ID A0A1Z5KB85_FISSO Unreviewed; 253 AA.
AC A0A1Z5KB85;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 28-JUN-2023, entry version 21.
DE RecName: Full=F-actin-capping protein subunit alpha {ECO:0000256|RuleBase:RU365077};
GN ORFNames=FisN_15Lh133 {ECO:0000313|EMBL:GAX23412.1};
OS Fistulifera solaris (Oleaginous diatom).
OC Eukaryota; Sar; Stramenopiles; Ochrophyta; Bacillariophyta;
OC Bacillariophyceae; Bacillariophycidae; Naviculales; Naviculaceae;
OC Fistulifera.
OX NCBI_TaxID=1519565 {ECO:0000313|EMBL:GAX23412.1, ECO:0000313|Proteomes:UP000198406};
RN [1] {ECO:0000313|EMBL:GAX23412.1, ECO:0000313|Proteomes:UP000198406}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JPCC DA0580 {ECO:0000313|EMBL:GAX23412.1,
RC ECO:0000313|Proteomes:UP000198406};
RX PubMed=25634988; DOI=10.1105/tpc.114.135194;
RA Tanaka T., Maeda Y., Veluchamy A., Tanaka M., Abida H., Marechal E.,
RA Bowler C., Muto M., Sunaga Y., Tanaka M., Yoshino T., Taniguchi T.,
RA Fukuda Y., Nemoto M., Matsumoto M., Wong P.S., Aburatani S., Fujibuchi W.;
RT "Oil accumulation by the oleaginous diatom Fistulifera solaris as revealed
RT by the genome and transcriptome.";
RL Plant Cell 27:162-176(2015).
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}.
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:GAX23412.1}.
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DR EMBL; BDSP01000201; GAX23412.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Z5KB85; -.
DR InParanoid; A0A1Z5KB85; -.
DR OrthoDB; 179910at2759; -.
DR Proteomes; UP000198406; 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; 3.90.1150.210; 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 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|ARBA:ARBA00023203,
KW ECO:0000256|RuleBase:RU365077}; Coiled coil {ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000198406}.
FT COILED 176..226
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 253 AA; 28505 MW; 045A7164688435E8 CRC64;
MSDTDFGRDV ILSLPPMETK DMAALKGQLT KLSAFNDDFM NELNDKTCSL RIDSNENATT
PLMTAIQGTV EEYQGRFAAK DLTPRLTMQA TPNAEKEGQI TAKTYVEKLE TPNCRAGGWS
TTWNITPKTE TQVEMGGTTH VHLHYYEGGS NIQLRATRQY PERPVGTEKE AVNAIVAKLE
ARNMSYDEKI AQATAKEIAA REKDFYEQMK GACEDAEESL KKMRRILPIT KTRFQWNSAA
QKQVRLLNDR KVS
//