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Protein

Copper chaperone for superoxide dismutase

Gene

Ccs

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Delivers copper to copper zinc superoxide dismutase (SOD1).By similarity

Cofactori

Protein has several cofactor binding sites:
  • Cu2+By similarityNote: Binds 2 copper ions per subunit.By similarity
  • Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi22 – 221Copper 1PROSITE-ProRule annotation
Metal bindingi25 – 251Copper 1PROSITE-ProRule annotation
Metal bindingi147 – 1471ZincPROSITE-ProRule annotation
Metal bindingi155 – 1551ZincPROSITE-ProRule annotation
Metal bindingi164 – 1641ZincPROSITE-ProRule annotation
Metal bindingi167 – 1671ZincPROSITE-ProRule annotation
Metal bindingi244 – 2441Copper 2PROSITE-ProRule annotation
Metal bindingi246 – 2461Copper 2PROSITE-ProRule annotation

GO - Molecular functioni

  • enzyme binding Source: RGD
  • superoxide dismutase activity Source: InterPro
  • superoxide dismutase copper chaperone activity Source: RGD

GO - Biological processi

  • metal ion transport Source: InterPro
  • positive regulation of catalytic activity Source: GOC
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Ligandi

Copper, Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Copper chaperone for superoxide dismutase
Alternative name(s):
Superoxide dismutase copper chaperone
Gene namesi
Name:Ccs
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi620403. Ccs.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 274274Copper chaperone for superoxide dismutasePRO_0000213546Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki76 – 76Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Disulfide bondi141 ↔ 227By similarity
Cross-linki189 – 189Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki216 – 216Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki241 – 241Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei267 – 2671PhosphoserineBy similarity

Post-translational modificationi

Ubiquitinion by XIAP/BIRC4 leads to enhancement of its chaperone activity toward its physiologic target, SOD1, rather than proteasomal degradation. XIAP/BIRC4 preferentially ubiquitinates at Lys-241.

Keywords - PTMi

Disulfide bond, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiQ9JK72.
PRIDEiQ9JK72.

PTM databases

iPTMnetiQ9JK72.
PhosphoSiteiQ9JK72.

Interactioni

Subunit structurei

Homodimer, and heterodimer with SOD1. Interacts with COMMD1 (By similarity). Interacts with XIAP/BIRC4 (By similarity).By similarity

GO - Molecular functioni

  • enzyme binding Source: RGD

Protein-protein interaction databases

IntActiQ9JK72. 1 interaction.
STRINGi10116.ENSRNOP00000065189.

Structurei

3D structure databases

ProteinModelPortaliQ9JK72.
SMRiQ9JK72. Positions 9-237.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini12 – 7564HMAPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni88 – 234147Superoxide dismutase-likeAdd
BLAST

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG410IPMW. Eukaryota.
COG2032. LUCA.
HOGENOMiHOG000263450.
HOVERGENiHBG018933.
InParanoidiQ9JK72.
KOiK04569.
OrthoDBiEOG776SR4.
PhylomeDBiQ9JK72.
TreeFamiTF105184.

Family and domain databases

Gene3Di2.60.40.200. 1 hit.
InterProiIPR024142. Ccs1.
IPR006121. HMA_dom.
IPR024134. SOD_Cu/Zn_/chaperone.
IPR018152. SOD_Cu/Zn_BS.
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]
PRINTSiPR00068. CUZNDISMTASE.
SUPFAMiSSF49329. SSF49329. 1 hit.
SSF55008. SSF55008. 1 hit.
PROSITEiPS50846. HMA_2. 1 hit.
PS00332. SOD_CU_ZN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9JK72-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASKSGDGGT MCALEFTVQM SCQSCVDAVH KTLKGAAGVQ NVEVQLENQM
60 70 80 90 100
VLVQTTLPSQ EVQALLESTG RQAVLKGMGS SQLKNLGAAV AIMEGSGTVQ
110 120 130 140 150
GVVRFLQLSS ELCLIEGTID GLEPGLHGLH VHQYGDLTKD CSSCGDHFNP
160 170 180 190 200
DGASHGGPQD TDRHRGDLGN VHAEASGRAT FRIEDKQLKV WDVIGRSLVV
210 220 230 240 250
DEGEDDLGRG GHPLSKVTGN SGKRLACGII ARSAGLFQNP KQICSCDGLT
260 270
IWEERGRPIA GQGRKDSAQP PAHL
Length:274
Mass (Da):28,890
Last modified:October 1, 2000 - v1
Checksum:i55C95B72C808C800
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti99 – 991V → I in AAI58587 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF255305 mRNA. Translation: AAF65572.1.
BC158586 mRNA. Translation: AAI58587.1.
RefSeqiNP_445877.1. NM_053425.1.
UniGeneiRn.12311.

Genome annotation databases

GeneIDi84485.
KEGGirno:84485.
UCSCiRGD:620403. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF255305 mRNA. Translation: AAF65572.1.
BC158586 mRNA. Translation: AAI58587.1.
RefSeqiNP_445877.1. NM_053425.1.
UniGeneiRn.12311.

3D structure databases

ProteinModelPortaliQ9JK72.
SMRiQ9JK72. Positions 9-237.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9JK72. 1 interaction.
STRINGi10116.ENSRNOP00000065189.

PTM databases

iPTMnetiQ9JK72.
PhosphoSiteiQ9JK72.

Proteomic databases

PaxDbiQ9JK72.
PRIDEiQ9JK72.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi84485.
KEGGirno:84485.
UCSCiRGD:620403. rat.

Organism-specific databases

CTDi9973.
RGDi620403. Ccs.

Phylogenomic databases

eggNOGiENOG410IPMW. Eukaryota.
COG2032. LUCA.
HOGENOMiHOG000263450.
HOVERGENiHBG018933.
InParanoidiQ9JK72.
KOiK04569.
OrthoDBiEOG776SR4.
PhylomeDBiQ9JK72.
TreeFamiTF105184.

Miscellaneous databases

NextBioi617016.
PROiQ9JK72.

Family and domain databases

Gene3Di2.60.40.200. 1 hit.
InterProiIPR024142. Ccs1.
IPR006121. HMA_dom.
IPR024134. SOD_Cu/Zn_/chaperone.
IPR018152. SOD_Cu/Zn_BS.
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]
PRINTSiPR00068. CUZNDISMTASE.
SUPFAMiSSF49329. SSF49329. 1 hit.
SSF55008. SSF55008. 1 hit.
PROSITEiPS50846. HMA_2. 1 hit.
PS00332. SOD_CU_ZN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning and characterization of a copper chaperone for copper/zinc superoxide dismutase from the rat."
    Hiromura M., Chino H., Sonoda T., Sakurai H.
    Biochem. Biophys. Res. Commun. 275:394-400(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBUNIT.
    Strain: Sprague-Dawley.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Spleen.

Entry informationi

Entry nameiCCS_RAT
AccessioniPrimary (citable) accession number: Q9JK72
Secondary accession number(s): B0BMW1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 31, 2002
Last sequence update: October 1, 2000
Last modified: May 11, 2016
This is version 116 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. 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.