P53615 (CAN_YEAST) Reviewed, UniProtKB/Swiss-Prot
Last modified
December 14, 2011.
Version 81.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Carbonic anhydrase EC=4.2.1.1 Alternative name(s): Carbonate dehydratase Non-classical export protein 3 | ||||||||
| Gene names |
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| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) | ||||||||
| Taxonomic identifier | 559292 [NCBI] | ||||||||
| Taxonomic lineage | Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces |
Protein attributes
| Sequence length | 221 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Catalyzes the reversible hydration of CO2 to H2CO3. The main role may be to provide inorganic carbon for the bicarbonate-dependent carboxylation reactions catalyzed by pyruvate carboxylase, acetyl-CoA carboxylase and carbamoyl-phosphate synthetase. Involved in protection against oxidative damage. Encodes a substrate for the non-classical protein export pathway for proteins that lack a cleavable signal sequence. Ref.4 Ref.7 Ref.8 Ref.10 |
| Catalytic activity | H2CO3 = CO2 + H2O. |
| Cofactor | Binds 1 zinc ion per subunit By similarity. |
| Subcellular location | |
| Induction | Transcription and activity down-regulated at elevated CO2 concentrations. Ref.9 Ref.10 |
| Miscellaneous | Present with 2330 molecules/cell in log phase SD medium. Ref.6 |
| Sequence similarities | Belongs to the beta-class carbonic anhydrase family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cytoplasm Nucleus |
| Ligand | Metal-binding Zinc |
| Molecular function | Lyase |
| Technical term | 3D-structure Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological process | carbon utilization Inferred from electronic annotation. Source: InterPro cellular response to oxidative stressInferred from mutant phenotype Ref.7. Source: SGD |
| Cellular component | cytoplasm Inferred from direct assay Ref.5. Source: SGD nucleusInferred from direct assay Ref.5. Source: SGD |
| Molecular function | carbonate dehydratase activity Inferred from direct assay Ref.7Ref.10. Source: SGD zinc ion bindingInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||||||||||||||||||||||||||||||||||||
Molecule processing | |||||||||||||||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 221 | 221 | Carbonic anhydrase | PRO_0000077468 | |||||||||||||||||||||||||||||||||||||||||
Sites | |||||||||||||||||||||||||||||||||||||||||||||
| Metal binding | 57 | 1 | Zinc By similarity | ||||||||||||||||||||||||||||||||||||||||||
| Metal binding | 59 | 1 | Zinc By similarity | ||||||||||||||||||||||||||||||||||||||||||
| Metal binding | 112 | 1 | Zinc By similarity | ||||||||||||||||||||||||||||||||||||||||||
| Metal binding | 115 | 1 | Zinc By similarity | ||||||||||||||||||||||||||||||||||||||||||
Experimental info | |||||||||||||||||||||||||||||||||||||||||||||
| Sequence conflict | 39 | 1 | L → W in AAC49352. Ref.1 | ||||||||||||||||||||||||||||||||||||||||||
Secondary structure | |||||||||||||||||||||||||||||||||||||||||||||
Helix Strand Turn | |||||||||||||||||||||||||||||||||||||||||||||
| Helix | 18 – 35 | 18 | |||||||||||||||||||||||||||||||||||||||||||
| Helix | 37 – 39 | 3 | |||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 51 – 55 | 5 | |||||||||||||||||||||||||||||||||||||||||||
| Helix | 64 – 66 | 3 | |||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 74 – 76 | 3 | |||||||||||||||||||||||||||||||||||||||||||
| Helix | 80 – 82 | 3 | |||||||||||||||||||||||||||||||||||||||||||
| Helix | 89 – 100 | 12 | |||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 105 – 109 | 5 | |||||||||||||||||||||||||||||||||||||||||||
| Helix | 119 – 122 | 4 | |||||||||||||||||||||||||||||||||||||||||||
| Helix | 126 – 128 | 3 | |||||||||||||||||||||||||||||||||||||||||||
| Helix | 130 – 132 | 3 | |||||||||||||||||||||||||||||||||||||||||||
| Helix | 135 – 140 | 6 | |||||||||||||||||||||||||||||||||||||||||||
| Helix | 142 – 150 | 9 | |||||||||||||||||||||||||||||||||||||||||||
| Helix | 152 – 155 | 4 | |||||||||||||||||||||||||||||||||||||||||||
| Helix | 161 – 180 | 20 | |||||||||||||||||||||||||||||||||||||||||||
| Helix | 184 – 191 | 8 | |||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 196 – 198 | 3 | |||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 217 – 219 | 3 | |||||||||||||||||||||||||||||||||||||||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "A new pathway for protein export in Saccharomyces cerevisiae." Cleves A.E., Cooper D.N.W., Barondes S.H., Kelly R.B. J. Cell Biol. 133:1017-1026(1996) [PubMed: 8655575] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: ATCC 26109 / X2180 / NCYC 826. |
| [2] | "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its evolutionary implications." Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K., Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K., Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M., Beinhauer J.D., Boskovic J., Buitrago M.J. Hani J.Nature 387:93-98(1997) [PubMed: 9169873] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c. |
| [3] | Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c. |
| [4] | "Deletion of the carbonic anhydrase-like gene NCE103 of the yeast Saccharomyces cerevisiae causes an oxygen-sensitive growth defect." Goetz R., Gnann A., Zimmermann F.K. Yeast 15:855-864(1999) [PubMed: 10407265] [Abstract] Cited for: FUNCTION. |
| [5] | "Global analysis of protein localization in budding yeast." Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K. Nature 425:686-691(2003) [PubMed: 14562095] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]. |
| [6] | "Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]. |
| [7] | "Complementation of the yeast deletion mutant DeltaNCE103 by members of the beta class of carbonic anhydrases is dependent on carbonic anhydrase activity rather than on antioxidant activity." Clark D., Rowlett R.S., Coleman J.R., Klessig D.F. Biochem. J. 379:609-615(2004) [PubMed: 15096093] [Abstract] Cited for: FUNCTION. |
| [8] | "Carbonic anhydrase (Nce103p): an essential biosynthetic enzyme for growth of Saccharomyces cerevisiae at atmospheric carbon dioxide pressure." Aguilera J., Van Dijken J.P., De Winde J.H., Pronk J.T. Biochem. J. 391:311-316(2005) [PubMed: 15948716] [Abstract] Cited for: FUNCTION. |
| [9] | "Physiological and genome-wide transcriptional responses of Saccharomyces cerevisiae to high carbon dioxide concentrations." Aguilera J., Petit T., de Winde J.H., Pronk J.T. FEMS Yeast Res. 5:579-593(2005) [PubMed: 15780657] [Abstract] Cited for: INDUCTION. |
| [10] | "The gene NCE103 (YNL036w) from Saccharomyces cerevisiae encodes a functional carbonic anhydrase and its transcription is regulated by the concentration of inorganic carbon in the medium." Amoroso G., Morell-Avrahov L., Mueller D., Klug K., Sueltemeyer D. Mol. Microbiol. 56:549-558(2005) [PubMed: 15813743] [Abstract] Cited for: FUNCTION, INDUCTION. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| EMBL GenBank DDBJ | U52369 mRNA. Translation: AAC49352.1. Z71312 Genomic DNA. Translation: CAA95901.1. BK006947 Genomic DNA. Translation: DAA10509.1. | ||||||||||||
| PIR | S62958. | ||||||||||||
| RefSeq | NP_014362.1. NM_001182875.1. | ||||||||||||
3D structure databases | |||||||||||||
| PDBe RCSB PDB PDBj |
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| ProteinModelPortal | P53615. | ||||||||||||
| SMR | P53615. Positions 17-221. | ||||||||||||
| ModBase | Search... | ||||||||||||
Protein-protein interaction databases | |||||||||||||
| DIP | DIP-968N. | ||||||||||||
| MINT | MINT-485874. | ||||||||||||
| STRING | P53615. | ||||||||||||
Proteomic databases | |||||||||||||
| PeptideAtlas | P53615. | ||||||||||||
Protocols and materials databases | |||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||
Genome annotation databases | |||||||||||||
| EnsemblFungi | YNL036W; YNL036W; YNL036W. | ||||||||||||
| GeneID | 855692. | ||||||||||||
| KEGG | sce:YNL036W. | ||||||||||||
| NMPDR | fig|4932.3.peg.5439. | ||||||||||||
Organism-specific databases | |||||||||||||
| CYGD | YNL036w. | ||||||||||||
| SGD | S000004981. NCE103. | ||||||||||||
Phylogenomic databases | |||||||||||||
| eggNOG | fuNOG06583. | ||||||||||||
| GeneTree | EFGT00050000003474. | ||||||||||||
| HOGENOM | HBG711150. | ||||||||||||
| OMA | PHRIKEL. | ||||||||||||
| OrthoDB | EOG4C2MKH. | ||||||||||||
Gene expression databases | |||||||||||||
| ArrayExpress | P53615. | ||||||||||||
| Genevestigator | P53615. | ||||||||||||
| GermOnline | YNL036W. Saccharomyces cerevisiae. | ||||||||||||
Family and domain databases | |||||||||||||
| InterPro | IPR001765. Carbonic_anhydrase. IPR015892. Carbonic_anhydrase_CS. [Graphical view] | ||||||||||||
| Gene3D | G3DSA:3.40.1050.10. CO_anhd_prok_pln. 1 hit. | ||||||||||||
| PANTHER | PTHR11002. Carbonic_anhydrase. 1 hit. | ||||||||||||
| Pfam | PF00484. Pro_CA. 1 hit. [Graphical view] | ||||||||||||
| SMART | SM00947. Pro_CA. 1 hit. [Graphical view] | ||||||||||||
| SUPFAM | SSF53056. Prok_plnt_COanhd. 1 hit. | ||||||||||||
| PROSITE | PS00704. PROK_CO2_ANHYDRASE_1. False negative. PS00705. PROK_CO2_ANHYDRASE_2. 1 hit. [Graphical view] | ||||||||||||
| ProtoNet | Search... | ||||||||||||
Other | |||||||||||||
| NextBio | 980010. | ||||||||||||
Entry information
| Entry name | CAN_YEAST | ||||||||
| Accession | Primary (citable) accession number: P53615 Secondary accession number(s): D6W1E3 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Fungal Protein Annotation Program | ||||||||
Relevant documents
| Yeast Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD |
| Yeast chromosome XIV Yeast (Saccharomyces cerevisiae) chromosome XIV: entries and gene names |
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

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