P62737 (ACTA_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Actin, aortic smooth muscle

Alternative name(s):
Alpha-actin-2

Gene names

Name:	Acta2
Synonyms:	Actsa, Actvs

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	377 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.
Subunit structure	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.
Subcellular location	Cytoplasm › cytoskeleton.
Post-translational modification	Oxidation of Met-46 by MICALs (MICAL1, MICAL2 or MICAL3) to form methionine sulfoxide promotes actin filament depolymerization. Methionine sulfoxide is produced stereospecifically, but it is not known whether the (S)-S-oxide or the (R)-S-oxide is produced By similarity.
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.
Sequence similarities	Belongs to the actin family.

Ontologies

Keywords
Cellular component	Cytoplasm Cytoskeleton
Ligand	ATP-binding Nucleotide-binding
Molecular function	Muscle protein
PTM	Acetylation Methylation Oxidation
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	glomerular mesangial cell development Inferred from electronic annotation. Source: Compara regulation of blood pressure Inferred from mutant phenotype PubMed 11053242. Source: MGI response to virus Inferred from electronic annotation. Source: Compara vascular smooth muscle contraction Inferred from mutant phenotype PubMed 11053242. Source: MGI
Cellular_component	actin cytoskeleton Inferred from direct assay PubMed 17882221. Source: MGI protein complex Inferred from electronic annotation. Source: Compara smooth muscle contractile fiber Inferred from direct assay PubMed 18332105. Source: MGI
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Propeptide	1 – 2	2	Removed in mature form		PRO_0000000740
	Chain	3 – 377	375	Actin, aortic smooth muscle		PRO_0000000741
Amino acid modifications
	Modified residue	3	1	N-acetylglutamate
	Modified residue	46	1	Methionine sulfoxide By similarity
	Modified residue	75	1	Tele-methylhistidine By similarity

Sequences

	Sequence		Length	Mass (Da)
	P62737 [UniParc]. Last modified August 16, 2004. Version 1. Checksum: 2D0543262DB35CA5	FASTA	377	42,009
	10 20 30 40 50 60 MCEEEDSTAL VCDNGSGLCK AGFAGDDAPR AVFPSIVGRP RHQGVMVGMG QKDSYVGDEA 70 80 90 100 110 120 QSKRGILTLK YPIEHGIITN WDDMEKIWHH SFYNELRVAP EEHPTLLTEA PLNPKANREK 130 140 150 160 170 180 MTQIMFETFN VPAMYVAIQA VLSLYASGRT TGIVLDSGDG VTHNVPIYEG YALPHAIMRL 190 200 210 220 230 240 DLAGRDLTDY LMKILTERGY SFVTTAEREI VRDIKEKLCY VALDFENEMA TAASSSSLEK 250 260 270 280 290 300 SYELPDGQVI TIGNERFRCP ETLFQPSFIG MESAGIHETT YNSIMKCDID IRKDLYANNV 310 320 330 340 350 360 LSGGTTMYPG IADRMQKEIT ALAPSTMKIK IIAPPERKYS VWIGGSILAS LSTFQQMWIS 370 KQEYDEAGPS IVHRKCF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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.
[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, MASS SPECTROMETRY. Strain: C57BL/6 and OF1. Tissue: Brain and Hippocampus.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X13297 mRNA. Translation: CAA31659.1. AK017374 mRNA. Translation: BAB30715.1. BC064800 mRNA. Translation: AAH64800.1. M57409 Genomic DNA. No translation available.
IPI	IPI00117043.
PIR	A22224. S02135.
RefSeq	NP_031418.1. NM_007392.3.
UniGene	Mm.213025.
3D structure databases
ProteinModelPortal	P62737.
ModBase	Search...
Protein-protein interaction databases
IntAct	P62737. 3 interactions.
PTM databases
PhosphoSite	P62737.
2D gel databases
REPRODUCTION-2DPAGE	P62737.
UCD-2DPAGE	P62737.
Proteomic databases
PaxDb	P62737.
PRIDE	P62737.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000039631; ENSMUSP00000048218; ENSMUSG00000035783.
GeneID	11475.
KEGG	mmu:11475.
Organism-specific databases
CTD	59.
MGI	MGI:87909. Acta2.
Phylogenomic databases
eggNOG	COG5277.
GeneTree	ENSGT00690000101919.
HOGENOM	HOG000233340.
HOVERGEN	HBG003771.
InParanoid	P62737.
KO	K12313.
OMA	NSICVIL.
OrthoDB	EOG4W9J40.
Gene expression databases
Bgee	P62737.
CleanEx	MM_ACTA2.
Genevestigator	P62737.
GermOnline	ENSMUSG00000035783. Mus musculus.
Family and domain databases
InterPro	IPR004000. Actin-related. IPR020902. Actin/actin-like_CS. IPR004001. Actin_CS. [Graphical view]
PANTHER	PTHR11937. PTHR11937. 1 hit.
Pfam	PF00022. Actin. 1 hit. [Graphical view]
PRINTS	PR00190. ACTIN.
SMART	SM00268. ACTIN. 1 hit. [Graphical view]
PROSITE	PS00406. ACTINS_1. 1 hit. PS00432. ACTINS_2. 1 hit. PS01132. ACTINS_ACT_LIKE. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	278816.
SOURCE	Search...

Entry information

Entry name

ACTA_MOUSE

Accession

Primary (citable) accession number: P62737
Secondary accession number(s): P03996, P04108

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 23, 1986
Last sequence update:	August 16, 2004
Last modified:	May 1, 2013
This is version 82 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program