ACT_CANGA
ID ACT_CANGA Reviewed; 375 AA.
AC P60009; P02579; Q6FLX6; Q7Z9T8;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 25-MAY-2022, entry version 116.
DE RecName: Full=Actin;
GN Name=ACT1; OrderedLocusNames=CAGL0K12694g;
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 [GENOMIC DNA].
RC STRAIN=ATCC 90876 / B73;
RA Kurzai O., Weig M., Muhlschlegel F.;
RT "Candida glabrata ACT1.";
RL Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
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).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 43-341.
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX PubMed=12748053; DOI=10.1016/s1567-1356(03)00012-6;
RA Kurtzman C.P., Robnett C.J.;
RT "Phylogenetic relationships among yeasts of the 'Saccharomyces complex'
RT determined from multigene sequence analyses.";
RL FEMS Yeast Res. 3:417-432(2003).
CC -!- FUNCTION: Actins are highly conserved proteins that are involved in
CC various types of cell motility and are ubiquitously expressed in all
CC eukaryotic cells.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
CC -!- SIMILARITY: Belongs to the actin family. {ECO:0000305}.
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DR EMBL; AF069746; AAC25760.1; -; Genomic_DNA.
DR EMBL; CR380957; CAG61731.2; -; Genomic_DNA.
DR EMBL; AF527926; AAP57891.1; -; Genomic_DNA.
DR RefSeq; XP_448768.2; XM_448768.2.
DR AlphaFoldDB; P60009; -.
DR SMR; P60009; -.
DR STRING; 5478.XP_448768.2; -.
DR EnsemblFungi; CAG61731; CAG61731; CAGL0K12694g.
DR GeneID; 2890423; -.
DR KEGG; cgr:CAGL0K12694g; -.
DR CGD; CAL0134579; ACT1.
DR VEuPathDB; FungiDB:CAGL0K12694g; -.
DR eggNOG; KOG0676; Eukaryota.
DR HOGENOM; CLU_027965_0_2_1; -.
DR InParanoid; P60009; -.
DR OMA; FHTTAER; -.
DR Proteomes; UP000002428; Chromosome K.
DR GO; GO:0030479; C:actin cortical patch; IEA:EnsemblFungi.
DR GO; GO:0005884; C:actin filament; IEA:EnsemblFungi.
DR GO; GO:0032432; C:actin filament bundle; IEA:EnsemblFungi.
DR GO; GO:0000142; C:cellular bud neck contractile ring; IEA:EnsemblFungi.
DR GO; GO:0005829; C:cytosol; IDA:CGD.
DR GO; GO:0005576; C:extracellular region; IDA:CGD.
DR GO; GO:0062040; C:fungal biofilm matrix; IDA:CGD.
DR GO; GO:0031011; C:Ino80 complex; IEA:EnsemblFungi.
DR GO; GO:0035267; C:NuA4 histone acetyltransferase complex; IEA:EnsemblFungi.
DR GO; GO:0000812; C:Swr1 complex; IEA:EnsemblFungi.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004402; F:histone acetyltransferase activity; IEA:EnsemblFungi.
DR GO; GO:0042802; F:identical protein binding; IEA:EnsemblFungi.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; IEA:EnsemblFungi.
DR GO; GO:0030476; P:ascospore wall assembly; IEA:EnsemblFungi.
DR GO; GO:0034599; P:cellular response to oxidative stress; IEA:EnsemblFungi.
DR GO; GO:0006338; P:chromatin remodeling; IEA:EnsemblFungi.
DR GO; GO:0006281; P:DNA repair; IEA:EnsemblFungi.
DR GO; GO:0006897; P:endocytosis; IEA:EnsemblFungi.
DR GO; GO:0030010; P:establishment of cell polarity; IEA:EnsemblFungi.
DR GO; GO:1902404; P:mitotic actomyosin contractile ring contraction; IEA:EnsemblFungi.
DR GO; GO:0009306; P:protein secretion; IEA:EnsemblFungi.
DR GO; GO:0000011; P:vacuole inheritance; IEA:EnsemblFungi.
DR InterPro; IPR004000; Actin.
DR InterPro; IPR020902; Actin/actin-like_CS.
DR InterPro; IPR004001; Actin_CS.
DR InterPro; IPR043129; ATPase_NBD.
DR PANTHER; PTHR11937; PTHR11937; 1.
DR Pfam; PF00022; Actin; 1.
DR PRINTS; PR00190; ACTIN.
DR SMART; SM00268; ACTIN; 1.
DR SUPFAM; SSF53067; SSF53067; 2.
DR PROSITE; PS00406; ACTINS_1; 1.
DR PROSITE; PS00432; ACTINS_2; 1.
DR PROSITE; PS01132; ACTINS_ACT_LIKE; 1.
PE 3: Inferred from homology;
KW Acetylation; ATP-binding; Cytoplasm; Cytoskeleton; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..375
FT /note="Actin"
FT /id="PRO_0000088905"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 375 AA; 41690 MW; 87AC19B0B0BC9E71 CRC64;
MDSEVAALVI DNGSGMCKAG FAGDDAPRAV FPSIVGRPRH QGIMVGMGQK DSYVGDEAQS
KRGILTLRYP IEHGIVTNWD DMEKIWHHTF YNELRVAPEE HPVLLTEAPM NPKSNREKMT
QIMFETFNVP AFYVSIQAVL SLYSSGRTTG IVLDSGDGVT HVVPIYAGFS LPHAILRIDL
AGRDLTDYLM KILSERGYSF STTAEREIVR DIKEKLCYVA LDFEQEMQTA AQSSSIEKSY
ELPDGQVITI GNERFRAPEA LFHPSVLGLE SAGIDQTTYN SIMKCDVDVR KELYGNIVMS
GGTTMFPGIA ERMQKEITAL APSSMKVKII APPERKYSVW IGGSILASLT TFQQMWISKQ
EYDESGPSIV HHKCF
