SODC2_DICDI
ID SODC2_DICDI Reviewed; 427 AA.
AC Q54RN1; Q52KB1;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Extracellular superoxide dismutase [Cu-Zn] 2;
DE Short=EC-SOD 2;
DE EC=1.15.1.1;
DE Flags: Precursor;
GN Name=sodB; ORFNames=DDB_G0283021;
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 IDENTIFICATION.
RX PubMed=12186757; DOI=10.1080/10258140290018711;
RA Tsuji A., Akaza Y., Kodaira K., Yasukawa H.;
RT "Copper/zinc superoxide dismutases in Dictyostelium discoideum: amino acid
RT sequences and expression kinetics.";
RL J. Biochem. Mol. Biol. Biophys. 6:215-220(2002).
CC -!- FUNCTION: Protect the extracellular space from toxic effect of reactive
CC oxygen intermediates by converting superoxyde radicals into hydrogen
CC peroxyde and oxygen. {ECO:0000250}.
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 -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}; Extracellular side {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family.
CC {ECO:0000305}.
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DR EMBL; AAFI02000049; EAL65954.1; -; Genomic_DNA.
DR EMBL; BR000219; FAA00021.1; -; mRNA.
DR RefSeq; XP_639320.1; XM_634228.1.
DR AlphaFoldDB; Q54RN1; -.
DR SMR; Q54RN1; -.
DR STRING; 44689.DDB0232188; -.
DR PaxDb; Q54RN1; -.
DR EnsemblProtists; EAL65954; EAL65954; DDB_G0283021.
DR GeneID; 8623891; -.
DR KEGG; ddi:DDB_G0283021; -.
DR dictyBase; DDB_G0283021; sodB.
DR eggNOG; KOG0441; Eukaryota.
DR HOGENOM; CLU_676923_0_0_1; -.
DR InParanoid; Q54RN1; -.
DR OMA; NICAYDA; -.
DR Reactome; R-DDI-3299685; Detoxification of Reactive Oxygen Species.
DR PRO; PR:Q54RN1; -.
DR Proteomes; UP000002195; Chromosome 4.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; 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:0042542; P:response to hydrogen peroxide; IEP:dictyBase.
DR GO; GO:0006979; P:response to oxidative stress; IEP:dictyBase.
DR GO; GO:0009411; P:response to UV; IEP:dictyBase.
DR Gene3D; 2.60.40.200; -; 2.
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 InterPro; IPR031078; SodC2/C3-like.
DR PANTHER; PTHR10003; PTHR10003; 1.
DR PANTHER; PTHR10003:SF73; PTHR10003:SF73; 1.
DR Pfam; PF00080; Sod_Cu; 1.
DR SUPFAM; SSF49329; SSF49329; 2.
DR PROSITE; PS00087; SOD_CU_ZN_1; 1.
PE 2: Evidence at transcript level;
KW Antioxidant; Cell membrane; Copper; Glutathionylation; Glycoprotein;
KW Membrane; Metal-binding; Oxidoreductase; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix; Zinc.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..427
FT /note="Extracellular superoxide dismutase [Cu-Zn] 2"
FT /id="PRO_0000327852"
FT TOPO_DOM 21..406
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 407..426
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 427
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 381..404
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 257
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 259
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 275
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 275
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000250"
FT BINDING 283
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000250"
FT BINDING 292
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000250"
FT BINDING 295
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000250"
FT BINDING 331
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT CARBOHYD 38
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 57
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 81
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 190
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 218
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 288
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 376
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 427 AA; 44568 MW; 1A8283B8A5F3E8FC CRC64;
MNKLIISLLI VLSAISIISA DYQYGYCKFG SVGTVNQNIT GYVTLTAQDG ALNLVYNISS
INLPTGSYAT AIMTYGYNPS NNTDLGGVFQ VDGKGTEQCQ SGGSRAGDLY NLYVNDNRIS
SNFDSLTSVS IVDSPNSIIG RSIAIFQESY SCDLLKSSVG TSVGPLTTVV ASCIIGIGNS
ANVPATNGVN TTTGNANTAG AYSSLSNTQY DAMVLLANTT KSPSAAIGGS VLFRSSSNSV
SVNGIVSGVA KSVHGFHIHA FGDLTTVDGA SIGGHWLSGA QVHAFPENTS RHFGDLGNLC
IFDNDFKNAY YYLSTSYFSF SGLVGRGFAV HAARDDGNTY VGGDRVAQGV VALIPKAATT
LNQVPSNWKY EVICSNGTYT GESTIEPSPT PSTTPTPTET SQPGTSSYLA PFFVLILSSL
ISVILIL
