Skip Header

Contribute Send feedback
Read comments (?) or add your own

P38995 (ATU2_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 119. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
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
EC=3.6.3.4
Alternative name(s):
Cu(2+)-ATPase
Gene names
Name:CCC2
Ordered Locus Names:YDR270W
ORF Names:D9954.6
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length1004 AA.
Sequence statusComplete.
Protein existenceEvidence at protein 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.

Catalytic activity

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

Subcellular location

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

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 – 10041004Copper-transporting ATPase
PRO_0000046318

Regions

Topological domain1 – 262262Cytoplasmic Potential
Transmembrane263 – 28321Helical; Potential
Topological domain284 – 30320Lumenal, vesicle Potential
Transmembrane304 – 32421Helical; Potential
Topological domain325 – 33511Cytoplasmic Potential
Transmembrane336 – 35621Helical; Potential
Topological domain357 – 37014Lumenal, vesicle Potential
Transmembrane371 – 39121Helical; Potential
Topological domain392 – 528137Cytoplasmic Potential
Transmembrane529 – 54921Helical; Potential
Topological domain550 – 57728Lumenal, vesicle Potential
Transmembrane578 – 59821Helical; Potential
Topological domain599 – 901303Cytoplasmic Potential
Transmembrane902 – 92423Helical; Potential
Topological domain925 – 9273Lumenal, vesicle Potential
Transmembrane928 – 95023Helical; Potential
Topological domain951 – 100454Cytoplasmic Potential
Domain3 – 6866HMA 1
Domain81 – 14767HMA 2

Sites

Active site62714-aspartylphosphate intermediate By similarity
Metal binding131Copper
Metal binding161Copper
Metal binding911Copper Potential
Metal binding941Copper Potential
Metal binding8381Magnesium By similarity
Metal binding8421Magnesium By similarity

Secondary structure

1 .............. 1004
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P38995 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: 571E9F73EA1F599F

FASTA1,004109,829
        10         20         30         40         50         60 
MREVILAVHG MTCSACTNTI NTQLRALKGV TKCDISLVTN ECQVTYDNEV TADSIKEIIE 

        70         80         90        100        110        120 
DCGFDCEILR DSEITAISTK EGLLSVQGMT CGSCVSTVTK QVEGIEGVES VVVSLVTEEC 

       130        140        150        160        170        180 
HVIYEPSKTT LETAREMIED CGFDSNIIMD GNGNADMTEK TVILKVTKAF EDESPLILSS 

       190        200        210        220        230        240 
VSERFQFLLD LGVKSIEISD DMHTLTIKYC CNELGIRDLL RHLERTGYKF TVFSNLDNTT 

       250        260        270        280        290        300 
QLRLLSKEDE IRFWKKNSIK STLLAIICML LYMIVPMMWP TIVQDRIFPY KETSFVRGLF 

       310        320        330        340        350        360 
YRDILGVILA SYIQFSVGFY FYKAAWASLK HGSGTMDTLV CVSTTCAYTF SVFSLVHNMF 

       370        380        390        400        410        420 
HPSSTGKLPR IVFDTSIMII SYISIGKYLE TLAKSQTSTA LSKLIQLTPS VCSIISDVER 

       430        440        450        460        470        480 
NETKEIPIEL LQVNDIVEIK PGMKIPADGI ITRGESEIDE SLMTGESILV PKKTGFPVIA 

       490        500        510        520        530        540 
GSVNGPGHFY FRTTTVGEET KLANIIKVMK EAQLSKAPIQ GYADYLASIF VPGILILAVL 

       550        560        570        580        590        600 
TFFIWCFILN ISANPPVAFT ANTKADNFFI CLQTATSVVI VACPCALGLA TPTAIMVGTG 

       610        620        630        640        650        660 
VGAQNGVLIK GGEVLEKFNS ITTFVFDKTG TLTTGFMVVK KFLKDSNWVG NVDEDEVLAC 

       670        680        690        700        710        720 
IKATESISDH PVSKAIIRYC DGLNCNKALN AVVLESEYVL GKGIVSKCQV NGNTYDICIG 

       730        740        750        760        770        780 
NEALILEDAL KKSGFINSNV DQGNTVSYVS VNGHVFGLFE INDEVKHDSY ATVQYLQRNG 

       790        800        810        820        830        840 
YETYMITGDN NSAAKRVARE VGISFENVYS DVSPTGKCDL VKKIQDKEGN NKVAVVGDGI 

       850        860        870        880        890        900 
NDAPALALSD LGIAISTGTE IAIEAADIVI LCGNDLNTNS LRGLANAIDI SLKTFKRIKL 

       910        920        930        940        950        960 
NLFWALCYNI FMIPIAMGVL IPWGITLPPM LAGLAMAFSS VSVVLSSLML KKWTPPDIES 

       970        980        990       1000 
HGISDFKSKF SIGNFWSRLF STRAIAGEQD IESQAGLMSN EEVL

« Hide

References

« Hide 'large scale' references
[1]"Sequence, mapping and disruption of CCC2, a gene that cross-complements the Ca(2+)-sensitive phenotype of csg1 mutants and encodes a P-type ATPase belonging to the Cu(2+)-ATPase subfamily."
Fu D., Beeler T.J., Dunn T.M.
Yeast 11:283-292(1995) [PubMed: 7785328] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T. expand/collapse author list , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
Nature 387:75-78(1997) [PubMed: 9169867] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204511 / S288c / AB972.
[3]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[4]"Characterization of the binding interface between the copper chaperone Atx1 and the first cytosolic domain of Ccc2 ATPase."
Arnesano F., Banci L., Bertini I., Cantini F., Ciofi-Baffoni S., Huffman D.L., O'Halloran T.V.
J. Biol. Chem. 276:41365-41376(2001) [PubMed: 11500502] [Abstract]
Cited for: METAL-BINDING SITES.
[5]"Solution structure of the yeast copper transporter domain Ccc2a in the apo and Cu(I)-loaded states."
Banci L., Bertini I., Ciofi-Baffoni S., Huffman D.L., O'Halloran T.V.
J. Biol. Chem. 276:8415-8426(2001) [PubMed: 11083871] [Abstract]
Cited for: STRUCTURE BY NMR OF 1-72 IN APO AND COPPER-BOUND FORMS.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		L36317 Genomic DNA. Translation: AAC37425.1.
U51030 Genomic DNA. Translation: AAB64451.1.
BK006938 Genomic DNA. Translation: DAA12113.1.
PIRS55353.
RefSeqNP_010556.1. NM_001180578.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1FVQNMR-A2-72[»]
1FVSNMR-A2-72[»]
1UV1model-B2-72[»]
1UV2model-B2-72[»]
2GGPNMR-B2-72[»]
ProteinModelPortalP38995.
SMRP38995. Positions 2-957.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-906N.
MINTMINT-367619.
STRINGP38995.

Protein family/group databases

TCDB3.A.3.5.17. P-type ATPase (P-ATPase) superfamily.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYDR270W; YDR270W; YDR270W.
GeneID851862.
KEGGsce:YDR270W.
NMPDRfig|4932.3.peg.1318.

Organism-specific databases

CYGDYDR270w.
SGDS000002678. CCC2.

Phylogenomic databases

eggNOGfuNOG05708.
GeneTreeEFGT00050000000742.
HOGENOMHBG507745.
OMAEDYSMAQ.
OrthoDBEOG4ZGSMH.

Gene expression databases

ArrayExpressP38995.
GenevestigatorP38995.
GermOnlineYDR270W. Saccharomyces cerevisiae.

Family and domain databases

InterProIPR008250. ATPase_P-typ_ATPase-assoc-dom.
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.
IPR006122. HMA_Cu_ion-bd.
[Graphical view]
Gene3DG3DSA:2.70.150.10. ATPase_P-typ_cyto_domA. 1 hit.
G3DSA:3.40.1110.10. ATPase_P-typ_cyto_domN. 2 hits.
G3DSA:3.40.50.1000. HAD-like_dom. 1 hit.
KOK01533.
PfamPF00122. E1-E2_ATPase. 1 hit.
PF00403. HMA. 2 hits.
PF00702. Hydrolase. 1 hit.
[Graphical view]
PRINTSPR00119. CATATPASE.
SUPFAMSSF56784. HAD-like_dom. 1 hit.
SSF55008. HeavyMe_transpt. 2 hits.
TIGRFAMsTIGR01525. ATPase-IB_hvy. 1 hit.
TIGR01494. ATPase_P-type. 2 hits.
TIGR00003. TIGR00003. 2 hits.
PROSITEPS00154. ATPASE_E1_E2. 1 hit.
PS01047. HMA_1. 2 hits.
PS50846. HMA_2. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio969806.

Entry information

Entry nameATU2_YEAST
AccessionPrimary (citable) accession number: P38995
Secondary accession number(s): D6VSQ3
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: December 14, 2011
This is version 119 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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