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CAPZB_YARLI
ID   CAPZB_YARLI             Reviewed;         260 AA.
AC   Q6CBA2;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 2.
DT   25-MAY-2022, entry version 92.
DE   RecName: Full=F-actin-capping protein subunit beta;
GN   Name=CAP2; OrderedLocusNames=YALI0C20735g;
OS   Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Dipodascaceae; Yarrowia.
OX   NCBI_TaxID=284591;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CLIB 122 / E 150;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
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 (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Heterodimer of an alpha and a beta subunit. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Nucleus
CC       {ECO:0000250}. Note=Septum. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the F-actin-capping protein beta subunit family.
CC       {ECO:0000305}.
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DR   EMBL; CR382129; CAG82380.2; -; Genomic_DNA.
DR   RefSeq; XP_502060.2; XM_502060.2.
DR   AlphaFoldDB; Q6CBA2; -.
DR   SMR; Q6CBA2; -.
DR   STRING; 4952.CAG82380; -.
DR   EnsemblFungi; CAG82380; CAG82380; YALI0_C20735g.
DR   GeneID; 2909862; -.
DR   KEGG; yli:YALI0C20735g; -.
DR   VEuPathDB; FungiDB:YALI0_C20735g; -.
DR   HOGENOM; CLU_045864_1_1_1; -.
DR   InParanoid; Q6CBA2; -.
DR   OMA; MIEDMEI; -.
DR   Proteomes; UP000001300; Chromosome C.
DR   GO; GO:0099079; C:actin body; IEA:EnsemblFungi.
DR   GO; GO:0030479; C:actin cortical patch; IBA:GO_Central.
DR   GO; GO:0005934; C:cellular bud tip; IEA:EnsemblFungi.
DR   GO; GO:0008290; C:F-actin capping protein complex; IBA:GO_Central.
DR   GO; GO:0000131; C:incipient cellular bud site; IEA:EnsemblFungi.
DR   GO; GO:0043332; C:mating projection tip; IEA:EnsemblFungi.
DR   GO; GO:0031097; C:medial cortex; IEA:EnsemblFungi.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR   GO; GO:0044396; P:actin cortical patch organization; IEA:EnsemblFungi.
DR   GO; GO:1904600; P:actin fusion focus assembly; IEA:EnsemblFungi.
DR   GO; GO:0051016; P:barbed-end actin filament capping; IBA:GO_Central.
DR   GO; GO:0000902; P:cell morphogenesis; IBA:GO_Central.
DR   GO; GO:0030447; P:filamentous growth; IEA:EnsemblFungi.
DR   GO; GO:1903475; P:mitotic actomyosin contractile ring assembly; IEA:EnsemblFungi.
DR   GO; GO:1902404; P:mitotic actomyosin contractile ring contraction; IEA:EnsemblFungi.
DR   GO; GO:0110055; P:negative regulation of actin filament annealing; IEA:EnsemblFungi.
DR   GO; GO:2000813; P:negative regulation of barbed-end actin filament capping; IEA:EnsemblFungi.
DR   GO; GO:0090339; P:negative regulation of formin-nucleated actin cable assembly; IEA:EnsemblFungi.
DR   GO; GO:2000601; P:positive regulation of Arp2/3 complex-mediated actin nucleation; IEA:EnsemblFungi.
DR   Gene3D; 1.20.58.570; -; 1.
DR   Gene3D; 3.90.1150.210; -; 1.
DR   InterPro; IPR037282; CapZ_alpha/beta.
DR   InterPro; IPR042276; CapZ_alpha/beta_2.
DR   InterPro; IPR001698; CAPZB.
DR   InterPro; IPR043175; CAPZB_N.
DR   InterPro; IPR019771; F-actin_capping_bsu_CS.
DR   PANTHER; PTHR10619; PTHR10619; 1.
DR   Pfam; PF01115; F_actin_cap_B; 1.
DR   PRINTS; PR00192; FACTINCAPB.
DR   SUPFAM; SSF90096; SSF90096; 1.
DR   PROSITE; PS00231; F_ACTIN_CAPPING_BETA; 1.
PE   3: Inferred from homology;
KW   Actin capping; Actin-binding; Cytoplasm; Cytoskeleton; Nucleus;
KW   Reference proteome.
FT   CHAIN           1..260
FT                   /note="F-actin-capping protein subunit beta"
FT                   /id="PRO_0000256843"
SQ   SEQUENCE   260 AA;  28749 MW;  4A36B636EE78448C CRC64;
     MSDEQYDAAL SLLRRLDPKN VSVNLNSLCK IAPELAEDLL SSVDQPLGVK TCKSTKKEYL
     TCDYNRDGDS FRSPWSGDYE PATDGPTPSA ALRKLEVLAN DSFDIYRDLY YEGGVSSVYL
     WDQGEGDNTN SFAGVVLLKK TSPSSSWDSI HVFEVETSRG EGIYRVTSTV ILDLGSKSPK
     LGLSGNLTRQ TEREMAVDEP SQHIANLGSI VEDVESKLRN QLQEVYFGKA RDIVGQVRSL
     GGVEDAKQKQ RQEEVIKGLQ
 
 
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