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P53615 (CAN_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 102. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Carbonic anhydrase

EC=4.2.1.1
Alternative name(s):
Carbonate dehydratase
Non-classical export protein 3
Gene names
Name:NCE103
Synonyms:NCE3
Ordered Locus Names:YNL036W
ORF Names:N2695
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length221 AA.
Sequence statusComplete.
Protein existenceEvidence 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 Ref.11

Catalytic activity

H2CO3 = CO2 + H2O. Ref.10 Ref.11

Cofactor

Binds 1 zinc ion per subunit By similarity.

Subcellular location

Cytoplasm. Nucleus. Mitochondrion intermembrane space Ref.5 Ref.12.

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.

Sequence similarities

Belongs to the beta-class carbonic anhydrase family.

Biophysicochemical properties

Kinetic parameters:

kcat is 940000 sec(-1) with CO2 as substrate. Ref.11

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 221221Carbonic anhydrase
PRO_0000077468

Sites

Metal binding571Zinc
Metal binding1121Zinc; via tele nitrogen
Metal binding1151Zinc

Experimental info

Sequence conflict391L → W in AAC49352. Ref.1

Secondary structure

........................................ 221
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P53615 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 96D0EBAA8BBD9790

FASTA22124,859
        10         20         30         40         50         60 
MSATESSSIF TLSHNSNLQD ILAANAKWAS QMNNIQPTLF PDHNAKGQSP HTLFIGCSDS 

        70         80         90        100        110        120 
RYNENCLGVL PGEVFTWKNV ANICHSEDLT LKATLEFAII CLKVNKVIIC GHTDCGGIKT 

       130        140        150        160        170        180 
CLTNQREALP KVNCSHLYKY LDDIDTMYHE ESQNLIHLKT QREKSHYLSH CNVKRQFNRI 

       190        200        210        220 
IENPTVQTAV QNGELQVYGL LYNVEDGLLQ TVSTYTKVTP K 

« Hide

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] [Europe PMC] [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. expand/collapse author list , Bussereau F., Coster F., Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F., Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C., Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A., Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H., Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L., Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R., Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D., Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A., Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C., Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F., Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G., Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M., Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.
Nature 387:93-98(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, INDUCTION.
[11]"Carbonic anhydrase inhibitors. Inhibition of the beta-class enzyme from the yeast Saccharomyces cerevisiae with anions."
Isik S., Kockar F., Arslan O., Guler O.O., Innocenti A., Supuran C.T.
Bioorg. Med. Chem. Lett. 18:6327-6331(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
[12]"Intermembrane space proteome of yeast mitochondria."
Voegtle F.N., Burkhart J.M., Rao S., Gerbeth C., Hinrichs J., Martinou J.C., Chacinska A., Sickmann A., Zahedi R.P., Meisinger C.
Mol. Cell. Proteomics 11:1840-1852(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
[13]"Structural insights into the substrate tunnel of Saccharomyces cerevisiae carbonic anhydrase Nce103."
Teng Y.B., Jiang Y.L., He Y.X., He W.W., Lian F.M., Chen Y., Zhou C.Z.
BMC Struct. Biol. 9:67-67(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.04 ANGSTROMS) OF 14-221.
+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.
PIRS62958.
RefSeqNP_014362.3. NM_001182875.3.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3EYXX-ray2.04A/B14-221[»]
ProteinModelPortalP53615.
SMRP53615. Positions 17-221.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid35788. 9 interactions.
DIPDIP-968N.
IntActP53615. 1 interaction.
MINTMINT-485874.
STRING4932.YNL036W.

Chemistry

BindingDBP53615.
ChEMBLCHEMBL5931.

Proteomic databases

MaxQBP53615.
PaxDbP53615.
PeptideAtlasP53615.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYNL036W; YNL036W; YNL036W.
GeneID855692.
KEGGsce:YNL036W.

Organism-specific databases

CYGDYNL036w.
SGDS000004981. NCE103.

Phylogenomic databases

eggNOGCOG0288.
HOGENOMHOG000125184.
OMAQIFTHRN.
OrthoDBEOG7TXKT4.

Enzyme and pathway databases

BioCycYEAST:G3O-33073-MONOMER.

Gene expression databases

GenevestigatorP53615.

Family and domain databases

Gene3D3.40.1050.10. 1 hit.
InterProIPR001765. Carbonic_anhydrase.
IPR015892. Carbonic_anhydrase_CS.
[Graphical view]
PANTHERPTHR11002. PTHR11002. 1 hit.
PfamPF00484. Pro_CA. 1 hit.
[Graphical view]
SMARTSM00947. Pro_CA. 1 hit.
[Graphical view]
SUPFAMSSF53056. SSF53056. 1 hit.
PROSITEPS00705. PROK_CO2_ANHYDRASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP53615.
NextBio980010.

Entry information

Entry nameCAN_YEAST
AccessionPrimary (citable) accession number: P53615
Secondary accession number(s): D6W1E3
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: May 14, 2014
This is version 102 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome XIV

Yeast (Saccharomyces cerevisiae) chromosome XIV: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references