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P62737

- ACTA_MOUSE

UniProt

P62737 - ACTA_MOUSE

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Protein

Actin, aortic smooth muscle

Gene

Acta2

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. ATP binding Source: UniProtKB-KW
  2. protein kinase binding Source: ParkinsonsUK-UCL

GO - Biological processi

  1. glomerular mesangial cell development Source: Ensembl
  2. regulation of blood pressure Source: MGI
  3. response to virus Source: Ensembl
  4. vascular smooth muscle contraction Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Muscle protein

Keywords - Ligandi

ATP-binding, Nucleotide-binding

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: Chromosome 19

Organism-specific databases

MGIiMGI:87909. Acta2.

Subcellular locationi

GO - Cellular componenti

  1. actin cytoskeleton Source: MGI
  2. cytoplasm Source: MGI
  3. cytoskeleton Source: MGI
  4. extracellular space Source: Ensembl
  5. protein complex Source: Ensembl
  6. 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

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.
GenevestigatoriP62737.

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.

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.
OMAiNSICVIL.
OrthoDBiEOG72RMZ1.
PhylomeDBiP62737.
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.

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:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
X13297 mRNA. Translation: CAA31659.1 .
AK017374 mRNA. Translation: BAB30715.1 .
BC064800 mRNA. Translation: AAH64800.1 .
M57409 Genomic DNA. No translation available.
CCDSi CCDS29757.1.
PIRi S02135. A22224.
RefSeqi NP_031418.1. NM_007392.3.
UniGenei Mm.213025.

3D structure databases

ProteinModelPortali P62737.
SMRi P62737. Positions 4-377.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 197952. 3 interactions.
IntActi P62737. 8 interactions.
MINTi MINT-4086753.

PTM databases

PhosphoSitei P62737.

2D gel databases

REPRODUCTION-2DPAGE P62737.
UCD-2DPAGE P62737.

Proteomic databases

MaxQBi P62737.
PaxDbi P62737.
PRIDEi P62737.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000039631 ; ENSMUSP00000048218 ; ENSMUSG00000035783 .
GeneIDi 11475.
KEGGi mmu:11475.
UCSCi uc008hgg.1. mouse.

Organism-specific databases

CTDi 59.
MGIi MGI:87909. Acta2.

Phylogenomic databases

eggNOGi COG5277.
GeneTreei ENSGT00760000118957.
HOGENOMi HOG000233340.
HOVERGENi HBG003771.
InParanoidi P62737.
KOi K12313.
OMAi NSICVIL.
OrthoDBi EOG72RMZ1.
PhylomeDBi P62737.
TreeFami TF354237.

Miscellaneous databases

NextBioi 278816.
PROi P62737.
SOURCEi Search...

Gene expression databases

Bgeei P62737.
CleanExi MM_ACTA2.
Genevestigatori P62737.

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. "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: October 29, 2014
This is version 95 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