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Database: UniProt
Entry: A0A1D6IN14_MAIZE
LinkDB: A0A1D6IN14_MAIZE
Original site: A0A1D6IN14_MAIZE 
ID   A0A1D6IN14_MAIZE        Unreviewed;       307 AA.
AC   A0A1D6IN14;
DT   30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2016, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   RecName: Full=F-actin-capping protein subunit alpha {ECO:0000256|ARBA:ARBA00014038, ECO:0000256|RuleBase:RU365077};
GN   ORFNames=ZEAMMB73_Zm00001d022465 {ECO:0000313|EMBL:ONM60673.1};
OS   Zea mays (Maize).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX   NCBI_TaxID=4577 {ECO:0000313|EMBL:ONM60673.1};
RN   [1] {ECO:0000313|EMBL:ONM60673.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Seedling {ECO:0000313|EMBL:ONM60673.1};
RG   Maize Genome Sequencing Project;
RA   Ware D.;
RT   "Update maize B73 reference genome by single molecule sequencing
RT   technologies.";
RL   Submitted (DEC-2015) 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|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   EMBL; CM007650; ONM60673.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1D6IN14; -.
DR   ExpressionAtlas; A0A1D6IN14; baseline and differential.
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}.
SQ   SEQUENCE   307 AA;  34164 MW;  077CC5B0F7BE9C2F CRC64;
     MSDEGGAGEP LSDRQKREIA TCSPSDPCSN DVAWRPCADV RALLGNDAVY EAAAAEAFPE
     YNKARLVSIE LPDRSGDIII STYGEIDKNN YLDPRTAQVA TIDHMKQTCT KLRPAEDEEL
     PSAYIEEFRC ALDVELSKYV SEAYPKGACA VYCTSGKDIE GPGADFSFAA VISAAKRSPQ
     NFCNGSWCSV WTIEFNYELQ FVDIKGKIQV DAHYFEEGNV QLDTNIDRKD STRMQSPDDC
     AVSISGIIRH HESEYLSSLE ESYLNLSDAT FKDLRRKLPV TRTLFPWHNT LVFGLTRDLA
     KELALGK
//
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