ATU2_YEAST
ID ATU2_YEAST Reviewed; 1004 AA.
AC P38995; D6VSQ3;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 200.
DE RecName: Full=Copper-transporting ATPase;
DE EC=7.2.2.8;
DE AltName: Full=Cu(2+)-ATPase;
GN Name=CCC2; OrderedLocusNames=YDR270W; ORFNames=D9954.6;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7785328; DOI=10.1002/yea.320110310;
RA Fu D., Beeler T.J., Dunn T.M.;
RT "Sequence, mapping and disruption of CCC2, a gene that cross-complements
RT the Ca(2+)-sensitive phenotype of csg1 mutants and encodes a P-type ATPase
RT belonging to the Cu(2+)-ATPase subfamily.";
RL Yeast 11:283-292(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP METAL-BINDING SITES.
RX PubMed=11500502; DOI=10.1074/jbc.m104807200;
RA Arnesano F., Banci L., Bertini I., Cantini F., Ciofi-Baffoni S.,
RA Huffman D.L., O'Halloran T.V.;
RT "Characterization of the binding interface between the copper chaperone
RT Atx1 and the first cytosolic domain of Ccc2 ATPase.";
RL J. Biol. Chem. 276:41365-41376(2001).
RN [5]
RP STRUCTURE BY NMR OF 1-72 IN APO AND COPPER-BOUND FORMS.
RX PubMed=11083871; DOI=10.1074/jbc.m008389200;
RA Banci L., Bertini I., Ciofi-Baffoni S., Huffman D.L., O'Halloran T.V.;
RT "Solution structure of the yeast copper transporter domain Ccc2a in the apo
RT and Cu(I)-loaded states.";
RL J. Biol. Chem. 276:8415-8426(2001).
CC -!- FUNCTION: Probably involved in copper transport and in the regulation
CC of cellular copper level. Retrieves copper from the metallochaperone
CC ATX1 and incorporates it into trans-Golgi vesicles.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + Cu(+)(in) + H2O = ADP + Cu(+)(out) + H(+) + phosphate;
CC Xref=Rhea:RHEA:25792, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:49552,
CC ChEBI:CHEBI:456216; EC=7.2.2.8;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane;
CC Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IB subfamily. {ECO:0000305}.
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DR EMBL; L36317; AAC37425.1; -; Genomic_DNA.
DR EMBL; U51030; AAB64451.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12113.1; -; Genomic_DNA.
DR PIR; S55353; S55353.
DR RefSeq; NP_010556.1; NM_001180578.1.
DR PDB; 1FVQ; NMR; -; A=2-72.
DR PDB; 1FVS; NMR; -; A=2-72.
DR PDB; 2GGP; NMR; -; B=2-72.
DR PDBsum; 1FVQ; -.
DR PDBsum; 1FVS; -.
DR PDBsum; 2GGP; -.
DR AlphaFoldDB; P38995; -.
DR SMR; P38995; -.
DR BioGRID; 32325; 72.
DR DIP; DIP-906N; -.
DR IntAct; P38995; 3.
DR MINT; P38995; -.
DR STRING; 4932.YDR270W; -.
DR TCDB; 3.A.3.5.17; the p-type atpase (p-atpase) superfamily.
DR iPTMnet; P38995; -.
DR MaxQB; P38995; -.
DR PaxDb; P38995; -.
DR PRIDE; P38995; -.
DR EnsemblFungi; YDR270W_mRNA; YDR270W; YDR270W.
DR GeneID; 851862; -.
DR KEGG; sce:YDR270W; -.
DR SGD; S000002678; CCC2.
DR VEuPathDB; FungiDB:YDR270W; -.
DR eggNOG; KOG0207; Eukaryota.
DR GeneTree; ENSGT00940000174979; -.
DR HOGENOM; CLU_001771_0_1_1; -.
DR InParanoid; P38995; -.
DR OMA; ITFFGWM; -.
DR BioCyc; YEAST:G3O-29839-MON; -.
DR BRENDA; 7.2.2.9; 984.
DR Reactome; R-SCE-936837; Ion transport by P-type ATPases.
DR EvolutionaryTrace; P38995; -.
DR PRO; PR:P38995; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P38995; protein.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0012510; C:trans-Golgi network transport vesicle membrane; IDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0019829; F:ATPase-coupled cation transmembrane transporter activity; IDA:SGD.
DR GO; GO:0005507; F:copper ion binding; IDA:SGD.
DR GO; GO:0043682; F:P-type divalent copper transporter activity; IBA:GO_Central.
DR GO; GO:0140581; F:P-type monovalent copper transporter activity; IEA:UniProtKB-EC.
DR GO; GO:0006879; P:cellular iron ion homeostasis; IMP:SGD.
DR GO; GO:0060003; P:copper ion export; IMP:SGD.
DR GO; GO:0055070; P:copper ion homeostasis; IBA:GO_Central.
DR GO; GO:0006825; P:copper ion transport; IGI:UniProtKB.
DR GO; GO:0055085; P:transmembrane transport; IMP:SGD.
DR CDD; cd00371; HMA; 2.
DR Gene3D; 3.40.1110.10; -; 1.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR023299; ATPase_P-typ_cyto_dom_N.
DR InterPro; IPR018303; ATPase_P-typ_P_site.
DR InterPro; IPR023298; ATPase_P-typ_TM_dom_sf.
DR InterPro; IPR008250; ATPase_P-typ_transduc_dom_A_sf.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR017969; Heavy-metal-associated_CS.
DR InterPro; IPR006122; HMA_Cu_ion-bd.
DR InterPro; IPR006121; HMA_dom.
DR InterPro; IPR036163; HMA_dom_sf.
DR InterPro; IPR027256; P-typ_ATPase_IB.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR Pfam; PF00403; HMA; 2.
DR SFLD; SFLDF00027; p-type_atpase; 1.
DR SUPFAM; SSF55008; SSF55008; 2.
DR SUPFAM; SSF56784; SSF56784; 1.
DR SUPFAM; SSF81653; SSF81653; 1.
DR SUPFAM; SSF81665; SSF81665; 1.
DR TIGRFAMs; TIGR01525; ATPase-IB_hvy; 1.
DR TIGRFAMs; TIGR01494; ATPase_P-type; 2.
DR TIGRFAMs; TIGR00003; TIGR00003; 2.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
DR PROSITE; PS01047; HMA_1; 2.
DR PROSITE; PS50846; HMA_2; 2.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Copper; Copper transport; Golgi apparatus;
KW Ion transport; Magnesium; Membrane; Metal-binding; Nucleotide-binding;
KW Reference proteome; Repeat; Translocase; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..1004
FT /note="Copper-transporting ATPase"
FT /id="PRO_0000046318"
FT TOPO_DOM 1..262
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 263..283
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 284..303
FT /note="Lumenal, vesicle"
FT /evidence="ECO:0000255"
FT TRANSMEM 304..324
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 325..335
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 336..356
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 357..370
FT /note="Lumenal, vesicle"
FT /evidence="ECO:0000255"
FT TRANSMEM 371..391
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 392..528
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 529..549
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 550..577
FT /note="Lumenal, vesicle"
FT /evidence="ECO:0000255"
FT TRANSMEM 578..598
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 599..901
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 902..924
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 925..927
FT /note="Lumenal, vesicle"
FT /evidence="ECO:0000255"
FT TRANSMEM 928..950
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 951..1004
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 2..67
FT /note="HMA 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT DOMAIN 80..146
FT /note="HMA 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT ACT_SITE 627
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250"
FT BINDING 13
FT /ligand="Cu(+)"
FT /ligand_id="ChEBI:CHEBI:49552"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT BINDING 16
FT /ligand="Cu(+)"
FT /ligand_id="ChEBI:CHEBI:49552"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT BINDING 91
FT /ligand="Cu(+)"
FT /ligand_id="ChEBI:CHEBI:49552"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT BINDING 94
FT /ligand="Cu(+)"
FT /ligand_id="ChEBI:CHEBI:49552"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT BINDING 838
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT BINDING 842
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT STRAND 2..8
FT /evidence="ECO:0007829|PDB:1FVQ"
FT HELIX 14..25
FT /evidence="ECO:0007829|PDB:1FVQ"
FT STRAND 27..33
FT /evidence="ECO:0007829|PDB:1FVQ"
FT TURN 37..40
FT /evidence="ECO:0007829|PDB:1FVQ"
FT STRAND 41..46
FT /evidence="ECO:0007829|PDB:1FVQ"
FT STRAND 48..50
FT /evidence="ECO:0007829|PDB:1FVS"
FT HELIX 52..62
FT /evidence="ECO:0007829|PDB:1FVQ"
FT STRAND 66..70
FT /evidence="ECO:0007829|PDB:1FVQ"
SQ SEQUENCE 1004 AA; 109829 MW; 571E9F73EA1F599F CRC64;
MREVILAVHG MTCSACTNTI NTQLRALKGV TKCDISLVTN ECQVTYDNEV TADSIKEIIE
DCGFDCEILR DSEITAISTK EGLLSVQGMT CGSCVSTVTK QVEGIEGVES VVVSLVTEEC
HVIYEPSKTT LETAREMIED CGFDSNIIMD GNGNADMTEK TVILKVTKAF EDESPLILSS
VSERFQFLLD LGVKSIEISD DMHTLTIKYC CNELGIRDLL RHLERTGYKF TVFSNLDNTT
QLRLLSKEDE IRFWKKNSIK STLLAIICML LYMIVPMMWP TIVQDRIFPY KETSFVRGLF
YRDILGVILA SYIQFSVGFY FYKAAWASLK HGSGTMDTLV CVSTTCAYTF SVFSLVHNMF
HPSSTGKLPR IVFDTSIMII SYISIGKYLE TLAKSQTSTA LSKLIQLTPS VCSIISDVER
NETKEIPIEL LQVNDIVEIK PGMKIPADGI ITRGESEIDE SLMTGESILV PKKTGFPVIA
GSVNGPGHFY FRTTTVGEET KLANIIKVMK EAQLSKAPIQ GYADYLASIF VPGILILAVL
TFFIWCFILN ISANPPVAFT ANTKADNFFI CLQTATSVVI VACPCALGLA TPTAIMVGTG
VGAQNGVLIK GGEVLEKFNS ITTFVFDKTG TLTTGFMVVK KFLKDSNWVG NVDEDEVLAC
IKATESISDH PVSKAIIRYC DGLNCNKALN AVVLESEYVL GKGIVSKCQV NGNTYDICIG
NEALILEDAL KKSGFINSNV DQGNTVSYVS VNGHVFGLFE INDEVKHDSY ATVQYLQRNG
YETYMITGDN NSAAKRVARE VGISFENVYS DVSPTGKCDL VKKIQDKEGN NKVAVVGDGI
NDAPALALSD LGIAISTGTE IAIEAADIVI LCGNDLNTNS LRGLANAIDI SLKTFKRIKL
NLFWALCYNI FMIPIAMGVL IPWGITLPPM LAGLAMAFSS VSVVLSSLML KKWTPPDIES
HGISDFKSKF SIGNFWSRLF STRAIAGEQD IESQAGLMSN EEVL
