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Database: UniProt/SWISS-PROT
Entry: SODC_CHICK
LinkDB: SODC_CHICK
Original site: SODC_CHICK 
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   16-JAN-2019, entry version 129.
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;
OC   Phasianidae; 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,
RP   ACETYLATION AT ALA-2, GLUTATHIONYLATION AT CYS-154, AND MASS
RP   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
RT   and identification of glutathionyl adducts at exposed cysteine
RT   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       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       Range=2-154; Evidence={ECO:0000269|PubMed:8647082};
CC   -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family.
CC       {ECO:0000305}.
DR   EMBL; U28407; AAB88059.1; -; mRNA.
DR   PIR; S65436; S65436.
DR   RefSeq; NP_990395.1; NM_205064.1.
DR   UniGene; Gga.3346; -.
DR   ProteinModelPortal; P80566; -.
DR   SMR; P80566; -.
DR   BioGrid; 676211; 1.
DR   IntAct; P80566; 1.
DR   STRING; 9031.ENSGALP00000035996; -.
DR   iPTMnet; P80566; -.
DR   PaxDb; P80566; -.
DR   PRIDE; P80566; -.
DR   GeneID; 395938; -.
DR   KEGG; gga:395938; -.
DR   CTD; 6647; -.
DR   eggNOG; KOG0441; Eukaryota.
DR   eggNOG; COG2032; LUCA.
DR   HOGENOM; HOG000263447; -.
DR   HOVERGEN; HBG000062; -.
DR   InParanoid; P80566; -.
DR   KO; K04565; -.
DR   OrthoDB; 1574423at2759; -.
DR   PhylomeDB; P80566; -.
DR   PRO; PR:P80566; -.
DR   Proteomes; UP000000539; Unplaced.
DR   GO; GO:0005623; C:cell; IDA:AgBase.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:0016532; F:superoxide dismutase copper chaperone activity; IBA:GO_Central.
DR   GO; GO:0008270; F:zinc ion binding; 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; -; 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   Acetylation; Antioxidant; Complete proteome; Copper; Cytoplasm;
KW   Direct protein sequencing; Disulfide bond; Glutathionylation;
KW   Lipoprotein; Metal-binding; Nucleus; Oxidoreductase; Palmitate;
KW   Reference proteome; Zinc.
FT   INIT_MET      1      1       Removed. {ECO:0000269|PubMed:8647082}.
FT   CHAIN         2    154       Superoxide dismutase [Cu-Zn].
FT                                /FTId=PRO_0000164069.
FT   METAL        47     47       Copper; catalytic. {ECO:0000250}.
FT   METAL        49     49       Copper; catalytic. {ECO:0000250}.
FT   METAL        64     64       Copper; catalytic. {ECO:0000250}.
FT   METAL        64     64       Zinc; structural. {ECO:0000250}.
FT   METAL        72     72       Zinc; structural. {ECO:0000250}.
FT   METAL        81     81       Zinc; structural. {ECO:0000250}.
FT   METAL        84     84       Zinc; structural. {ECO:0000250}.
FT   METAL       120    120       Copper; catalytic. {ECO:0000250}.
FT   MOD_RES       2      2       N-acetylalanine.
FT                                {ECO:0000269|PubMed:8647082}.
FT   MOD_RES     154    154       S-glutathionyl cysteine.
FT                                {ECO:0000269|PubMed:8647082}.
FT   LIPID         8      8       S-palmitoyl cysteine. {ECO:0000250}.
FT   DISULFID     58    146       {ECO:0000250}.
FT   CONFLICT     14     14       A -> G (in Ref. 2; AA sequence).
FT                                {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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