Reviewed, UniProtKB/Swiss-Prot P08228 (SODC_MOUSE)

Names and origin

Protein names

Recommended name:
    Superoxide dismutase [Cu-Zn]
    EC=1.15.1.1

Gene names

Name:

Sod1

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	154 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 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 copper ion per subunit By similarity. Binds 1 zinc ion per subunit By similarity.
Subunit structure	Homodimer.
Subcellular location	Cytoplasm.
Sequence similarities	Belongs to the Cu-Zn superoxide dismutase family.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	Copper Metal-binding Zinc
Molecular function	Antioxidant Oxidoreductase
PTM	Acetylation Disulfide bond Phosphoprotein
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	DNA fragmentation involved in apoptosis Inferred from direct assay. Source: MGI activation of MAPK activity Inferred from direct assay. Source: MGI auditory receptor cell stereocilium organization Inferred from mutant phenotype. Source: MGI cell aging Inferred from sequence or structural similarity. Source: UniProtKB cellular iron ion homeostasis Inferred from mutant phenotype. Source: MGI double-strand break repair Inferred from mutant phenotype. Source: MGI embryo implantation Inferred from mutant phenotype. Source: MGI glutathione metabolic process Inferred from mutant phenotype. Source: MGI heart contraction Inferred from mutant phenotype. Source: MGI hydrogen peroxide biosynthetic process Inferred from mutant phenotype. Source: MGI locomotory behavior Inferred from mutant phenotype. Source: MGI muscle homeostasis Inferred from mutant phenotype. Source: MGI myelin maintenance in the peripheral nervous system Inferred from mutant phenotype. Source: MGI myeloid cell homeostasis Inferred from genetic interaction. Source: MGI negative regulation of cholesterol biosynthetic process Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of neuron apoptosis Inferred from mutant phenotype. Source: MGI neurofilament cytoskeleton organization Inferred from genetic interaction. Source: MGI ovarian follicle development Inferred from mutant phenotype. Source: MGI oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW positive regulation of cytokine production Inferred from sequence or structural similarity. Source: UniProtKB regulation of blood pressure Inferred from mutant phenotype. Source: MGI regulation of mitochondrial membrane potential Inferred from sequence or structural similarity. Source: UniProtKB regulation of multicellular organism growth Inferred from mutant phenotype. Source: MGI relaxation of vascular smooth muscle Inferred from mutant phenotype. Source: MGI removal of superoxide radicals Inferred from mutant phenotype. Source: MGI response to axon injury Inferred from mutant phenotype. Source: MGI response to drug Inferred from mutant phenotype. Source: MGI response to ethanol Inferred from mutant phenotype. Source: MGI response to heat Inferred from mutant phenotype. Source: MGI response to hydrogen peroxide Inferred from mutant phenotype. Source: MGI response to superoxide Inferred from mutant phenotype. Source: MGI retina homeostasis Inferred from mutant phenotype. Source: MGI sensory perception of sound Inferred from mutant phenotype. Source: MGI spermatogenesis Inferred from mutant phenotype. Source: MGI superoxide anion generation Inferred from direct assay. Source: MGI
Cellular component	cell soma Inferred from sequence or structural similarity. Source: UniProtKB cytoplasmic vesicle Inferred from sequence or structural similarity. Source: UniProtKB cytosol Inferred from sequence or structural similarity. Source: UniProtKB dendrite cytoplasm Inferred from sequence or structural similarity. Source: UniProtKB extracellular matrix Inferred from sequence or structural similarity. Source: UniProtKB extracellular space Inferred from sequence or structural similarity. Source: UniProtKB mitochondrion Inferred from sequence or structural similarity. Source: UniProtKB nucleus Inferred from sequence or structural similarity. Source: UniProtKB protein complex Inferred from sequence or structural similarity. Source: UniProtKB
Molecular function	antioxidant activity Inferred from electronic annotation. Source: UniProtKB-KW chaperone binding Inferred from sequence or structural similarity. Source: UniProtKB copper ion binding Inferred from sequence or structural similarity. Source: UniProtKB protein phosphatase 2B binding Inferred from sequence or structural similarity. Source: UniProtKB superoxide dismutase activity Inferred from direct assay. Source: MGI zinc ion binding Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed
	Chain	2 – 154	153	Superoxide dismutase [Cu-Zn]		PRO_0000164062
Sites
	Metal binding	47	1	Copper; catalytic By similarity
	Metal binding	49	1	Copper; catalytic By similarity
	Metal binding	64	1	Copper; catalytic By similarity
	Metal binding	64	1	Zinc; structural By similarity
	Metal binding	72	1	Zinc; structural By similarity
	Metal binding	81	1	Zinc; structural By similarity
	Metal binding	84	1	Zinc; structural By similarity
	Metal binding	121	1	Copper; catalytic By similarity
Amino acid modifications
	Modified residue	71	1	N6-acetyllysine Ref.7
	Modified residue	99	1	Phosphoserine By similarity
	Modified residue	123	1	N6-acetyllysine By similarity
	Disulfide bond	58 ↔ 147		By similarity
Experimental info
	Sequence conflict	102	1	D → H in AAA40121. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P08228-1 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: CAE548C66043BAC4	FASTA	154	15,943
	10 20 30 40 50 60 MAMKAVCVLK GDGPVQGTIH FEQKASGEPV VLSGQITGLT EGQHGFHVHQ YGDNTQGCTS 70 80 90 100 110 120 AGPHFNPHSK KHGGPADEER HVGDLGNVTA GKDGVANVSI EDRVISLSGE HSIIGRTMVV 130 140 150 HEKQDDLGKG GNEESTKTGN AGSRLACGVI GIAQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"cDNA and deduced amino acid sequence of murine Cu-Zn superoxide dismutase." Bewley G.C. Nucleic Acids Res. 16:2728-2728(1988) [PubMed: 3362683] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: SWR/J. Tissue: Liver.
[2]	"Isolation and analysis of the mouse genomic sequence encoding Cu(2+)-Zn2+ superoxide dismutase." Benedetto M.T., Anzai Y., Gordon J.W. Gene 99:191-195(1991) [PubMed: 2022332] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"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: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Ovary, Urinary bladder and Uterus.
[4]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Liver, Mammary gland and Retina.
[5]	"Purification of an inhibitor of erythroid progenitor cell cycling and antagonist to interleukin 3 from mouse marrow cell supernatants and its identification as cytosolic superoxide dismutase." Pluthero F.G., Shreeve M., Eskinazi D., van der Gaag H., Huang K.S., Hulmes J.D., Blum M., Axelrad A.A. J. Cell Biol. 111:1217-1223(1990) [PubMed: 2391363] [Abstract] Cited for: PROTEIN SEQUENCE OF 4-23.
[6]	Lubec G., Klug S., Sunyer B., Chen W.-Q. Submitted (JAN-2009) to UniProtKB Cited for: PROTEIN SEQUENCE OF 11-24 AND 104-116, MASS SPECTROMETRY. Strain: OF1. Tissue: Hippocampus.
[7]	"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: 16916647] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-71, MASS SPECTROMETRY. Tissue: Liver.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X06683 mRNA. Translation: CAA29880.1. M60798 , M60794, M60795, M60796, M60797 Genomic DNA. Translation: AAA40121.1. M35725 mRNA. Translation: AAA37518.1. AK020624 mRNA. Translation: BAB32154.1. AK077284 mRNA. Translation: BAC36730.1. BC002066 mRNA. Translation: AAH02066.1. BC048874 mRNA. Translation: AAH48874.1. BC086886 mRNA. Translation: AAH86886.1.
IPI	IPI00130589.
PIR	JQ0915.
RefSeq	NP_035564.1.
UniGene	Mm.276325 Mm.466779
3D structure databases
HSSP	HSSP built from PDB template 1HL5 based on UniProtKB P00441.
SMR	P08228. Positions 2-154.
ModBase	Search...
Protein-protein interaction databases
STRING	P08228.
PTM databases
PhosphoSite	P08228.
2-D gel databases
SWISS-2DPAGE	P08228.
DOSAC-COBS-2DPAGE	P08228.
REPRODUCTION-2DPAGE	P08228.
Proteomic databases
PRIDE	P08228.
Genome annotation databases
Ensembl	ENSMUST00000023707; ENSMUSP00000023707; ENSMUSG00000022982; Mus musculus. [Genome view]
GeneID	20655.
KEGG	mmu:20655.
NMPDR	fig|10090.3.peg.1866.
UCSC	uc007zvz.1. mouse.
Organism-specific databases
CTD	20655.
MGI	MGI:98351. Sod1.
Phylogenomic databases
HOGENOM	P08228.
HOVERGEN	P08228.
OMA	GPHFNPN.
Enzyme and pathway databases
BRENDA	1.15.1.1. 244.
Gene expression databases
Bgee	P08228.
CleanEx	MM_SOD1.
Genevestigator	P08228.
GermOnline	ENSMUSG00000047905. Mus musculus.
Family and domain databases
InterPro	IPR018152. SOD_Cu/Zn_BS. IPR001424. SOD_Cu_Zn. [Graphical view]
Gene3D	G3DSA:2.60.40.200. SOD_Cu_Zn. 1 hit.
PANTHER	PTHR10003. SOD_Cu_Zn. 1 hit.
Pfam	PF00080. Sod_Cu. 1 hit. [Graphical view]
PRINTS	PR00068. CUZNDISMTASE.
ProDom	PD000469. SOD_CU_ZN. 1 hit. [Graphical view] [Entries sharing at least one domain]
PROSITE	PS00087. SOD_CU_ZN_1. 1 hit. PS00332. SOD_CU_ZN_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	299081.
SOURCE	Search...

Entry information

Entry name

SODC_MOUSE

Accession

Primary (citable) accession number: P08228

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1988
Last sequence update:	January 23, 2007
Last modified:	November 3, 2009
This is version 115 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)