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P68033

- ACTC_MOUSE

UniProt

P68033 - ACTC_MOUSE

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Protein

Actin, alpha cardiac muscle 1

Gene
Actc1, Actc
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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
Complete GO annotation...

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
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

PTM / Processingi

Molecule processing

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

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei3 – 31N-acetylaspartate By similarity
Modified residuei46 – 461Methionine (R)-sulfoxide
Modified residuei49 – 491Methionine (R)-sulfoxide
Modified residuei75 – 751Tele-methylhistidine By similarity
Modified residuei86 – 861N6-methyllysine By 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.
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.

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.

Family & Domainsi

Sequence similaritiesi

Belongs to the actin family.

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 87 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

Similar proteinsi