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Q9VIM5

- ARPC2_DROME

UniProt

Q9VIM5 - ARPC2_DROME

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
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    • History
      Entry version 99 (01 Oct 2014)
      Sequence version 2 (27 Jan 2003)
      Previous versions | rss
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    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

    Keywords - Ligandi

    Actin-binding

    Enzyme and pathway databases

    ReactomeiREACT_181315. Regulation of actin dynamics for phagocytic cup formation.

    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-SubCell

    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

    MILLEINNRI IEETLLVKYR NAQAGLKPES IDIRIADFDG VLYHISNVNG    50
    DKTKVRISIS LKFYKQLQEH GADELLKREY GSLLTDTEEG YNVSVLINLE 100
    EIPEDCEQIA KRIGLLKRNC FASVFEKYFD YQEQGEEGQK RAVINYRNDE 150
    TLYVEAKPDR VTVVFSTIFR DEDDVIIGKV FMQELREGRR ASHTAPQVLF 200
    SHREPPLELA NTDARVGDNI GYVTFVLFPR HTNKETRDNT INLIHMFRDY 250
    LHYHIKCSKA YIHSRMRAKT SDFLKVLNRA RPEPKNTEKK TITGRTFKRI 300
    D 301
    Length:301
    Mass (Da):35,104
    Last modified:January 27, 2003 - v2
    Checksum:iBD1C82C1343CA5AF
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE014134 Genomic DNA. Translation: AAF53892.2.
    AY060391 mRNA. Translation: AAL25430.1.
    RefSeqiNP_610033.1. NM_136189.3.
    UniGeneiDm.4005.

    Genome annotation databases

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

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE014134 Genomic DNA. Translation: AAF53892.2 .
    AY060391 mRNA. Translation: AAL25430.1 .
    RefSeqi NP_610033.1. NM_136189.3.
    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.

    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

    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: October 1, 2014
    This is version 99 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