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
//