Reviewed, UniProtKB/Swiss-Prot Q54TU5 (SODC4_DICDI)

Names and origin

Protein names

Recommended name:
    Superoxide dismutase [Cu-Zn] 4
    EC=1.15.1.1

Gene names

Name:	sodD
ORF Names:	DDB_G0281493

Organism

Dictyostelium discoideum (Slime mold) [Complete proteome]

Taxonomic identifier

44689 [NCBI]

Taxonomic lineage

Eukaryota › Amoebozoa › Mycetozoa › Dictyosteliida › Dictyostelium

Protein attributes

Sequence length	151 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	Destroys radicals which are normally produced within the cells and which are toxic to biological systems By similarity. Protects spores from cellular damage caused by UV-light.
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 By similarity.
Subcellular location	Cytoplasm By similarity.
Developmental stage	Expressed at late-developmental stages. Spore cell specific. Ref.2
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	Disulfide bond
Technical term	Complete proteome
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
	Chain	1 – 151	151	Superoxide dismutase [Cu-Zn] 4		PRO_0000311821
Sites
	Metal binding	45	1	Copper; catalytic By similarity
	Metal binding	47	1	Copper; catalytic By similarity
	Metal binding	62	1	Copper; catalytic By similarity
	Metal binding	62	1	Zinc; structural By similarity
	Metal binding	70	1	Zinc; structural By similarity
	Metal binding	79	1	Zinc; structural By similarity
	Metal binding	82	1	Zinc; structural By similarity
	Metal binding	120	1	Copper; catalytic By similarity
Amino acid modifications
	Disulfide bond	56 ↔ 145		By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q54TU5-1 [UniParc]. Last modified May 24, 2005. Version 1. Checksum: 8099D8BB4A7A3C74	FASTA	151	15,471
	10 20 30 40 50 60 MVKAICVVKG AVVNGTIIFS QENEGSPVYV NGTISGLSGG LHGFHIHEFG DTSNGCLSAG 70 80 90 100 110 120 AHFNPFHVEH GGPNSAIRHV GDLGNITSCP SSKVANVLIQ DNVISLFGDL SIIGRTLVVH 130 140 150 ENQDDLGLGG NLSKTTGNAG ARVACGILAK I

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The genome of the social amoeba Dictyostelium discoideum." Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T., Lehmann R., Hamlin N. , Davies R., Gaudet P., Fey P., Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T., Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D., Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A. Nature 435:43-57(2005) [PubMed: 15875012] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: AX4.
[2]	"Analysis of the gene encoding copper/zinc superoxide dismutase homolog in Dictyostelium discoideum." Akaza Y., Tsuji A., Yasukawa H. Biol. Pharm. Bull. 25:1528-1532(2002) [PubMed: 12499634] [Abstract] Cited for: FUNCTION, DEVELOPMENTAL STAGE.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AAFI02000041 Genomic DNA. Translation: EAL66728.1. BR000217 mRNA. Translation: FAA00019.1.
RefSeq	XP_640716.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	3391797.
GenomeReviews	Gene locus sodD in contig CM000152_GR.
KEGG	ddi:DDB_0232182.
Organism-specific databases
dictyBase	DDB_G0281493. sodD.
Phylogenomic databases
OMA	KAVCVIN.
Enzyme and pathway databases
BRENDA	1.15.1.1. 424.
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. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

SODC4_DICDI

Accession

Primary (citable) accession number: Q54TU5
Secondary accession number(s): Q52KB3

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 4, 2007
Last sequence update:	May 24, 2005
Last modified:	November 3, 2009
This is version 35 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)