SODC_CAMDR
ID SODC_CAMDR Reviewed; 153 AA.
AC H6BDU4;
DT 30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2012, sequence version 1.
DT 03-AUG-2022, entry version 35.
DE RecName: Full=Superoxide dismutase [Cu-Zn] {ECO:0000255|RuleBase:RU000393, ECO:0000303|PubMed:22312292};
DE EC=1.15.1.1 {ECO:0000250|UniProtKB:P00442, ECO:0000255|RuleBase:RU000393};
GN Name=SOD1 {ECO:0000303|PubMed:22312292};
OS Camelus dromedarius (Dromedary) (Arabian camel).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Tylopoda; Camelidae; Camelus.
OX NCBI_TaxID=9838 {ECO:0000312|EMBL:AEF32527.1};
RN [1] {ECO:0000312|EMBL:AEF32527.1}
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND PHYLOGENETIC ANALYSIS.
RX PubMed=22312292; DOI=10.3390/ijms13010879;
RA Ataya F.S., Fouad D., Al-Olayan E., Malik A.;
RT "Molecular cloning, characterization and predicted structure of a putative
RT copper-zinc SOD from the camel, Camelus dromedarius.";
RL Int. J. Mol. Sci. 13:879-900(2012).
CC -!- FUNCTION: Destroys radicals which are normally produced within the
CC cells and which are toxic to biological systems.
CC {ECO:0000250|UniProtKB:P00442, ECO:0000255|RuleBase:RU000393}.
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:0000250|UniProtKB:P00442,
CC ECO:0000255|RuleBase:RU000393};
CC -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC Evidence={ECO:0000250|UniProtKB:P00441,
CC ECO:0000255|RuleBase:RU000393};
CC Note=Binds 1 copper ion per subunit. {ECO:0000250|UniProtKB:P00441,
CC ECO:0000255|RuleBase:RU000393};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P00441,
CC ECO:0000255|RuleBase:RU000393};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P00441,
CC ECO:0000255|RuleBase:RU000393};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P00442}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P00441}. Nucleus
CC {ECO:0000250|UniProtKB:P00441}.
CC -!- TISSUE SPECIFICITY: Highly expressed in liver. Also expressed in testis
CC and to a lesser extent in kidney, lung and spleen.
CC {ECO:0000269|PubMed:22312292}.
CC -!- PTM: Palmitoylation helps nuclear targeting and decreases catalytic
CC activity. {ECO:0000250|UniProtKB:P00441}.
CC -!- PTM: Succinylation, adjacent to copper catalytic site, probably
CC inhibits activity. Desuccinylation by SIRT5 enhances activity.
CC {ECO:0000250|UniProtKB:P00441}.
CC -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family.
CC {ECO:0000255|RuleBase:RU000393, ECO:0000305}.
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DR EMBL; JF758876; AEF32527.1; -; mRNA.
DR RefSeq; XP_010975659.1; XM_010977357.1.
DR AlphaFoldDB; H6BDU4; -.
DR SMR; H6BDU4; -.
DR STRING; 9838.ENSCDRP00005002504; -.
DR Ensembl; ENSCDRT00005002758; ENSCDRP00005002504; ENSCDRG00005001811.
DR OrthoDB; 1574423at2759; -.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005507; F:copper ion binding; ISS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0004784; F:superoxide dismutase activity; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR GO; GO:0019430; P:removal of superoxide radicals; ISS: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 2: Evidence at transcript level;
KW Acetylation; Antioxidant; Copper; Cytoplasm; Disulfide bond; Lipoprotein;
KW Metal-binding; Nucleus; Oxidoreductase; Palmitate; Phosphoprotein; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P00442"
FT CHAIN 2..153
FT /note="Superoxide dismutase [Cu-Zn]"
FT /id="PRO_0000438320"
FT REGION 59..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 46
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P00442"
FT BINDING 48
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P00442"
FT BINDING 63
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P00442"
FT BINDING 63
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000250|UniProtKB:P00442"
FT BINDING 71
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000250|UniProtKB:P00442"
FT BINDING 80
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000250|UniProtKB:P00442"
FT BINDING 83
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000250|UniProtKB:P00442"
FT BINDING 120
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P00442"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P00442"
FT MOD_RES 4
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P08228"
FT MOD_RES 10
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P08228"
FT MOD_RES 91
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P08228"
FT MOD_RES 98
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P00441"
FT MOD_RES 105
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P07632"
FT MOD_RES 107
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P08228"
FT MOD_RES 122
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P00441"
FT MOD_RES 122
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P00441"
FT MOD_RES 136
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P08228"
FT MOD_RES 136
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P08228"
FT LIPID 7
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P00441"
FT DISULFID 57..146
FT /evidence="ECO:0000250|UniProtKB:P00442"
SQ SEQUENCE 153 AA; 15743 MW; 3756F1B50E53B76E CRC64;
MALKAVCVLK GDGQVQGTIH FEQKENGPVM VSGSISGLAE GDHGFHVHQF GDNTQGCTSA
GPHFNPLSKK HGGPKDQERH VGDLGNVTAG KDGVAIVSIE DPVISLSGDH SIIGRTMVVH
EKPDDLGKGG NEESTKTGNA GSRLACGVIG IAQ
