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Identification |
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Name | Copper-transporting ATPase |
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Synonyms | |
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Gene Name | CCC2 |
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Enzyme Class | |
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Biological Properties |
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General Function | Involved in nucleotide binding |
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Specific 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 |
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Cellular Location | Golgi apparatus, trans-Golgi network membrane; Multi-pass membrane protein |
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SMPDB Pathways | Not Available |
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KEGG Pathways | Not Available |
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SMPDB Reactions | Not Available |
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KEGG Reactions | Not Available |
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Metabolites | YMDB ID | Name | View |
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YMDB00109 | Adenosine triphosphate | Show | YMDB00207 | Copper(2+) | Show | YMDB00907 | phosphate | Show | YMDB00914 | ADP | Show |
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GO Classification | Component |
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cell part | membrane | membrane part | intrinsic to membrane | integral to membrane | Function |
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adenyl nucleotide binding | hydrolase activity, acting on acid anhydrides | adenyl ribonucleotide binding | hydrolase activity, acting on acid anhydrides, catalyzing transmembrane movement of substances | ATP binding | ion binding | cation binding | 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 | copper-transporting ATPase activity | substrate-specific transmembrane transporter activity | copper-exporting ATPase activity | ion transmembrane transporter activity | binding | catalytic activity | nucleoside binding | ATPase activity, coupled to transmembrane movement of ions | purine nucleoside binding | ATPase activity, coupled to transmembrane movement of ions, phosphorylative mechanism | Process |
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cation transport | purine nucleoside triphosphate biosynthetic process | purine ribonucleoside triphosphate biosynthetic 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 | metal ion transport | ion transport | metabolic process |
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Gene Properties |
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Chromosome Location | chromosome 4 |
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Locus | YDR270W |
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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 |
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Protein Properties |
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Pfam Domain Function | |
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Protein Residues | 1004 |
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Protein Molecular Weight | 109828.0 |
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Protein Theoretical pI | 4.79 |
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PDB File | show |
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Signalling Regions | |
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Transmembrane Regions | - 263-283
- 304-324
- 336-356
- 371-391
- 529-549
- 578-598
- 902-924
- 928-950
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Protein Sequence | >Copper-transporting ATPase
MREVILAVHGMTCSACTNTINTQLRALKGVTKCDISLVTNECQVTYDNEVTADSIKEIIE
DCGFDCEILRDSEITAISTKEGLLSVQGMTCGSCVSTVTKQVEGIEGVESVVVSLVTEEC
HVIYEPSKTTLETAREMIEDCGFDSNIIMDGNGNADMTEKTVILKVTKAFEDESPLILSS
VSERFQFLLDLGVKSIEISDDMHTLTIKYCCNELGIRDLLRHLERTGYKFTVFSNLDNTT
QLRLLSKEDEIRFWKKNSIKSTLLAIICMLLYMIVPMMWPTIVQDRIFPYKETSFVRGLF
YRDILGVILASYIQFSVGFYFYKAAWASLKHGSGTMDTLVCVSTTCAYTFSVFSLVHNMF
HPSSTGKLPRIVFDTSIMIISYISIGKYLETLAKSQTSTALSKLIQLTPSVCSIISDVER
NETKEIPIELLQVNDIVEIKPGMKIPADGIITRGESEIDESLMTGESILVPKKTGFPVIA
GSVNGPGHFYFRTTTVGEETKLANIIKVMKEAQLSKAPIQGYADYLASIFVPGILILAVL
TFFIWCFILNISANPPVAFTANTKADNFFICLQTATSVVIVACPCALGLATPTAIMVGTG
VGAQNGVLIKGGEVLEKFNSITTFVFDKTGTLTTGFMVVKKFLKDSNWVGNVDEDEVLAC
IKATESISDHPVSKAIIRYCDGLNCNKALNAVVLESEYVLGKGIVSKCQVNGNTYDICIG
NEALILEDALKKSGFINSNVDQGNTVSYVSVNGHVFGLFEINDEVKHDSYATVQYLQRNG
YETYMITGDNNSAAKRVAREVGISFENVYSDVSPTGKCDLVKKIQDKEGNNKVAVVGDGI
NDAPALALSDLGIAISTGTEIAIEAADIVILCGNDLNTNSLRGLANAIDISLKTFKRIKL
NLFWALCYNIFMIPIAMGVLIPWGITLPPMLAGLAMAFSSVSVVLSSLMLKKWTPPDIES
HGISDFKSKFSIGNFWSRLFSTRAIAGEQDIESQAGLMSNEEVL |
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References |
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External Links | |
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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
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