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Database: UniProt
Entry: Q4ZJI8_ARATH
LinkDB: Q4ZJI8_ARATH
Original site: Q4ZJI8_ARATH 
ID   Q4ZJI8_ARATH            Unreviewed;       218 AA.
AC   Q4ZJI8;
DT   07-JUN-2005, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2005, sequence version 1.
DT   27-MAR-2024, entry version 89.
DE   SubName: Full=Copper/zinc superoxide dismutase chaperone {ECO:0000313|EMBL:AAY22967.1};
DE   Flags: Fragment;
GN   OrderedLocusNames=At1g12520 {ECO:0000313|EMBL:AAY22967.1};
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702 {ECO:0000313|EMBL:AAY22967.1};
RN   [1] {ECO:0000313|EMBL:AAY22967.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=16126858; DOI=10.1104/pp.105.065284;
RA   Chu C.C., Lee W.C., Guo W.Y., Pan S.M., Chen L.J., Li H.M., Jinn T.L.;
RT   "A copper chaperone for superoxide dismutase that confers three types of
RT   copper/zinc superoxide dismutase activity in Arabidopsis.";
RL   Plant Physiol. 139:425-436(2005).
RN   [2] {ECO:0000313|EMBL:AAY22967.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Chu C.-C., Lee W.-C., Pan S.-M., Jinn T.-L.;
RL   Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC         Evidence={ECO:0000256|ARBA:ARBA00001935};
CC   -!- COFACTOR:
CC       Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
CC         Evidence={ECO:0000256|ARBA:ARBA00001973};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
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DR   EMBL; DQ003054; AAY22966.1; -; mRNA.
DR   EMBL; DQ003055; AAY22967.1; -; mRNA.
DR   EMBL; DQ003056; AAY22968.1; -; mRNA.
DR   EMBL; DQ003057; AAY22969.1; -; mRNA.
DR   AlphaFoldDB; Q4ZJI8; -.
DR   Gramene; AT1G12520.1; AT1G12520.1; AT1G12520.
DR   ExpressionAtlas; Q4ZJI8; baseline and differential.
DR   GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR   GO; GO:0006801; P:superoxide metabolic process; IEA:InterPro.
DR   CDD; cd00371; HMA; 1.
DR   Gene3D; 3.30.70.100; -; 1.
DR   Gene3D; 2.60.40.200; Superoxide dismutase, copper/zinc binding domain; 1.
DR   InterPro; IPR006121; HMA_dom.
DR   InterPro; IPR036163; HMA_dom_sf.
DR   InterPro; IPR036423; SOD-like_Cu/Zn_dom_sf.
DR   InterPro; IPR024134; SOD_Cu/Zn_/chaperone.
DR   PANTHER; PTHR10003:SF86; COPPER CHAPERONE FOR SUPEROXIDE DISMUTASE; 1.
DR   PANTHER; PTHR10003; SUPEROXIDE DISMUTASE CU-ZN -RELATED; 1.
DR   Pfam; PF00403; HMA; 1.
DR   SUPFAM; SSF49329; Cu,Zn superoxide dismutase-like; 1.
DR   SUPFAM; SSF55008; HMA, heavy metal-associated domain; 1.
DR   PROSITE; PS50846; HMA_2; 1.
PE   2: Evidence at transcript level;
KW   Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW   Copper {ECO:0000256|ARBA:ARBA00023008}.
FT   DOMAIN          86..149
FT                   /note="HMA"
FT                   /evidence="ECO:0000259|PROSITE:PS50846"
FT   NON_TER         218
FT                   /evidence="ECO:0000313|EMBL:AAY22967.1"
SQ   SEQUENCE   218 AA;  23107 MW;  21D1C31C08549B63 CRC64;
     MASILRSVAT TSAVVAAASA IPIAIAFSSS SSSSSTNPKS QSLNFSFLSR SSPRLLGLSR
     SFVSSPMATA LTSDRNLHQE DRAMPQLLTE FMVDMTCEGC VNAVKNKLET IEGIEKVEVD
     LSNQVVRILG SSPVKAMTQA LEQTGRKARL IGQGVPQDFL VSAAVAEFKG PDIFGVVRFA
     QVSMELARIE ANFTGLSPGT HSWCINEYGD LTNGAAST
//
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