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O59666 (ATU2_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 88. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Copper-transporting ATPase ccc2
EC=3.6.3.4
Alternative name(s):
Cu(2+)-ATPase
Gene names
Name:ccc2
ORF Names:SPBC29A3.01
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

Protein attributes

Sequence length904 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Probably involved in copper transport and in the regulation of cellular copper level. Retrieves copper from the metallochaperone atx1 and incorporates it into trans-Golgi vesicles By similarity.

Catalytic activity

ATP + H2O + Cu2+(In) = ADP + phosphate + Cu2+(Out).

Subcellular location

Golgi apparatus › trans-Golgi network membrane; Multi-pass membrane protein Ref.2.

Sequence similarities

Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IB subfamily. [View classification]

Contains 2 HMA domains.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 904904Copper-transporting ATPase ccc2
PRO_0000314753

Regions

Topological domain1 – 172172Cytoplasmic By similarity
Transmembrane173 – 19321Helical; Potential
Topological domain194 – 1974Lumenal, vesicle By similarity
Transmembrane198 – 21821Helical; Potential
Topological domain219 – 24628Cytoplasmic By similarity
Transmembrane247 – 26721Helical; Potential
Topological domain268 – 27811Lumenal, vesicle By similarity
Transmembrane279 – 29618Helical; Potential
Topological domain297 – 431135Cytoplasmic By similarity
Transmembrane432 – 45221Helical; Potential
Topological domain453 – 46917Lumenal, vesicle By similarity
Transmembrane470 – 49021Helical; Potential
Topological domain491 – 805315Cytoplasmic By similarity
Transmembrane806 – 82621Helical; Potential
Topological domain827 – 8282Lumenal, vesicle By similarity
Transmembrane829 – 84921Helical; Potential
Topological domain850 – 90455Cytoplasmic By similarity
Domain3 – 6967HMA
Compositional bias480 – 4834Poly-Val
Compositional bias645 – 6484Poly-Ser

Sites

Active site52914-aspartylphosphate intermediate By similarity
Metal binding131Copper By similarity
Metal binding161Copper By similarity
Metal binding7421Magnesium By similarity
Metal binding7461Magnesium By similarity

Sequences

Sequence LengthMass (Da)Tools
O59666 [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: 546EE3C8AAECE146

FASTA90497,895
        10         20         30         40         50         60 
MYTTTLSVQG MTCTSCVASI QSMLEGVEGI EQFTISLLLE RAIAVHDPSI ISPDQIAEKI 

        70         80         90        100        110        120 
EDCGFDASVI SSTEGEHGVM ANYLLLSPMQ AEQWTKVHNH INELQGVLSV NCSSSPDAAI 

       130        140        150        160        170        180 
RVIYDSEITG PRSIMKEILS MGVKCTFQPV DSSTSRILSL QRGSQIRVWK IRFIISISFS 

       190        200        210        220        230        240 
LAVMFLPQIF DSCDSMRAAF LVPHYFGICA GHIISLVLSL PVQFGVGRVY YSAAYHALKR 

       250        260        270        280        290        300 
GTANMDVLVS LGSTVAFAAS IFFMILYSAR HADNPAPIFF DTADMLLTFV TLGRYLESKA 

       310        320        330        340        350        360 
KGSTSAALSQ LLSLAPSSAT IIEDNEQIEI LADLIERGDL ILVKPGEIIP VDGTVVEGSS 

       370        380        390        400        410        420 
YVDESSVSGE PVPVHKTIDD ELLSGTANGN GRLLVKATKS PRESQLAVIV DLVQRAQISH 

       430        440        450        460        470        480 
APIQQFADRV AGIFVPVIVA LSISTFTFWF LFTKYSSKYP SVFDDPMGKF AVCLKLTISV 

       490        500        510        520        530        540 
VVVACPCALG LSTPTAVMVG TGVGALNGII IKGGEILERL NQVDTVVFDK TGTLTVGKLS 

       550        560        570        580        590        600 
VTDISIVDNL EELLDIPKNI FWAFVKASES SSEHPIGKAI TEKASEFTDV SEIGIESFNA 

       610        620        630        640        650        660 
VPGEGVDVVL RWKERTFHAL LGNSLLLEHN NVSIPDDFDS KLKLSSSSGL TCVRIAIDGQ 

       670        680        690        700        710        720 
FVGFLGCMDQ VRPDSYQTVS ALKQLGKKVC LLTGDQKATA RRVAQGLEID FSDVYAEAVP 

       730        740        750        760        770        780 
SQKAEIIQKL KDQKHCVAMV GDGINDSPSL VLADVGIAPI NGSGIALESA DVILVRKGVL 

       790        800        810        820        830        840 
LDTAVSFDLS RVIVKRIKMN LVWACIYNFV MIPIAMGFFL PWGIYLNPMW ASAAMMFSSL 

       850        860        870        880        890        900 
SVLASSLLLR RWKKPKSLIF SEADDVETES STNSSVLQKV YTATRSIFGR NKSSNKYQPV 


ANEV

« Hide

References

[1]"The genome sequence of Schizosaccharomyces pombe."
Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. expand/collapse author list , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
Nature 415:871-880(2002) [PubMed: 11859360] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 972 / ATCC 24843.
[2]"ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe."
Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., Yoshida M.
Nat. Biotechnol. 24:841-847(2006) [PubMed: 16823372] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CU329671 Genomic DNA. Translation: CAA18378.1.
PIRT40072.
RefSeqNP_595829.1. NM_001021733.1.

3D structure databases

HSSPHSSP built from PDB template 1Y3J based on UniProtKB Q04656.
ProteinModelPortalO59666.
ModBaseSearch...

Protein-protein interaction databases

STRINGO59666.

Protein family/group databases

TCDB3.A.3.5.29. P-type ATPase (P-ATPase) superfamily.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPBC29A3.01.1; SPBC29A3.01.1:pep; SPBC29A3.01.
GeneID2540525.
GenomeReviewsGene locus ccc2 in contig CU329671_GR.
KEGGspo:SPBC29A3.01.
NMPDRfig|4896.1.peg.1695.

Organism-specific databases

GeneDB_SpombeSPBC29A3.01.

Phylogenomic databases

eggNOGfuNOG05708.
GeneTreeEFGT00050000000742.
HOGENOMHBG507745.
OMAMASHEAK.
OrthoDBEOG4ZGSMH.

Gene expression databases

ArrayExpressO59666.

Family and domain databases

InterProIPR008250. ATPase_P-typ_ATPase-assoc-dom.
IPR006403. ATPase_P-typ_cat/Cu-transptr.
IPR023300. ATPase_P-typ_cyto_domA.
IPR023299. ATPase_P-typ_cyto_domN.
IPR006416. ATPase_P-typ_heavy-metal.
IPR001757. ATPase_P-typ_ion-transptr.
IPR018303. ATPase_P-typ_P_site.
IPR005834. Dehalogen-like_hydro.
IPR023214. HAD-like_dom.
IPR017969. Heavy-metal-associated_CS.
IPR006121. HeavyMe-assoc_HMA.
[Graphical view]
Gene3DG3DSA:2.70.150.10. ATPase_P-typ_cyto_domA. 1 hit.
G3DSA:3.40.1110.10. ATPase_P-typ_cyto_domN. 1 hit.
G3DSA:3.40.50.1000. HAD-like_dom. 2 hits.
KOK01533.
PfamPF00122. E1-E2_ATPase. 1 hit.
PF00403. HMA. 1 hit.
PF00702. Hydrolase. 1 hit.
[Graphical view]
PRINTSPR00119. CATATPASE.
PR00942. CUATPASEI.
SUPFAMSSF56784. HAD-like_dom. 1 hit.
SSF55008. HeavyMe_transpt. 1 hit.
TIGRFAMsTIGR01525. ATPase-IB_hvy. 1 hit.
TIGR01494. ATPase_P-type. 2 hits.
PROSITEPS00154. ATPASE_E1_E2. 1 hit.
PS01047. HMA_1. 1 hit.
PS50846. HMA_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameATU2_SCHPO
AccessionPrimary (citable) accession number: O59666
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: August 1, 1998
Last modified: December 14, 2011
This is version 88 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents