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Protein

Copper chaperone for superoxide dismutase, chloroplastic/cytosolic

Gene

CCS

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Copper chaperone for the superoxide dismutases CSD1, CSD2 and CSD3. Binds copper ions and delivers them specifically to CSDs. Is required for assistance in CSDs disulfide bond formation and thereby activation of CSDs. May be involved in the negative regulation of heat stress-responsive genes and thermotolerance.4 Publications

Cofactori

Cu2+PROSITE-ProRule annotationNote: Binds 2 copper ions per subunit.PROSITE-ProRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi97 – 971Copper 1PROSITE-ProRule annotation
Metal bindingi100 – 1001Copper 1PROSITE-ProRule annotation
Metal bindingi300 – 3001Copper 2PROSITE-ProRule annotation
Metal bindingi302 – 3021Copper 2PROSITE-ProRule annotation

GO - Molecular functioni

  • superoxide dismutase copper chaperone activity Source: TAIR
  • zinc ion binding Source: GO_Central

GO - Biological processi

  • cellular copper ion homeostasis Source: TAIR
  • metal ion transport Source: InterPro
  • oxidation-reduction process Source: InterPro
  • positive regulation of catalytic activity Source: GOC
  • superoxide metabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Biological processi

Stress response

Keywords - Ligandi

Copper, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Copper chaperone for superoxide dismutase, chloroplastic/cytosolic
Short name:
AtCCS
Alternative name(s):
Superoxide dismutase copper chaperone
Gene namesi
Name:CCS
Ordered Locus Names:At1g12520
ORF Names:F5O11.26, T12C24.6
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 1

Organism-specific databases

TAIRiAT1G12520.

Subcellular locationi

GO - Cellular componenti

  • chloroplast Source: TAIR
  • chloroplast stroma Source: TAIR
  • cytosol Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Cytoplasm, Plastid

Pathology & Biotechi

Disruption phenotypei

No visible phenotype under normal growth conditions, but mutant plants have increased tolerance to heat stress.2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 6767ChloroplastSequence analysisAdd
BLAST
Chaini68 – 320253Copper chaperone for superoxide dismutase, chloroplastic/cytosolicPRO_0000422757Add
BLAST

Proteomic databases

PaxDbiQ9LD47.
PRIDEiQ9LD47.

Expressioni

Tissue specificityi

Expressed in roots, shoots, stems and flowers, and at lower levels in rosette and cauline leaves.1 Publication

Inductioni

By copper and senescence. Down-regulated by heat stress.2 Publications

Gene expression databases

GenevisibleiQ9LD47. AT.

Interactioni

Subunit structurei

Interacts with CSD1.1 Publication

Protein-protein interaction databases

BioGridi23048. 4 interactions.
IntActiQ9LD47. 5 interactions.
STRINGi3702.AT1G12520.1.

Structurei

3D structure databases

ProteinModelPortaliQ9LD47.
SMRiQ9LD47. Positions 90-309.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini87 – 15064HMAPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

In the C-terminal section; belongs to the Cu-Zn superoxide dismutase family.Curated
Contains 1 HMA domain.PROSITE-ProRule annotation

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG4656. Eukaryota.
COG2608. LUCA.
HOGENOMiHOG000263450.
InParanoidiQ9LD47.
KOiK04569.
OMAiIWEVIGH.
PhylomeDBiQ9LD47.

Family and domain databases

Gene3Di2.60.40.200. 1 hit.
InterProiIPR024142. Ccs1.
IPR006121. HMA_dom.
IPR024134. SOD_Cu/Zn_/chaperone.
IPR001424. SOD_Cu_Zn_dom.
[Graphical view]
PANTHERiPTHR10003. PTHR10003. 1 hit.
PTHR10003:SF27. PTHR10003:SF27. 1 hit.
PfamiPF00403. HMA. 1 hit.
PF00080. Sod_Cu. 1 hit.
[Graphical view]
SUPFAMiSSF49329. SSF49329. 1 hit.
SSF55008. SSF55008. 1 hit.
PROSITEiPS50846. HMA_2. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9LD47-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MASILRSVAT TSAVVAAASA IPIAIAFSSS SSSSSTNPKS QSLNFSFLSR
60 70 80 90 100
SSPRLLGLSR SFVSSPMATA LTSDRNLHQE DRAMPQLLTE FMVDMTCEGC
110 120 130 140 150
VNAVKNKLET IEGIEKVEVD LSNQVVRILG SSPVKAMTQA LEQTGRKARL
160 170 180 190 200
IGQGVPQDFL VSAAVAEFKG PDIFGVVRFA QVSMELARIE ANFTGLSPGT
210 220 230 240 250
HSWCINEYGD LTNGAASTGS LYNPFQDQTG TEPLGDLGTL EADKNGEAFY
260 270 280 290 300
SGKKEKLKVA DLIGRAVVVY KTDDNKSGPG LTAAVIARSA GVGENYKKLC
310 320
SCDGTVIWEA TNSDFVASKV
Length:320
Mass (Da):33,851
Last modified:October 1, 2000 - v1
Checksum:iFCD7A30742B91840
GO
Isoform 2 (identifier: Q9LD47-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-91: Missing.

Note: No experimental confirmation available.
Show »
Length:229
Mass (Da):24,319
Checksum:iD22CD688EA8D04D9
GO
Isoform 3 (identifier: Q9LD47-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-136: Missing.

Note: No experimental confirmation available.
Show »
Length:184
Mass (Da):19,489
Checksum:i1073BECE557618CE
GO

Sequence cautioni

The sequence AAK91374.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti239 – 2391T → A in AAY22970 (PubMed:16126858).Curated
Sequence conflicti313 – 3131S → N in AAY22970 (PubMed:16126858).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 136136Missing in isoform 3. 1 PublicationVSP_046612Add
BLAST
Alternative sequencei1 – 9191Missing in isoform 2. 1 PublicationVSP_046613Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ003058 mRNA. Translation: AAY22970.1.
AC025416 Genomic DNA. Translation: AAF79650.1.
AC025417 Genomic DNA. Translation: AAF88100.1.
CP002684 Genomic DNA. Translation: AEE28891.1.
CP002684 Genomic DNA. Translation: AEE28892.1.
CP002684 Genomic DNA. Translation: AEE28893.1.
AK175663 mRNA. Translation: BAD43426.1.
AK176660 mRNA. Translation: BAD44423.1.
AK221656 mRNA. Translation: BAD95327.1.
AY050357 mRNA. Translation: AAK91374.1. Different initiation.
AY094034 mRNA. Translation: AAM16190.1.
AF179371 mRNA. Translation: AAD52685.1.
PIRiD86259.
RefSeqiNP_001031029.1. NM_001035952.2. [Q9LD47-2]
NP_001031030.1. NM_001035953.2. [Q9LD47-3]
NP_563910.2. NM_101123.3. [Q9LD47-1]
UniGeneiAt.10574.
At.75575.

Genome annotation databases

EnsemblPlantsiAT1G12520.1; AT1G12520.1; AT1G12520. [Q9LD47-1]
GeneIDi837808.
KEGGiath:AT1G12520.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ003058 mRNA. Translation: AAY22970.1.
AC025416 Genomic DNA. Translation: AAF79650.1.
AC025417 Genomic DNA. Translation: AAF88100.1.
CP002684 Genomic DNA. Translation: AEE28891.1.
CP002684 Genomic DNA. Translation: AEE28892.1.
CP002684 Genomic DNA. Translation: AEE28893.1.
AK175663 mRNA. Translation: BAD43426.1.
AK176660 mRNA. Translation: BAD44423.1.
AK221656 mRNA. Translation: BAD95327.1.
AY050357 mRNA. Translation: AAK91374.1. Different initiation.
AY094034 mRNA. Translation: AAM16190.1.
AF179371 mRNA. Translation: AAD52685.1.
PIRiD86259.
RefSeqiNP_001031029.1. NM_001035952.2. [Q9LD47-2]
NP_001031030.1. NM_001035953.2. [Q9LD47-3]
NP_563910.2. NM_101123.3. [Q9LD47-1]
UniGeneiAt.10574.
At.75575.

3D structure databases

ProteinModelPortaliQ9LD47.
SMRiQ9LD47. Positions 90-309.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi23048. 4 interactions.
IntActiQ9LD47. 5 interactions.
STRINGi3702.AT1G12520.1.

Proteomic databases

PaxDbiQ9LD47.
PRIDEiQ9LD47.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT1G12520.1; AT1G12520.1; AT1G12520. [Q9LD47-1]
GeneIDi837808.
KEGGiath:AT1G12520.

Organism-specific databases

TAIRiAT1G12520.

Phylogenomic databases

eggNOGiKOG4656. Eukaryota.
COG2608. LUCA.
HOGENOMiHOG000263450.
InParanoidiQ9LD47.
KOiK04569.
OMAiIWEVIGH.
PhylomeDBiQ9LD47.

Miscellaneous databases

PROiQ9LD47.

Gene expression databases

GenevisibleiQ9LD47. AT.

Family and domain databases

Gene3Di2.60.40.200. 1 hit.
InterProiIPR024142. Ccs1.
IPR006121. HMA_dom.
IPR024134. SOD_Cu/Zn_/chaperone.
IPR001424. SOD_Cu_Zn_dom.
[Graphical view]
PANTHERiPTHR10003. PTHR10003. 1 hit.
PTHR10003:SF27. PTHR10003:SF27. 1 hit.
PfamiPF00403. HMA. 1 hit.
PF00080. Sod_Cu. 1 hit.
[Graphical view]
SUPFAMiSSF49329. SSF49329. 1 hit.
SSF55008. SSF55008. 1 hit.
PROSITEiPS50846. HMA_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A copper chaperone for superoxide dismutase that confers three types of copper/zinc superoxide dismutase activity in Arabidopsis."
    Chu C.C., Lee W.C., Guo W.Y., Pan S.M., Chen L.J., Li H.M., Jinn T.L.
    Plant Physiol. 139:425-436(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH CSD1, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.
  2. "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."
    Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K.
    , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.
    Nature 408:816-820(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  3. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  4. "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."
    Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.
    , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K.
    Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
    Strain: cv. Columbia.
  5. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
    Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
    , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
    Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 4-320 (ISOFORM 1).
    Strain: cv. Columbia.
  6. "Arabidopsis thaliana chloroplast copper chaperone for Cu,Zn superoxide dismutase."
    Nersissian A.M., Valentine J.S.
    Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 11-320 (ISOFORM 1).
  7. Cited for: FUNCTION, SUBCELLULAR LOCATION, INDUCTION.
  8. "Copper chaperone-dependent and -independent activation of three copper-zinc superoxide dismutase homologs localized in different cellular compartments in Arabidopsis."
    Huang C.H., Kuo W.Y., Weiss C., Jinn T.L.
    Plant Physiol. 158:737-746(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  9. "Heat stress induction of miR398 triggers a regulatory loop that is critical for thermotolerance in Arabidopsis."
    Guan Q., Lu X., Zeng H., Zhang Y., Zhu J.
    Plant J. 74:840-851(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INDUCTION, DISRUPTION PHENOTYPE.

Entry informationi

Entry nameiCCS_ARATH
AccessioniPrimary (citable) accession number: Q9LD47
Secondary accession number(s): Q4ZJI5
, Q67Y08, Q681F4, Q94A55, Q9SPD6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 26, 2013
Last sequence update: October 1, 2000
Last modified: February 17, 2016
This is version 108 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.