Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Actin-5C

Gene

Act5C

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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.
Multiple isoforms are involved in various cellular functions such as cytoskeleton structure, cell mobility, chromosome movement and muscle contraction.

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • structural constituent of cytoskeleton Source: FlyBase

GO - Biological processi

  • chromatin remodeling Source: FlyBase
  • cytoskeleton organization Source: FlyBase
  • inter-male aggressive behavior Source: FlyBase
  • maintenance of protein location in cell Source: FlyBase
  • mitotic cytokinesis Source: FlyBase
  • mushroom body development Source: FlyBase
  • phagocytosis Source: FlyBase
  • sperm individualization Source: FlyBase
  • tube formation Source: FlyBase
Complete GO annotation...

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-DME-445355. Smooth Muscle Contraction.
SignaLinkiP10987.

Names & Taxonomyi

Protein namesi
Recommended name:
Actin-5C
Gene namesi
Name:Act5C
ORF Names:CG4027
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome X

Organism-specific databases

FlyBaseiFBgn0000042. Act5C.

Subcellular locationi

GO - Cellular componenti

  • actin filament Source: FlyBase
  • brahma complex Source: FlyBase
  • cytoplasm Source: UniProtKB-KW
  • Ino80 complex Source: FlyBase
  • lipid particle Source: FlyBase
  • microtubule associated complex Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi45M → L: Abolishes formation of methionine-sulfoxide and subsequent depolymerization. 1 Publication1
Mutagenesisi48M → L: Depolymerizes in the presence of Mical. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
PropeptideiPRO_00000006561 – 2Removed in mature formBy similarity2
ChainiPRO_00000006573 – 376Actin-5CAdd BLAST374

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei3N-acetylaspartateBy similarity1
Modified residuei45Methionine sulfoxide1 Publication1
Modified residuei48Methionine sulfoxide1 Publication1

Post-translational modificationi

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.1 Publication

Keywords - PTMi

Acetylation, Oxidation

Proteomic databases

PaxDbiP10987.
PRIDEiP10987.

Expressioni

Gene expression databases

BgeeiFBgn0000042.
ExpressionAtlasiP10987. baseline.
GenevisibleiP10987. DM.

Interactioni

Subunit structurei

Interacts with Rab6.1 Publication

Protein-protein interaction databases

BioGridi58020. 62 interactors.
DIPiDIP-18961N.
IntActiP10987. 10 interactors.
MINTiMINT-799448.
STRINGi7227.FBpp0100124.

Structurei

Secondary structure

1376
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi9 – 12Combined sources4
Beta strandi15 – 22Combined sources8
Beta strandi25 – 27Combined sources3
Beta strandi29 – 34Combined sources6
Beta strandi36 – 39Combined sources4
Beta strandi41 – 43Combined sources3
Beta strandi46 – 48Combined sources3
Beta strandi54 – 56Combined sources3
Helixi57 – 61Combined sources5
Helixi63 – 65Combined sources3
Beta strandi66 – 69Combined sources4
Turni71 – 74Combined sources4
Beta strandi76 – 78Combined sources3
Helixi80 – 92Combined sources13
Turni93 – 95Combined sources3
Helixi99 – 101Combined sources3
Beta strandi104 – 108Combined sources5
Helixi114 – 126Combined sources13
Beta strandi131 – 137Combined sources7
Helixi138 – 145Combined sources8
Beta strandi149 – 156Combined sources8
Beta strandi161 – 167Combined sources7
Helixi173 – 175Combined sources3
Beta strandi177 – 180Combined sources4
Helixi183 – 197Combined sources15
Helixi204 – 217Combined sources14
Helixi224 – 233Combined sources10
Beta strandi239 – 242Combined sources4
Beta strandi248 – 251Combined sources4
Helixi254 – 260Combined sources7
Turni261 – 263Combined sources3
Helixi265 – 268Combined sources4
Helixi275 – 284Combined sources10
Helixi288 – 290Combined sources3
Helixi291 – 295Combined sources5
Beta strandi298 – 302Combined sources5
Helixi303 – 305Combined sources3
Helixi310 – 321Combined sources12
Helixi336 – 338Combined sources3
Helixi339 – 348Combined sources10
Helixi351 – 356Combined sources6
Beta strandi357 – 359Combined sources3
Helixi360 – 366Combined sources7
Helixi370 – 374Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1N58model-A1-376[»]
2HF3X-ray1.80A3-376[»]
2HF4X-ray1.80A3-376[»]
3EKSX-ray1.80A2-376[»]
3EKUX-ray2.50A2-376[»]
3EL2X-ray2.50A2-376[»]
3MMVX-ray2.80A3-376[»]
3MN6X-ray2.00A/F/K3-376[»]
3MN7X-ray2.00A3-376[»]
3MN9X-ray2.00A3-376[»]
4JHDX-ray2.91A/B/D/E1-376[»]
4M63X-ray2.75C/D/E1-376[»]
4RWTX-ray2.98A/B1-376[»]
ProteinModelPortaliP10987.
SMRiP10987.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP10987.

Family & Domainsi

Sequence similaritiesi

Belongs to the actin family.Curated

Phylogenomic databases

eggNOGiKOG0676. Eukaryota.
COG5277. LUCA.
InParanoidiP10987.
KOiK05692.
OMAiPFHTTAE.
OrthoDBiEOG091G08LD.
PhylomeDBiP10987.

Family and domain databases

InterProiIPR004000. Actin.
IPR020902. Actin/actin-like_CS.
IPR004001. Actin_CS.
[Graphical view]
PANTHERiPTHR11937. PTHR11937. 1 hit.
PfamiPF00022. Actin. 1 hit.
[Graphical view]
PRINTSiPR00190. ACTIN.
SMARTiSM00268. ACTIN. 1 hit.
[Graphical view]
PROSITEiPS00406. ACTINS_1. 1 hit.
PS00432. ACTINS_2. 1 hit.
PS01132. ACTINS_ACT_LIKE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P10987-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MCDEEVAALV VDNGSGMCKA GFAGDDAPRA VFPSIVGRPR HQGVMVGMGQ
60 70 80 90 100
KDSYVGDEAQ SKRGILTLKY PIEHGIVTNW DDMEKIWHHT FYNELRVAPE
110 120 130 140 150
EHPVLLTEAP LNPKANREKM TQIMFETFNT PAMYVAIQAV LSLYASGRTT
160 170 180 190 200
GIVLDSGDGV SHTVPIYEGY ALPHAILRLD LAGRDLTDYL MKILTERGYS
210 220 230 240 250
FTTTAEREIV RDIKEKLCYV ALDFEQEMAT AASSSSLEKS YELPDGQVIT
260 270 280 290 300
IGNERFRCPE ALFQPSFLGM EACGIHETTY NSIMKCDVDI RKDLYANTVL
310 320 330 340 350
SGGTTMYPGI ADRMQKEITA LAPSTMKIKI IAPPERKYSV WIGGSILASL
360 370
STFQQMWISK QEYDESGPSI VHRKCF
Length:376
Mass (Da):41,822
Last modified:December 1, 2000 - v4
Checksum:iBDAF13C191BB1BBC
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti264Q → H in AAA28316 (Ref. 1) Curated1
Sequence conflicti272A → S in AAA28316 (Ref. 1) Curated1
Sequence conflicti350L → S in AAA28316 (Ref. 1) Curated1
Sequence conflicti358I → T in AAA28316 (Ref. 1) Curated1
Sequence conflicti366 – 367SG → AW in CAA30474 (PubMed:2896018).Curated2

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiA28258.
RefSeqiNP_001014725.1. NM_001014725.2.
NP_001014726.1. NM_001014726.2.
NP_001284915.1. NM_001297986.1.
NP_511052.1. NM_078497.4.
NP_727048.1. NM_167053.2.
UniGeneiDm.2951.

Genome annotation databases

EnsemblMetazoaiFBtr0070822; FBpp0070787; FBgn0000042.
FBtr0070823; FBpp0070788; FBgn0000042.
FBtr0100662; FBpp0100124; FBgn0000042.
FBtr0100663; FBpp0100125; FBgn0000042.
FBtr0345894; FBpp0311818; FBgn0000042.
GeneIDi31521.
KEGGidme:Dmel_CG4027.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiA28258.
RefSeqiNP_001014725.1. NM_001014725.2.
NP_001014726.1. NM_001014726.2.
NP_001284915.1. NM_001297986.1.
NP_511052.1. NM_078497.4.
NP_727048.1. NM_167053.2.
UniGeneiDm.2951.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1N58model-A1-376[»]
2HF3X-ray1.80A3-376[»]
2HF4X-ray1.80A3-376[»]
3EKSX-ray1.80A2-376[»]
3EKUX-ray2.50A2-376[»]
3EL2X-ray2.50A2-376[»]
3MMVX-ray2.80A3-376[»]
3MN6X-ray2.00A/F/K3-376[»]
3MN7X-ray2.00A3-376[»]
3MN9X-ray2.00A3-376[»]
4JHDX-ray2.91A/B/D/E1-376[»]
4M63X-ray2.75C/D/E1-376[»]
4RWTX-ray2.98A/B1-376[»]
ProteinModelPortaliP10987.
SMRiP10987.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi58020. 62 interactors.
DIPiDIP-18961N.
IntActiP10987. 10 interactors.
MINTiMINT-799448.
STRINGi7227.FBpp0100124.

Proteomic databases

PaxDbiP10987.
PRIDEiP10987.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0070822; FBpp0070787; FBgn0000042.
FBtr0070823; FBpp0070788; FBgn0000042.
FBtr0100662; FBpp0100124; FBgn0000042.
FBtr0100663; FBpp0100125; FBgn0000042.
FBtr0345894; FBpp0311818; FBgn0000042.
GeneIDi31521.
KEGGidme:Dmel_CG4027.

Organism-specific databases

CTDi31521.
FlyBaseiFBgn0000042. Act5C.

Phylogenomic databases

eggNOGiKOG0676. Eukaryota.
COG5277. LUCA.
InParanoidiP10987.
KOiK05692.
OMAiPFHTTAE.
OrthoDBiEOG091G08LD.
PhylomeDBiP10987.

Enzyme and pathway databases

ReactomeiR-DME-445355. Smooth Muscle Contraction.
SignaLinkiP10987.

Miscellaneous databases

ChiTaRSiAct5C. fly.
EvolutionaryTraceiP10987.
GenomeRNAii31521.
PROiP10987.

Gene expression databases

BgeeiFBgn0000042.
ExpressionAtlasiP10987. baseline.
GenevisibleiP10987. DM.

Family and domain databases

InterProiIPR004000. Actin.
IPR020902. Actin/actin-like_CS.
IPR004001. Actin_CS.
[Graphical view]
PANTHERiPTHR11937. PTHR11937. 1 hit.
PfamiPF00022. Actin. 1 hit.
[Graphical view]
PRINTSiPR00190. ACTIN.
SMARTiSM00268. ACTIN. 1 hit.
[Graphical view]
PROSITEiPS00406. ACTINS_1. 1 hit.
PS00432. ACTINS_2. 1 hit.
PS01132. ACTINS_ACT_LIKE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiACT1_DROME
AccessioniPrimary (citable) accession number: P10987
Secondary accession number(s): A4V404
, Q24227, Q6YN46, Q9U5X7, Q9W460
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: December 1, 2000
Last modified: November 30, 2016
This is version 166 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Miscellaneous

In Drosophila there are 6 closely related actin genes.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.