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Q9VIM5

- ARPC2_DROME

UniProt

Q9VIM5 - ARPC2_DROME

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Protein

Actin-related protein 2/3 complex subunit 2

Gene

Arpc2

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 3 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

  1. actin binding Source: FlyBase

GO - Biological processi

  1. cell morphogenesis Source: FlyBase
  2. cell projection assembly Source: FlyBase
  3. cortical actin cytoskeleton organization Source: FlyBase
  4. lateral inhibition Source: FlyBase
  5. regulation of actin filament polymerization Source: InterPro
  6. regulation of cell shape Source: FlyBase
Complete GO annotation...

Keywords - Ligandi

Actin-binding

Enzyme and pathway databases

ReactomeiREACT_181315. Regulation of actin dynamics for phagocytic cup formation.
REACT_238518. EPHB-mediated forward signaling.

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: Chromosome 2L

Organism-specific databases

FlyBaseiFBgn0032859. Arpc2.

Subcellular locationi

Cytoplasmcytoskeleton By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
  2. cytoskeleton Source: UniProtKB-KW
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.

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.

Structurei

3D structure databases

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

Family & Domainsi

Sequence similaritiesi

Belongs to the ARPC2 family.Curated

Phylogenomic databases

eggNOGiNOG327379.
GeneTreeiENSGT00390000016794.
InParanoidiQ9VIM5.
KOiK05758.
OMAiYFKFQEE.
OrthoDBiEOG73JKVS.
PhylomeDBiQ9VIM5.

Family and domain databases

InterProiIPR007188. P34-arc.
[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.
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 .
RefSeqi NP_001286102.1. NM_001299173.1.
NP_610033.1. NM_136189.4.
UniGenei Dm.4005.

3D structure databases

ProteinModelPortali Q9VIM5.
SMRi Q9VIM5. Positions 1-283.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 61277. 14 interactions.
DIPi DIP-19044N.
IntActi Q9VIM5. 3 interactions.
MINTi MINT-980672.

Proteomic databases

PaxDbi Q9VIM5.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblMetazoai FBtr0081358 ; FBpp0080890 ; FBgn0032859 .
GeneIDi 35311.
KEGGi dme:Dmel_CG10954.
UCSCi CG10954-RA. d. melanogaster.

Organism-specific databases

CTDi 10109.
FlyBasei FBgn0032859. Arpc2.

Phylogenomic databases

eggNOGi NOG327379.
GeneTreei ENSGT00390000016794.
InParanoidi Q9VIM5.
KOi K05758.
OMAi YFKFQEE.
OrthoDBi EOG73JKVS.
PhylomeDBi Q9VIM5.

Enzyme and pathway databases

Reactomei REACT_181315. Regulation of actin dynamics for phagocytic cup formation.
REACT_238518. EPHB-mediated forward signaling.

Miscellaneous databases

GenomeRNAii 35311.
NextBioi 792904.
PROi Q9VIM5.

Gene expression databases

Bgeei Q9VIM5.

Family and domain databases

InterProi IPR007188. P34-arc.
[Graphical view ]
PANTHERi PTHR12058. PTHR12058. 1 hit.
Pfami PF04045. P34-Arc. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: November 26, 2014
This is version 101 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