ID A0A093FLD3_GAVST Unreviewed; 273 AA.
AC A0A093FLD3;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=F-actin-capping protein subunit alpha {ECO:0000256|RuleBase:RU365077};
DE Flags: Fragment;
GN ORFNames=N328_07518 {ECO:0000313|EMBL:KFV57450.1};
OS Gavia stellata (Red-throated diver) (Colymbus stellatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Gaviiformes; Gaviidae; Gavia.
OX NCBI_TaxID=37040 {ECO:0000313|EMBL:KFV57450.1, ECO:0000313|Proteomes:UP000054313};
RN [1] {ECO:0000313|EMBL:KFV57450.1, ECO:0000313|Proteomes:UP000054313}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N328 {ECO:0000313|EMBL:KFV57450.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) 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|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; KK634197; KFV57450.1; -; Genomic_DNA.
DR RefSeq; XP_009814915.1; XM_009816613.1.
DR AlphaFoldDB; A0A093FLD3; -.
DR KEGG; gste:104260794; -.
DR CTD; 829; -.
DR OrthoDB; 179910at2759; -.
DR Proteomes; UP000054313; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
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:SF5; F-ACTIN-CAPPING PROTEIN SUBUNIT ALPHA-1; 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}; Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Reference proteome {ECO:0000313|Proteomes:UP000054313}.
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFV57450.1"
FT NON_TER 273
FT /evidence="ECO:0000313|EMBL:KFV57450.1"
SQ SEQUENCE 273 AA; 31407 MW; D1596BC5FF575EEA CRC64;
VRIAAKFITH APPGEFNEVF NDVRLLLNND NLLREGAAHA FAQYNMDQFT PVKIEGYDDQ
VLITEHGDLG NGRFLDPRNK LSFKFDHLRK EASDPQPEDT ESALKQWRDA CDSALRAYVK
DHYPNGFCTV YGKSIDGQQT IIACIESHQF QPKNFWNGRW RSEWKFTITP PTAQVAAVLK
IQVHYYEDGN VQLVSHKDIQ DSVQVSSDVQ TAKEFIKIIE NAENEYQTAI SENYQTMSDT
TFKALRRQLP VTRTKIDWNK ILSYKIGKEM QNA
//
