P10987 (ACT1_DROME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Actin-5C

Gene names

Name:	Act5C
ORF Names:	CG4027

Organism

Drosophila melanogaster (Fruit fly) [Reference proteome]

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Protostomia › Ecdysozoa › Panarthropoda › Arthropoda › Mandibulata › Pancrustacea › Hexapoda › Insecta › Dicondylia › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Eremoneura › Cyclorrhapha › Schizophora › Acalyptratae › Ephydroidea › Drosophilidae › Drosophilinae › Drosophilini › Drosophilina › Drosophiliti › Drosophila › Sophophora › melanogaster group › melanogaster subgroup

Protein attributes

Sequence length	376 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
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. Multiple isoforms are involved in various cellular functions such as cytoskeleton structure, cell mobility, chromosome movement and muscle contraction.
Subcellular location	Cytoplasm › cytoskeleton.
Post-translational modification	Oxidation of Met-45 by Mical to form methionine sulfoxide promotes actin filament depolymerization. Methionine sulfoxide is produced stereospecifically, but it is not known whether the (S)-S-oxide or the (R)-S-oxide is produced.
Miscellaneous	In Drosophila there are 6 closely related actin genes.
Sequence similarities	Belongs to the actin family.

Ontologies

Keywords
Cellular component	Cytoplasm Cytoskeleton
Ligand	ATP-binding Nucleotide-binding
PTM	Acetylation Oxidation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cytokinesis Inferred from mutant phenotype PubMed 15380073PubMed 15547975PubMed 16174742. Source: FlyBase cytoskeleton organization Inferred from sequence or structural similarity PubMed 10908588. Source: FlyBase inter-male aggressive behavior Inferred from mutant phenotype PubMed 19519879. Source: FlyBase maintenance of protein location in cell Inferred from mutant phenotype PubMed 16174742. Source: FlyBase mushroom body development Inferred from mutant phenotype PubMed 19519879. Source: FlyBase phagocytosis, engulfment Inferred from mutant phenotype PubMed 16336044. Source: FlyBase sperm individualization Inferred from expression pattern PubMed 12642486. Source: FlyBase
Cellular_component	Ino80 complex Inferred from direct assay PubMed 16618800. Source: FlyBase actin filament Inferred from sequence or structural similarity PubMed 10908588. Source: FlyBase lipid particle Inferred from direct assay PubMed 16543254. Source: FlyBase microtubule associated complex Inferred from direct assay PubMed 18433294. Source: FlyBase
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW structural constituent of cytoskeleton Inferred from sequence or structural similarity PubMed 10908588. Source: FlyBase
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Propeptide

1 – 2

2

Removed in mature form By similarity

PRO_0000000656

Chain

3 – 376

374

Actin-5C

PRO_0000000657

Amino acid modifications

Modified residue

3

1

N-acetylaspartate By similarity

Modified residue

45

1

Methionine sulfoxide

Modified residue

48

1

Methionine sulfoxide

Experimental info

Mutagenesis

45

1

M → L: Abolishes formation of methionine-sulfoxide and subsequent depolymerization. Ref.9

Mutagenesis

48

1

M → L: Depolymerizes in the presence of Mical. Ref.9

Sequence conflict

264

1

Q → H in AAA28316. Ref.1

Sequence conflict

272

1

A → S in AAA28316. Ref.1

Sequence conflict

350

1

L → S in AAA28316. Ref.1

Sequence conflict

358

1

I → T in AAA28316. Ref.1

Sequence conflict

366 – 367

2

SG → AW in CAA30474. Ref.8

Secondary structure

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376

Helix Strand Turn

Details...

Beta strand

9 – 12

4

Beta strand

15 – 22

8

Beta strand

25 – 27

3

Beta strand

29 – 34

6

Beta strand

36 – 39

4

Beta strand

46 – 48

3

Beta strand

54 – 56

3

Helix

57 – 61

5

Helix

63 – 65

3

Beta strand

66 – 69

4

Turn

71 – 74

4

Helix

80 – 92

13

Turn

93 – 95

3

Helix

99 – 101

3

Beta strand

104 – 108

5

Helix

114 – 126

13

Beta strand

131 – 137

7

Helix

138 – 145

8

Beta strand

149 – 156

8

Beta strand

161 – 167

7

Helix

173 – 175

3

Beta strand

177 – 180

4

Helix

183 – 197

15

Helix

204 – 217

14

Helix

224 – 233

10

Beta strand

239 – 242

4

Beta strand

248 – 251

4

Helix

254 – 260

7

Turn

261 – 263

3

Helix

265 – 268

4

Helix

275 – 284

10

Helix

288 – 290

3

Helix

291 – 295

5

Beta strand

298 – 302

5

Helix

303 – 305

3

Helix

310 – 321

12

Helix

336 – 338

3

Helix

339 – 348

10

Helix

351 – 356

6

Beta strand

357 – 359

3

Helix

360 – 366

7

Helix

370 – 374

5

Sequences

	Sequence		Length	Mass (Da)
	P10987 [UniParc]. Last modified December 1, 2000. Version 4. Checksum: BDAF13C191BB1BBC	FASTA	376	41,822
	10 20 30 40 50 60 MCDEEVAALV VDNGSGMCKA GFAGDDAPRA VFPSIVGRPR HQGVMVGMGQ KDSYVGDEAQ 70 80 90 100 110 120 SKRGILTLKY PIEHGIVTNW DDMEKIWHHT FYNELRVAPE EHPVLLTEAP LNPKANREKM 130 140 150 160 170 180 TQIMFETFNT PAMYVAIQAV LSLYASGRTT GIVLDSGDGV SHTVPIYEGY ALPHAILRLD 190 200 210 220 230 240 LAGRDLTDYL MKILTERGYS FTTTAEREIV RDIKEKLCYV ALDFEQEMAT AASSSSLEKS 250 260 270 280 290 300 YELPDGQVIT IGNERFRCPE ALFQPSFLGM EACGIHETTY NSIMKCDVDI RKDLYANTVL 310 320 330 340 350 360 SGGTTMYPGI ADRMQKEITA LAPSTMKIKI IAPPERKYSV WIGGSILASL STFQQMWISK 370 QEYDESGPSI VHRKCF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	Fyrberg E.A., Bond B.J., Hershey N.D., Mixter K.S., Davidson N. Submitted (DEC-1987) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"The genome sequence of Drosophila melanogaster." Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C. Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Berkeley.
[3]	"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review." Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E. Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed] [Europe PMC] [Abstract] Cited for: GENOME REANNOTATION. Strain: Berkeley.
[4]	"A Drosophila full-length cDNA resource." Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E. Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Berkeley. Tissue: Embryo.
[5]	"Stage-specific selection of alternative transcriptional initiation sites from the 5C actin gene of Drosophila melanogaster." Vigoreaux J.O., Tobin S.L. Genes Dev. 1:1161-1171(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-84 AND 324-376.
[6]	"The actin genes of Drosophila: protein coding regions are highly conserved but intron positions are not." Fyrberg E.A., Bond B.J., Hershey N.D., Mixter K.S., Davidson N. Cell 24:107-116(1981) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-75.
[7]	"The Drosophila melanogaster actin 5C gene uses two transcription initiation sites and three polyadenylation sites to express multiple mRNA species." Bond B.J., Davidson N. Mol. Cell. Biol. 6:2080-2088(1986) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-12.
[8]	"Transcriptional activity at the 3' end of the actin gene at 5C on the X chromosome of Drosophila melanogaster." Rao J.P., Zafar R.S., Sodja A. Biochim. Biophys. Acta 950:30-44(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 366-376. Strain: Canton-S.
[9]	"Direct redox regulation of F-actin assembly and disassembly by Mical." Hung R.J., Pak C.W., Terman J.R. Science 334:1710-1713(2011) [PubMed] [Europe PMC] [Abstract] Cited for: OXIDATION AT MET-45 AND MET-48, MUTAGENESIS OF MET-45 AND MET-48.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

K00667 Genomic DNA. Translation: AAA28316.1.
AE014298 Genomic DNA. Translation: AAF46098.1.
AE014298 Genomic DNA. Translation: AAN09154.1.
AE014298 Genomic DNA. Translation: AAX52479.1.
AE014298 Genomic DNA. Translation: AAX52480.1.
AY089562 mRNA. Translation: AAL90300.1.
X06383 Genomic DNA. Translation: CAA29681.1.
X06384 Genomic DNA. Translation: CAB61444.1.
M13587 Genomic DNA. Translation: AAA28315.1.
X07627 Genomic DNA. Translation: CAA30474.1.

PIR

A28258.

RefSeq

NP_001014725.1. NM_001014725.2.
NP_001014726.1. NM_001014726.2.
NP_511052.1. NM_078497.3.
NP_727048.1. NM_167053.2.

UniGene

Dm.2951.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1N58	model	-	A	1-376	[»]
2HF3	X-ray	1.80	A	3-376	[»]
2HF4	X-ray	1.80	A	3-376	[»]
3EKS	X-ray	1.80	A	2-376	[»]
3EKU	X-ray	2.50	A	2-376	[»]
3EL2	X-ray	2.50	A	2-376	[»]
3MMV	X-ray	2.80	A	3-376	[»]
3MN6	X-ray	2.00	A/F/K	3-376	[»]
3MN7	X-ray	2.00	A	3-376	[»]
3MN9	X-ray	2.00	A	3-376	[»]

ProteinModelPortal

P10987.

SMR

P10987. Positions 3-376.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-18961N.

IntAct

P10987. 8 interactions.

MINT

MINT-799448.

Proteomic databases

PaxDb

P10987.

PRIDE

P10987.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblMetazoa

FBtr0070822; FBpp0070787; FBgn0000042.
FBtr0070823; FBpp0070788; FBgn0000042.
FBtr0100662; FBpp0100124; FBgn0000042.
FBtr0100663; FBpp0100125; FBgn0000042.

GeneID

31521.

KEGG

dme:Dmel_CG4027.

Organism-specific databases

CTD

31521.

FlyBase

FBgn0000042. Act5C.

Phylogenomic databases

eggNOG

COG5277.

GeneTree

ENSGT00690000101979.

InParanoid

P10987.

KO

K05692.

OMA

IKNLMER.

OrthoDB

EOG4Z34W3.

PhylomeDB

P10987.

Gene expression databases

Bgee

P10987.

GermOnline

CG4027. Drosophila melanogaster.

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

ChiTaRS

Act5C. drosophila.

EvolutionaryTrace

P10987.

GenomeRNAi

31521.

NextBio

774032.

Entry information

Entry name

ACT1_DROME

Accession

Primary (citable) accession number: P10987
Secondary accession number(s): A4V404 , Q24227, Q6YN46, Q9U5X7, Q9W460

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	December 1, 2000
Last modified:	April 3, 2013
This is version 130 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project