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Database: UniProt
Entry: SODC_CHICK
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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
//
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