SODC4_DICDI
ID SODC4_DICDI Reviewed; 151 AA.
AC Q54TU5; Q52KB3;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Superoxide dismutase [Cu-Zn] 4;
DE EC=1.15.1.1;
GN Name=sodD; ORFNames=DDB_G0281493;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [2]
RP FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=12499634; DOI=10.1248/bpb.25.1528;
RA Akaza Y., Tsuji A., Yasukawa H.;
RT "Analysis of the gene encoding copper/zinc superoxide dismutase homolog in
RT Dictyostelium discoideum.";
RL Biol. Pharm. Bull. 25:1528-1532(2002).
CC -!- FUNCTION: Destroys radicals which are normally produced within the
CC cells and which are toxic to biological systems (By similarity).
CC Protects spores from cellular damage caused by UV LIGHT. {ECO:0000250,
CC ECO:0000269|PubMed:12499634}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 H(+) + 2 superoxide = H2O2 + O2; Xref=Rhea:RHEA:20696,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:18421; EC=1.15.1.1;
CC -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378; Evidence={ECO:0000250};
CC Note=Binds 1 copper ion per subunit. {ECO:0000250};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- DEVELOPMENTAL STAGE: Expressed at late-developmental stages. Spore cell
CC specific. {ECO:0000269|PubMed:12499634}.
CC -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family.
CC {ECO:0000305}.
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DR EMBL; AAFI02000041; EAL66728.1; -; Genomic_DNA.
DR EMBL; BR000217; FAA00019.1; -; mRNA.
DR RefSeq; XP_640716.1; XM_635624.1.
DR AlphaFoldDB; Q54TU5; -.
DR SMR; Q54TU5; -.
DR STRING; 44689.DDB0232182; -.
DR PaxDb; Q54TU5; -.
DR EnsemblProtists; EAL66728; EAL66728; DDB_G0281493.
DR GeneID; 8623104; -.
DR KEGG; ddi:DDB_G0281493; -.
DR dictyBase; DDB_G0281493; sodD.
DR eggNOG; KOG0441; Eukaryota.
DR HOGENOM; CLU_056632_4_1_1; -.
DR InParanoid; Q54TU5; -.
DR OMA; CGTIWIK; -.
DR PhylomeDB; Q54TU5; -.
DR Reactome; R-DDI-3299685; Detoxification of Reactive Oxygen Species.
DR PRO; PR:Q54TU5; -.
DR Proteomes; UP000002195; Chromosome 3.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005507; F:copper ion binding; IBA:GO_Central.
DR GO; GO:0004784; F:superoxide dismutase activity; IBA:GO_Central.
DR GO; GO:0019430; P:removal of superoxide radicals; IBA:GO_Central.
DR GO; GO:0009411; P:response to UV; IMP:dictyBase.
DR CDD; cd00305; Cu-Zn_Superoxide_Dismutase; 1.
DR Gene3D; 2.60.40.200; -; 1.
DR InterPro; IPR036423; SOD-like_Cu/Zn_dom_sf.
DR InterPro; IPR024134; SOD_Cu/Zn_/chaperone.
DR InterPro; IPR018152; SOD_Cu/Zn_BS.
DR InterPro; IPR001424; SOD_Cu_Zn_dom.
DR PANTHER; PTHR10003; PTHR10003; 1.
DR Pfam; PF00080; Sod_Cu; 1.
DR PRINTS; PR00068; CUZNDISMTASE.
DR SUPFAM; SSF49329; SSF49329; 1.
DR PROSITE; PS00087; SOD_CU_ZN_1; 1.
PE 2: Evidence at transcript level;
KW Antioxidant; Copper; Cytoplasm; Disulfide bond; Metal-binding;
KW Oxidoreductase; Reference proteome; Zinc.
FT CHAIN 1..151
FT /note="Superoxide dismutase [Cu-Zn] 4"
FT /id="PRO_0000311821"
FT BINDING 45
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 47
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 62
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 62
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000250"
FT BINDING 70
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000250"
FT BINDING 79
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000250"
FT BINDING 82
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000250"
FT BINDING 120
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT DISULFID 56..145
FT /evidence="ECO:0000250"
SQ SEQUENCE 151 AA; 15471 MW; 8099D8BB4A7A3C74 CRC64;
MVKAICVVKG AVVNGTIIFS QENEGSPVYV NGTISGLSGG LHGFHIHEFG DTSNGCLSAG
AHFNPFHVEH GGPNSAIRHV GDLGNITSCP SSKVANVLIQ DNVISLFGDL SIIGRTLVVH
ENQDDLGLGG NLSKTTGNAG ARVACGILAK I
