Q08420 (SODE_RAT) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Extracellular superoxide dismutase [Cu-Zn]
Short name=EC-SOD
EC=1.15.1.1

Alternative name(s):
Superoxide dismutase B

Gene names

Name:	Sod3
Synonyms:	Sod-3

Organism

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	244 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	Protect the extracellular space from toxic effect of reactive oxygen intermediates by converting superoxide radicals into hydrogen peroxide and oxygen By similarity.
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	Secreted › extracellular space.
Sequence similarities	Belongs to the Cu-Zn superoxide dismutase family.

Ontologies

Keywords
Cellular component	Secreted
Domain	Signal
Ligand	Copper Metal-binding Zinc
Molecular function	Antioxidant Oxidoreductase
PTM	Disulfide bond Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	removal of superoxide radicals Inferred from Biological aspect of Ancestor. Source: RefGenome response to copper ion Inferred from mutant phenotype. Source: RGD
Cellular component	extracellular matrix Inferred from direct assay. Source: RGD extracellular space Inferred from Biological aspect of Ancestor. Source: RefGenome nucleus Inferred from direct assay. Source: RGD
Molecular function	copper ion binding Inferred from Biological aspect of Ancestor. Source: RefGenome superoxide dismutase activity Inferred from direct assay Ref.3. Source: RGD zinc ion binding Inferred from Biological aspect of Ancestor. Source: RefGenome
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 15	15	Potential
	Chain	16 – 244	229	Extracellular superoxide dismutase [Cu-Zn]		PRO_0000032859
Sites
	Metal binding	121	1	Copper; catalytic By similarity
	Metal binding	123	1	Copper; catalytic By similarity
	Metal binding	138	1	Copper; catalytic By similarity
	Metal binding	138	1	Zinc; structural By similarity
	Metal binding	146	1	Zinc; structural By similarity
	Metal binding	149	1	Zinc; structural By similarity
	Metal binding	152	1	Zinc; structural By similarity
	Metal binding	188	1	Copper; catalytic By similarity
Amino acid modifications
	Glycosylation	114	1	N-linked (GlcNAc...) Potential
	Disulfide bond	70 ↔ 215		By similarity
	Disulfide bond	132 ↔ 214		By similarity
Experimental info
	Mutagenesis	48	1	D → V: Homotetramerization.
	Sequence conflict	235 – 237	3	RRR → WRW in CAA48177. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q08420 [UniParc]. Last modified July 15, 1999. Version 2. Checksum: B66726301CE5B614	FASTA	244	26,620
	10 20 30 40 50 60 MVAFLFCNLL LVACGSVTWT MSDTGESGVD LADRLDLVEK IGDTHSKDLE IWMELGKQRE 70 80 90 100 110 120 ADAREMHAVC RVQPSAMLPP DQPQITGLVL FRQLGPSSRL EASFNLEGFP AEQNTSNHAI 130 140 150 160 170 180 HVHEFGDLSQ GCESTGPHYN PLGVPHPQHP GDFGNFVVRD GRLWKHRMGL ATSLAGPHSI 190 200 210 220 230 240 LGRAVVVHAG EDDLGKGGNQ ASVQNGNAGR RLACCVVGTS NSEAWESQTK ERKKRRRESE CKTT

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Isolation and characterization of a rat cDNA clone encoding a secreted superoxide dismutase reveals the epididymis to be a major site of its expression." Perry A.C.F., Jones R., Hall L. Biochem. J. 293:21-25(1993) [PubMed: 8328962] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Epididymis.
[2]	"Purification and sequence of rat extracellular superoxide dismutase B secreted by C6 glioma." Willems J., Zwijsen A., Slegers H., Nicolai S., Bettadapura J., Raymackers J., Scarcez T. J. Biol. Chem. 268:24614-24621(1993) [PubMed: 8227019] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION.
[3]	"The rat extracellular superoxide dismutase dimer is converted to a tetramer by the exchange of a single amino acid." Carlsson L.M., Marklund S.M., Edlund T. Proc. Natl. Acad. Sci. U.S.A. 93:5219-5222(1996) [PubMed: 8643556] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], MUTAGENESIS. Strain: Sprague-Dawley. Tissue: 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]. Tissue: Prostate.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X68041 mRNA. Translation: CAA48177.1. Z24721 mRNA. Translation: CAA80849.1. X94371 mRNA. Translation: CAA64149.1. BC061861 mRNA. Translation: AAH61861.1.
IPI	IPI00200507.
PIR	A49097.
RefSeq	NP_037012.1. NM_012880.1.
UniGene	Rn.10358.
3D structure databases
ProteinModelPortal	Q08420.
ModBase	Search...
Protein-protein interaction databases
STRING	Q08420.
Proteomic databases
PRIDE	Q08420.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSRNOT00000005155; ENSRNOP00000005155; ENSRNOG00000003869.
GeneID	25352.
KEGG	rno:25352.
UCSC	NM_012880. rat.
Organism-specific databases
CTD	6649.
RGD	3733. Sod3.
Phylogenomic databases
eggNOG	roNOG14745.
GeneTree	ENSGT00530000063226.
HOVERGEN	HBG000062.
InParanoid	Q08420.
OMA	HPRHPGD.
OrthoDB	EOG4MCX1S.
PhylomeDB	Q08420.
Gene expression databases
ArrayExpress	Q08420.
Genevestigator	Q08420.
GermOnline	ENSRNOG00000003869. Rattus norvegicus.
Family and domain databases
InterPro	IPR024134. SOD_Cu/Zn_/chaperones. IPR018152. SOD_Cu/Zn_BS. IPR024141. SOD_Cu/Zn_extracel. IPR001424. SOD_Cu_Zn_dom. [Graphical view]
Gene3D	G3DSA:2.60.40.200. SOD_Cu_Zn. 1 hit.
KO	K00518.
PANTHER	PTHR10003:SF10. PTHR10003:SF10. 1 hit. 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	606301.

Entry information

Entry name

SODE_RAT

Accession

Primary (citable) accession number: Q08420
Secondary accession number(s): Q64667

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1994
Last sequence update:	July 15, 1999
Last modified:	November 16, 2011
This is version 97 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program