Reviewed, UniProtKB/Swiss-Prot P10987 (ACT1_DROME)

Names and origin

Protein names

Recommended name:
    Actin-5C

Gene names

Name:	Act5C
ORF Names:	CG4027

Organism

Drosophila melanogaster (Fruit fly) [Complete proteome]

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

Protein attributes

Sequence length	376 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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.
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
Molecular function	Structural protein
PTM	Acetylation
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	cytokinesis Inferred from mutant phenotype. Source: FlyBase phagocytosis, engulfment Inferred from mutant phenotype. Source: FlyBase sperm individualization Inferred from expression pattern. Source: FlyBase visual behavior Inferred from mutant phenotype. Source: FlyBase
Cellular component	INO80 complex Inferred from direct assay. Source: FlyBase lipid particle Inferred from direct assay. Source: FlyBase plasma membrane Inferred from direct assay. Source: FlyBase
Molecular function	protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
	Q9VML9	1	EBI-130188,EBI-111235
capt	Q9VPX7	1	EBI-130188,EBI-151736

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Molecule processing

Propeptide

1 – 2

2

Removed in mature form By similarity

Chain

3 – 376

374

Actin-5C

Amino acid modifications

Modified residue

3

1

N-acetylaspartate By similarity

Experimental info

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

29 – 34

6

Beta strand

36 – 39

4

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)
	P10987-1 [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: 10731132] [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: 12537572] [Abstract] Cited for: GENOME REANNOTATION.
[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: 12537569] [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: 3123314] [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: 6263481] [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: 3097509] [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: 2896018] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 366-376. Strain: Canton-S.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

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.
NP_001014726.1.
NP_511052.1.
NP_727048.1.

UniGene

Dm.2951

3D structure databases

PDBMSD

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	[»]