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)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › 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.
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	DNA fragmentation involved in apoptotic nuclear change Inferred from direct assay. Source: MGI activation of MAPK activity Inferred from direct assay. Source: MGI anterograde axon cargo transport Inferred from mutant phenotype. Source: BHF-UCL auditory receptor cell stereocilium organization Inferred from mutant phenotype. Source: MGI 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 cell homeostasis Inferred from mutant phenotype. Source: MGI myeloid cell homeostasis Inferred from mutant phenotype. 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 mutant phenotype. Source: MGI ovarian follicle development Inferred from mutant phenotype. Source: MGI peripheral nervous system myelin maintenance Inferred from mutant phenotype. Source: MGI 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 retina homeostasis Inferred from mutant phenotype. Source: MGI retrograde axon cargo transport Inferred from mutant phenotype. Source: BHF-UCL 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	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 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. 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; 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

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

.

.

.

.

.

.

.

.

.

154

Helix Strand Turn

Details...

Beta strand

100 – 106

7

Beta strand

117 – 123

7

Helix

133 – 137

5

Beta strand

144 – 147

4

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: 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.
[8]	"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: 20727846] [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

P08228.

PTM databases

PhosphoSite

P08228.

2D gel databases

SWISS-2DPAGE

P08228.

DOSAC-COBS-2DPAGE

P08228.

REPRODUCTION-2DPAGE

IPI00130589.
P08228.

UCD-2DPAGE

P08228.

Proteomic databases

PRIDE

P08228.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000023707; ENSMUSP00000023707; ENSMUSG00000022982.

GeneID

20655.

KEGG

mmu:20655.

NMPDR

fig|10090.3.peg.1866.

UCSC

uc007zvz.1. mouse.

Organism-specific databases

CTD

6647.

MGI

MGI:98351. Sod1.

Phylogenomic databases

eggNOG

roNOG15892.

GeneTree

ENSGT00530000063226.

HOGENOM

HBG609879.

HOVERGEN

HBG000062.

InParanoid

P08228.

OMA

IHFEQKA.

OrthoDB

EOG45HRZM.

PhylomeDB

P08228.

Gene expression databases

ArrayExpress

P08228.

Bgee

P08228.

CleanEx

MM_SOD1.

Genevestigator

P08228.

GermOnline

ENSMUSG00000047905. Mus musculus.

Family and domain databases

InterPro

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

Gene3D

G3DSA:2.60.40.200. SOD_Cu_Zn. 1 hit.

KO

K04565.

PANTHER

PTHR10003. SOD_Cu_Zn. 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

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:	January 25, 2012
This is version 139 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program