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Protein

Actin, alpha cardiac muscle 1

Gene

Actc1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: 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: MGI
  2. ATP binding Source: MGI
  3. myosin binding Source: MGI

GO - Biological processi

  1. actin filament-based movement Source: MGI
  2. actin-mediated cell contraction Source: MGI
  3. actin-myosin filament sliding Source: MGI
  4. actomyosin structure organization Source: MGI
  5. ATP catabolic process Source: MGI
  6. cardiac muscle contraction Source: Ensembl
  7. cardiac muscle tissue morphogenesis Source: MGI
  8. cardiac myofibril assembly Source: MGI
  9. heart contraction Source: MGI
  10. negative regulation of apoptotic process Source: MGI
  11. response to drug Source: Ensembl
  12. response to ethanol Source: Ensembl
  13. skeletal muscle thin filament assembly Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Muscle protein

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_232053. Striated Muscle Contraction.

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. actin filament Source: MGI
  2. actomyosin, actin portion Source: MGI
  3. blood microparticle Source: MGI
  4. cytoplasm Source: MGI
  5. extracellular space Source: MGI
  6. extracellular vesicular exosome Source: MGI
  7. focal adhesion Source: MGI
  8. I band Source: MGI
  9. membrane Source: MGI
  10. sarcomere Source: MGI
Complete GO annotation...

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 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

Methylation, Oxidation

Proteomic databases

MaxQBiP68033.
PRIDEiP68033.

PTM databases

PhosphoSiteiP68033.

Expressioni

Gene expression databases

BgeeiP68033.
CleanExiMM_ACTC1.
ExpressionAtlasiP68033. baseline and differential.
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.
OMAiQMITIGA.
OrthoDBiEOG72RMZ1.
PhylomeDBiP68033.
TreeFamiTF354237.

Family and domain databases

InterProiIPR004000. Actin.
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

        10         20         30         40         50
MCDDEETTAL VCDNGSGLVK AGFAGDDAPR AVFPSIVGRP RHQGVMVGMG
60 70 80 90 100
QKDSYVGDEA QSKRGILTLK YPIEHGIITN WDDMEKIWHH TFYNELRVAP
110 120 130 140 150
EEHPTLLTEA PLNPKANREK MTQIMFETFN VPAMYVAIQA VLSLYASGRT
160 170 180 190 200
TGIVLDSGDG VTHNVPIYEG YALPHAIMRL DLAGRDLTDY LMKILTERGY
210 220 230 240 250
SFVTTAEREI VRDIKEKLCY VALDFENEMA TAASSSSLEK SYELPDGQVI
260 270 280 290 300
TIGNERFRCP ETLFQPSFIG MESAGIHETT YNSIMKCDID IRKDLYANNV
310 320 330 340 350
LSGGTTMYPG IADRMQKEIT ALAPSTMKIK IIAPPERKYS VWIGGSILAS
360 370
LSTFQQMWIS KQEYDEAGPS IVHRKCF
Length:377
Mass (Da):42,019
Last modified:March 20, 1987 - v1
Checksum:iE5C10FA19730CAD2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

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

Protein-protein interaction databases

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

PTM databases

PhosphoSiteiP68033.

Proteomic databases

MaxQBiP68033.
PRIDEiP68033.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi70.
MGIiMGI:87905. Actc1.

Phylogenomic databases

HOGENOMiHOG000233340.
HOVERGENiHBG003771.
InParanoidiP68033.
KOiK12314.
OMAiQMITIGA.
OrthoDBiEOG72RMZ1.
PhylomeDBiP68033.
TreeFamiTF354237.

Enzyme and pathway databases

ReactomeiREACT_232053. Striated Muscle Contraction.

Miscellaneous databases

NextBioi278788.
PROiP68033.
SOURCEiSearch...

Gene expression databases

BgeeiP68033.
CleanExiMM_ACTC1.
ExpressionAtlasiP68033. baseline and differential.
GenevestigatoriP68033.

Family and domain databases

InterProiIPR004000. Actin.
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]
ProtoNetiSearch...

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: March 4, 2015
This is version 93 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

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.