ID SODC_CHICK Reviewed; 154 AA.
AC P80566; Q92059;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 27-MAR-2024, entry version 145.
DE RecName: Full=Superoxide dismutase [Cu-Zn];
DE EC=1.15.1.1;
GN Name=SOD1;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Spinal cord;
RX PubMed=8988375; DOI=10.3109/10425179609047575;
RA Stanton J.L., Wilton S.D., Laing N.G.;
RT "Characterisation of the chicken Cu,Zn superoxide dismutase gene.";
RL DNA Seq. 6:357-360(1996).
RN [2]
RP PROTEIN SEQUENCE OF 2-154, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT
RP ALA-2, GLUTATHIONYLATION AT CYS-154, AND MASS SPECTROMETRY.
RC TISSUE=Erythrocyte;
RX PubMed=8647082; DOI=10.1111/j.1432-1033.1996.0433k.x;
RA Schinina M.E., Carlini P., Polticelli F., Zappacosta F., Bossa F.,
RA Calabrese L.;
RT "Amino acid sequence of chicken Cu,Zn-containing superoxide dismutase and
RT identification of glutathionyl adducts at exposed cysteine residues.";
RL Eur. J. Biochem. 237:433-439(1996).
CC -!- FUNCTION: Destroys radicals which are normally produced within the
CC cells and which are toxic to biological systems.
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 -!- SUBUNIT: Homodimer.
CC -!- INTERACTION:
CC P80566; Q8AYS8: KCNMA1; NbExp=3; IntAct=EBI-1637015, EBI-1635766;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus {ECO:0000250}.
CC -!- MASS SPECTROMETRY: Mass=15600; Mass_error=2; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:8647082};
CC -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family.
CC {ECO:0000305}.
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DR EMBL; U28407; AAB88059.1; -; mRNA.
DR PIR; S65436; S65436.
DR RefSeq; NP_990395.1; NM_205064.1.
DR AlphaFoldDB; P80566; -.
DR SMR; P80566; -.
DR BioGRID; 676211; 1.
DR IntAct; P80566; 1.
DR STRING; 9031.ENSGALP00000035996; -.
DR iPTMnet; P80566; -.
DR PaxDb; 9031-ENSGALP00000035996; -.
DR GeneID; 395938; -.
DR KEGG; gga:395938; -.
DR CTD; 6647; -.
DR VEuPathDB; HostDB:geneid_395938; -.
DR eggNOG; KOG0441; Eukaryota.
DR InParanoid; P80566; -.
DR PhylomeDB; P80566; -.
DR PRO; PR:P80566; -.
DR Proteomes; UP000000539; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005777; C:peroxisome; IBA:GO_Central.
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 CDD; cd00305; Cu-Zn_Superoxide_Dismutase; 1.
DR Gene3D; 2.60.40.200; Superoxide dismutase, copper/zinc binding domain; 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:SF103; SUPEROXIDE DISMUTASE [CU-ZN]; 1.
DR PANTHER; PTHR10003; SUPEROXIDE DISMUTASE CU-ZN -RELATED; 1.
DR Pfam; PF00080; Sod_Cu; 1.
DR PRINTS; PR00068; CUZNDISMTASE.
DR SUPFAM; SSF49329; Cu,Zn superoxide dismutase-like; 1.
DR PROSITE; PS00087; SOD_CU_ZN_1; 1.
DR PROSITE; PS00332; SOD_CU_ZN_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Antioxidant; Copper; Cytoplasm; Direct protein sequencing;
KW Disulfide bond; Glutathionylation; Lipoprotein; Metal-binding; Nucleus;
KW Oxidoreductase; Palmitate; Reference proteome; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:8647082"
FT CHAIN 2..154
FT /note="Superoxide dismutase [Cu-Zn]"
FT /id="PRO_0000164069"
FT BINDING 47
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 49
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 64
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 64
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000250"
FT BINDING 72
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000250"
FT BINDING 81
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000250"
FT BINDING 84
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000250"
FT BINDING 120
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|PubMed:8647082"
FT MOD_RES 154
FT /note="S-glutathionyl cysteine"
FT /evidence="ECO:0000269|PubMed:8647082"
FT LIPID 8
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT DISULFID 58..146
FT /evidence="ECO:0000250"
FT CONFLICT 14
FT /note="A -> G (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 154 AA; 15704 MW; F06FEF9FCBB7FB9E CRC64;
MATLKAVCVM KGDAPVEGVI HFQQQGSGPV KVTGKITGLS DGDHGFHVHE FGDNTNGCTS
AGAHFNPEGK QHGGPKDADR HVGDLGNVTA KGGVAEVEIE DSVISLTGPH CIIGRTMVVH
AKSDDLGRGG DNESKLTGNA GPRLACGVIG IAKC
//