ID B0WVY1_CULQU Unreviewed; 287 AA.
AC B0WVY1;
DT 08-APR-2008, integrated into UniProtKB/TrEMBL.
DT 08-APR-2008, sequence version 1.
DT 24-JAN-2024, entry version 75.
DE RecName: Full=F-actin-capping protein subunit alpha {ECO:0000256|RuleBase:RU365077};
GN Name=6043973 {ECO:0000313|EnsemblMetazoa:CPIJ011271-PA};
GN ORFNames=CpipJ_CPIJ011271 {ECO:0000313|EMBL:EDS35813.1};
OS Culex quinquefasciatus (Southern house mosquito) (Culex pungens).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Culicinae; Culicini; Culex; Culex.
OX NCBI_TaxID=7176;
RN [1] {ECO:0000313|EMBL:EDS35813.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JHB {ECO:0000313|EMBL:EDS35813.1};
RG The Broad Institute Genome Sequencing Platform;
RA Atkinson P.W., Hemingway J., Christensen B.M., Higgs S., Kodira C.,
RA Hannick L., Megy K., O'Leary S., Pearson M., Haas B.J., Mauceli E.,
RA Wortman J.R., Lee N.H., Guigo R., Stanke M., Alvarado L., Amedeo P.,
RA Antoine C.H., Arensburger P., Bidwell S.L., Crawford M., Camaro F.,
RA Devon K., Engels R., Hammond M., Howarth C., Koehrsen M., Lawson D.,
RA Montgomery P., Nene V., Nusbaum C., Puiu D., Romero-Severson J.,
RA Severson D.W., Shumway M., Sisk P., Stolte C., Zeng Q., Eisenstadt E.,
RA Fraser-Liggett C., Strausberg R., Galagan J., Birren B., Collins F.H.;
RT "Annotation of Culex pipiens quinquefasciatus.";
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:CPIJ011271-PA}
RP IDENTIFICATION.
RC STRAIN=JHB {ECO:0000313|EnsemblMetazoa:CPIJ011271-PA};
RG EnsemblMetazoa;
RL Submitted (FEB-2021) 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|RuleBase:RU365077}.
CC -!- SIMILARITY: Belongs to the F-actin-capping protein alpha subunit
CC family. {ECO:0000256|RuleBase:RU365077}.
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DR EMBL; DS232134; EDS35813.1; -; Genomic_DNA.
DR RefSeq; XP_001861553.1; XM_001861518.1.
DR AlphaFoldDB; B0WVY1; -.
DR STRING; 7176.B0WVY1; -.
DR EnsemblMetazoa; CPIJ011271-RA; CPIJ011271-PA; CPIJ011271.
DR KEGG; cqu:CpipJ_CPIJ011271; -.
DR VEuPathDB; VectorBase:CPIJ011271; -.
DR VEuPathDB; VectorBase:CQUJHB006101; -.
DR eggNOG; KOG0836; Eukaryota.
DR HOGENOM; CLU_970619_0_0_1; -.
DR InParanoid; B0WVY1; -.
DR OrthoDB; 179910at2759; -.
DR Proteomes; UP000002320; 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 InterPro; IPR002189; CapZ_alpha.
DR InterPro; IPR037282; CapZ_alpha/beta.
DR InterPro; IPR042489; CapZ_alpha_1.
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 SUPFAM; SSF90096; Subunits of heterodimeric actin filament capping protein Capz; 1.
PE 3: Inferred from homology;
KW Actin capping {ECO:0000256|RuleBase:RU365077};
KW Actin-binding {ECO:0000256|RuleBase:RU365077};
KW Reference proteome {ECO:0000313|Proteomes:UP000002320}.
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..37
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 287 AA; 31433 MW; 89C5379AB461595C CRC64;
MCMSNWYHCQ SPPHRSTGRR SGSKSELPST TLTEVSASKK GGEAKNDTRI LCKCQKGRGW
LSEQNRGQQQ QQHPKKMADV DDVISDQEKI RIVNDFILHA PPGEFNEVFN DVRELLNDDR
LLKDGASAAC SQYNKDQLTP VILEGSELAV LVTEFNDLVK IPSVGAAVAD WLRCSLCKRM
VLGSIPICSQ RESIGNINLE TLNMNEKSKS LESGFDPSSL GLAVGGVGAS LLDGRDDDSY
KCPIVTGSRA LWLIVISSRF YVTTSSTVQK SVEIFASHFT IVTGFSA
//