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Protein

Superoxide dismutase 1 copper chaperone

Gene

CCS1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Copper chaperone for apo superoxide dismutase 1 (SOD1). Binds copper ions and delivers them specifically to apo-SOD1.1 Publication

Cofactori

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi16 – 161Zinc; shared with apo-SOD1PROSITE-ProRule annotationCombined sources1 Publication
Metal bindingi17 – 171Copper 1PROSITE-ProRule annotation
Metal bindingi20 – 201Copper 1PROSITE-ProRule annotation
Metal bindingi229 – 2291Copper 2PROSITE-ProRule annotation
Metal bindingi231 – 2311Copper 2PROSITE-ProRule annotation

GO - Molecular functioni

  • superoxide dismutase copper chaperone activity Source: SGD

GO - Biological processi

  • intracellular copper ion transport Source: SGD
  • oxidation-reduction process Source: InterPro
  • positive regulation of catalytic activity Source: GOC
  • protein targeting to mitochondrion Source: Reactome
  • superoxide metabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Ligandi

Copper, Metal-binding, Zinc

Enzyme and pathway databases

BioCyciYEAST:G3O-32743-MONOMER.
ReactomeiR-SCE-1268020. Mitochondrial protein import.

Names & Taxonomyi

Protein namesi
Recommended name:
Superoxide dismutase 1 copper chaperone
Gene namesi
Name:CCS1
Synonyms:LYS7
Ordered Locus Names:YMR038C
ORF Names:YM9532.03C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XIII

Organism-specific databases

EuPathDBiFungiDB:YMR038C.
SGDiS000004641. CCS1.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: SGD
  • mitochondrial inner membrane Source: SGD
  • mitochondrial intermembrane space Source: Reactome
  • nucleus Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 249249Superoxide dismutase 1 copper chaperonePRO_0000213542Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi27 ↔ 64Combined sources1 Publication
Disulfide bondi229 – 229Interchain (with C-58 in apo-SOD1)Combined sources1 Publication

Keywords - PTMi

Disulfide bond

Proteomic databases

MaxQBiP40202.
PeptideAtlasiP40202.

PTM databases

iPTMnetiP40202.

Interactioni

Subunit structurei

Homodimer, and heterodimer with apo-SOD1. Zinc-binding at His-16 of CCS1 and 'Glu-43' of apo-SOD1 is required for this heterodimerization.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
SOD1P004452EBI-10287,EBI-17635

Protein-protein interaction databases

BioGridi35210. 177 interactions.
DIPiDIP-4507N.
IntActiP40202. 2 interactions.
MINTiMINT-429630.

Structurei

Secondary structure

1
249
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 53Combined sources
Beta strandi7 – 126Combined sources
Beta strandi17 – 193Combined sources
Helixi20 – 289Combined sources
Beta strandi34 – 407Combined sources
Turni41 – 444Combined sources
Beta strandi45 – 528Combined sources
Helixi54 – 6310Combined sources
Beta strandi69 – 713Combined sources
Beta strandi79 – 857Combined sources
Beta strandi100 – 11011Combined sources
Beta strandi113 – 12513Combined sources
Beta strandi127 – 1359Combined sources
Helixi142 – 1454Combined sources
Beta strandi148 – 1525Combined sources
Beta strandi157 – 1593Combined sources
Beta strandi161 – 1644Combined sources
Turni165 – 1684Combined sources
Beta strandi169 – 17911Combined sources
Helixi182 – 1843Combined sources
Turni185 – 1873Combined sources
Beta strandi188 – 1958Combined sources
Helixi199 – 2013Combined sources
Beta strandi202 – 2054Combined sources
Beta strandi208 – 2147Combined sources
Beta strandi216 – 2183Combined sources
Helixi236 – 2438Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1EJ8X-ray1.55A78-217[»]
1JK9X-ray2.90B/D1-249[»]
1QUPX-ray1.80A/B2-223[»]
ProteinModelPortaliP40202.
SMRiP40202. Positions 3-245.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP40202.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini7 – 7064HMAPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the CCS1 family.Curated
Contains 1 HMA domain.PROSITE-ProRule annotation

Phylogenomic databases

GeneTreeiENSGT00810000126870.
HOGENOMiHOG000263450.
InParanoidiP40202.
KOiK04569.
OMAiIWEVIGH.
OrthoDBiEOG7G4QR6.

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]

Sequencei

Sequence statusi: Complete.

P40202-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTTNDTYEAT YAIPMHCENC VNDIKACLKN VPGINSLNFD IEQQIMSVES
60 70 80 90 100
SVAPSTIINT LRNCGKDAII RGAGKPNSSA VAILETFQKY TIDQKKDTAV
110 120 130 140 150
RGLARIVQVG ENKTLFDITV NGVPEAGNYH ASIHEKGDVS KGVESTGKVW
160 170 180 190 200
HKFDEPIECF NESDLGKNLY SGKTFLSAPL PTWQLIGRSF VISKSLNHPE
210 220 230 240
NEPSSVKDYS FLGVIARSAG VWENNKQVCA CTGKTVWEER KDALANNIK
Length:249
Mass (Da):27,330
Last modified:February 1, 1995 - v1
Checksum:i81DB7E728CDF9366
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U17378 Genomic DNA. Translation: AAC49068.1.
Z48502 Genomic DNA. Translation: CAA88404.1.
AY558398 Genomic DNA. Translation: AAS56724.1.
BK006946 Genomic DNA. Translation: DAA09937.1.
PIRiS50245.
RefSeqiNP_013752.1. NM_001182535.1.

Genome annotation databases

EnsemblFungiiYMR038C; YMR038C; YMR038C.
GeneIDi855054.
KEGGisce:YMR038C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U17378 Genomic DNA. Translation: AAC49068.1.
Z48502 Genomic DNA. Translation: CAA88404.1.
AY558398 Genomic DNA. Translation: AAS56724.1.
BK006946 Genomic DNA. Translation: DAA09937.1.
PIRiS50245.
RefSeqiNP_013752.1. NM_001182535.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1EJ8X-ray1.55A78-217[»]
1JK9X-ray2.90B/D1-249[»]
1QUPX-ray1.80A/B2-223[»]
ProteinModelPortaliP40202.
SMRiP40202. Positions 3-245.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi35210. 177 interactions.
DIPiDIP-4507N.
IntActiP40202. 2 interactions.
MINTiMINT-429630.

PTM databases

iPTMnetiP40202.

Proteomic databases

MaxQBiP40202.
PeptideAtlasiP40202.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYMR038C; YMR038C; YMR038C.
GeneIDi855054.
KEGGisce:YMR038C.

Organism-specific databases

EuPathDBiFungiDB:YMR038C.
SGDiS000004641. CCS1.

Phylogenomic databases

GeneTreeiENSGT00810000126870.
HOGENOMiHOG000263450.
InParanoidiP40202.
KOiK04569.
OMAiIWEVIGH.
OrthoDBiEOG7G4QR6.

Enzyme and pathway databases

BioCyciYEAST:G3O-32743-MONOMER.
ReactomeiR-SCE-1268020. Mitochondrial protein import.

Miscellaneous databases

EvolutionaryTraceiP40202.
PROiP40202.

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. "Cloning and characterization of the Saccharomyces cerevisiae LYS7 gene: evidence for function outside of lysine biosynthesis."
    Horecka J., Kinsey P.T., Sprague G.F. Jr.
    Gene 162:87-92(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  5. Cited for: FUNCTION, SUBCELLULAR LOCATION.
  6. "A fraction of yeast Cu,Zn-superoxide dismutase and its metallochaperone, CCS, localize to the intermembrane space of mitochondria. A physiological role for SOD1 in guarding against mitochondrial oxidative damage."
    Sturtz L.A., Diekert K., Jensen L.T., Lill R., Culotta V.C.
    J. Biol. Chem. 276:38084-38089(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  7. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  8. "Heterodimer formation between superoxide dismutase and its copper chaperone."
    Lamb A.L., Torres A.S., O'Halloran T.V., Rosenzweig A.C.
    Biochemistry 39:14720-14727(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT.
  9. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
    Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
    J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  10. Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 2-223, SUBUNIT, DISULFIDE BONDS.
  11. "X-ray crystallographic and analytical ultracentrifugation analyses of truncated and full-length yeast copper chaperones for SOD (LYS7): a dimer-dimer model of LYS7-SOD association and copper delivery."
    Hall L.T., Sanchez R.J., Holloway S.P., Zhu H., Stine J.E., Lyons T.J., Demeler B., Schirf V., Hansen J.C., Nersissian A.M., Valentine J.S., Hart P.J.
    Biochemistry 39:3611-3623(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 78-217, SUBUNIT.
  12. "Heterodimeric structure of superoxide dismutase in complex with its metallochaperone."
    Lamb A.L., Torres A.S., O'Halloran T.V., Rosenzweig A.C.
    Nat. Struct. Biol. 8:751-755(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) IN COMPLEX WITH ZINC AND SOD1, SUBUNIT, DISULFIDE BONDS.

Entry informationi

Entry nameiCCS1_YEAST
AccessioniPrimary (citable) accession number: P40202
Secondary accession number(s): D6VZL3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: June 8, 2016
This is version 152 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 12000 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome XIII
    Yeast (Saccharomyces cerevisiae) chromosome XIII: entries and gene names

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.