P60010 (ACT_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Actin

Gene names

Name:	ACT1
Synonyms:	ABY1, END7
Ordered Locus Names:	YFL039C

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	375 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.
Subunit structure	Component of the INO80 complex. Component of the SWR1 complex. Component of the NuA4 complex.
Subcellular location	Cytoplasm › cytoskeleton.
Sequence similarities	Belongs to the actin family.

Ontologies

Keywords
Cellular component	Cytoplasm Cytoskeleton
Ligand	ATP-binding Nucleotide-binding
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	DNA repair Inferred from direct assay PubMed 16135807. Source: SGD actomyosin contractile ring contraction Inferred from direct assay PubMed 9732290. Source: SGD ascospore wall assembly Inferred from direct assay PubMed 17118118. Source: SGD budding cell isotropic bud growth Traceable author statement PubMed 10652251. Source: SGD cellular response to oxidative stress Inferred from genetic interaction PubMed 17287397. Source: SGD chronological cell aging Inferred from mutant phenotype PubMed 15024029. Source: SGD endocytosis Inferred from mutant phenotype PubMed 8590801. Source: SGD establishment of mitotic spindle orientation Traceable author statement PubMed 10652251. Source: SGD exocytosis Traceable author statement PubMed 10652251. Source: SGD histone acetylation Inferred from direct assay PubMed 10911987. Source: SGD mitochondrion inheritance Traceable author statement PubMed 10652251. Source: SGD regulation of transcription from RNA polymerase II promoter Inferred from direct assay PubMed 10911987. Source: SGD vacuole inheritance Inferred from genetic interaction PubMed 8978821. Source: SGD vesicle transport along actin filament Traceable author statement PubMed 10652251. Source: SGD
Cellular_component	Ino80 complex Inferred from physical interaction PubMed 10952318. Source: SGD NuA4 histone acetyltransferase complex Inferred from physical interaction PubMed 15485911. Source: SGD Swr1 complex Inferred from direct assay PubMed 14645854PubMed 14690608PubMed 16299513. Source: SGD actin cortical patch Inferred from direct assay PubMed 3967297PubMed 6365930PubMed 8163554. Source: SGD actin filament bundle Inferred from direct assay PubMed 3967297PubMed 6365930PubMed 8163554. Source: SGD cellular bud neck contractile ring Inferred from direct assay PubMed 3967297PubMed 8163554. Source: SGD
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
groL	P0A6F5	5	EBI-2169,EBI-543750	From a different organism.
HSP82	P02829	2	EBI-2169,EBI-8659
LAS17	Q12446	3	EBI-2169,EBI-10022
SRV2	P17555	5	EBI-2169,EBI-4024
SWR1	Q05471	5	EBI-2169,EBI-22102
TCP1	P12612	2	EBI-2169,EBI-19045

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 375

375

Actin

PRO_0000089051

Amino acid modifications

Modified residue

1

1

N-acetylmethionine Ref.9

Modified residue

199

1

Phosphoserine Ref.12

Modified residue

201

1

Phosphoserine Ref.12

Modified residue

323

1

Phosphoserine Ref.12

Modified residue

324

1

Phosphoserine Ref.12

Natural variations

Natural variant

143

1

Y → F in strain: CBS 1907.

Experimental info

Sequence conflict

178

1

I → L in CAA24598. Ref.2

Sequence conflict

308

1

G → S in CAA24598. Ref.2

Secondary structure

1

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375

Helix Strand Turn

Details...

Beta strand

8 – 12

5

Beta strand

14 – 21

8

Beta strand

28 – 32

5

Beta strand

35 – 40

6

Turn

45 – 47

3

Helix

56 – 60

5

Helix

62 – 64

3

Beta strand

65 – 68

4

Beta strand

70 – 72

3

Beta strand

75 – 77

3

Helix

79 – 91

13

Turn

92 – 94

3

Helix

98 – 100

3

Beta strand

103 – 107

5

Helix

113 – 125

13

Beta strand

130 – 136

7

Helix

137 – 144

8

Beta strand

148 – 155

8

Beta strand

160 – 166

7

Helix

172 – 174

3

Beta strand

176 – 179

4

Helix

182 – 194

13

Turn

195 – 197

3

Helix

203 – 216

14

Helix

223 – 228

6

Turn

229 – 231

3

Beta strand

234 – 236

3

Beta strand

238 – 241

4

Beta strand

247 – 250

4

Helix

253 – 256

4

Helix

258 – 261

4

Helix

264 – 267

4

Helix

274 – 283

10

Helix

287 – 294

8

Beta strand

297 – 301

5

Helix

302 – 304

3

Helix

309 – 320

12

Turn

333 – 336

4

Helix

338 – 348

11

Helix

350 – 354

5

Beta strand

356 – 358

3

Helix

359 – 365

7

Helix

367 – 369

3

Helix

370 – 373

4

Sequences

	Sequence		Length	Mass (Da)
	P60010 [UniParc]. Last modified July 21, 1986. Version 1. Checksum: 87AC19B0B0BC9E71	FASTA	375	41,690
	10 20 30 40 50 60 MDSEVAALVI DNGSGMCKAG FAGDDAPRAV FPSIVGRPRH QGIMVGMGQK DSYVGDEAQS 70 80 90 100 110 120 KRGILTLRYP IEHGIVTNWD DMEKIWHHTF YNELRVAPEE HPVLLTEAPM NPKSNREKMT 130 140 150 160 170 180 QIMFETFNVP AFYVSIQAVL SLYSSGRTTG IVLDSGDGVT HVVPIYAGFS LPHAILRIDL 190 200 210 220 230 240 AGRDLTDYLM KILSERGYSF STTAEREIVR DIKEKLCYVA LDFEQEMQTA AQSSSIEKSY 250 260 270 280 290 300 ELPDGQVITI GNERFRAPEA LFHPSVLGLE SAGIDQTTYN SIMKCDVDVR KELYGNIVMS 310 320 330 340 350 360 GGTTMFPGIA ERMQKEITAL APSSMKVKII APPERKYSVW IGGSILASLT TFQQMWISKQ 370 EYDESGPSIV HHKCF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Structure of a split yeast gene: complete nucleotide sequence of the actin gene in Saccharomyces cerevisiae." Gallwitz D., Sures I. Proc. Natl. Acad. Sci. U.S.A. 77:2546-2550(1980) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Isolation and sequence of the gene for actin in Saccharomyces cerevisiae." Ng R., Abelson J. Proc. Natl. Acad. Sci. U.S.A. 77:3912-3916(1980) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Lariat structures are in vivo intermediates in yeast pre-mRNA splicing." Domdey H., Apostol B., Lin R.J., Newman A., Brody E., Abelson J. Cell 39:611-621(1984) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 4-58.
[4]	"Molecular cloning of the actin gene from yeast Saccharomyces cerevisiae." Gallwitz D., Seidel R. Nucleic Acids Res. 8:1043-1059(1980) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 5-57.
[5]	"The nucleotide sequences of the actin genes from Saccharomyces carlsbergensis and Saccharomyces cerevisiae are identical except for their introns." Nellen W., Donath C., Moos M., Gallwitz D. J. Mol. Appl. Genet. 1:239-244(1981) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: Carlsbergensis.
[6]	"Analysis of the nucleotide sequence of chromosome VI from Saccharomyces cerevisiae." Murakami Y., Naitou M., Hagiwara H., Shibata T., Ozawa M., Sasanuma S., Sasanuma M., Tsuchiya Y., Soeda E., Yokoyama K., Yamazaki M., Tashiro H., Eki T. Nat. Genet. 10:261-268(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[7]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[8]	"Partial sequence analysis of the actin gene and its potential for studying the phylogeny of Candida species and their teleomorphs." Daniel H.-M., Sorrell T.C., Meyer W. Int. J. Syst. Evol. Microbiol. 51:1593-1606(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 33-358. Strain: ATCC 18824 / CBS 1171 / DSM 70449 / IFO 10217 / NRRL Y-12632 and CBS 1907.
[9]	"Unusual metabolism of the yeast actin amino terminus." Cook R.K., Sheff D.R., Rubenstein P.A. J. Biol. Chem. 266:16825-16833(1991) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION AT MET-1, PROTEIN SEQUENCE OF N-TERMINUS.
[10]	"Protein expression during exponential growth in 0.7 M NaCl medium of Saccharomyces cerevisiae." Norbeck J., Blomberg A. FEMS Microbiol. Lett. 137:1-8(1996) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 19-25. Strain: ATCC 38531 / Y41.
[11]	"Site-directed mutagenesis of the yeast actin gene: a test for actin function in vivo." Johannes F.-Z., Gallwitz D. EMBO J. 10:3951-3958(1991) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS.
[12]	"A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-199; SER-201; SER-323 AND SER-324, MASS SPECTROMETRY.
[13]	"The structure of nonvertebrate actin: implications for the ATP hydrolytic mechanism." Vorobiev S., Strokopytov B., Drubin D.G., Frieden C., Ono S., Condeelis J., Rubenstein P.A., Almo S.C. Proc. Natl. Acad. Sci. U.S.A. 100:5760-5765(2003) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

PIR

ATBY. A03005.
JS0702.

RefSeq

NP_116614.1. NM_001179927.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1YAG	X-ray	1.90	A	1-375	[»]
1YVN	X-ray	2.10	A	1-375	[»]

ProteinModelPortal

P60010.

SMR

P60010. Positions 4-375.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-310N.

IntAct

P60010. 119 interactions.

MINT

MINT-374866.

2D gel databases

SWISS-2DPAGE

P60010.

Proteomic databases

PaxDb

P60010.

PeptideAtlas

P60010.

PRIDE

P60010.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YFL039C; YFL039C; YFL039C.

GeneID

850504.

KEGG

sce:YFL039C.

Organism-specific databases

CYGD

YFL039c.

SGD

S000001855. ACT1.

Phylogenomic databases

eggNOG

COG5277.

GeneTree

ENSGT00690000101979.

HOGENOM

HOG000233340.

KO

K05692.

OMA

IKNLMER.

OrthoDB

EOG4HHS9X.

Gene expression databases

ArrayExpress

P60010.

Genevestigator

P60010.

GermOnline

YFL039C. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR004000. Actin-related.
IPR020902. Actin/actin-like_CS.
IPR004001. Actin_CS.
[Graphical view]

PANTHER

PTHR11937. PTHR11937. 1 hit.

Pfam

PF00022. Actin. 1 hit.
[Graphical view]

PRINTS

PR00190. ACTIN.

SMART

SM00268. ACTIN. 1 hit.
[Graphical view]

PROSITE

PS00406. ACTINS_1. 1 hit.
PS00432. ACTINS_2. 1 hit.
PS01132. ACTINS_ACT_LIKE. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P60010.

NextBio

966206.

Entry information

Entry name

ACT_YEAST

Accession

Primary (citable) accession number: P60010
Secondary accession number(s): D6VTJ1 , P02579, Q9P3X6, Q9P3X7

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	July 21, 1986
Last modified:	April 3, 2013
This is version 110 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program