Reviewed, UniProtKB/Swiss-Prot P80566 (SODC_CHICK)

Names and origin

Protein names

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

Gene names

Name:

SOD1

Organism

Gallus gallus (Chicken)

Taxonomic identifier

9031 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Archosauria › Dinosauria › Saurischia › Theropoda › Coelurosauria › Aves › Neognathae › Galliformes › Phasianidae › Phasianinae › Gallus

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.
Mass spectrometry	Molecular mass is 15600±2 Da from positions 2 - 154. Determined by ESI. Ref.2

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	Copper Metal-binding Zinc
Molecular function	Antioxidant Oxidoreductase
PTM	Acetylation Disulfide bond Glutathionylation
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW superoxide metabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	antioxidant activity Inferred from electronic annotation. Source: UniProtKB-KW copper ion binding Inferred from electronic annotation. Source: UniProtKB-KW superoxide dismutase activity Inferred from electronic annotation. Source: EC zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.2
	Chain	2 – 154	153	Superoxide dismutase [Cu-Zn]		PRO_0000164069
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	120	1	Copper; catalytic By similarity
Amino acid modifications
	Modified residue	2	1	N-acetylalanine
	Modified residue	154	1	S-glutathionyl cysteine
	Disulfide bond	58 ↔ 146		By similarity
Experimental info
	Sequence conflict	14	1	A → G AA sequence Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P80566-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: F06FEF9FCBB7FB9E	FASTA	154	15,704
	10 20 30 40 50 60 MATLKAVCVM KGDAPVEGVI HFQQQGSGPV KVTGKITGLS DGDHGFHVHE FGDNTNGCTS 70 80 90 100 110 120 AGAHFNPEGK QHGGPKDADR HVGDLGNVTA KGGVAEVEIE DSVISLTGPH CIIGRTMVVH 130 140 150 AKSDDLGRGG DNESKLTGNA GPRLACGVIG IAKC

References

[1]	"Characterisation of the chicken Cu,Zn superoxide dismutase gene." Stanton J.L., Wilton S.D., Laing N.G. DNA Seq. 6:357-360(1996) [PubMed: 8988375] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Spinal cord.
[2]	"Amino acid sequence of chicken Cu,Zn-containing superoxide dismutase and identification of glutathionyl adducts at exposed cysteine residues." Schinina M.E., Carlini P., Polticelli F., Zappacosta F., Bossa F., Calabrese L. Eur. J. Biochem. 237:433-439(1996) [PubMed: 8647082] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-154, MASS SPECTROMETRY. Tissue: Erythrocyte.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U28407 mRNA. Translation: AAB88059.1.
IPI	IPI00598533.
PIR	S65436.
RefSeq	NP_990395.1.
UniGene	Gga.3346
3D structure databases
HSSP	HSSP built from PDB template 1HL4 based on UniProtKB P00441.
SMR	P80566. Positions 5-153.
ModBase	Search...
Protein-protein interaction databases
STRING	P80566.
Proteomic databases
PRIDE	P80566.
Genome annotation databases
Ensembl	ENSGALT00000036785; ENSGALP00000035996; ENSGALG00000015844; Gallus gallus. [Genome view]
GeneID	395938.
KEGG	gga:395938.
Organism-specific databases
CTD	395938.
Phylogenomic databases
HOGENOM	P80566.
HOVERGEN	P80566.
Enzyme and pathway databases
BRENDA	1.15.1.1. 4.
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...

Entry information

Entry name

SODC_CHICK

Accession

Primary (citable) accession number: P80566
Secondary accession number(s): Q92059

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1996
Last sequence update:	January 23, 2007
Last modified:	September 1, 2009
This is version 72 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)