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Protein

Actin

Gene

ACT1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.

GO - Molecular functioni

  • ATP binding Source: WormBase
  • identical protein binding Source: IntAct
  • structural constituent of cytoskeleton Source: SGD

GO - Biological processi

  • actomyosin contractile ring contraction Source: SGD
  • ascospore wall assembly Source: SGD
  • budding cell isotropic bud growth Source: SGD
  • cellular response to oxidative stress Source: SGD
  • chronological cell aging Source: SGD
  • DNA repair Source: SGD
  • endocytosis Source: SGD
  • establishment of cell polarity Source: SGD
  • establishment of mitotic spindle orientation Source: SGD
  • exocytosis Source: SGD
  • fungal-type cell wall organization Source: SGD
  • histone acetylation Source: SGD
  • mitochondrion inheritance Source: SGD
  • protein secretion Source: SGD
  • vacuole inheritance Source: SGD
  • vesicle transport along actin filament Source: SGD

Keywordsi

LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-30423-MONOMER
ReactomeiR-SCE-2029482 Regulation of actin dynamics for phagocytic cup formation
R-SCE-5626467 RHO GTPases activate IQGAPs
R-SCE-5663213 RHO GTPases Activate WASPs and WAVEs
R-SCE-6798695 Neutrophil degranulation

Protein family/group databases

MoonDBiP60010 Predicted

Names & Taxonomyi

Protein namesi
Recommended name:
Actin
Gene namesi
Name:ACT1
Synonyms:ABY1, END7
Ordered Locus Names:YFL039C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome VI

Organism-specific databases

EuPathDBiFungiDB:YFL039C
SGDiS000001855 ACT1

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi183R → K: No effect on growth kinetics nor on actin cytoskeleton morphology. Resistant to Chivosazole F inhibition of polymerization. Increases penetrance of Latrunculin A inhibition of polymerization. No effect on Chondramide inhibition of polymerization. 1 Publication1
Mutagenesisi335R → K: No effect on growth kinetics nor on actin cytoskeleton morphology. Resistant to Chivosazole F and Latrunculin A inhibition of polymerization. No effect on Chondramide inhibition of polymerization. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000890511 – 375ActinAdd BLAST375

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineCombined sources1 Publication1
Cross-linki191Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei73Not methylated1 Publication1

Keywords - PTMi

Acetylation, Isopeptide bond, Ubl conjugation

Proteomic databases

MaxQBiP60010
PaxDbiP60010
PRIDEiP60010

2D gel databases

SWISS-2DPAGEiP60010

PTM databases

CarbonylDBiP60010
iPTMnetiP60010

Interactioni

Subunit structurei

Polymerization of globular actin (G-actin) leads to a structural filament (F-actin) in the form of a two-stranded helix (Probable). Treatments with Lantrunculin A, the microbial peptide Chondramide or the microbial metabolite Chivazole F inhibit actin polymerization (PubMed:28796488). Each actin can bind to 4 others. Interacts with YIH1 (via C-terminus); this interaction occurs in a GCN1-independent manner (PubMed:15126500, PubMed:21239490). Component of the INO80 complex. Component of the SWR1 complex. Component of the NuA4 complex.Curated3 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

  • identical protein binding Source: IntAct

Protein-protein interaction databases

BioGridi31107, 2286 interactors
ComplexPortaliCPX-2122 Swr1 chromatin remodelling complex
CPX-3155 NuA4 histone acetyltransferase complex
CPX-863 INO80 chromatin remodeling complex
DIPiDIP-310N
IntActiP60010, 238 interactors
MINTiP60010
STRINGi4932.YFL039C

Chemistry databases

BindingDBiP60010

Structurei

Secondary structure

1375
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi8 – 12Combined sources5
Beta strandi14 – 21Combined sources8
Beta strandi28 – 32Combined sources5
Beta strandi35 – 40Combined sources6
Turni45 – 47Combined sources3
Helixi56 – 60Combined sources5
Helixi62 – 64Combined sources3
Beta strandi65 – 68Combined sources4
Beta strandi70 – 72Combined sources3
Beta strandi75 – 77Combined sources3
Helixi79 – 91Combined sources13
Turni92 – 94Combined sources3
Helixi98 – 100Combined sources3
Beta strandi103 – 107Combined sources5
Helixi113 – 125Combined sources13
Beta strandi130 – 136Combined sources7
Helixi137 – 144Combined sources8
Beta strandi148 – 155Combined sources8
Beta strandi160 – 166Combined sources7
Helixi172 – 174Combined sources3
Beta strandi176 – 179Combined sources4
Helixi182 – 194Combined sources13
Turni195 – 197Combined sources3
Helixi203 – 216Combined sources14
Helixi223 – 228Combined sources6
Turni229 – 231Combined sources3
Beta strandi234 – 236Combined sources3
Beta strandi238 – 241Combined sources4
Beta strandi247 – 250Combined sources4
Helixi253 – 256Combined sources4
Helixi258 – 261Combined sources4
Helixi264 – 267Combined sources4
Helixi274 – 283Combined sources10
Helixi287 – 294Combined sources8
Beta strandi297 – 301Combined sources5
Helixi302 – 304Combined sources3
Helixi309 – 320Combined sources12
Turni333 – 336Combined sources4
Helixi338 – 348Combined sources11
Helixi350 – 354Combined sources5
Beta strandi356 – 358Combined sources3
Helixi359 – 365Combined sources7
Helixi367 – 369Combined sources3
Helixi370 – 373Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1YAGX-ray1.90A1-375[»]
1YVNX-ray2.10A1-375[»]
5Y81electron microscopy4.70G1-375[»]
ProteinModelPortaliP60010
SMRiP60010
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP60010

Family & Domainsi

Sequence similaritiesi

Belongs to the actin family.Curated

Phylogenomic databases

GeneTreeiENSGT00760000118957
HOGENOMiHOG000233340
InParanoidiP60010
KOiK05692
OMAiMERGYPF
OrthoDBiEOG092C2KFK

Family and domain databases

InterProiView protein in InterPro
IPR004000 Actin
IPR020902 Actin/actin-like_CS
IPR004001 Actin_CS
PANTHERiPTHR11937 PTHR11937, 1 hit
PfamiView protein in Pfam
PF00022 Actin, 1 hit
PRINTSiPR00190 ACTIN
SMARTiView protein in SMART
SM00268 ACTIN, 1 hit
PROSITEiView protein in PROSITE
PS00406 ACTINS_1, 1 hit
PS00432 ACTINS_2, 1 hit
PS01132 ACTINS_ACT_LIKE, 1 hit

Sequencei

Sequence statusi: Complete.

P60010-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDSEVAALVI DNGSGMCKAG FAGDDAPRAV FPSIVGRPRH QGIMVGMGQK
60 70 80 90 100
DSYVGDEAQS KRGILTLRYP IEHGIVTNWD DMEKIWHHTF YNELRVAPEE
110 120 130 140 150
HPVLLTEAPM NPKSNREKMT QIMFETFNVP AFYVSIQAVL SLYSSGRTTG
160 170 180 190 200
IVLDSGDGVT HVVPIYAGFS LPHAILRIDL AGRDLTDYLM KILSERGYSF
210 220 230 240 250
STTAEREIVR DIKEKLCYVA LDFEQEMQTA AQSSSIEKSY ELPDGQVITI
260 270 280 290 300
GNERFRAPEA LFHPSVLGLE SAGIDQTTYN SIMKCDVDVR KELYGNIVMS
310 320 330 340 350
GGTTMFPGIA ERMQKEITAL APSSMKVKII APPERKYSVW IGGSILASLT
360 370
TFQQMWISKQ EYDESGPSIV HHKCF
Length:375
Mass (Da):41,690
Last modified:July 21, 1986 - v1
Checksum:i87AC19B0B0BC9E71
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti178I → L in CAA24598 (PubMed:7001447).Curated1
Sequence conflicti308G → S in CAA24598 (PubMed:7001447).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti143Y → F in strain: CBS 1907. 1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V01288 Genomic DNA Translation: CAA24597.1
V01289 Genomic DNA Translation: CAA24598.1 Sequence problems.
V01290 Genomic DNA Translation: CAA24599.1
L00026 Genomic DNA Translation: AAA34391.1
D50617 Genomic DNA Translation: BAA21512.1
AJ389075 Genomic DNA Translation: CAC00716.1
AJ389076 Genomic DNA Translation: CAC00717.1
BK006940 Genomic DNA Translation: DAA12401.1
PIRiA03005 ATBY
JS0702
RefSeqiNP_116614.1, NM_001179927.1

Genome annotation databases

EnsemblFungiiBAA21512; BAA21512; BAA21512
YFL039C; YFL039C; YFL039C
GeneIDi850504
KEGGisce:YFL039C

Similar proteinsi

Entry informationi

Entry nameiACT_YEAST
AccessioniPrimary (citable) accession number: P60010
Secondary accession number(s): D6VTJ1
, P02579, Q9P3X6, Q9P3X7
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: June 20, 2018
This is version 161 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome VI
    Yeast (Saccharomyces cerevisiae) chromosome VI: entries and gene names

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