SODM_CRYNH
ID SODM_CRYNH Reviewed; 225 AA.
AC J9VWW9;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2012, sequence version 1.
DT 03-AUG-2022, entry version 40.
DE RecName: Full=Superoxide dismutase [Mn], mitochondrial {ECO:0000305};
DE EC=1.15.1.1 {ECO:0000305|PubMed:33567338};
DE Flags: Precursor;
GN Name=SOD2 {ECO:0000303|PubMed:15643059};
GN ORFNames=CNAG_04388 {ECO:0000312|EMBL:AFR97119.1};
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|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 [2] {ECO:0000305}
RP FUNCTION.
RX PubMed=15643059; DOI=10.1128/ec.4.1.46-54.2005;
RA Giles S.S., Batinic-Haberle I., Perfect J.R., Cox G.M.;
RT "Cryptococcus neoformans mitochondrial superoxide dismutase: an essential
RT link between antioxidant function and high-temperature growth.";
RL Eukaryot. Cell 4:46-54(2005).
RN [3] {ECO:0000305}
RP FUNCTION, AND DISRUPTION 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 [4] {ECO:0000305}
RP FUNCTION (ISOFORMS 1 AND 2), CATALYTIC ACTIVITY, SUBCELLULAR LOCATION
RP (ISOFORMS 1 AND 2), ALTERNATIVE SPLICING (ISOFORMS 1 AND 2), INDUCTION,
RP DISRUPTION PHENOTYPE, AND MUTAGENESIS OF 1-MET--THR-21.
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.
CC {ECO:0000269|PubMed:15643059, ECO:0000269|PubMed:16524904}.
CC -!- FUNCTION: [Isoform 1]: Destroys mitochondrial radicals produced by
CC oxidative stress. {ECO:0000269|PubMed:33567338}.
CC -!- FUNCTION: [Isoform 2]: Destroys cytoplasmic radicals produced in low
CC copper environments; a condition which inactivates the cytoplasmic
CC copper-dependent superoxide dismutase SOD1.
CC {ECO:0000269|PubMed:33567338}.
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:33567338};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:Q9UQX0};
CC Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000250|UniProtKB:Q9UQX0};
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Mitochondrion
CC {ECO:0000269|PubMed:33567338}. Note=Localizes to the mitochondrion both
CC in copper-replete and copper-limiting conditions.
CC {ECO:0000269|PubMed:33567338}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm
CC {ECO:0000269|PubMed:33567338}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1 {ECO:0000303|PubMed:33567338};
CC IsoId=J9VWW9-1; Sequence=Displayed;
CC Name=2 {ECO:0000303|PubMed:33567338};
CC IsoId=J9VWW9-2; Sequence=VSP_061114;
CC -!- INDUCTION: [Isoform 2]: Repressed when copper levels are low in a CUF1-
CC dependent manner (at protein level). {ECO:0000269|PubMed:33567338}.
CC -!- DISRUPTION PHENOTYPE: Decreases cellular superoxide dismutase activity
CC (PubMed:16524904). Sensitive to thermal stress, and menadione (induces
CC oxidative stress) (PubMed:33567338). Decreases virulence in a mouse
CC model of infection (PubMed:33567338). {ECO:0000269|PubMed:16524904,
CC ECO:0000269|PubMed:33567338}.
CC -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase family.
CC {ECO:0000305}.
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DR EMBL; CP003828; AFR97119.1; -; Genomic_DNA.
DR RefSeq; XP_012051781.1; XM_012196391.1.
DR SMR; J9VWW9; -.
DR EnsemblFungi; AFR97119; AFR97119; CNAG_04388. [J9VWW9-1]
DR GeneID; 23887823; -.
DR VEuPathDB; FungiDB:CNAG_04388; -.
DR HOGENOM; CLU_031625_2_0_1; -.
DR Proteomes; UP000010091; Chromosome 9.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; 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 Gene3D; 1.10.287.990; -; 1.
DR Gene3D; 3.55.40.20; -; 1.
DR InterPro; IPR001189; Mn/Fe_SOD.
DR InterPro; IPR019833; Mn/Fe_SOD_BS.
DR InterPro; IPR019832; Mn/Fe_SOD_C.
DR InterPro; IPR019831; Mn/Fe_SOD_N.
DR InterPro; IPR036324; Mn/Fe_SOD_N_sf.
DR InterPro; IPR036314; SOD_C_sf.
DR Pfam; PF02777; Sod_Fe_C; 1.
DR Pfam; PF00081; Sod_Fe_N; 1.
DR PIRSF; PIRSF000349; SODismutase; 1.
DR PRINTS; PR01703; MNSODISMTASE.
DR SUPFAM; SSF46609; SSF46609; 1.
DR SUPFAM; SSF54719; SSF54719; 1.
DR PROSITE; PS00088; SOD_MN; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Antioxidant; Cytoplasm; Manganese; Metal-binding;
KW Mitochondrion; Oxidoreductase; Transit peptide.
FT TRANSIT 1..27
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:33567338"
FT CHAIN 28..225
FT /note="Superoxide dismutase [Mn], mitochondrial"
FT /evidence="ECO:0000255"
FT /id="PRO_0000453195"
FT BINDING 53
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P04179"
FT BINDING 101
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P04179"
FT BINDING 187
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P04179"
FT BINDING 191
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P04179"
FT VAR_SEQ 1..21
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000269|PubMed:33567338"
FT /id="VSP_061114"
FT MUTAGEN 1..21
FT /note="Missing: Sensitive to thermal stress."
FT /evidence="ECO:0000269|PubMed:33567338"
SQ SEQUENCE 225 AA; 24887 MW; 39686C17C98D251C CRC64;
MITAITRTAL PRATLRTSLA TMSTIRAKHT LPPLPYAYDA LEPSISAEIM NLHHTKHHQT
YVNGLNAAEE SLQKASADGD FKTAISLQPA LKFNGGGHIN HSLFWKNLAP TGSAQVKVPT
SGVFYDQVQA DFGGFENLKK EMNAKTAAIQ GSGWGWLGYN KATKKLEIVT TPNQDPLLSH
VPIIGIDIWE HAFYLQYKNV KPDYLNAIWN VINYEEAESR LKAAQ
