CAPZB_DEBHA
ID CAPZB_DEBHA Reviewed; 297 AA.
AC Q6BXG6;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
DT 25-MAY-2022, entry version 87.
DE RecName: Full=F-actin-capping protein subunit beta;
GN Name=CAP2; OrderedLocusNames=DEHA2B03190g;
OS Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX NCBI_TaxID=284592;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
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; CR382134; CAG85094.2; -; Genomic_DNA.
DR RefSeq; XP_457103.2; XM_457103.1.
DR AlphaFoldDB; Q6BXG6; -.
DR SMR; Q6BXG6; -.
DR STRING; 4959.XP_457103.2; -.
DR PRIDE; Q6BXG6; -.
DR EnsemblFungi; CAG85094; CAG85094; DEHA2B03190g.
DR GeneID; 2913125; -.
DR KEGG; dha:DEHA2B03190g; -.
DR eggNOG; KOG3174; Eukaryota.
DR HOGENOM; CLU_045864_1_1_1; -.
DR InParanoid; Q6BXG6; -.
DR OMA; MIEDMEI; -.
DR OrthoDB; 1076134at2759; -.
DR Proteomes; UP000000599; Chromosome B.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0008290; C:F-actin capping protein complex; IEA:InterPro.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0030036; P:actin cytoskeleton organization; IEA:InterPro.
DR GO; GO:0051016; P:barbed-end actin filament capping; IEA:InterPro.
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..297
FT /note="F-actin-capping protein subunit beta"
FT /id="PRO_0000256838"
FT REGION 276..297
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 276..290
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 297 AA; 33477 MW; 40D7752ACA684193 CRC64;
MTSYDDKLDA SLDLMRRLDP KNITKNLNDI CTLIQNDGSE TSEELTQDLL SSVDVPLRTQ
KCDETGKEYL CCDYNRDGDS YRSPWSNKYF PVVAQDSDEL PPPFPSNILR ELEVKANDSF
DIYRDLYYEG AGTSSVYFWD TNEEDDEQET LDNGFAGVVL FKKETEDGSG KWDSIHVIEV
IPEASSNATY KVTSSVILDL QNKKSSSLSL AGSLTRQLEL TQSLSLDSAL NVETAHLINL
GTLIEKSEYN LRNLLQDVYF DKLRDIVMKD LRSVGDLSGK ESDDKRQSEL VKGLQSL