Q9WU84 (CCS_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Copper chaperone for superoxide dismutase

Alternative name(s):
Superoxide dismutase copper chaperone

Gene names

Name:	Ccs
Synonyms:	Ccsd

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	274 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Delivers copper to copper zinc superoxide dismutase (SOD1).
Cofactor	Binds 2 copper ions per subunit By similarity. Binds 1 zinc ion per subunit By similarity.
Subunit structure	Homodimer, and heterodimer with SOD1. Interacts with COMMD1 By similarity.
Subcellular location	Cytoplasm By similarity.
Tissue specificity	Ubiquitous.
Sequence similarities	In the C-terminal section; belongs to the Cu-Zn superoxide dismutase family. Contains 1 HMA domain.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	Copper Metal-binding Zinc
Molecular function	Chaperone
PTM	Disulfide bond Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	intracellular copper ion transport Inferred from Biological aspect of Ancestor. Source: RefGenome positive regulation of oxidoreductase activity Inferred from mutant phenotype. Source: MGI removal of superoxide radicals Inferred from Biological aspect of Ancestor. Source: RefGenome
Cellular component	cytosol Inferred from Biological aspect of Ancestor. Source: RefGenome mitochondrial inner membrane Inferred from Biological aspect of Ancestor. Source: RefGenome nucleus Inferred from Biological aspect of Ancestor. Source: RefGenome
Molecular function	superoxide dismutase activity Inferred from electronic annotation. Source: InterPro superoxide dismutase copper chaperone activity Inferred from Biological aspect of Ancestor. Source: RefGenome zinc ion binding Inferred from Biological aspect of Ancestor. Source: RefGenome
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 274	274	Copper chaperone for superoxide dismutase		PRO_0000213544
Regions
	Domain	12 – 75	64	HMA
	Region	88 – 234	147	Superoxide dismutase-like
Sites
	Metal binding	22	1	Copper 1 By similarity
	Metal binding	25	1	Copper 1 By similarity
	Metal binding	147	1	Zinc By similarity
	Metal binding	155	1	Zinc By similarity
	Metal binding	164	1	Zinc By similarity
	Metal binding	167	1	Zinc By similarity
	Metal binding	244	1	Copper 2 By similarity
	Metal binding	246	1	Copper 2 By similarity
Amino acid modifications
	Modified residue	267	1	Phosphoserine Ref.5
	Disulfide bond	141 ↔ 227		By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9WU84 [UniParc]. Last modified November 1, 1999. Version 1. Checksum: 19DCE48376C9D5A2	FASTA	274	28,912
	10 20 30 40 50 60 MASKSGDGGT VCALEFAVQM SCQSCVDAVH KTLKGVAGVQ NVDVQLENQM VLVQTTLPSQ 70 80 90 100 110 120 EVQALLESTG RQAVLKGMGS SQLQNLGAAV AILEGCGSIQ GVVRFLQLSS ELCLIEGTID 130 140 150 160 170 180 GLEPGLHGLH VHQYGDLTRD CNSCGDHFNP DGASHGGPQD TDRHRGDLGN VRAEAGGRAT 190 200 210 220 230 240 FRIEDKQLKV WDVIGRSLVI DEGEDDLGRG GHPLSKITGN SGKRLACGII ARSAGLFQNP 250 260 270 KQICSCDGLT IWEERGRPIA GQGRKDSAQP PAHL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Copper chaperone for superoxide dismutase is essential to activate mammalian Cu/Zn superoxide dismutase." Wong P.C., Waggoner D., Subramaniam J.R., Tessarollo L., Bartnikas T.B., Culotta V.C., Price D.L., Rothstein J., Gitlin J.D. Proc. Natl. Acad. Sci. U.S.A. 97:2886-2891(2000) [PubMed: 10694572] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Brain.
[2]	"Cloning and mapping of murine superoxide dismutase copper chaperone (Ccsd) and mapping of the human ortholog." Moore S.D., Chen M.M., Cox D.W. Cytogenet. Cell Genet. 88:35-37(2000) [PubMed: 10773661] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: NOD. Tissue: Brain.
[3]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Mammary gland.
[4]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 103-274. Strain: C57BL/6J. Tissue: Embryonic stem cell.
[5]	"Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry." Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M. J. Proteome Res. 7:5314-5326(2008) [PubMed: 19367708] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-267, MASS SPECTROMETRY. Tissue: Melanoma.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF121906 mRNA. Translation: AAD23832.1. AF173379 mRNA. Translation: AAF70242.1. AK010264 mRNA. Translation: BAB26806.1. BC026938 mRNA. Translation: AAH26938.1.
IPI	IPI00124103.
RefSeq	NP_058588.1. NM_016892.3.
UniGene	Mm.434411.
3D structure databases
ProteinModelPortal	Q9WU84.
SMR	Q9WU84. Positions 9-237.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-48692N.
STRING	Q9WU84.
PTM databases
PhosphoSite	Q9WU84.
Proteomic databases
PRIDE	Q9WU84.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000037246; ENSMUSP00000035486; ENSMUSG00000034108.
GeneID	12460.
KEGG	mmu:12460.
Organism-specific databases
CTD	9973.
MGI	MGI:1333783. Ccs.
Phylogenomic databases
GeneTree	ENSGT00530000063226.
HOGENOM	HBG324056.
HOVERGEN	HBG018933.
InParanoid	Q9WU84.
OMA	CDGVTLW.
OrthoDB	EOG45TCNZ.
PhylomeDB	Q9WU84.
Gene expression databases
ArrayExpress	Q9WU84.
Bgee	Q9WU84.
CleanEx	MM_CCS.
Genevestigator	Q9WU84.
GermOnline	ENSMUSG00000034108. Mus musculus.
Family and domain databases
InterPro	IPR006121. HeavyMe-assoc_HMA. IPR024134. SOD_Cu/Zn_/chaperones. IPR018152. SOD_Cu/Zn_BS. IPR024142. SOD_Cu_chaperone. IPR001424. SOD_Cu_Zn_dom. [Graphical view]
Gene3D	G3DSA:2.60.40.200. SOD_Cu_Zn. 1 hit.
KO	K04569.
PANTHER	PTHR10003:SF27. PTHR10003:SF27. 1 hit. PTHR10003. SOD_Cu_Zn. 1 hit.
Pfam	PF00403. HMA. 1 hit. PF00080. Sod_Cu. 1 hit. [Graphical view]
PRINTS	PR00068. CUZNDISMTASE.
SUPFAM	SSF55008. HeavyMe_transpt. 1 hit. SSF49329. SOD_Cu_Zn. 1 hit.
PROSITE	PS01047. HMA_1. False negative. PS50846. HMA_2. 1 hit. PS00087. SOD_CU_ZN_1. False negative. PS00332. SOD_CU_ZN_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	281316.
SOURCE	Search...

Entry information

Entry name

CCS_MOUSE

Accession

Primary (citable) accession number: Q9WU84
Secondary accession number(s): Q9CRJ9

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 31, 2002
Last sequence update:	November 1, 1999
Last modified:	November 16, 2011
This is version 94 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program