SODC_HUMLT
ID SODC_HUMLT Reviewed; 153 AA.
AC P83684;
DT 28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Superoxide dismutase [Cu-Zn];
DE EC=1.15.1.1 {ECO:0000269|PubMed:11390695};
DE AltName: Full=HlSOD;
OS Humicola lutea.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Chaetomiaceae; Humicola.
OX NCBI_TaxID=253246 {ECO:0000305};
RN [1]
RP PROTEIN SEQUENCE OF 2-153, INDUCTION BY COPPER, DISULFIDE BOND, MASS
RP SPECTROMETRY, AND GLYCOSYLATION.
RC STRAIN=103;
RX PubMed=15094369; DOI=10.1016/j.bbrc.2004.03.142;
RA Dolashka-Angelova P., Stevanovic S., Dolashki A., Angelova M.,
RA Serkedjieva J., Krumova E., Pashova S., Zacharieva S., Voelter W.;
RT "Structural and functional analysis of glycosylated Cu/Zn-superoxide
RT dismutase from the fungal strain Humicola lutea 103.";
RL Biochem. Biophys. Res. Commun. 317:1006-1016(2004).
RN [2] {ECO:0000305}
RP PROTEIN SEQUENCE OF 2-36, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT,
RP AND MASS SPECTROMETRY.
RC STRAIN=103 {ECO:0000269|PubMed:11390695};
RC TISSUE=Mycelium {ECO:0000269|PubMed:11390695};
RX PubMed=11390695; DOI=10.1099/00221287-147-6-1641;
RA Angelova M., Dolashka-Angelova P., Ivanova E., Serkedjieva J., Slokoska L.,
RA Pashova S., Toshkova R., Vassilev S., Simeonov I., Hartmann H.-J.,
RA Stoeva S., Weser U., Voelter W.;
RT "A novel glycosylated Cu/Zn-containing superoxide dismutase: production and
RT potential therapeutic effect.";
RL Microbiology 147:1641-1650(2001).
CC -!- FUNCTION: Destroys radicals which are normally produced within the
CC cells and which are toxic to biological systems.
CC {ECO:0000269|PubMed:11390695}.
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:0000269|PubMed:11390695};
CC -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC Evidence={ECO:0000269|PubMed:11390695};
CC Note=Binds 1 copper ion per subunit. {ECO:0000269|PubMed:11390695};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:11390695};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:11390695};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:11390695}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P00445}.
CC -!- INDUCTION: By high concentrations of copper. Inhibited by copper
CC starvation. {ECO:0000269|PubMed:15094369}.
CC -!- MASS SPECTROMETRY: Mass=15935; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:15094369};
CC -!- MASS SPECTROMETRY: Mass=15844.6; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:11390695};
CC -!- MISCELLANEOUS: Protects mice from mortality after experimental
CC infection with influenza A virus (strain A/Aichi/2/68).
CC -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family.
CC {ECO:0000305}.
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DR AlphaFoldDB; P83684; -.
DR SMR; P83684; -.
DR iPTMnet; P83684; -.
DR PRIDE; P83684; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004784; F:superoxide dismutase activity; IEA:UniProtKB-EC.
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; Copper; Cytoplasm; Direct protein sequencing; Disulfide bond;
KW Glycoprotein; Metal-binding; Oxidoreductase; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:11390695,
FT ECO:0000269|PubMed:15094369"
FT CHAIN 2..153
FT /note="Superoxide dismutase [Cu-Zn]"
FT /id="PRO_0000164121"
FT REGION 126..145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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_note="structural"
FT /evidence="ECO:0000250|UniProtKB:P00445"
FT BINDING 72
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
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_note="structural"
FT /evidence="ECO:0000250|UniProtKB:P00445"
FT BINDING 84
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
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 CARBOHYD 24
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:15094369"
FT DISULFID 58..147
FT /evidence="ECO:0000269|PubMed:15094369"
SQ SEQUENCE 153 AA; 15864 MW; A228E978B7DA5BD7 CRC64;
MVKAVAVLRG DSKITGTVTF EQANESAPTT VSWNITGHDP NAERGMHIHQ FGDNTNGCTS
AGPHYNPFKK THGAPTDEVR HVGDLGNIKT DAEGNAVGSV QDKLIKVIGA ESILGRTIVV
HAGTDDLGRG GNEESKKTGN AGPRPACGVI GIA
