CAN_YEAST
ID CAN_YEAST Reviewed; 221 AA.
AC P53615; D6W1E3;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Carbonic anhydrase;
DE EC=4.2.1.1;
DE AltName: Full=Carbonate dehydratase;
DE AltName: Full=Non-classical export protein 3;
GN Name=NCE103; Synonyms=NCE3; OrderedLocusNames=YNL036W; ORFNames=N2695;
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 [MRNA].
RC STRAIN=ATCC 26109 / X2180 / NCYC 826;
RX PubMed=8655575; DOI=10.1083/jcb.133.5.1017;
RA Cleves A.E., Cooper D.N.W., Barondes S.H., Kelly R.B.;
RT "A new pathway for protein export in Saccharomyces cerevisiae.";
RL J. Cell Biol. 133:1017-1026(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169873;
RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT evolutionary implications.";
RL Nature 387:93-98(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 FUNCTION.
RX PubMed=10407265;
RX DOI=10.1002/(sici)1097-0061(199907)15:10a<855::aid-yea425>3.0.co;2-c;
RA Goetz R., Gnann A., Zimmermann F.K.;
RT "Deletion of the carbonic anhydrase-like gene NCE103 of the yeast
RT Saccharomyces cerevisiae causes an oxygen-sensitive growth defect.";
RL Yeast 15:855-864(1999).
RN [5]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [6]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [7]
RP FUNCTION.
RX PubMed=15096093; DOI=10.1042/bj20031711;
RA Clark D., Rowlett R.S., Coleman J.R., Klessig D.F.;
RT "Complementation of the yeast deletion mutant DeltaNCE103 by members of the
RT beta class of carbonic anhydrases is dependent on carbonic anhydrase
RT activity rather than on antioxidant activity.";
RL Biochem. J. 379:609-615(2004).
RN [8]
RP FUNCTION.
RX PubMed=15948716; DOI=10.1042/bj20050556;
RA Aguilera J., Van Dijken J.P., De Winde J.H., Pronk J.T.;
RT "Carbonic anhydrase (Nce103p): an essential biosynthetic enzyme for growth
RT of Saccharomyces cerevisiae at atmospheric carbon dioxide pressure.";
RL Biochem. J. 391:311-316(2005).
RN [9]
RP INDUCTION.
RX PubMed=15780657; DOI=10.1016/j.femsyr.2004.09.009;
RA Aguilera J., Petit T., de Winde J.H., Pronk J.T.;
RT "Physiological and genome-wide transcriptional responses of Saccharomyces
RT cerevisiae to high carbon dioxide concentrations.";
RL FEMS Yeast Res. 5:579-593(2005).
RN [10]
RP FUNCTION, CATALYTIC ACTIVITY, AND INDUCTION.
RX PubMed=15813743; DOI=10.1111/j.1365-2958.2005.04560.x;
RA Amoroso G., Morell-Avrahov L., Mueller D., Klug K., Sueltemeyer D.;
RT "The gene NCE103 (YNL036w) from Saccharomyces cerevisiae encodes a
RT functional carbonic anhydrase and its transcription is regulated by the
RT concentration of inorganic carbon in the medium.";
RL Mol. Microbiol. 56:549-558(2005).
RN [11]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=18993072; DOI=10.1016/j.bmcl.2008.10.100;
RA Isik S., Kockar F., Arslan O., Guler O.O., Innocenti A., Supuran C.T.;
RT "Carbonic anhydrase inhibitors. Inhibition of the beta-class enzyme from
RT the yeast Saccharomyces cerevisiae with anions.";
RL Bioorg. Med. Chem. Lett. 18:6327-6331(2008).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RX PubMed=22984289; DOI=10.1074/mcp.m112.021105;
RA Voegtle F.N., Burkhart J.M., Rao S., Gerbeth C., Hinrichs J.,
RA Martinou J.C., Chacinska A., Sickmann A., Zahedi R.P., Meisinger C.;
RT "Intermembrane space proteome of yeast mitochondria.";
RL Mol. Cell. Proteomics 11:1840-1852(2012).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.04 ANGSTROMS) OF 14-221 IN COMPLEX WITH ZINC ION,
RP AND COFACTOR.
RX PubMed=19852838; DOI=10.1186/1472-6807-9-67;
RA Teng Y.B., Jiang Y.L., He Y.X., He W.W., Lian F.M., Chen Y., Zhou C.Z.;
RT "Structural insights into the substrate tunnel of Saccharomyces cerevisiae
RT carbonic anhydrase Nce103.";
RL BMC Struct. Biol. 9:67-67(2009).
CC -!- FUNCTION: Catalyzes the reversible hydration of CO(2) to H(2)CO(3). The
CC main role may be to provide inorganic carbon for the bicarbonate-
CC dependent carboxylation reactions catalyzed by pyruvate carboxylase,
CC acetyl-CoA carboxylase and carbamoyl-phosphate synthetase. Involved in
CC protection against oxidative damage. Encodes a substrate for the non-
CC classical protein export pathway for proteins that lack a cleavable
CC signal sequence. {ECO:0000269|PubMed:10407265,
CC ECO:0000269|PubMed:15096093, ECO:0000269|PubMed:15813743,
CC ECO:0000269|PubMed:15948716, ECO:0000269|PubMed:18993072}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + hydrogencarbonate = CO2 + H2O; Xref=Rhea:RHEA:10748,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:17544; EC=4.2.1.1; Evidence={ECO:0000269|PubMed:15813743,
CC ECO:0000269|PubMed:18993072};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:19852838};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:19852838};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC Note=kcat is 940000 sec(-1) with CO(2) as substrate.
CC {ECO:0000269|PubMed:18993072};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus
CC {ECO:0000269|PubMed:14562095}. Mitochondrion intermembrane space
CC {ECO:0000269|PubMed:22984289}.
CC -!- INDUCTION: Transcription and activity down-regulated at elevated CO(2)
CC concentrations. {ECO:0000269|PubMed:15780657,
CC ECO:0000269|PubMed:15813743}.
CC -!- MISCELLANEOUS: Present with 2330 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the beta-class carbonic anhydrase family.
CC {ECO:0000305}.
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DR EMBL; U52369; AAC49352.1; -; mRNA.
DR EMBL; Z71312; CAA95901.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10509.1; -; Genomic_DNA.
DR PIR; S62958; S62958.
DR RefSeq; NP_014362.3; NM_001182875.3.
DR PDB; 3EYX; X-ray; 2.04 A; A/B=14-221.
DR PDBsum; 3EYX; -.
DR AlphaFoldDB; P53615; -.
DR SMR; P53615; -.
DR BioGRID; 35788; 76.
DR DIP; DIP-968N; -.
DR IntAct; P53615; 1.
DR MINT; P53615; -.
DR STRING; 4932.YNL036W; -.
DR BindingDB; P53615; -.
DR ChEMBL; CHEMBL5931; -.
DR DrugCentral; P53615; -.
DR iPTMnet; P53615; -.
DR MaxQB; P53615; -.
DR PaxDb; P53615; -.
DR PRIDE; P53615; -.
DR EnsemblFungi; YNL036W_mRNA; YNL036W; YNL036W.
DR GeneID; 855692; -.
DR KEGG; sce:YNL036W; -.
DR SGD; S000004981; NCE103.
DR VEuPathDB; FungiDB:YNL036W; -.
DR eggNOG; KOG1578; Eukaryota.
DR GeneTree; ENSGT00500000045239; -.
DR HOGENOM; CLU_053879_3_1_1; -.
DR InParanoid; P53615; -.
DR OMA; WHYIIET; -.
DR BioCyc; YEAST:G3O-33073-MON; -.
DR BRENDA; 4.2.1.1; 984.
DR EvolutionaryTrace; P53615; -.
DR PRO; PR:P53615; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P53615; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005758; C:mitochondrial intermembrane space; IDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0004089; F:carbonate dehydratase activity; IDA:SGD.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0015976; P:carbon utilization; IEA:InterPro.
DR GO; GO:0071244; P:cellular response to carbon dioxide; IMP:SGD.
DR GO; GO:0034599; P:cellular response to oxidative stress; IMP:SGD.
DR Gene3D; 3.40.1050.10; -; 1.
DR InterPro; IPR001765; Carbonic_anhydrase.
DR InterPro; IPR015892; Carbonic_anhydrase_CS.
DR InterPro; IPR036874; Carbonic_anhydrase_sf.
DR PANTHER; PTHR11002; PTHR11002; 1.
DR Pfam; PF00484; Pro_CA; 1.
DR SMART; SM00947; Pro_CA; 1.
DR SUPFAM; SSF53056; SSF53056; 1.
DR PROSITE; PS00705; PROK_CO2_ANHYDRASE_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Lyase; Metal-binding; Mitochondrion; Nucleus;
KW Reference proteome; Zinc.
FT CHAIN 1..221
FT /note="Carbonic anhydrase"
FT /id="PRO_0000077468"
FT BINDING 57
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:19852838,
FT ECO:0007744|PDB:3EYX"
FT BINDING 59
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P61517"
FT BINDING 112
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:19852838,
FT ECO:0007744|PDB:3EYX"
FT BINDING 115
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:19852838,
FT ECO:0007744|PDB:3EYX"
FT CONFLICT 39
FT /note="L -> W (in Ref. 1; AAC49352)"
FT /evidence="ECO:0000305"
FT HELIX 18..35
FT /evidence="ECO:0007829|PDB:3EYX"
FT HELIX 37..39
FT /evidence="ECO:0007829|PDB:3EYX"
FT STRAND 51..57
FT /evidence="ECO:0007829|PDB:3EYX"
FT HELIX 64..67
FT /evidence="ECO:0007829|PDB:3EYX"
FT STRAND 73..79
FT /evidence="ECO:0007829|PDB:3EYX"
FT HELIX 80..82
FT /evidence="ECO:0007829|PDB:3EYX"
FT HELIX 89..100
FT /evidence="ECO:0007829|PDB:3EYX"
FT STRAND 105..114
FT /evidence="ECO:0007829|PDB:3EYX"
FT HELIX 116..122
FT /evidence="ECO:0007829|PDB:3EYX"
FT HELIX 126..128
FT /evidence="ECO:0007829|PDB:3EYX"
FT HELIX 130..132
FT /evidence="ECO:0007829|PDB:3EYX"
FT HELIX 135..140
FT /evidence="ECO:0007829|PDB:3EYX"
FT HELIX 142..150
FT /evidence="ECO:0007829|PDB:3EYX"
FT HELIX 152..155
FT /evidence="ECO:0007829|PDB:3EYX"
FT HELIX 161..180
FT /evidence="ECO:0007829|PDB:3EYX"
FT HELIX 184..191
FT /evidence="ECO:0007829|PDB:3EYX"
FT STRAND 196..202
FT /evidence="ECO:0007829|PDB:3EYX"
FT TURN 204..206
FT /evidence="ECO:0007829|PDB:3EYX"
FT STRAND 209..215
FT /evidence="ECO:0007829|PDB:3EYX"
FT STRAND 217..219
FT /evidence="ECO:0007829|PDB:3EYX"
SQ SEQUENCE 221 AA; 24859 MW; 96D0EBAA8BBD9790 CRC64;
MSATESSSIF TLSHNSNLQD ILAANAKWAS QMNNIQPTLF PDHNAKGQSP HTLFIGCSDS
RYNENCLGVL PGEVFTWKNV ANICHSEDLT LKATLEFAII CLKVNKVIIC GHTDCGGIKT
CLTNQREALP KVNCSHLYKY LDDIDTMYHE ESQNLIHLKT QREKSHYLSH CNVKRQFNRI
IENPTVQTAV QNGELQVYGL LYNVEDGLLQ TVSTYTKVTP K
