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-related protein 2/3 complex subunit 2

Gene

Arpc2

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Functions as actin-binding component of the Arp2/3 complex which is involved in regulation of actin polymerization and together with an activating nucleation-promoting factor (NPF) mediates the formation of branched actin networks. Seems to contact the mother actin filament (By similarity).By similarity

GO - Molecular functioni

  • actin binding Source: FlyBase
  • structural constituent of cytoskeleton Source: FlyBase

GO - Biological processi

  • Arp2/3 complex-mediated actin nucleation Source: FlyBase
  • cell morphogenesis Source: FlyBase
  • cell projection assembly Source: FlyBase
  • cortical actin cytoskeleton organization Source: FlyBase
  • lateral inhibition Source: FlyBase
  • regulation of cell shape Source: FlyBase
Complete GO annotation...

Keywords - Ligandi

Actin-binding

Enzyme and pathway databases

ReactomeiREACT_282671. Regulation of actin dynamics for phagocytic cup formation.
REACT_303345. EPHB-mediated forward signaling.
REACT_359184. RHO GTPases Activate WASPs and WAVEs.

Names & Taxonomyi

Protein namesi
Recommended name:
Actin-related protein 2/3 complex subunit 2
Alternative name(s):
Arp2/3 complex 34 kDa subunit
Short name:
p34-ARC
Gene namesi
Name:Arpc2
Synonyms:Arc-p34
ORF Names:CG10954
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803 Componenti: Chromosome 2L

Organism-specific databases

FlyBaseiFBgn0032859. Arpc2.

Subcellular locationi

GO - Cellular componenti

  • apical cortex Source: FlyBase
  • Arp2/3 protein complex Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 301301Actin-related protein 2/3 complex subunit 2PRO_0000124039Add
BLAST

Proteomic databases

PaxDbiQ9VIM5.

Expressioni

Gene expression databases

BgeeiQ9VIM5.
ExpressionAtlasiQ9VIM5. differential.
GenevisibleiQ9VIM5. DM.

Interactioni

Subunit structurei

Component of the Arp2/3 complex.By similarity

Protein-protein interaction databases

BioGridi61277. 14 interactions.
DIPiDIP-19044N.
IntActiQ9VIM5. 3 interactions.
MINTiMINT-980672.
STRINGi7227.FBpp0080890.

Structurei

3D structure databases

ProteinModelPortaliQ9VIM5.
SMRiQ9VIM5. Positions 1-283.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ARPC2 family.Curated

Phylogenomic databases

eggNOGiNOG327379.
InParanoidiQ9VIM5.
KOiK05758.
OMAiVFIQEFV.
OrthoDBiEOG73JKVS.
PhylomeDBiQ9VIM5.

Family and domain databases

InterProiIPR007188. ARPC2.
[Graphical view]
PANTHERiPTHR12058. PTHR12058. 1 hit.
PfamiPF04045. P34-Arc. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9VIM5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MILLEINNRI IEETLLVKYR NAQAGLKPES IDIRIADFDG VLYHISNVNG
60 70 80 90 100
DKTKVRISIS LKFYKQLQEH GADELLKREY GSLLTDTEEG YNVSVLINLE
110 120 130 140 150
EIPEDCEQIA KRIGLLKRNC FASVFEKYFD YQEQGEEGQK RAVINYRNDE
160 170 180 190 200
TLYVEAKPDR VTVVFSTIFR DEDDVIIGKV FMQELREGRR ASHTAPQVLF
210 220 230 240 250
SHREPPLELA NTDARVGDNI GYVTFVLFPR HTNKETRDNT INLIHMFRDY
260 270 280 290 300
LHYHIKCSKA YIHSRMRAKT SDFLKVLNRA RPEPKNTEKK TITGRTFKRI

D
Length:301
Mass (Da):35,104
Last modified:January 27, 2003 - v2
Checksum:iBD1C82C1343CA5AF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014134 Genomic DNA. Translation: AAF53892.2.
AY060391 mRNA. Translation: AAL25430.1.
RefSeqiNP_001286102.1. NM_001299173.1.
NP_610033.1. NM_136189.4.
UniGeneiDm.4005.

Genome annotation databases

EnsemblMetazoaiFBtr0081358; FBpp0080890; FBgn0032859.
FBtr0346418; FBpp0312086; FBgn0032859.
GeneIDi35311.
KEGGidme:Dmel_CG10954.
UCSCiCG10954-RA. d. melanogaster.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014134 Genomic DNA. Translation: AAF53892.2.
AY060391 mRNA. Translation: AAL25430.1.
RefSeqiNP_001286102.1. NM_001299173.1.
NP_610033.1. NM_136189.4.
UniGeneiDm.4005.

3D structure databases

ProteinModelPortaliQ9VIM5.
SMRiQ9VIM5. Positions 1-283.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi61277. 14 interactions.
DIPiDIP-19044N.
IntActiQ9VIM5. 3 interactions.
MINTiMINT-980672.
STRINGi7227.FBpp0080890.

Proteomic databases

PaxDbiQ9VIM5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0081358; FBpp0080890; FBgn0032859.
FBtr0346418; FBpp0312086; FBgn0032859.
GeneIDi35311.
KEGGidme:Dmel_CG10954.
UCSCiCG10954-RA. d. melanogaster.

Organism-specific databases

CTDi10109.
FlyBaseiFBgn0032859. Arpc2.

Phylogenomic databases

eggNOGiNOG327379.
InParanoidiQ9VIM5.
KOiK05758.
OMAiVFIQEFV.
OrthoDBiEOG73JKVS.
PhylomeDBiQ9VIM5.

Enzyme and pathway databases

ReactomeiREACT_282671. Regulation of actin dynamics for phagocytic cup formation.
REACT_303345. EPHB-mediated forward signaling.
REACT_359184. RHO GTPases Activate WASPs and WAVEs.

Miscellaneous databases

GenomeRNAii35311.
NextBioi792904.
PROiQ9VIM5.

Gene expression databases

BgeeiQ9VIM5.
ExpressionAtlasiQ9VIM5. differential.
GenevisibleiQ9VIM5. DM.

Family and domain databases

InterProiIPR007188. ARPC2.
[Graphical view]
PANTHERiPTHR12058. PTHR12058. 1 hit.
PfamiPF04045. P34-Arc. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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.
  2. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Embryo.

Entry informationi

Entry nameiARPC2_DROME
AccessioniPrimary (citable) accession number: Q9VIM5
Secondary accession number(s): Q95T07
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: January 27, 2003
Last modified: June 24, 2015
This is version 107 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.