ID M3JA42_CANMX Unreviewed; 262 AA.
AC M3JA42;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=F-actin-capping protein subunit alpha {ECO:0000256|ARBA:ARBA00014038, ECO:0000256|RuleBase:RU365077};
GN ORFNames=G210_0358 {ECO:0000313|EMBL:EMG48978.1};
OS Candida maltosa (strain Xu316) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=1245528 {ECO:0000313|EMBL:EMG48978.1, ECO:0000313|Proteomes:UP000011777};
RN [1] {ECO:0000313|EMBL:EMG48978.1, ECO:0000313|Proteomes:UP000011777}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Xu316 {ECO:0000313|Proteomes:UP000011777};
RA Yu J., Wang Q., Geng X., Bao W., He P., Cai J.;
RT "Genome sequence of Candida maltosa Xu316, a potential industrial strain
RT for xylitol and ethanol production.";
RL Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
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|ARBA:ARBA00025389,
CC 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}.
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:EMG48978.1}.
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DR EMBL; AOGT01000880; EMG48978.1; -; Genomic_DNA.
DR AlphaFoldDB; M3JA42; -.
DR STRING; 1245528.M3JA42; -.
DR eggNOG; KOG0836; Eukaryota.
DR HOGENOM; CLU_045161_3_0_1; -.
DR OMA; VACIEDH; -.
DR OrthoDB; 179910at2759; -.
DR Proteomes; UP000011777; 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; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000011777}.
SQ SEQUENCE 262 AA; 29855 MW; 4DFC282345C79290 CRC64;
MSLKLTEIVD SLIESAPPVE LKEVSQSLSA LTTTSIDDNI EKFAQDKTIA IDNNNTIVSK
YNKDSQSSKY IDYVHKKLFN VDWKHGKVID IEPYHNGTTD YPAVYDELVD KLAKYGDDYY
PSTFAYTVIP ESEGLRIIII GQRANHENFY TGQWKSNYVV SERGITGDVS LDIHYFEDGN
VRLKFNESIN DEGDFVGSAS KIVNFINDQE NQIVIKIVDQ FNNLNQQSFK NLRRLLPVTR
SKINWGSAIG NYRLGSDVVY KK
//
