Reviewed, UniProtKB/Swiss-Prot P38995 (ATU2_YEAST)

Names and origin

Protein names

Recommended 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

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	1004 AA.
Sequence status	Complete.
Protein existence	Evidence 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) family. Type IB subfamily. Contains 2 HMA domains.

Ontologies

Keywords
Biological process	Copper transport Ion transport Transport
Cellular component	Golgi apparatus Membrane
Domain	Repeat Transmembrane
Ligand	ATP-binding Copper Magnesium Metal-binding Nucleotide-binding
Molecular function	Hydrolase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	ATP biosynthetic process Inferred from electronic annotation. Source: InterPro cellular iron ion homeostasis Inferred from mutant phenotype. Source: SGD intracellular copper ion transport Inferred from mutant phenotype. Source: SGD transmembrane transport Inferred from mutant phenotype. Source: SGD
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell trans-Golgi network transport vesicle membrane Inferred from direct assay. Source: SGD
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW cation-transporting ATPase activity Inferred from direct assay. Source: SGD copper ion binding Inferred from direct assay. Source: SGD copper-exporting ATPase activity Inferred from electronic annotation. Source: EC magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1004

1004

Copper-transporting ATPase

PRO_0000046318

Regions

Topological domain

1 – 262

262

Cytoplasmic Potential

Transmembrane

263 – 283

21

Potential

Topological domain

284 – 303

20

Lumenal, vesicle Potential

Transmembrane

304 – 324

21

Potential

Topological domain

325 – 335

11

Cytoplasmic Potential

Transmembrane

336 – 356

21

Potential

Topological domain

357 – 370

14

Lumenal, vesicle Potential

Transmembrane

371 – 391

21

Potential

Topological domain

392 – 528

137

Cytoplasmic Potential

Transmembrane

529 – 549

21

Potential

Topological domain

550 – 577

28

Lumenal, vesicle Potential

Transmembrane

578 – 598

21

Potential

Topological domain

599 – 901

303

Cytoplasmic Potential

Transmembrane

902 – 924

23

Potential

Topological domain

925 – 927

3

Lumenal, vesicle Potential

Transmembrane

928 – 950

23

Potential

Topological domain

951 – 1004

54

Cytoplasmic Potential

Domain

3 – 68

66

HMA 1

Domain

81 – 147

67

HMA 2

Sites

Active site

627

1

4-aspartylphosphate intermediate By similarity

Metal binding

13

1

Copper

Metal binding

16

1

Copper

Metal binding

91

1

Copper Potential

Metal binding

94

1

Copper Potential

Metal binding

838

1

Magnesium By similarity

Metal binding

842

1

Magnesium By similarity

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

1004

Helix Strand Turn

Details...

Beta strand

2 – 8

7

Helix

14 – 25

12

Beta strand

27 – 33

7

Turn

37 – 40

4

Beta strand

41 – 46

6

Helix

52 – 62

11

Beta strand

66 – 70

5

Sequences

	Sequence		Length	Mass (Da)
	P38995-1 [UniParc]. Last modified February 1, 1995. Version 1. Checksum: 571E9F73EA1F599F	FASTA	1,004	109,829
	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

References

	« Hide 'large scale' referencesShow '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. , 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]	"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.
[4]	"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.

PIR

S55353.

RefSeq

NP_010556.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1FVQ	NMR	-	A	2-72	[»]
1FVS	NMR	-	A	2-72	[»]
1UV1	model	-	B	2-72	[»]
1UV2	model	-	B	2-72	[»]
2GGP	NMR	-	B	2-72	[»]

SMR

P38995. Positions 78-233, 384-929, 395-959.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-906N.

STRING

P38995.

Protein family/group databases

TCDB

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

Genome annotation databases

Ensembl

YDR270W; YDR270W; YDR270W; Saccharomyces cerevisiae. [Genome view]

GeneID

851862.

KEGG

sce:YDR270W.

NMPDR

fig|4932.3.peg.1318.

Organism-specific databases

CYGD

YDR270w.

SGD

S000002678. CCC2.

Phylogenomic databases

eggNOG

fuNOG05708.

HOGENOM

HBG507745.

OMA

SAIEDCG.

OrthoDB

EOG9FR28K.

PhylomeDB

P38995.

Enzyme and pathway databases

BRENDA

3.6.3.4. 250.

Gene expression databases

ArrayExpress

P38995.

Genevestigator

P38995.

GermOnline

YDR270W. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR008250. ATPase_P-typ_ATPase-assoc-dom.
IPR006403. ATPase_P-typ_cat/Cu-transptr.
IPR006416. ATPase_P-typ_heavy-metal.
IPR001757. ATPase_P-typ_ion-transptr.
IPR018303. ATPase_P-typ_P_site.
IPR005834. Dehalogen-like_hydro.
IPR017969. Heavy-metal-associated_CS.
IPR006121. HeavyMe_transpt.
[Graphical view]

PANTHER

PTHR11939. ATPase_P. 1 hit.

Pfam

PF00122. E1-E2_ATPase. 1 hit.
PF00403. HMA. 2 hits.
PF00702. Hydrolase. 1 hit.
[Graphical view]

PRINTS

PR00119. CATATPASE.

TIGRFAMs

TIGR01511. ATPase-IB1_Cu. 1 hit.
TIGR01525. ATPase-IB_hvy. 1 hit.
TIGR01494. ATPase_P-type. 2 hits.

PROSITE

PS00154. ATPASE_E1_E2. 1 hit.
PS01047. HMA_1. 2 hits.
PS50846. HMA_2. 2 hits.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

969806.

Entry information

Entry name

ATU2_YEAST

Accession

Primary (citable) accession number: P38995

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	February 1, 1995
Last modified:	February 9, 2010
This is version 102 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)