUBUNIT ALPHA; 1.
DR   PANTHER; PTHR10653:SF0; F-ACTIN-CAPPING PROTEIN SUBUNIT ALPHA; 1.
DR   Pfam; PF01267; F-actin_cap_A; 1.
DR   PRINTS; PR00191; FACTINCAPA.
DR   SUPFAM; SSF90096; Subunits of heterodimeric actin filament capping protein Capz; 1.
DR   PROSITE; PS00748; F_ACTIN_CAPPING_A_1; 1.
DR   PROSITE; PS00749; F_ACTIN_CAPPING_A_2; 1.
PE   3: Inferred from homology;
KW   Actin capping {ECO:0000256|RuleBase:RU365077};
KW   Actin-binding {ECO:0000256|ARBA:ARBA00023203,
KW   ECO:0000256|RuleBase:RU365077}; Coiled coil {ECO:0000256|SAM:Coils}.
FT   COILED          218..245
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   286 AA;  32950 MW;  11B92B03A11E9A75 CRC64;
     MEQTQISDAE KVRIVSDFIL HAPPGEFNEV FNDVRELLKN DALLKEGANH AFAQYNKDQL
     TPVRIEGTEH NAVISEYNDL GGGRFYDPRT KQSFKYDHLR KEASDYQDVE PDAIAESWRQ
     ALDIEALAYT ASHYRHGVCS VFGKSQNGQI VLTVCIEDHQ FQPKNYWNGR WRSQWHVSFQ
     AGTSNAELKG VLKVQVHYYE DGNVQLVSSK ECRESVVLTS EQQMAKEVVR LIEESENEYQ
     LAISENYQTM SDTTFKAMRR QLPITRTKID WTKIVSYSIG KELKTQ
//