ID   CAPZB_CANGA             Reviewed;         270 AA.
AC   Q6FQL7;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 96.
DE   RecName: Full=F-actin-capping protein subunit beta;
GN   Name=CAP2; OrderedLocusNames=CAGL0I05214g;
OS   Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS   Y-65) (Yeast) (Torulopsis glabrata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC   Nakaseomyces/Candida clade.
OX   NCBI_TaxID=284593;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
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; CR380955; CAG60414.1; -; Genomic_DNA.
DR   RefSeq; XP_447477.1; XM_447477.1.
DR   AlphaFoldDB; Q6FQL7; -.
DR   SMR; Q6FQL7; -.
DR   STRING; 5478.XP_447477.1; -.
DR   PRIDE; Q6FQL7; -.
DR   EnsemblFungi; CAG60414; CAG60414; CAGL0I05214g.
DR   GeneID; 2889199; -.
DR   KEGG; cgr:CAGL0I05214g; -.
DR   CGD; CAL0130003; CAP2.
DR   VEuPathDB; FungiDB:CAGL0I05214g; -.
DR   eggNOG; KOG3174; Eukaryota.
DR   HOGENOM; CLU_045864_1_1_1; -.
DR   InParanoid; Q6FQL7; -.
DR   OMA; MIEDMEI; -.
DR   Proteomes; UP000002428; Chromosome I.
DR   GO; GO:0099079; C:actin body; IEA:EnsemblFungi.
DR   GO; GO:0030479; C:actin cortical patch; IEA:EnsemblFungi.
DR   GO; GO:0005934; C:cellular bud tip; IEA:EnsemblFungi.
DR   GO; GO:0008290; C:F-actin capping protein complex; IEA:EnsemblFungi.
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; IEA:EnsemblFungi.
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; IEA:EnsemblFungi.
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..270
FT                   /note="F-actin-capping protein subunit beta"
FT                   /id="PRO_0000256837"
FT   REGION          245..270
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        248..270
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   270 AA;  30953 MW;  7A8B59C40362196F CRC64;
     MDEKYDAALD LLRRLNPNNL TENLQRIIGL EPELAEDLLS SIDVPLKVQQ DSKQSGRPFL
     CCDYNRDVDS YRSPWSNEYF PELSAEDLQE SPFPSESLRS LEVLANDSFD VYRDLYYEGG
     ISSVYLWDLD EEGEFAGVVL FKKEGSNKES WDSIHVIEAT KGNDDETFTY RLTSTIILAL
     DNKQNDTSLA GNLTRQTEKE AKIDTSNTDI SHITNLGTLI EDIESQLRTQ LEIVYFEKTR
     DIFHQTRSQK STTDSQEQQQ KEVIKGLQNL