P09671 (SODM_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Superoxide dismutase [Mn], mitochondrial
EC=1.15.1.1

Gene names

Name:	Sod2
Synonyms:	Sod-2

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	222 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	Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems.
Catalytic activity	2 superoxide + 2 H+ = O2 + H2O2.
Cofactor	Binds 1 manganese ion per subunit By similarity.
Subunit structure	Homotetramer.
Subcellular location	Mitochondrion matrix.
Induction	Expression is regulated by KRIT1. Ref.9
Post-translational modification	Nitrated under oxidative stress. Nitration coupled with oxidation inhibits the catalytic activity By similarity.
Sequence similarities	Belongs to the iron/manganese superoxide dismutase family.

Ontologies

Keywords
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	Manganese Metal-binding
Molecular function	Oxidoreductase
PTM	Acetylation Nitration
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	age-dependent response to reactive oxygen species Inferred from sequence or structural similarity. Source: UniProtKB cellular response to ethanol Inferred from electronic annotation. Source: Compara detection of oxygen Inferred from mutant phenotype PubMed 11156968. Source: MGI erythrophore differentiation Inferred from mutant phenotype PubMed 15205258. Source: MGI glutathione metabolic process Inferred from mutant phenotype PubMed 10049502. Source: MGI heart development Inferred from mutant phenotype PubMed 7493016. Source: MGI hemopoiesis Inferred from mutant phenotype PubMed 16219542PubMed 8790408. Source: MGI hydrogen peroxide biosynthetic process Inferred from electronic annotation. Source: Compara iron ion homeostasis Inferred from mutant phenotype PubMed 15205258. Source: MGI liver development Inferred from mutant phenotype PubMed 17367743. Source: MGI locomotory behavior Inferred from mutant phenotype PubMed 8790408. Source: MGI negative regulation of apoptotic process Inferred from mutant phenotype PubMed 15642323. Source: MGI negative regulation of fat cell differentiation Inferred from mutant phenotype PubMed 16219542. Source: MGI negative regulation of fibroblast proliferation Inferred from direct assay PubMed 18218638. Source: MGI negative regulation of neuron apoptotic process Inferred from electronic annotation. Source: Compara neuron development Inferred from mutant phenotype PubMed 8790408. Source: MGI oxygen homeostasis Inferred from electronic annotation. Source: Compara positive regulation of nitric oxide biosynthetic process Inferred from mutant phenotype PubMed 15637112. Source: MGI post-embryonic development Inferred from mutant phenotype PubMed 7493016PubMed 8790408. Source: MGI protein homotetramerization Inferred from electronic annotation. Source: Compara regulation of catalytic activity Inferred from mutant phenotype PubMed 9927656. Source: MGI regulation of mitochondrial membrane potential Inferred from mutant phenotype PubMed 17367743. Source: MGI regulation of transcription from RNA polymerase II promoter Inferred from sequence or structural similarity. Source: UniProtKB release of cytochrome c from mitochondria Inferred from mutant phenotype PubMed 10212301PubMed 15642323. Source: MGI removal of superoxide radicals Inferred from mutant phenotype PubMed 16873728. Source: MGI respiratory electron transport chain Inferred from mutant phenotype PubMed 11226230PubMed 19478076. Source: MGI response to L-ascorbic acid Inferred from electronic annotation. Source: Compara response to activity Inferred from mutant phenotype PubMed 15781740. Source: MGI response to axon injury Inferred from mutant phenotype PubMed 16677818. Source: MGI response to cadmium ion Inferred from electronic annotation. Source: Compara response to drug Inferred from electronic annotation. Source: Compara response to electrical stimulus Inferred from electronic annotation. Source: Compara response to gamma radiation Inferred from genetic interaction PubMed 15182862. Source: MGI response to hydrogen peroxide Inferred from mutant phenotype PubMed 15642323. Source: MGI response to hyperoxia Inferred from mutant phenotype PubMed 11796207. Source: MGI response to hypoxia Inferred from electronic annotation. Source: Compara response to lipopolysaccharide Inferred from electronic annotation. Source: Compara response to manganese ion Inferred from electronic annotation. Source: Compara response to selenium ion Inferred from electronic annotation. Source: Compara response to silicon dioxide Inferred from electronic annotation. Source: Compara response to zinc ion Inferred from electronic annotation. Source: Compara superoxide anion generation Inferred from mutant phenotype PubMed 10212301PubMed 15781740PubMed 16677818. Source: MGI vasodilation by acetylcholine involved in regulation of systemic arterial blood pressure Inferred from mutant phenotype PubMed 16873728. Source: MGI
Cellular_component	mitochondrial inner membrane Inferred from direct assay PubMed 12865426. Source: MGI mitochondrial nucleoid Inferred from electronic annotation. Source: Compara
Molecular_function	DNA binding Inferred from electronic annotation. Source: Compara manganese ion binding Inferred from sequence or structural similarity. Source: UniProtKB oxygen binding Inferred from electronic annotation. Source: Compara superoxide dismutase activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Polg	P54099	2	EBI-1635071,EBI-863636
Tp53	P02340	2	EBI-1635071,EBI-474016

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 24	24	Mitochondrion
	Chain	25 – 222	198	Superoxide dismutase [Mn], mitochondrial		PRO_0000032871
Sites
	Metal binding	50	1	Manganese By similarity
	Metal binding	98	1	Manganese By similarity
	Metal binding	183	1	Manganese By similarity
	Metal binding	187	1	Manganese By similarity
Amino acid modifications
	Modified residue	58	1	Nitrated tyrosine By similarity
	Modified residue	68	1	N6-acetyllysine Ref.8
	Modified residue	130	1	N6-acetyllysine By similarity
Experimental info
	Sequence conflict	5	1	A → G in AAH18173. Ref.5
	Sequence conflict	18	1	G → V in CAA28645. Ref.1
	Sequence conflict	138	1	V → M Ref.1
	Sequence conflict	138	1	V → M Ref.3

Sequences

	Sequence		Length	Mass (Da)
	P09671 [UniParc]. Last modified July 15, 1998. Version 3. Checksum: 9AE804C55A8357D9	FASTA	222	24,603
	10 20 30 40 50 60 MLCRAACSTG RRLGPVAGAA GSRHKHSLPD LPYDYGALEP HINAQIMQLH HSKHHAAYVN 70 80 90 100 110 120 NLNATEEKYH EALAKGDVTT QVALQPALKF NGGGHINHTI FWTNLSPKGG GEPKGELLEA 130 140 150 160 170 180 IKRDFGSFEK FKEKLTAVSV GVQGSGWGWL GFNKEQGRLQ IAACSNQDPL QGTTGLIPLL 190 200 210 220 GIDVWEHAYY LQYKNVRPDY LKAIWNVINW ENVTERYTAC KK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence of a cDNA coding for mouse manganese superoxide dismutase." Hallewell R.A., Mullenbach G.T., Stempien M.M., Bell G.I. Nucleic Acids Res. 14:9539-9539(1986) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Placenta.
[2]	"Sequence of manganese superoxide dismutase-encoding cDNAs from multiple mouse organs." Sun Y., Hegamyer G., Colburn N.M. Gene 131:301-302(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: BALB/c and C3H.
[3]	"Cloning and characterization of the murine manganous superoxide dismutase-encoding gene." Jones P.L., Kucera G., Gordon H.M., Boss J.M. Gene 153:155-161(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]	"Structure and DNA sequence of the mouse MnSOD gene." Disilvestre D., Kleeberger S.R., Johns J., Levitt R.C. Mamm. Genome 6:281-284(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]	"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: Embryo and Kidney.
[6]	"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: Mammary gland.
[7]	Lubec G., Kang S.U., Klug S., Yang J.W., Zigmond M. Submitted (JUL-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 54-68; 76-108; 115-130 AND 203-216, MASS SPECTROMETRY. Strain: C57BL/6. Tissue: Brain and Hippocampus.
[8]	"Substrate and functional diversity of lysine acetylation revealed by a proteomics survey." Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T., Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y. Mol. Cell 23:607-618(2006) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-68, MASS SPECTROMETRY. Tissue: Liver.
[9]	"KRIT1 regulates the homeostasis of intracellular reactive oxygen species." Goitre L., Balzac F., Degani S., Degan P., Marchi S., Pinton P., Retta S.F. PLoS ONE 5:E11786-E11786(2010) [PubMed] [Europe PMC] [Abstract] Cited for: INDUCTION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X04972 mRNA. Translation: CAA28645.1. Z18857 mRNA. Translation: CAA79308.1. L35528 , L35525, L35526, L35527 Genomic DNA. Translation: AAB60902.1. S78846 , S78832, S78842, S78844 Genomic DNA. Translation: AAB34899.1. AK002428 mRNA. Translation: BAB22095.1. AK002534 mRNA. Translation: BAB22170.1. AK012354 mRNA. Translation: BAB28183.1. BC010548 mRNA. Translation: AAH10548.1. BC018173 mRNA. Translation: AAH18173.1.
IPI	IPI00109109.
PIR	I57023.
RefSeq	NP_038699.2. NM_013671.3.
UniGene	Mm.290876.
3D structure databases
ProteinModelPortal	P09671.
SMR	P09671. Positions 25-222.
ModBase	Search...
Protein-protein interaction databases
IntAct	P09671. 3 interactions.
PTM databases
PhosphoSite	P09671.
2D gel databases
REPRODUCTION-2DPAGE	IPI00109109. P09671.
SWISS-2DPAGE	P09671.
Proteomic databases
PaxDb	P09671.
PRIDE	P09671.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000007012; ENSMUSP00000007012; ENSMUSG00000006818.
GeneID	20656.
KEGG	mmu:20656.
Organism-specific databases
CTD	6648.
MGI	MGI:98352. Sod2.
Phylogenomic databases
eggNOG	COG0605.
HOGENOM	HOG000013583.
HOVERGEN	HBG004451.
InParanoid	P09671.
KO	K04564.
OMA	MAPPGKG.
OrthoDB	EOG4R503R.
Gene expression databases
ArrayExpress	P09671.
Bgee	P09671.
CleanEx	MM_SOD2.
Genevestigator	P09671.
GermOnline	ENSMUSG00000006818. Mus musculus.
Family and domain databases
InterPro	IPR001189. Mn/Fe_SOD. IPR019833. Mn/Fe_SOD_BS. IPR019832. Mn/Fe_SOD_C. IPR019831. Mn/Fe_SOD_N. [Graphical view]
PANTHER	PTHR11404. PTHR11404. 1 hit.
Pfam	PF02777. Sod_Fe_C. 1 hit. PF00081. Sod_Fe_N. 1 hit. [Graphical view]
PIRSF	PIRSF000349. SODismutase. 1 hit.
PRINTS	PR01703. MNSODISMTASE.
SUPFAM	SSF46609. SODismutase. 1 hit. SSF54719. SODismutase. 1 hit.
PROSITE	PS00088. SOD_MN. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	SOD2. mouse.
NextBio	299085.
SOURCE	Search...

Entry information

Entry name

SODM_MOUSE

Accession

Primary (citable) accession number: P09671
Secondary accession number(s): Q64670, Q8VEM5

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	July 15, 1998
Last modified:	April 3, 2013
This is version 138 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program