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Protein

Actin, aortic smooth muscle

Gene

Acta2

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

  • ATP binding Source: UniProtKB-KW
  • protein kinase binding Source: ParkinsonsUK-UCL

GO - Biological processi

  • glomerular mesangial cell development Source: Ensembl
  • mesenchyme migration Source: AgBase
  • positive regulation of gene expression Source: AgBase
  • regulation of blood pressure Source: MGI
  • response to virus Source: Ensembl
  • vascular smooth muscle contraction Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Muscle protein

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_324232. Smooth Muscle Contraction.

Names & Taxonomyi

Protein namesi
Recommended name:
Actin, aortic smooth muscle
Alternative name(s):
Alpha-actin-2
Gene namesi
Name:Acta2
Synonyms:Actsa, Actvs
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 19

Organism-specific databases

MGIiMGI:87909. Acta2.

Subcellular locationi

GO - Cellular componenti

  • actin cytoskeleton Source: MGI
  • cell body Source: AgBase
  • cytoplasm Source: MGI
  • cytoskeleton Source: MGI
  • extracellular exosome Source: MGI
  • extracellular space Source: MGI
  • filopodium Source: AgBase
  • lamellipodium Source: AgBase
  • protein complex Source: Ensembl
  • smooth muscle contractile fiber Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Propeptidei1 – 22Removed in mature form1 PublicationPRO_0000000740
Chaini3 – 377375Actin, aortic smooth musclePRO_0000000741Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei3 – 31N-acetylglutamate1 Publication
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

MaxQBiP62737.
PaxDbiP62737.
PRIDEiP62737.

2D gel databases

REPRODUCTION-2DPAGEP62737.
UCD-2DPAGEP62737.

PTM databases

PhosphoSiteiP62737.

Expressioni

Gene expression databases

BgeeiP62737.
CleanExiMM_ACTA2.
GenevisibleiP62737. MM.

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

BioGridi197952. 3 interactions.
IntActiP62737. 8 interactions.
MINTiMINT-4086753.
STRINGi10090.ENSMUSP00000048218.

Structurei

3D structure databases

ProteinModelPortaliP62737.
SMRiP62737. Positions 4-377.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the actin family.Curated

Phylogenomic databases

eggNOGiCOG5277.
GeneTreeiENSGT00760000118957.
HOGENOMiHOG000233340.
HOVERGENiHBG003771.
InParanoidiP62737.
KOiK12313.
OMAiAMCEEED.
OrthoDBiEOG72RMZ1.
PhylomeDBiP62737.
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.

P62737-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MCEEEDSTAL VCDNGSGLCK AGFAGDDAPR AVFPSIVGRP RHQGVMVGMG
60 70 80 90 100
QKDSYVGDEA QSKRGILTLK YPIEHGIITN WDDMEKIWHH SFYNELRVAP
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):42,009
Last modified:August 16, 2004 - v1
Checksum:i2D0543262DB35CA5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X13297 mRNA. Translation: CAA31659.1.
AK017374 mRNA. Translation: BAB30715.1.
BC064800 mRNA. Translation: AAH64800.1.
M57409 Genomic DNA. No translation available.
CCDSiCCDS29757.1.
PIRiS02135. A22224.
RefSeqiNP_031418.1. NM_007392.3.
UniGeneiMm.213025.

Genome annotation databases

EnsembliENSMUST00000039631; ENSMUSP00000048218; ENSMUSG00000035783.
GeneIDi11475.
KEGGimmu:11475.
UCSCiuc008hgg.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X13297 mRNA. Translation: CAA31659.1.
AK017374 mRNA. Translation: BAB30715.1.
BC064800 mRNA. Translation: AAH64800.1.
M57409 Genomic DNA. No translation available.
CCDSiCCDS29757.1.
PIRiS02135. A22224.
RefSeqiNP_031418.1. NM_007392.3.
UniGeneiMm.213025.

3D structure databases

ProteinModelPortaliP62737.
SMRiP62737. Positions 4-377.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi197952. 3 interactions.
IntActiP62737. 8 interactions.
MINTiMINT-4086753.
STRINGi10090.ENSMUSP00000048218.

PTM databases

PhosphoSiteiP62737.

2D gel databases

REPRODUCTION-2DPAGEP62737.
UCD-2DPAGEP62737.

Proteomic databases

MaxQBiP62737.
PaxDbiP62737.
PRIDEiP62737.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000039631; ENSMUSP00000048218; ENSMUSG00000035783.
GeneIDi11475.
KEGGimmu:11475.
UCSCiuc008hgg.1. mouse.

Organism-specific databases

CTDi59.
MGIiMGI:87909. Acta2.

Phylogenomic databases

eggNOGiCOG5277.
GeneTreeiENSGT00760000118957.
HOGENOMiHOG000233340.
HOVERGENiHBG003771.
InParanoidiP62737.
KOiK12313.
OMAiAMCEEED.
OrthoDBiEOG72RMZ1.
PhylomeDBiP62737.
TreeFamiTF354237.

Enzyme and pathway databases

ReactomeiREACT_324232. Smooth Muscle Contraction.

Miscellaneous databases

NextBioi278816.
PROiP62737.
SOURCEiSearch...

Gene expression databases

BgeeiP62737.
CleanExiMM_ACTA2.
GenevisibleiP62737. MM.

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. "Nucleotide sequence of a mouse vascular smooth muscle alpha-actin cDNA."
    Min B.H., Strauch A.R., Foster D.N.
    Nucleic Acids Res. 16:10374-10374(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: C3H.
  2. "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.
  3. "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: C3H/He.
    Tissue: Osteoblast.
  4. "A vascular smooth muscle alpha-isoactin biosynthetic intermediate in BC3H1 cells. Identification of acetylcysteine at the NH2 terminus."
    Strauch A.R., Rubenstein P.A.
    J. Biol. Chem. 259:7224-7229(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 3-20, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT GLU-3.
  5. "The 5'-flanking region of the mouse vascular smooth muscle alpha-actin gene contains evolutionarily conserved sequence motifs within a functional promoter."
    Min B.H., Foster D.N., Strauch A.R.
    J. Biol. Chem. 265:16667-16675(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-7.
  6. Lubec G., Kang S.U., Sunyer B., Chen W.-Q.
    Submitted (JAN-2009) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 21-41; 53-63; 71-86; 98-115; 186-193; 241-256 AND 318-328, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: C57BL/6 and OF1.
    Tissue: Brain and Hippocampus.
  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-46 AND MET-49, DEOXIDATION AT MET-46 AND MET-49.

Entry informationi

Entry nameiACTA_MOUSE
AccessioniPrimary (citable) accession number: P62737
Secondary accession number(s): P03996, P04108
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 23, 1986
Last sequence update: August 16, 2004
Last modified: June 24, 2015
This is version 102 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.