Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P10987

- ACT1_DROME

UniProt

P10987 - ACT1_DROME

Protein

Actin-5C

Gene

Act5C

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 141 (01 Oct 2014)
      Sequence version 4 (01 Dec 2000)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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

    1. ATP binding Source: UniProtKB-KW
    2. structural constituent of cytoskeleton Source: FlyBase

    GO - Biological processi

    1. cytoskeleton organization Source: FlyBase
    2. inter-male aggressive behavior Source: FlyBase
    3. maintenance of protein location in cell Source: FlyBase
    4. mitotic cytokinesis Source: FlyBase
    5. mushroom body development Source: FlyBase
    6. phagocytosis Source: FlyBase
    7. sperm individualization Source: FlyBase

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_180258. Factors involved in megakaryocyte development and platelet production.
    REACT_180852. Translocation of GLUT4 to the plasma membrane.
    REACT_181315. Regulation of actin dynamics for phagocytic cup formation.
    REACT_208005. Formation of annular gap junctions.
    REACT_209888. Adherens junctions interactions.
    REACT_79920. Interaction between L1 and Ankyrins.
    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
    ProteomesiUP000000803: Chromosome X

    Organism-specific databases

    FlyBaseiFBgn0000042. Act5C.

    Subcellular locationi

    GO - Cellular componenti

    1. actin filament Source: FlyBase
    2. cytoplasm Source: UniProtKB-KW
    3. Ino80 complex Source: FlyBase
    4. lipid particle Source: FlyBase
    5. microtubule associated complex Source: FlyBase

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi45 – 451M → L: Abolishes formation of methionine-sulfoxide and subsequent depolymerization. 1 Publication
    Mutagenesisi48 – 481M → L: Depolymerizes in the presence of Mical. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Propeptidei1 – 22Removed in mature formBy similarityPRO_0000000656
    Chaini3 – 376374Actin-5CPRO_0000000657Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei3 – 31N-acetylaspartateBy similarity
    Modified residuei45 – 451Methionine sulfoxide1 Publication
    Modified residuei48 – 481Methionine sulfoxide1 Publication

    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

    BgeeiP10987.

    Interactioni

    Subunit structurei

    Interacts with Rab6.1 Publication

    Protein-protein interaction databases

    BioGridi58020. 61 interactions.
    DIPiDIP-18961N.
    IntActiP10987. 10 interactions.
    MINTiMINT-799448.

    Structurei

    Secondary structure

    1
    376
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi9 – 124
    Beta strandi15 – 228
    Beta strandi25 – 273
    Beta strandi29 – 346
    Beta strandi36 – 394
    Beta strandi46 – 483
    Beta strandi54 – 563
    Helixi57 – 615
    Helixi63 – 653
    Beta strandi66 – 694
    Turni71 – 744
    Beta strandi76 – 783
    Helixi80 – 9213
    Turni93 – 953
    Helixi99 – 1013
    Beta strandi104 – 1085
    Helixi114 – 12613
    Beta strandi131 – 1377
    Helixi138 – 1458
    Beta strandi149 – 1568
    Beta strandi161 – 1677
    Helixi173 – 1753
    Beta strandi177 – 1804
    Helixi183 – 19715
    Helixi204 – 21714
    Helixi224 – 23310
    Beta strandi239 – 2424
    Beta strandi248 – 2514
    Helixi254 – 2607
    Turni261 – 2633
    Helixi265 – 2684
    Helixi275 – 28410
    Helixi288 – 2903
    Helixi291 – 2955
    Beta strandi298 – 3025
    Helixi303 – 3053
    Helixi310 – 32112
    Helixi336 – 3383
    Helixi339 – 34810
    Helixi351 – 3566
    Beta strandi357 – 3593
    Helixi360 – 3667
    Helixi370 – 3745

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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[»]
    ProteinModelPortaliP10987.
    SMRiP10987. Positions 3-376.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP10987.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the actin family.Curated

    Phylogenomic databases

    eggNOGiCOG5277.
    GeneTreeiENSGT00710000106384.
    InParanoidiP10987.
    KOiK05692.
    OMAiDARAPIM.
    OrthoDBiEOG72RMZ1.
    PhylomeDBiP10987.

    Family and domain databases

    InterProiIPR004000. Actin-related.
    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

    MCDEEVAALV VDNGSGMCKA GFAGDDAPRA VFPSIVGRPR HQGVMVGMGQ    50
    KDSYVGDEAQ SKRGILTLKY PIEHGIVTNW DDMEKIWHHT FYNELRVAPE 100
    EHPVLLTEAP LNPKANREKM TQIMFETFNT PAMYVAIQAV LSLYASGRTT 150
    GIVLDSGDGV SHTVPIYEGY ALPHAILRLD LAGRDLTDYL MKILTERGYS 200
    FTTTAEREIV RDIKEKLCYV ALDFEQEMAT AASSSSLEKS YELPDGQVIT 250
    IGNERFRCPE ALFQPSFLGM EACGIHETTY NSIMKCDVDI RKDLYANTVL 300
    SGGTTMYPGI ADRMQKEITA LAPSTMKIKI IAPPERKYSV WIGGSILASL 350
    STFQQMWISK QEYDESGPSI VHRKCF 376
    Length:376
    Mass (Da):41,822
    Last modified:December 1, 2000 - v4
    Checksum:iBDAF13C191BB1BBC
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti264 – 2641Q → H in AAA28316. 1 PublicationCurated
    Sequence conflicti272 – 2721A → S in AAA28316. 1 PublicationCurated
    Sequence conflicti350 – 3501L → S in AAA28316. 1 PublicationCurated
    Sequence conflicti358 – 3581I → T in AAA28316. 1 PublicationCurated
    Sequence conflicti366 – 3672SG → AW in CAA30474. (PubMed:2896018)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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_511052.1. NM_078497.3.
    NP_727048.1. NM_167053.2.
    UniGeneiDm.2951.

    Genome annotation databases

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

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    PIRi A28258.
    RefSeqi NP_001014725.1. NM_001014725.2.
    NP_001014726.1. NM_001014726.2.
    NP_511052.1. NM_078497.3.
    NP_727048.1. NM_167053.2.
    UniGenei Dm.2951.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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 [» ]
    3EKS X-ray 1.80 A 2-376 [» ]
    3EKU X-ray 2.50 A 2-376 [» ]
    3EL2 X-ray 2.50 A 2-376 [» ]
    3MMV X-ray 2.80 A 3-376 [» ]
    3MN6 X-ray 2.00 A/F/K 3-376 [» ]
    3MN7 X-ray 2.00 A 3-376 [» ]
    3MN9 X-ray 2.00 A 3-376 [» ]
    4JHD X-ray 2.91 A/B/D/E 1-376 [» ]
    4M63 X-ray 2.75 C/D/E 1-376 [» ]
    ProteinModelPortali P10987.
    SMRi P10987. Positions 3-376.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 58020. 61 interactions.
    DIPi DIP-18961N.
    IntActi P10987. 10 interactions.
    MINTi MINT-799448.

    Proteomic databases

    PaxDbi P10987.
    PRIDEi P10987.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai FBtr0070822 ; FBpp0070787 ; FBgn0000042 .
    FBtr0070823 ; FBpp0070788 ; FBgn0000042 .
    FBtr0100662 ; FBpp0100124 ; FBgn0000042 .
    FBtr0100663 ; FBpp0100125 ; FBgn0000042 .
    GeneIDi 31521.
    KEGGi dme:Dmel_CG4027.

    Organism-specific databases

    CTDi 31521.
    FlyBasei FBgn0000042. Act5C.

    Phylogenomic databases

    eggNOGi COG5277.
    GeneTreei ENSGT00710000106384.
    InParanoidi P10987.
    KOi K05692.
    OMAi DARAPIM.
    OrthoDBi EOG72RMZ1.
    PhylomeDBi P10987.

    Enzyme and pathway databases

    Reactomei REACT_180258. Factors involved in megakaryocyte development and platelet production.
    REACT_180852. Translocation of GLUT4 to the plasma membrane.
    REACT_181315. Regulation of actin dynamics for phagocytic cup formation.
    REACT_208005. Formation of annular gap junctions.
    REACT_209888. Adherens junctions interactions.
    REACT_79920. Interaction between L1 and Ankyrins.
    SignaLinki P10987.

    Miscellaneous databases

    ChiTaRSi Act5C. drosophila.
    EvolutionaryTracei P10987.
    GenomeRNAii 31521.
    NextBioi 774032.

    Gene expression databases

    Bgeei P10987.

    Family and domain databases

    InterProi IPR004000. Actin-related.
    IPR020902. Actin/actin-like_CS.
    IPR004001. Actin_CS.
    [Graphical view ]
    PANTHERi PTHR11937. PTHR11937. 1 hit.
    Pfami PF00022. Actin. 1 hit.
    [Graphical view ]
    PRINTSi PR00190. ACTIN.
    SMARTi SM00268. ACTIN. 1 hit.
    [Graphical view ]
    PROSITEi PS00406. ACTINS_1. 1 hit.
    PS00432. ACTINS_2. 1 hit.
    PS01132. ACTINS_ACT_LIKE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Berkeley.
    3. Cited for: GENOME REANNOTATION.
      Strain: Berkeley.
    4. 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 366-376.
      Strain: Canton-S.
    9. "Direct redox regulation of F-actin assembly and disassembly by Mical."
      Hung R.J., Pak C.W., Terman J.R.
      Science 334:1710-1713(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: OXIDATION AT MET-45 AND MET-48, MUTAGENESIS OF MET-45 AND MET-48.
    10. "Involvement of Rab6 in the regulation of phagocytosis against virus infection in invertebrates."
      Ye T., Tang W., Zhang X.
      J. Proteome Res. 11:4834-4846(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RAB6.

    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: October 1, 2014
    This is version 141 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

    External Data

    Dasty 3