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P63260

- ACTG_MOUSE

UniProt

P63260 - ACTG_MOUSE

Protein

Actin, cytoplasmic 2

Gene

Actg1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 103 (01 Oct 2014)
      Sequence version 1 (21 Jul 1986)
      Previous versions | rss
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    Functioni

    Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. protein binding Source: IntAct
    3. structural constituent of cytoskeleton Source: MGI

    GO - Biological processi

    1. sarcomere organization Source: MGI

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_198374. Regulation of actin dynamics for phagocytic cup formation.
    REACT_199054. Translocation of GLUT4 to the plasma membrane.
    REACT_209040. Gap junction degradation.
    REACT_220352. Formation of annular gap junctions.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Actin, cytoplasmic 2
    Alternative name(s):
    Gamma-actin
    Cleaved into the following chain:
    Gene namesi
    Name:Actg1
    Synonyms:Actg
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 11

    Organism-specific databases

    MGIiMGI:87906. Actg1.

    Subcellular locationi

    GO - Cellular componenti

    1. actin cytoskeleton Source: MGI
    2. costamere Source: MGI
    3. cytosol Source: Reactome
    4. extracellular vesicular exosome Source: Ensembl
    5. filamentous actin Source: MGI
    6. myofibril Source: MGI

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 375375Actin, cytoplasmic 2PRO_0000367101Add
    BLAST
    Initiator methioninei1 – 11Removed; alternate1 Publication
    Chaini2 – 375374Actin, cytoplasmic 2, N-terminally processedPRO_0000000833Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionineBy similarity
    Modified residuei2 – 21N-acetylglutamate; in Actin, cytoplasmic 2, N-terminally processed1 Publication
    Modified residuei44 – 441Methionine (R)-sulfoxide1 Publication
    Modified residuei47 – 471Methionine (R)-sulfoxide1 Publication
    Modified residuei73 – 731Tele-methylhistidine1 Publication
    Modified residuei84 – 841N6-methyllysineBy similarity

    Post-translational modificationi

    Oxidation of Met-44 and Met-47 by MICALs (MICAL1, MICAL2 or MICAL3) to form methionine sulfoxide promotes actin filament depolymerization. MICAL1 and MICAL2 produce the (R)-S-oxide form. The (R)-S-oxide form is reverted by MSRB1 and MSRB2, which promote actin repolymerization.1 Publication
    Monomethylation at Lys-84 (K84me1) regulates actin-myosin interaction and actomyosin-dependent processes. Demethylation by ALKBH4 is required for maintaining actomyosin dynamics supporting normal cleavage furrow ingression during cytokinesis and cell migration By similarity.By similarity

    Keywords - PTMi

    Acetylation, Methylation, Oxidation

    Proteomic databases

    MaxQBiP63260.
    PRIDEiP63260.

    2D gel databases

    COMPLUYEAST-2DPAGEP63260.
    REPRODUCTION-2DPAGEP63260.
    UCD-2DPAGEP63260.

    PTM databases

    PhosphoSiteiP63260.

    Miscellaneous databases

    PMAP-CutDBP63260.

    Expressioni

    Gene expression databases

    BgeeiP63260.
    CleanExiMM_ACTG1.
    GenevestigatoriP63260.

    Interactioni

    Subunit structurei

    Polymerization of globular actin (G-actin) leads to a structural filament (F-actin) in the form of a two-stranded helix. Each actin can bind to 4 others.

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Kcnma1Q084604EBI-351301,EBI-1633915

    Protein-protein interaction databases

    BioGridi197946. 19 interactions.
    IntActiP63260. 25 interactions.

    Structurei

    3D structure databases

    ProteinModelPortaliP63260.
    SMRiP63260. Positions 6-375.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the actin family.Curated

    Phylogenomic databases

    HOGENOMiHOG000233340.
    HOVERGENiHBG003771.
    KOiK05692.
    OMAiDARAPIM.
    OrthoDBiEOG72RMZ1.
    PhylomeDBiP63260.
    TreeFamiTF354237.

    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.

    P63260-1 [UniParc]FASTAAdd to Basket

    « Hide

    MEEEIAALVI DNGSGMCKAG FAGDDAPRAV FPSIVGRPRH QGVMVGMGQK    50
    DSYVGDEAQS KRGILTLKYP IEHGIVTNWD DMEKIWHHTF YNELRVAPEE 100
    HPVLLTEAPL NPKANREKMT QIMFETFNTP AMYVAIQAVL SLYASGRTTG 150
    IVMDSGDGVT HTVPIYEGYA LPHAILRLDL AGRDLTDYLM KILTERGYSF 200
    TTTAEREIVR DIKEKLCYVA LDFEQEMATA ASSSSLEKSY ELPDGQVITI 250
    GNERFRCPEA LFQPSFLGME SCGIHETTFN SIMKCDVDIR KDLYANTVLS 300
    GGTTMYPGIA DRMQKEITAL APSTMKIKII APPERKYSVW IGGSILASLS 350
    TFQQMWISKQ EYDESGPSIV HRKCF 375
    Length:375
    Mass (Da):41,793
    Last modified:July 21, 1986 - v1
    Checksum:i54D08F986964EFD5
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X13055 mRNA. Translation: CAA31455.1.
    AK076081 mRNA. Translation: BAC36167.1.
    AK087983 mRNA. Translation: BAC40075.1.
    BC003337 mRNA. Translation: AAH03337.1.
    BC021796 mRNA. Translation: AAH21796.1.
    BC023248 mRNA. Translation: AAH23248.1.
    M21495 mRNA. Translation: AAA37168.1.
    CCDSiCCDS25730.1.
    PIRiA30243. ATMSG.
    RefSeqiNP_033739.1. NM_009609.2.
    UniGeneiMm.196173.
    Mm.426706.
    Mm.470166.

    Genome annotation databases

    EnsembliENSMUST00000071555; ENSMUSP00000071486; ENSMUSG00000062825.
    ENSMUST00000106215; ENSMUSP00000101822; ENSMUSG00000062825.
    GeneIDi11465.
    KEGGimmu:11465.
    UCSCiuc007msi.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X13055 mRNA. Translation: CAA31455.1 .
    AK076081 mRNA. Translation: BAC36167.1 .
    AK087983 mRNA. Translation: BAC40075.1 .
    BC003337 mRNA. Translation: AAH03337.1 .
    BC021796 mRNA. Translation: AAH21796.1 .
    BC023248 mRNA. Translation: AAH23248.1 .
    M21495 mRNA. Translation: AAA37168.1 .
    CCDSi CCDS25730.1.
    PIRi A30243. ATMSG.
    RefSeqi NP_033739.1. NM_009609.2.
    UniGenei Mm.196173.
    Mm.426706.
    Mm.470166.

    3D structure databases

    ProteinModelPortali P63260.
    SMRi P63260. Positions 6-375.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 197946. 19 interactions.
    IntActi P63260. 25 interactions.

    PTM databases

    PhosphoSitei P63260.

    2D gel databases

    COMPLUYEAST-2DPAGE P63260.
    REPRODUCTION-2DPAGE P63260.
    UCD-2DPAGE P63260.

    Proteomic databases

    MaxQBi P63260.
    PRIDEi P63260.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000071555 ; ENSMUSP00000071486 ; ENSMUSG00000062825 .
    ENSMUST00000106215 ; ENSMUSP00000101822 ; ENSMUSG00000062825 .
    GeneIDi 11465.
    KEGGi mmu:11465.
    UCSCi uc007msi.1. mouse.

    Organism-specific databases

    CTDi 71.
    MGIi MGI:87906. Actg1.

    Phylogenomic databases

    HOGENOMi HOG000233340.
    HOVERGENi HBG003771.
    KOi K05692.
    OMAi DARAPIM.
    OrthoDBi EOG72RMZ1.
    PhylomeDBi P63260.
    TreeFami TF354237.

    Enzyme and pathway databases

    Reactomei REACT_198374. Regulation of actin dynamics for phagocytic cup formation.
    REACT_199054. Translocation of GLUT4 to the plasma membrane.
    REACT_209040. Gap junction degradation.
    REACT_220352. Formation of annular gap junctions.

    Miscellaneous databases

    ChiTaRSi ACTG1. mouse.
    NextBioi 278792.
    PMAP-CutDB P63260.
    PROi P63260.
    SOURCEi Search...

    Gene expression databases

    Bgeei P63260.
    CleanExi MM_ACTG1.
    Genevestigatori P63260.

    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. "Actin amino-acid sequences. Comparison of actins from calf thymus, bovine brain, and SV40-transformed mouse 3T3 cells with rabbit skeletal muscle actin."
      Vandekerckhove J., Weber K.
      Eur. J. Biochem. 90:451-462(1978) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-375, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT GLU-2, METHYLATION AT HIS-73.
    2. "Isolation of cDNA clones for mouse cytoskeletal gamma-actin and differential expression of cytoskeletal actin mRNAs in mouse cells."
      Tokunaga K., Takeda K., Kamiyama K., Kageyama H., Takenaga K., Sakiyama S.
      Mol. Cell. Biol. 8:3929-3933(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J and NOD.
      Tissue: Thymus.
    4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: FVB/N and NMRI.
      Tissue: Colon and Mammary tumor.
    5. "Mouse cytoskeletal gamma-actin: analysis and implications of the structure of cloned cDNA and processed pseudogenes."
      Peter B., Man Y.M., Begg C.E., Gall I., Leader D.P.
      J. Mol. Biol. 203:665-675(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 8-375.
    6. Lubec G., Yang J.W., Zigmond M.
      Submitted (JUL-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 29-39.
      Tissue: Brain.
    7. "MsrB1 and MICALs regulate actin assembly and macrophage function via reversible stereoselective methionine oxidation."
      Lee B.C., Peterfi Z., Hoffmann F.W., Moore R.E., Kaya A., Avanesov A., Tarrago L., Zhou Y., Weerapana E., Fomenko D.E., Hoffmann P.R., Gladyshev V.N.
      Mol. Cell 51:397-404(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: OXIDATION AT MET-44 AND MET-47, DEOXIDATION AT MET-44 AND MET-47.

    Entry informationi

    Entry nameiACTG_MOUSE
    AccessioniPrimary (citable) accession number: P63260
    Secondary accession number(s): P02571, P14104, P99022
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: July 21, 1986
    Last modified: October 1, 2014
    This is version 103 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    In vertebrates 3 main groups of actin isoforms, alpha, beta and gamma have been identified. The alpha actins are found in muscle tissues and are a major constituent of the contractile apparatus. The beta and gamma actins coexist in most cell types as components of the cytoskeleton and as mediators of internal cell motility.

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3