P08228 (SODC_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

Gene names

Name:

Sod1

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	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.
Disruption phenotype	40% reduction in hepatic GPX1 activity. Ref.8
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	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	activation of MAPK activity Inferred from direct assay PubMed 12223545. Source: MGI aging Inferred from mutant phenotype PubMed 16377630. Source: MGI anterograde axon cargo transport Inferred from mutant phenotype PubMed 20510358. Source: BHF-UCL auditory receptor cell stereocilium organization Inferred from mutant phenotype PubMed 10464373PubMed 10466888. Source: MGI cell aging Inferred from electronic annotation. Source: Compara cellular iron ion homeostasis Inferred from mutant phenotype PubMed 16377630. Source: MGI embryo implantation Inferred from mutant phenotype PubMed 9516486. Source: MGI glutathione metabolic process Inferred from mutant phenotype PubMed 16377630. Source: MGI heart contraction Inferred from mutant phenotype PubMed 10679476. Source: MGI hydrogen peroxide biosynthetic process Inferred from mutant phenotype PubMed 14679182. Source: MGI locomotory behavior Inferred from mutant phenotype PubMed 10433959. Source: MGI muscle cell homeostasis Inferred from mutant phenotype PubMed 16716900. Source: MGI myeloid cell homeostasis Inferred from mutant phenotype PubMed 11493445. Source: MGI negative regulation of cholesterol biosynthetic process Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of neuron apoptotic process Inferred from mutant phenotype PubMed 10464373. Source: MGI neurofilament cytoskeleton organization Inferred from mutant phenotype PubMed 11343650. Source: MGI ovarian follicle development Inferred from mutant phenotype PubMed 9724058. Source: MGI peripheral nervous system myelin maintenance Inferred from mutant phenotype PubMed 10433959. Source: MGI positive regulation of cytokine production Inferred from sequence or structural similarity. Source: UniProtKB regulation of blood pressure Inferred from mutant phenotype PubMed 12433839. Source: MGI regulation of mitochondrial membrane potential Inferred from sequence or structural similarity. Source: UniProtKB regulation of multicellular organism growth Inferred from mutant phenotype PubMed 16377630. Source: MGI relaxation of vascular smooth muscle Inferred from mutant phenotype PubMed 12433839PubMed 14679182. Source: MGI removal of superoxide radicals Inferred from mutant phenotype PubMed 10436316PubMed 10471451PubMed 10679476PubMed 11493445PubMed 12433839PubMed 17448893PubMed 8673102PubMed 9516486PubMed 9788901. Source: MGI response to amphetamine Inferred from electronic annotation. Source: Compara response to axon injury Inferred from mutant phenotype PubMed 8673102. Source: MGI response to copper ion Inferred from electronic annotation. Source: Compara response to drug Inferred from mutant phenotype PubMed 16831125. Source: MGI response to ethanol Inferred from mutant phenotype PubMed 17448893. Source: MGI response to heat Inferred from mutant phenotype PubMed 16942767. Source: MGI response to hydrogen peroxide Inferred from mutant phenotype PubMed 15642323. Source: MGI response to nutrient levels Inferred from electronic annotation. Source: Compara retina homeostasis Inferred from mutant phenotype PubMed 16844785. Source: MGI retrograde axon cargo transport Inferred from mutant phenotype PubMed 20510358. Source: BHF-UCL sensory perception of sound Inferred from mutant phenotype PubMed 10436316PubMed 10464373PubMed 16055286. Source: MGI spermatogenesis Inferred from mutant phenotype PubMed 16036348. Source: MGI superoxide anion generation Inferred from direct assay PubMed 15317809. Source: MGI
Cellular_component	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 neuronal cell body Inferred from sequence or structural similarity. Source: UniProtKB nucleus Inferred from sequence or structural similarity. Source: UniProtKB peroxisome Inferred from electronic annotation. Source: Compara plasma membrane Inferred from electronic annotation. Source: Compara protein complex Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	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 PubMed 12646716PubMed 12968068PubMed 15317809PubMed 291939PubMed 7444718. 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 By similarity

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; via pros nitrogen

Metal binding

72

1

Zinc; via pros nitrogen

Metal binding

81

1

Zinc; via pros nitrogen

Metal binding

84

1

Zinc; structural

Metal binding

121

1

Copper; catalytic By similarity

Amino acid modifications

Modified residue

2

1

N-acetylalanine By similarity

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

Secondary structure

1

.

.

.

.

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154

Helix Strand Turn

Details...

Beta strand

3 – 10

8

Beta strand

12 – 14

3

Beta strand

16 – 25

10

Beta strand

30 – 38

9

Beta strand

41 – 50

10

Turn

55 – 58

4

Helix

59 – 61

3

Beta strand

84 – 90

7

Beta strand

96 – 104

9

Beta strand

106 – 109

4

Beta strand

116 – 123

8

Beta strand

130 – 132

3

Helix

133 – 138

6

Beta strand

143 – 149

7

Sequences

	Sequence		Length	Mass (Da)
	P08228 [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-71, MASS SPECTROMETRY. Tissue: Liver.
[8]	"Knockout of SOD1 promotes conversion of selenocysteine to dehydroalanine in murine hepatic GPX1 protein." Wang S.K., Weaver J.D., Zhang S., Lei X.G. Free Radic. Biol. Med. 51:197-204(2011) [PubMed] [Europe PMC] [Abstract] Cited for: DISRUPTION PHENOTYPE. Tissue: Liver.
[9]	"Structures of mouse SOD1 and human/mouse SOD1 chimeras." Seetharaman S.V., Taylor A.B., Holloway S., Hart P.J. Arch. Biochem. Biophys. 503:183-190(2010) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 2-154 IN COMPLEX WITH ZINC.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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. NM_011434.1.

UniGene

Mm.276325.
Mm.466779.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3GTT	X-ray	2.40	A/B/C/D/E/F	2-154	[»]
3GTV	X-ray	2.20	A/B/C/D/E/F/G/H/I/J/K/L	82-154	[»]

ProteinModelPortal

P08228.

SMR

P08228. Positions 2-154.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-48691N.

IntAct

P08228. 3 interactions.

STRING

10090.ENSMUSP00000023707.

PTM databases

PhosphoSite

P08228.

2D gel databases

DOSAC-COBS-2DPAGE

P08228.

REPRODUCTION-2DPAGE

IPI00130589.
P08228.

SWISS-2DPAGE

P08228.

UCD-2DPAGE

P08228.

Proteomic databases

PaxDb

P08228.

PRIDE

P08228.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000023707; ENSMUSP00000023707; ENSMUSG00000022982.

GeneID

20655.

KEGG

mmu:20655.

UCSC

uc007zvz.1. mouse.

Organism-specific databases

CTD

6647.

MGI

MGI:98351. Sod1.

Phylogenomic databases

eggNOG

COG2032.

GeneTree

ENSGT00530000063226.

HOGENOM

HOG000263447.

HOVERGEN

HBG000062.

InParanoid

P08228.

KO

K04565.

OMA

NDPNAER.

OrthoDB

EOG45HRZM.

Gene expression databases

Bgee

P08228.

CleanEx

MM_SOD1.

Genevestigator

P08228.

GermOnline

ENSMUSG00000047905. Mus musculus.

Family and domain databases

Gene3D

2.60.40.200. 1 hit.

InterPro

IPR024134. SOD_Cu/Zn_/chaperones.
IPR018152. SOD_Cu/Zn_BS.
IPR001424. SOD_Cu_Zn_dom.
[Graphical view]

PANTHER

PTHR10003. PTHR10003. 1 hit.

Pfam

PF00080. Sod_Cu. 1 hit.
[Graphical view]

PRINTS

PR00068. CUZNDISMTASE.

SUPFAM

SSF49329. SOD_Cu_Zn. 1 hit.

PROSITE

PS00087. SOD_CU_ZN_1. 1 hit.
PS00332. SOD_CU_ZN_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

SOD1. mouse.

EvolutionaryTrace

P08228.

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:	May 1, 2013
This is version 150 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program