ID   ACT_KLULA               Reviewed;         375 AA.
AC   P17128; Q6CRZ0;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2004, sequence version 2.
DT   03-AUG-2022, entry version 126.
DE   RecName: Full=Actin;
GN   Name=ACT; OrderedLocusNames=KLLA0D05357g;
OS   Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS   NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX   NCBI_TaxID=284590;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2664472; DOI=10.1128/mcb.9.5.2208-2213.1989;
RA   Deshler J.O., Larson G.P., Rossi J.J.;
RT   "Kluyveromyces lactis maintains Saccharomyces cerevisiae intron-encoded
RT   splicing signals.";
RL   Mol. Cell. Biol. 9:2208-2213(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
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: 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; M25826; AAA35251.1; -; Genomic_DNA.
DR   EMBL; CR382124; CAH00395.1; -; Genomic_DNA.
DR   PIR; A32798; A32798.
DR   RefSeq; XP_453299.1; XM_453299.1.
DR   AlphaFoldDB; P17128; -.
DR   SMR; P17128; -.
DR   STRING; 28985.XP_453299.1; -.
DR   PRIDE; P17128; -.
DR   EnsemblFungi; CAH00395; CAH00395; KLLA0_D05357g.
DR   GeneID; 2893427; -.
DR   KEGG; kla:KLLA0_D05357g; -.
DR   eggNOG; KOG0676; Eukaryota.
DR   HOGENOM; CLU_027965_0_2_1; -.
DR   InParanoid; P17128; -.
DR   OMA; FHTTAER; -.
DR   Proteomes; UP000000598; Chromosome D.
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: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   ATP-binding; Cytoplasm; Cytoskeleton; Nucleotide-binding;
KW   Reference proteome.
FT   CHAIN           1..375
FT                   /note="Actin"
FT                   /id="PRO_0000088951"
FT   CONFLICT        109
FT                   /note="P -> S (in Ref. 1; AAA35251)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   375 AA;  41659 MW;  8923AF184F9D9DDD CRC64;
     MDSEVAALVI DNGSGMCKAG FAGDDAPRAV FPSIVGRPRH QGIMVGMGQK DSYVGDEAQS
     KRGILTLRYP IEHGIVTNWD DMEKIWHHTF YNELRVAPEE HPVLLTEAPM NPKNNREKMT
     QILFETFNVP AFYVSIQAVL SLYSSGRTTG IVLDSGDGVT HVVPIYAGFS LPHAILRIDL
     AGRDITDYLM KILAERGYSF STTAEREIVR DIKEKLCYVA LDFEQEMQTA SQSSAVEKSY
     ELPDGQVITI GNERFRAPEA LFHPSVLSLE AAGIDQTTYN SIMKCDVDVR KELYGNIVMS
     GGTTMFPGIA ERMQKEITAL APSSMKVKII APPERKYSVW IGGSILASLT TFQQMWISKQ
     EYDESGPSIV HLKCF