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Database: UniProt
Entry: P81082
LinkDB: P81082
Original site: P81082 
ID   SODCP_PINPS             Reviewed;          15 AA.
AC   P81082;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1998, sequence version 1.
DT   25-MAY-2022, entry version 75.
DE   RecName: Full=Probable superoxide dismutase [Cu-Zn], chloroplastic;
DE            EC=1.15.1.1;
DE   AltName: Full=Water stress-responsive protein 15;
DE   Flags: Fragment;
OS   Pinus pinaster (Maritime pine).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Pinopsida; Pinidae; Conifers I; Pinales; Pinaceae; Pinus;
OC   Pinus subgen. Pinus.
OX   NCBI_TaxID=71647;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   TISSUE=Needle;
RX   PubMed=9747804; DOI=10.1023/a:1006006132120;
RA   Costa P., Bahrman N., Frigerio J.-M., Kremer A., Plomion C.;
RT   "Water-deficit-responsive proteins in maritime pine.";
RL   Plant Mol. Biol. 38:587-596(1998).
RN   [2]
RP   PROTEIN SEQUENCE.
RC   TISSUE=Needle;
RX   PubMed=10344291;
RX   DOI=10.1002/(sici)1522-2683(19990101)20:4/5<1098::aid-elps1098>3.0.co;2-z;
RA   Costa P., Pionneau C., Bauw G., Dubos C., Bahrman N., Kremer A.,
RA   Frigerio J.-M., Plomion C.;
RT   "Separation and characterization of needle and xylem maritime pine
RT   proteins.";
RL   Electrophoresis 20:1098-1108(1999).
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. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC   -!- INDUCTION: By water stress.
CC   -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family.
CC       {ECO:0000305}.
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DR   GO; GO:0009507; C:chloroplast; 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.
PE   1: Evidence at protein level;
KW   Antioxidant; Chloroplast; Copper; Direct protein sequencing; Metal-binding;
KW   Oxidoreductase; Plastid; Stress response; Zinc.
FT   CHAIN           <1..>15
FT                   /note="Probable superoxide dismutase [Cu-Zn],
FT                   chloroplastic"
FT                   /id="PRO_0000164179"
FT   NON_TER         1
FT   NON_TER         15
SQ   SEQUENCE   15 AA;  1381 MW;  0369BF9DBBB69CA8 CRC64;
     HAGDLGNIVA GSDGV
//
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