SODC_CRYNH
ID SODC_CRYNH Reviewed; 154 AA.
AC J9VLJ9; Q9C0S4;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2012, sequence version 1.
DT 03-AUG-2022, entry version 43.
DE RecName: Full=Superoxide dismutase [Cu-Zn] {ECO:0000255|RuleBase:RU000393};
DE EC=1.15.1.1 {ECO:0000305|PubMed:12496163, ECO:0000305|PubMed:16524904};
DE AltName: Full=CnSOD1 {ECO:0000303|PubMed:11368899};
GN Name=SOD1 {ECO:0000303|PubMed:11368899};
GN ORFNames=CNAG_01019 {ECO:0000312|EMBL:AFR95128.1};
OS Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 /
OS CBS 10515 / FGSC 9487) (Filobasidiella neoformans var. grubii).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus;
OC Cryptococcus neoformans species complex.
OX NCBI_TaxID=235443 {ECO:0000312|Proteomes:UP000010091};
RN [1] {ECO:0000312|EMBL:AAK31915.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC STRAIN=H99 / ATCC 208821 / CBS 10515 / FGSC 9487 {ECO:0000305};
RX PubMed=11368899; DOI=10.1016/s0378-1119(01)00408-5;
RA Chaturvedi S., Hamilton A.J., Hobby P., Zhu G., Lowry C.V., Chaturvedi V.;
RT "Molecular cloning, phylogenetic analysis and three-dimensional modeling of
RT Cu,Zn superoxide dismutase (CnSOD1) from three varieties of Cryptococcus
RT neoformans.";
RL Gene 268:41-51(2001).
RN [2] {ECO:0000312|Proteomes:UP000010091}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H99 / ATCC 208821 / CBS 10515 / FGSC 9487;
RX PubMed=24743168; DOI=10.1371/journal.pgen.1004261;
RA Janbon G., Ormerod K.L., Paulet D., Byrnes E.J. III, Yadav V.,
RA Chatterjee G., Mullapudi N., Hon C.-C., Billmyre R.B., Brunel F.,
RA Bahn Y.-S., Chen W., Chen Y., Chow E.W.L., Coppee J.-Y., Floyd-Averette A.,
RA Gaillardin C., Gerik K.J., Goldberg J., Gonzalez-Hilarion S., Gujja S.,
RA Hamlin J.L., Hsueh Y.-P., Ianiri G., Jones S., Kodira C.D., Kozubowski L.,
RA Lam W., Marra M., Mesner L.D., Mieczkowski P.A., Moyrand F., Nielsen K.,
RA Proux C., Rossignol T., Schein J.E., Sun S., Wollschlaeger C., Wood I.A.,
RA Zeng Q., Neuveglise C., Newlon C.S., Perfect J.R., Lodge J.K., Idnurm A.,
RA Stajich J.E., Kronstad J.W., Sanyal K., Heitman J., Fraser J.A.,
RA Cuomo C.A., Dietrich F.S.;
RT "Analysis of the genome and transcriptome of Cryptococcus neoformans var.
RT grubii reveals complex RNA expression and microevolution leading to
RT virulence attenuation.";
RL PLoS Genet. 10:E1004261-E1004261(2014).
RN [3] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=12496163; DOI=10.1128/iai.71.1.173-180.2003;
RA Cox G.M., Harrison T.S., McDade H.C., Taborda C.P., Heinrich G.,
RA Casadevall A., Perfect J.R.;
RT "Superoxide dismutase influences the virulence of Cryptococcus neoformans
RT by affecting growth within macrophages.";
RL Infect. Immun. 71:173-180(2003).
RN [4] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=16524904; DOI=10.1128/ec.5.3.488-498.2006;
RA Siafakas A.R., Wright L.C., Sorrell T.C., Djordjevic J.T.;
RT "Lipid rafts in Cryptococcus neoformans concentrate the virulence
RT determinants phospholipase B1 and Cu/Zn superoxide dismutase.";
RL Eukaryot. Cell 5:488-498(2006).
RN [5] {ECO:0000305}
RP SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=33567338; DOI=10.1016/j.jbc.2021.100391;
RA Smith A.D., Garcia-Santamarina S., Ralle M., Loiselle D.R., Haystead T.A.,
RA Thiele D.J.;
RT "Transcription factor-driven alternative localization of Cryptococcus
RT neoformans superoxide dismutase.";
RL J. Biol. Chem. 296:100391-100391(2021).
CC -!- FUNCTION: Destroys radicals which are normally produced within the
CC cells and which are toxic to biological systems (PubMed:16524904,
CC PubMed:12496163). Destroys radicals produced by host defense mechanisms
CC (PubMed:12496163). {ECO:0000269|PubMed:12496163,
CC ECO:0000269|PubMed:16524904}.
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 Evidence={ECO:0000305|PubMed:12496163, ECO:0000305|PubMed:16524904};
CC -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC Evidence={ECO:0000250|UniProtKB:P00445};
CC Note=Binds 1 copper ion per subunit. {ECO:0000250|UniProtKB:P00445};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P00445};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P00445};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P85978}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:33567338}.
CC Mitochondrion {ECO:0000269|PubMed:33567338}. Cell membrane
CC {ECO:0000269|PubMed:16524904}; Peripheral membrane protein
CC {ECO:0000305}. Note=Localizes to lipid rafts in the cell membrane.
CC {ECO:0000269|PubMed:16524904}.
CC -!- INDUCTION: Repressed when copper levels are low in a CUF1-dependent
CC manner (at protein level) (PubMed:33567338). Induced by high
CC temperature (PubMed:12496163). {ECO:0000269|PubMed:12496163,
CC ECO:0000269|PubMed:33567338}.
CC -!- DISRUPTION PHENOTYPE: Decreases cellular superoxide dismutase activity
CC (PubMed:16524904). Sensitive to oxygen radicals (PubMed:12496163).
CC Decreases virulence in a mouse inhalation model of infection
CC (PubMed:12496163). {ECO:0000269|PubMed:12496163,
CC ECO:0000269|PubMed:16524904}.
CC -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family.
CC {ECO:0000305}.
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DR EMBL; AF248045; AAK31914.1; -; mRNA.
DR EMBL; AF248046; AAK31915.1; -; Genomic_DNA.
DR EMBL; CP003824; AFR95128.1; -; Genomic_DNA.
DR RefSeq; XP_012049259.1; XM_012193869.1.
DR SMR; J9VLJ9; -.
DR SwissPalm; J9VLJ9; -.
DR EnsemblFungi; AFR95128; AFR95128; CNAG_01019.
DR GeneID; 23884765; -.
DR VEuPathDB; FungiDB:CNAG_01019; -.
DR HOGENOM; CLU_056632_4_1_1; -.
DR Proteomes; UP000010091; Chromosome 5.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0019897; C:extrinsic component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0044853; C:plasma membrane raft; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004784; F:superoxide dismutase activity; IMP:UniProtKB.
DR GO; GO:0019430; P:removal of superoxide radicals; IMP:UniProtKB.
DR GO; GO:0052164; P:symbiont defense to host-produced reactive oxygen species; IMP:UniProtKB.
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.
DR PROSITE; PS00332; SOD_CU_ZN_2; 1.
PE 1: Evidence at protein level;
KW Antioxidant; Cell membrane; Copper; Cytoplasm; Disulfide bond; Membrane;
KW Metal-binding; Mitochondrion; Oxidoreductase; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P00445"
FT CHAIN 2..154
FT /note="Superoxide dismutase [Cu-Zn]"
FT /id="PRO_0000453194"
FT BINDING 47
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P00445"
FT BINDING 49
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P00445"
FT BINDING 64
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P00445"
FT BINDING 64
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="structural"
FT /evidence="ECO:0000250|UniProtKB:P00445"
FT BINDING 72
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="structural"
FT /evidence="ECO:0000250|UniProtKB:P00445"
FT BINDING 81
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="structural"
FT /evidence="ECO:0000250|UniProtKB:P00445"
FT BINDING 84
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="structural"
FT /evidence="ECO:0000250|UniProtKB:P00445"
FT BINDING 121
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P00445"
FT BINDING 144
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00445"
FT DISULFID 58..147
FT /evidence="ECO:0000250|UniProtKB:P00445"
SQ SEQUENCE 154 AA; 16148 MW; 21C3A9287355F40D CRC64;
MVKAVVVLKG ESYVHGTVCF TQESENAPVC ITGEIKDMDA DAKRGMHVHE FGDNTNGCTS
AGPHYNPFKK HHGAPTDSER HVGDLGNIQT NSCGAAQLDF SDKIISLYGP HSIIGRSLVV
HASTDDLGKG GNEESLKTGN AGARLACGVI GIST
