CCS_ARATH
ID CCS_ARATH Reviewed; 320 AA.
AC Q9LD47; Q4ZJI5; Q67Y08; Q681F4; Q94A55; Q9SPD6;
DT 26-JUN-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Copper chaperone for superoxide dismutase, chloroplastic/cytosolic;
DE Short=AtCCS;
DE AltName: Full=Superoxide dismutase copper chaperone;
DE Flags: Precursor;
GN Name=CCS; OrderedLocusNames=At1g12520; ORFNames=F5O11.26, T12C24.6;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH CSD1, TISSUE
RP SPECIFICITY, AND DISRUPTION PHENOTYPE.
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 4-320 (ISOFORM 1).
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 11-320 (ISOFORM 1).
RA Nersissian A.M., Valentine J.S.;
RT "Arabidopsis thaliana chloroplast copper chaperone for Cu,Zn superoxide
RT dismutase.";
RL Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=15848163; DOI=10.1016/j.febslet.2005.03.025;
RA Abdel-Ghany S.E., Burkhead J.L., Gogolin K.A., Andres-Colas N.,
RA Bodecker J.R., Puig S., Penarrubia L., Pilon M.;
RT "AtCCS is a functional homolog of the yeast copper chaperone Ccs1/Lys7.";
RL FEBS Lett. 579:2307-2312(2005).
RN [8]
RP FUNCTION.
RX PubMed=22186608; DOI=10.1104/pp.111.190223;
RA Huang C.H., Kuo W.Y., Weiss C., Jinn T.L.;
RT "Copper chaperone-dependent and -independent activation of three copper-
RT zinc superoxide dismutase homologs localized in different cellular
RT compartments in Arabidopsis.";
RL Plant Physiol. 158:737-746(2012).
RN [9]
RP FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=23480361; DOI=10.1111/tpj.12169;
RA Guan Q., Lu X., Zeng H., Zhang Y., Zhu J.;
RT "Heat stress induction of miR398 triggers a regulatory loop that is
RT critical for thermotolerance in Arabidopsis.";
RL Plant J. 74:840-851(2013).
CC -!- FUNCTION: Copper chaperone for the superoxide dismutases CSD1, CSD2 and
CC CSD3. Binds copper ions and delivers them specifically to CSDs. Is
CC required for assistance in CSDs disulfide bond formation and thereby
CC activation of CSDs. May be involved in the negative regulation of heat
CC stress-responsive genes and thermotolerance.
CC {ECO:0000269|PubMed:15848163, ECO:0000269|PubMed:16126858,
CC ECO:0000269|PubMed:22186608, ECO:0000269|PubMed:23480361}.
CC -!- COFACTOR:
CC Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00280};
CC Note=Binds 2 copper ions per subunit. {ECO:0000255|PROSITE-
CC ProRule:PRU00280};
CC -!- SUBUNIT: Interacts with CSD1. {ECO:0000269|PubMed:16126858}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:15848163}. Cytoplasm, cytosol
CC {ECO:0000269|PubMed:15848163}. Note=It is unclear whether the
CC chloroplastic and cytosolic proteins result from 2 different
CC transcripts or from alternative translation initiation from the same
CC transcript. {ECO:0000269|PubMed:16126858}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9LD47-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9LD47-2; Sequence=VSP_046613;
CC Name=3;
CC IsoId=Q9LD47-3; Sequence=VSP_046612;
CC -!- TISSUE SPECIFICITY: Expressed in roots, shoots, stems and flowers, and
CC at lower levels in rosette and cauline leaves.
CC {ECO:0000269|PubMed:16126858}.
CC -!- INDUCTION: By copper and senescence. Down-regulated by heat stress.
CC {ECO:0000269|PubMed:15848163, ECO:0000269|PubMed:23480361}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but mutant plants have increased tolerance to heat stress.
CC {ECO:0000269|PubMed:16126858, ECO:0000269|PubMed:23480361}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the Cu-Zn superoxide
CC dismutase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK91374.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; DQ003058; AAY22970.1; -; mRNA.
DR EMBL; AC025416; AAF79650.1; -; Genomic_DNA.
DR EMBL; AC025417; AAF88100.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE28891.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE28892.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE28893.1; -; Genomic_DNA.
DR EMBL; AK175663; BAD43426.1; -; mRNA.
DR EMBL; AK176660; BAD44423.1; -; mRNA.
DR EMBL; AK221656; BAD95327.1; -; mRNA.
DR EMBL; AY050357; AAK91374.1; ALT_INIT; mRNA.
DR EMBL; AY094034; AAM16190.1; -; mRNA.
DR EMBL; AF179371; AAD52685.1; -; mRNA.
DR PIR; D86259; D86259.
DR RefSeq; NP_001031029.1; NM_001035952.3. [Q9LD47-2]
DR RefSeq; NP_001031030.1; NM_001035953.2. [Q9LD47-3]
DR RefSeq; NP_563910.2; NM_101123.4. [Q9LD47-1]
DR AlphaFoldDB; Q9LD47; -.
DR SMR; Q9LD47; -.
DR BioGRID; 23048; 4.
DR IntAct; Q9LD47; 5.
DR STRING; 3702.AT1G12520.1; -.
DR PaxDb; Q9LD47; -.
DR PRIDE; Q9LD47; -.
DR ProteomicsDB; 223966; -. [Q9LD47-1]
DR EnsemblPlants; AT1G12520.1; AT1G12520.1; AT1G12520. [Q9LD47-1]
DR EnsemblPlants; AT1G12520.2; AT1G12520.2; AT1G12520. [Q9LD47-2]
DR EnsemblPlants; AT1G12520.3; AT1G12520.3; AT1G12520. [Q9LD47-3]
DR GeneID; 837808; -.
DR Gramene; AT1G12520.1; AT1G12520.1; AT1G12520. [Q9LD47-1]
DR Gramene; AT1G12520.2; AT1G12520.2; AT1G12520. [Q9LD47-2]
DR Gramene; AT1G12520.3; AT1G12520.3; AT1G12520. [Q9LD47-3]
DR KEGG; ath:AT1G12520; -.
DR Araport; AT1G12520; -.
DR TAIR; locus:2034740; AT1G12520.
DR eggNOG; KOG4656; Eukaryota.
DR HOGENOM; CLU_056632_0_1_1; -.
DR InParanoid; Q9LD47; -.
DR OMA; KGMGSDQ; -.
DR OrthoDB; 1527306at2759; -.
DR PhylomeDB; Q9LD47; -.
DR PRO; PR:Q9LD47; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9LD47; baseline and differential.
DR Genevisible; Q9LD47; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005507; F:copper ion binding; IBA:GO_Central.
DR GO; GO:0016532; F:superoxide dismutase copper chaperone activity; IMP:TAIR.
DR GO; GO:0006878; P:cellular copper ion homeostasis; TAS:TAIR.
DR GO; GO:0019430; P:removal of superoxide radicals; IBA:GO_Central.
DR CDD; cd00371; HMA; 1.
DR Gene3D; 2.60.40.200; -; 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 InterPro; IPR001424; SOD_Cu_Zn_dom.
DR PANTHER; PTHR10003; PTHR10003; 1.
DR Pfam; PF00403; HMA; 1.
DR Pfam; PF00080; Sod_Cu; 1.
DR SUPFAM; SSF49329; SSF49329; 1.
DR SUPFAM; SSF55008; SSF55008; 1.
DR PROSITE; PS50846; HMA_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Chaperone; Chloroplast; Copper; Cytoplasm;
KW Metal-binding; Plastid; Reference proteome; Stress response;
KW Transit peptide.
FT TRANSIT 1..67
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 68..320
FT /note="Copper chaperone for superoxide dismutase,
FT chloroplastic/cytosolic"
FT /id="PRO_0000422757"
FT DOMAIN 86..149
FT /note="HMA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT BINDING 97
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT BINDING 100
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT BINDING 300
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT BINDING 302
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT VAR_SEQ 1..136
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_046612"
FT VAR_SEQ 1..91
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_046613"
FT CONFLICT 239
FT /note="T -> A (in Ref. 1; AAY22970)"
FT /evidence="ECO:0000305"
FT CONFLICT 313
FT /note="S -> N (in Ref. 1; AAY22970)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 320 AA; 33851 MW; FCD7A30742B91840 CRC64;
MASILRSVAT TSAVVAAASA IPIAIAFSSS SSSSSTNPKS QSLNFSFLSR SSPRLLGLSR
SFVSSPMATA LTSDRNLHQE DRAMPQLLTE FMVDMTCEGC VNAVKNKLET IEGIEKVEVD
LSNQVVRILG SSPVKAMTQA LEQTGRKARL IGQGVPQDFL VSAAVAEFKG PDIFGVVRFA
QVSMELARIE ANFTGLSPGT HSWCINEYGD LTNGAASTGS LYNPFQDQTG TEPLGDLGTL
EADKNGEAFY SGKKEKLKVA DLIGRAVVVY KTDDNKSGPG LTAAVIARSA GVGENYKKLC
SCDGTVIWEA TNSDFVASKV
