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Reviewed, UniProtKB/Swiss-Prot Q54RN1 (SODC2_DICDI)

Last modified February 9, 2010. Version 43. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Extracellular superoxide dismutase [Cu-Zn] 2
      Short name=EC-SOD 2
    EC=1.15.1.1
Gene names
Name: sodB
ORF Names: DDB_G0283021
OrganismDictyostelium discoideum (Slime mold) [Complete proteome]
Taxonomic identifier44689 [NCBI]
Taxonomic lineageEukaryota › Amoebozoa › Mycetozoa › Dictyosteliida › Dictyostelium

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Protein attributes

Sequence length427 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level.

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General annotation (Comments)

Function

Protect the extracellular space from toxic effect of reactive oxygen intermediates by converting superoxyde radicals into hydrogen peroxyde 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.

Subcellular location

Cell membrane; Single-pass type I membrane protein; Extracellular side Potential.

Sequence similarities

Belongs to the Cu-Zn superoxide dismutase family.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Potential
Chain21 – 427407Extracellular superoxide dismutase [Cu-Zn] 2
PRO_0000327852

Regions

Topological domain21 – 406386Extracellular Potential
Transmembrane407 – 42620 Potential
Topological domain4271Cytoplasmic Potential

Sites

Metal binding2571Copper; catalytic By similarity
Metal binding2591Copper; catalytic By similarity
Metal binding2751Copper; catalytic By similarity
Metal binding2751Zinc; structural By similarity
Metal binding2831Zinc; structural By similarity
Metal binding2921Zinc; structural By similarity
Metal binding2951Zinc; structural By similarity
Metal binding3311Copper; catalytic By similarity

Amino acid modifications

Glycosylation381N-linked (GlcNAc...) Potential
Glycosylation571N-linked (GlcNAc...) Potential
Glycosylation811N-linked (GlcNAc...) Potential
Glycosylation1901N-linked (GlcNAc...) Potential
Glycosylation2181N-linked (GlcNAc...) Potential
Glycosylation2881N-linked (GlcNAc...) Potential
Glycosylation3761N-linked (GlcNAc...) Potential

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Sequences

Sequence LengthMass (Da)Tools
Q54RN1-1 [UniParc].

Last modified May 24, 2005. Version 1.
Checksum: 1A8283B8A5F3E8FC

FASTA42744,568
        10         20         30         40         50         60 
MNKLIISLLI VLSAISIISA DYQYGYCKFG SVGTVNQNIT GYVTLTAQDG ALNLVYNISS 

        70         80         90        100        110        120 
INLPTGSYAT AIMTYGYNPS NNTDLGGVFQ VDGKGTEQCQ SGGSRAGDLY NLYVNDNRIS 

       130        140        150        160        170        180 
SNFDSLTSVS IVDSPNSIIG RSIAIFQESY SCDLLKSSVG TSVGPLTTVV ASCIIGIGNS 

       190        200        210        220        230        240 
ANVPATNGVN TTTGNANTAG AYSSLSNTQY DAMVLLANTT KSPSAAIGGS VLFRSSSNSV 

       250        260        270        280        290        300 
SVNGIVSGVA KSVHGFHIHA FGDLTTVDGA SIGGHWLSGA QVHAFPENTS RHFGDLGNLC 

       310        320        330        340        350        360 
IFDNDFKNAY YYLSTSYFSF SGLVGRGFAV HAARDDGNTY VGGDRVAQGV VALIPKAATT 

       370        380        390        400        410        420 
LNQVPSNWKY EVICSNGTYT GESTIEPSPT PSTTPTPTET SQPGTSSYLA PFFVLILSSL 


ISVILIL

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References

« Hide '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. expand/collapse author list , 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]"Copper/zinc superoxide dismutases in Dictyostelium discoideum: amino acid sequences and expression kinetics."
Tsuji A., Akaza Y., Kodaira K., Yasukawa H.
J. Biochem. Mol. Biol. Biophys. 6:215-220(2002) [PubMed: 12186757] [Abstract]
Cited for: IDENTIFICATION.
+Additional computationally mapped references.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AAFI02000049 Genomic DNA. Translation: EAL65954.1.
BR000219 mRNA. Translation: FAA00021.1.
RefSeqXP_639320.1.

3D structure databases

HSSPHSSP built from PDB template 1TO4 based on UniProtKB Q01137.
SMRQ54RN1. Positions 37-178, 226-352.
ModBaseSearch...

Genome annotation databases

GeneID8623891.
KEGGddi:DDB_0232188.

Organism-specific databases

dictyBaseDDB_G0283021. sodB.

Phylogenomic databases

eggNOGKOG0441.
HOGENOMHBG080616.
PhylomeDBQ54RN1.

Enzyme and pathway databases

BRENDA1.15.1.1. 424.

Family and domain databases

InterProIPR018152. SOD_Cu/Zn_BS.
IPR001424. SOD_Cu_Zn.
[Graphical view]
Gene3DG3DSA:2.60.40.200. SOD_Cu_Zn. 2 hits.
PANTHERPTHR10003. SOD_Cu_Zn. 1 hit.
PfamPF00080. Sod_Cu. 2 hits.
[Graphical view]
PROSITEPS00087. SOD_CU_ZN_1. 1 hit.
PS00332. SOD_CU_ZN_2. False negative.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameSODC2_DICDI
AccessionPrimary (citable) accession number: Q54RN1
Secondary accession number(s): Q52KB1
Entry history
Integrated into UniProtKB/Swiss-Prot: April 8, 2008
Last sequence update: May 24, 2005
Last modified: February 9, 2010
This is version 43 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

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Relevant documents

Dictyostelium discoideum

Dictyostelium discoideum: entries, gene names and cross-references to dictyBase

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents