Copper-transporting ATPase (P38995)

Identification
NameCopper-transporting ATPase
Synonyms
  • Cu(2+)-ATPase
Gene NameCCC2
Enzyme Class
Biological Properties
General FunctionInvolved in nucleotide binding
Specific FunctionProbably 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
Cellular LocationGolgi apparatus, trans-Golgi network membrane; Multi-pass membrane protein
SMPDB PathwaysNot Available
KEGG PathwaysNot Available
SMPDB ReactionsNot Available
KEGG ReactionsNot Available
Metabolites
YMDB IDNameView
YMDB00109Adenosine triphosphateShow
YMDB00207Copper(2+)Show
YMDB00907phosphateShow
YMDB00914ADPShow
GO Classification
Component
cell part
membrane
membrane part
intrinsic to membrane
integral to membrane
Function
metal ion binding
metal ion transmembrane transporter activity
transporter activity
cation transmembrane transporter activity
transmembrane transporter activity
inorganic cation transmembrane transporter activity
di-, tri-valent inorganic cation transmembrane transporter activity
copper ion transmembrane transporter activity
hydrolase activity
substrate-specific transmembrane transporter activity
copper-transporting ATPase activity
ion transmembrane transporter activity
copper-exporting ATPase activity
binding
ATPase activity, coupled to transmembrane movement of ions
catalytic activity
nucleoside binding
ATPase activity, coupled to transmembrane movement of ions, phosphorylative mechanism
purine nucleoside binding
hydrolase activity, acting on acid anhydrides
adenyl nucleotide binding
hydrolase activity, acting on acid anhydrides, catalyzing transmembrane movement of substances
adenyl ribonucleotide binding
ATP binding
ion binding
cation binding
Process
ATP biosynthetic process
nitrogen compound metabolic process
cellular nitrogen compound metabolic process
nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
nucleobase, nucleoside and nucleotide metabolic process
establishment of localization
nucleoside phosphate metabolic process
transport
nucleotide metabolic process
purine nucleotide metabolic process
purine nucleotide biosynthetic process
ion transport
metal ion transport
metabolic process
cation transport
purine nucleoside triphosphate biosynthetic process
purine ribonucleoside triphosphate biosynthetic process
Gene Properties
Chromosome Locationchromosome 4
LocusYDR270W
Gene Sequence>3015 bp ATGAGAGAAGTGATACTTGCTGTACATGGAATGACATGCAGCGCCTGTACTAATACAATC AATACGCAGTTACGAGCTTTAAAGGGTGTAACAAAATGTGATATTAGTTTAGTGACTAAT GAGTGCCAGGTGACATACGATAACGAGGTTACCGCCGATTCTATTAAGGAAATTATAGAG GATTGTGGATTTGACTGTGAGATACTAAGAGATTCTGAAATTACAGCCATAAGTACGAAG GAAGGACTACTGAGTGTACAAGGTATGACCTGTGGGTCTTGTGTTTCTACAGTCACCAAA CAAGTGGAAGGCATTGAGGGTGTTGAATCGGTAGTCGTTTCCTTGGTAACGGAAGAGTGC CATGTTATTTATGAACCGTCCAAGACAACGCTAGAAACCGCCAGAGAAATGATTGAAGAC TGTGGATTTGACTCAAATATTATTATGGATGGCAACGGGAATGCAGACATGACCGAAAAA ACGGTGATCTTGAAAGTAACTAAGGCTTTCGAGGACGAATCCCCACTCATACTTTCTTCA GTAAGCGAAAGGTTTCAATTTTTGTTAGACCTAGGTGTAAAATCGATAGAAATTTCTGAT GATATGCACACACTCACCATAAAATACTGTTGTAACGAACTCGGCATTAGAGATTTATTG AGGCACCTTGAGAGGACCGGATATAAATTCACTGTATTTTCCAATTTAGATAATACTACC CAGTTAAGGCTTCTCTCTAAAGAGGACGAGATAAGATTCTGGAAAAAAAACAGCATAAAA TCCACCCTTTTGGCTATAATATGTATGCTATTGTATATGATTGTCCCTATGATGTGGCCA ACAATTGTTCAGGACCGCATATTCCCTTACAAAGAAACCTCCTTTGTTAGAGGTCTGTTC TACAGAGATATTTTGGGTGTAATATTGGCAAGCTATATTCAGTTCAGCGTTGGTTTTTAC TTTTACAAGGCAGCATGGGCATCTTTAAAGCACGGTTCAGGAACCATGGATACACTAGTT TGTGTTTCCACTACTTGTGCATACACATTTTCTGTGTTTTCTTTAGTTCACAATATGTTC CATCCCTCAAGTACTGGCAAACTCCCAAGGATCGTTTTCGACACATCAATCATGATCATT TCATATATTTCCATCGGGAAATATTTGGAAACTTTAGCTAAATCACAAACATCAACCGCA CTTTCTAAATTAATTCAGCTCACTCCATCGGTGTGTTCAATTATATCTGACGTGGAGCGG AATGAAACCAAGGAAATTCCCATAGAATTATTGCAAGTGAACGATATAGTGGAGATTAAA CCAGGGATGAAAATTCCTGCTGATGGCATCATAACAAGAGGTGAATCTGAAATTGACGAG TCGTTAATGACAGGCGAATCCATTTTGGTGCCCAAGAAAACTGGTTTTCCGGTTATTGCT GGTTCTGTTAATGGACCTGGACATTTCTACTTCAGAACTACTACCGTTGGGGAGGAAACT AAATTAGCAAATATTATCAAGGTAATGAAAGAAGCACAATTGAGTAAAGCTCCCATTCAG GGGTATGCAGATTATTTAGCCTCTATTTTTGTTCCGGGGATCCTAATTTTGGCAGTATTG ACTTTCTTTATTTGGTGTTTTATTTTAAACATCTCGGCTAATCCTCCCGTCGCTTTCACC GCAAATACTAAGGCTGATAATTTTTTTATTTGCTTACAAACTGCTACTTCTGTTGTCATC GTCGCATGCCCATGTGCATTGGGACTTGCCACGCCGACTGCTATAATGGTGGGTACAGGG GTTGGAGCTCAGAATGGTGTCTTAATAAAGGGCGGAGAAGTATTGGAAAAATTCAATAGT ATTACTACTTTTGTTTTTGATAAAACAGGTACCTTAACTACAGGTTTTATGGTTGTGAAA AAGTTCCTTAAAGATTCAAATTGGGTTGGAAACGTGGATGAAGACGAAGTTCTCGCCTGT ATAAAAGCAACGGAATCCATTAGTGACCATCCAGTTTCGAAAGCAATTATACGTTATTGT GATGGTTTGAACTGTAATAAGGCTTTAAATGCCGTTGTTTTAGAAAGCGAATACGTGCTT GGAAAGGGAATAGTCTCAAAGTGTCAAGTTAATGGAAATACTTATGATATTTGTATTGGG AACGAGGCGCTGATTTTGGAGGATGCATTAAAAAAATCCGGATTTATTAACAGTAATGTC GACCAAGGAAACACTGTATCATACGTATCAGTAAACGGGCATGTGTTTGGCTTGTTCGAG ATTAATGATGAAGTTAAACATGATTCTTACGCAACAGTTCAGTATCTACAAAGAAATGGA TATGAAACGTATATGATTACTGGCGATAATAACTCAGCAGCAAAAAGAGTCGCTAGAGAA GTAGGTATAAGCTTCGAAAATGTTTACAGCGATGTGTCACCCACAGGCAAATGTGATCTC GTGAAAAAAATTCAAGATAAAGAAGGTAATAACAAGGTTGCTGTTGTTGGCGATGGCATT AACGACGCTCCCGCTTTAGCACTGAGTGATCTAGGTATTGCCATTTCAACAGGTACGGAG ATTGCTATTGAAGCAGCTGATATTGTTATACTGTGCGGTAATGATCTGAATACTAATAGT TTGAGAGGACTGGCCAACGCCATCGATATTTCACTAAAAACGTTCAAAAGAATAAAGCTG AATTTGTTCTGGGCACTTTGCTATAATATATTCATGATTCCGATTGCTATGGGTGTGCTC ATTCCTTGGGGCATAACTCTTCCTCCAATGCTCGCCGGTTTAGCGATGGCATTCAGCTCG GTCAGTGTCGTTCTAAGTTCATTGATGTTGAAGAAGTGGACTCCACCGGATATTGAATCA CATGGGATTTCAGATTTCAAGTCCAAATTTTCGATTGGGAATTTTTGGTCAAGGCTTTTT TCTACGCGGGCTATTGCAGGTGAGCAAGACATAGAATCACAGGCCGGACTAATGTCAAAC GAAGAAGTCTTGTAA
Protein Properties
Pfam Domain Function
Protein Residues1004
Protein Molecular Weight109828.0
Protein Theoretical pI4.79
PDB Fileshow
Signalling Regions
  • None
Transmembrane Regions
  • 263-283
  • 304-324
  • 336-356
  • 371-391
  • 529-549
  • 578-598
  • 902-924
  • 928-950
Protein Sequence>Copper-transporting ATPase MREVILAVHGMTCSACTNTINTQLRALKGVTKCDISLVTNECQVTYDNEVTADSIKEIIE DCGFDCEILRDSEITAISTKEGLLSVQGMTCGSCVSTVTKQVEGIEGVESVVVSLVTEEC HVIYEPSKTTLETAREMIEDCGFDSNIIMDGNGNADMTEKTVILKVTKAFEDESPLILSS VSERFQFLLDLGVKSIEISDDMHTLTIKYCCNELGIRDLLRHLERTGYKFTVFSNLDNTT QLRLLSKEDEIRFWKKNSIKSTLLAIICMLLYMIVPMMWPTIVQDRIFPYKETSFVRGLF YRDILGVILASYIQFSVGFYFYKAAWASLKHGSGTMDTLVCVSTTCAYTFSVFSLVHNMF HPSSTGKLPRIVFDTSIMIISYISIGKYLETLAKSQTSTALSKLIQLTPSVCSIISDVER NETKEIPIELLQVNDIVEIKPGMKIPADGIITRGESEIDESLMTGESILVPKKTGFPVIA GSVNGPGHFYFRTTTVGEETKLANIIKVMKEAQLSKAPIQGYADYLASIFVPGILILAVL TFFIWCFILNISANPPVAFTANTKADNFFICLQTATSVVIVACPCALGLATPTAIMVGTG VGAQNGVLIKGGEVLEKFNSITTFVFDKTGTLTTGFMVVKKFLKDSNWVGNVDEDEVLAC IKATESISDHPVSKAIIRYCDGLNCNKALNAVVLESEYVLGKGIVSKCQVNGNTYDICIG NEALILEDALKKSGFINSNVDQGNTVSYVSVNGHVFGLFEINDEVKHDSYATVQYLQRNG YETYMITGDNNSAAKRVAREVGISFENVYSDVSPTGKCDLVKKIQDKEGNNKVAVVGDGI NDAPALALSDLGIAISTGTEIAIEAADIVILCGNDLNTNSLRGLANAIDISLKTFKRIKL NLFWALCYNIFMIPIAMGVLIPWGITLPPMLAGLAMAFSSVSVVLSSLMLKKWTPPDIES HGISDFKSKFSIGNFWSRLFSTRAIAGEQDIESQAGLMSNEEVL
References
External Links
ResourceLink
Saccharomyces Genome Database CCC2
Uniprot IDP38995
Uniprot NameATU2_YEAST
GenBank Gene IDL36317
Genebank Protein ID538515
PDB ID
1FVS
General Reference
  • Fu, D., Beeler, T. J., Dunn, T. M. (1995). "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." Yeast 11:283-292.7785328
  • Jacq, C., Alt-Morbe, J., Andre, B., Arnold, W., Bahr, A., Ballesta, J. P., Bargues, M., Baron, L., Becker, A., Biteau, N., Blocker, H., Blugeon, C., Boskovic, J., Brandt, P., Bruckner, 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., Zaccaria, P., et, a. l. .. (1997). "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV." Nature 387:75-78.9169867
  • Arnesano, F., Banci, L., Bertini, I., Cantini, F., Ciofi-Baffoni, S., Huffman, D. L., O'Halloran, T. V. (2001). "Characterization of the binding interface between the copper chaperone Atx1 and the first cytosolic domain of Ccc2 ATPase." J Biol Chem 276:41365-41376.11500502
  • Banci, L., Bertini, I., Ciofi-Baffoni, S., Huffman, D. L., O'Halloran, T. V. (2001). "Solution structure of the yeast copper transporter domain Ccc2a in the apo and Cu(I)-loaded states." J Biol Chem 276:8415-8426.11083871