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P68033

- ACTC_MOUSE

UniProt

P68033 - ACTC_MOUSE

Protein

Actin, alpha cardiac muscle 1

Gene

Actc1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 88 (01 Oct 2014)
      Sequence version 1 (20 Mar 1987)
      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. ATPase activity Source: Ensembl
    2. ATP binding Source: UniProtKB-KW

    GO - Biological processi

    1. actin-mediated cell contraction Source: MGI
    2. actin-myosin filament sliding Source: Ensembl
    3. actomyosin structure organization Source: MGI
    4. cardiac muscle contraction Source: Ensembl
    5. cardiac muscle tissue morphogenesis Source: MGI
    6. cardiac myofibril assembly Source: MGI
    7. negative regulation of apoptotic process Source: MGI
    8. response to drug Source: Ensembl
    9. response to ethanol Source: Ensembl
    10. skeletal muscle thin filament assembly Source: MGI

    Keywords - Molecular functioni

    Muscle protein

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Actin, alpha cardiac muscle 1
    Alternative name(s):
    Alpha-cardiac actin
    Gene namesi
    Name:Actc1
    Synonyms:Actc
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 2

    Organism-specific databases

    MGIiMGI:87905. Actc1.

    Subcellular locationi

    GO - Cellular componenti

    1. actomyosin, actin portion Source: Ensembl
    2. extracellular vesicular exosome Source: Ensembl
    3. I band Source: MGI

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Propeptidei1 – 22Removed in mature formBy similarityPRO_0000000814
    Chaini3 – 377375Actin, alpha cardiac muscle 1PRO_0000000815Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei3 – 31N-acetylaspartateBy similarity
    Modified residuei46 – 461Methionine (R)-sulfoxide1 Publication
    Modified residuei49 – 491Methionine (R)-sulfoxide1 Publication
    Modified residuei75 – 751Tele-methylhistidineBy similarity
    Modified residuei86 – 861N6-methyllysineBy similarity

    Post-translational modificationi

    Oxidation of Met-46 and Met-49 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-86 (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

    PRIDEiP68033.

    PTM databases

    PhosphoSiteiP68033.

    Expressioni

    Gene expression databases

    ArrayExpressiP68033.
    BgeeiP68033.
    CleanExiMM_ACTC1.
    GenevestigatoriP68033.

    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.

    Protein-protein interaction databases

    BioGridi197945. 6 interactions.
    IntActiP68033. 3 interactions.
    MINTiMINT-1868869.

    Structurei

    3D structure databases

    ProteinModelPortaliP68033.
    SMRiP68033. Positions 6-377.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the actin family.Curated

    Phylogenomic databases

    HOGENOMiHOG000233340.
    HOVERGENiHBG003771.
    InParanoidiP68033.
    KOiK12314.
    OMAiGGERFRC.
    OrthoDBiEOG72RMZ1.
    PhylomeDBiP68033.
    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.

    P68033-1 [UniParc]FASTAAdd to Basket

    « Hide

    MCDDEETTAL VCDNGSGLVK AGFAGDDAPR AVFPSIVGRP RHQGVMVGMG    50
    QKDSYVGDEA QSKRGILTLK YPIEHGIITN WDDMEKIWHH TFYNELRVAP 100
    EEHPTLLTEA PLNPKANREK MTQIMFETFN VPAMYVAIQA VLSLYASGRT 150
    TGIVLDSGDG VTHNVPIYEG YALPHAIMRL DLAGRDLTDY LMKILTERGY 200
    SFVTTAEREI VRDIKEKLCY VALDFENEMA TAASSSSLEK SYELPDGQVI 250
    TIGNERFRCP ETLFQPSFIG MESAGIHETT YNSIMKCDID IRKDLYANNV 300
    LSGGTTMYPG IADRMQKEIT ALAPSTMKIK IIAPPERKYS VWIGGSILAS 350
    LSTFQQMWIS KQEYDEAGPS IVHRKCF 377
    Length:377
    Mass (Da):42,019
    Last modified:March 20, 1987 - v1
    Checksum:iE5C10FA19730CAD2
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK014303 mRNA. Translation: BAB29258.1.
    BC062138 mRNA. Translation: AAH62138.1.
    M15501 mRNA. Translation: AAA37167.1.
    CCDSiCCDS16564.1.
    PIRiA54728.
    RefSeqiNP_033738.1. NM_009608.3.
    UniGeneiMm.686.

    Genome annotation databases

    EnsembliENSMUST00000090269; ENSMUSP00000087736; ENSMUSG00000068614.
    GeneIDi11464.
    KEGGimmu:11464.
    UCSCiuc008lpz.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK014303 mRNA. Translation: BAB29258.1 .
    BC062138 mRNA. Translation: AAH62138.1 .
    M15501 mRNA. Translation: AAA37167.1 .
    CCDSi CCDS16564.1.
    PIRi A54728.
    RefSeqi NP_033738.1. NM_009608.3.
    UniGenei Mm.686.

    3D structure databases

    ProteinModelPortali P68033.
    SMRi P68033. Positions 6-377.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 197945. 6 interactions.
    IntActi P68033. 3 interactions.
    MINTi MINT-1868869.

    PTM databases

    PhosphoSitei P68033.

    Proteomic databases

    PRIDEi P68033.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000090269 ; ENSMUSP00000087736 ; ENSMUSG00000068614 .
    GeneIDi 11464.
    KEGGi mmu:11464.
    UCSCi uc008lpz.1. mouse.

    Organism-specific databases

    CTDi 70.
    MGIi MGI:87905. Actc1.

    Phylogenomic databases

    HOGENOMi HOG000233340.
    HOVERGENi HBG003771.
    InParanoidi P68033.
    KOi K12314.
    OMAi GGERFRC.
    OrthoDBi EOG72RMZ1.
    PhylomeDBi P68033.
    TreeFami TF354237.

    Miscellaneous databases

    NextBioi 278788.
    PROi P68033.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P68033.
    Bgeei P68033.
    CleanExi MM_ACTC1.
    Genevestigatori P68033.

    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. "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.
      Tissue: Head.
    2. "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].
      Tissue: Limb.
    3. "The structure of a cDNA clone corresponding to mouse cardiac muscle actin mRNA."
      Leader D.P., Gall I., Campbell P.C.
      Biosci. Rep. 6:741-747(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 3-377.
    4. Lubec G., Sunyer B., Chen W.-Q.
      Submitted (JAN-2009) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 71-97 AND 241-256, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: OF1.
      Tissue: Hippocampus.
    5. "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-46 AND MET-49, DEOXIDATION AT MET-46 AND MET-49.

    Entry informationi

    Entry nameiACTC_MOUSE
    AccessioniPrimary (citable) accession number: P68033
    Secondary accession number(s): P04270
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 20, 1987
    Last sequence update: March 20, 1987
    Last modified: October 1, 2014
    This is version 88 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