ID CAH1_HUMAN Reviewed; 261 AA. AC P00915; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 27-MAR-2024, entry version 226. DE RecName: Full=Carbonic anhydrase 1; DE EC=4.2.1.1 {ECO:0000269|PubMed:10550681, ECO:0000269|PubMed:16686544, ECO:0000269|PubMed:16807956, ECO:0000269|PubMed:17127057, ECO:0000269|PubMed:19186056, ECO:0000269|PubMed:19206230}; DE AltName: Full=Carbonate dehydratase I; DE AltName: Full=Carbonic anhydrase B; DE Short=CAB; DE AltName: Full=Carbonic anhydrase I; DE Short=CA-I; DE AltName: Full=Cyanamide hydratase CA1 {ECO:0000305}; DE EC=4.2.1.69 {ECO:0000269|PubMed:10550681}; GN Name=CA1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=3104879; DOI=10.1093/nar/15.5.2386; RA Barlow J.H., Lowe N., Edwards Y.H., Butterworth P.H.W.; RT "Human carbonic anhydrase I cDNA."; RL Nucleic Acids Res. 15:2386-2386(1987). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=2121614; DOI=10.1016/0378-1119(90)90236-k; RA Lowe N., Brady H.J.M., Barlow J.H., Sowden J.C., Edwards M., RA Butterworth P.H.W.; RT "Structure and methylation patterns of the gene encoding human carbonic RT anhydrase I."; RL Gene 93:277-283(1990). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Pancreas, and Spleen; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP PROTEIN SEQUENCE OF 2-261, CLEAVAGE OF INITIATOR METHIONINE, AND RP ACETYLATION AT ALA-2. RX PubMed=4217196; DOI=10.1016/s0300-9084(74)80093-3; RA Giraud N., Marriq C., Laurent-Tabusse G.; RT "Primary structure of human B erythrocyte carbonic anhydrase. 3. Sequence RT of CNBr fragment I and III (residues 149-260)."; RL Biochimie 56:1031-1043(1974). RN [5] RP PROTEIN SEQUENCE OF 20-261. RX PubMed=4625868; DOI=10.1016/0006-291x(72)90400-7; RA Andersson B., Nyman P.O., Strid L.; RT "Amino acid sequence of human erythrocyte carbonic anhydrase B."; RL Biochem. Biophys. Res. Commun. 48:670-677(1972). RN [6] RP PROTEIN SEQUENCE OF 12-261. RX PubMed=4632246; DOI=10.1016/s0021-9258(19)44161-6; RA Lin K.-T.D., Deutsch H.F.; RT "Human carbonic anhydrases. XI. The complete primary structure of carbonic RT anhydrase B."; RL J. Biol. Chem. 248:1885-1893(1973). RN [7] RP SEQUENCE REVISION. RX PubMed=4207120; DOI=10.1016/s0021-9258(19)42734-8; RA Lin K.-T.D., Deutsch H.F.; RT "Human carbonic anhydrases. XII. The complete primary structure of the C RT isozyme."; RL J. Biol. Chem. 249:2329-2337(1974). RN [8] RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=10550681; DOI=10.1007/s007750050375; RA Briganti F., Mangani S., Scozzafava A., Vernaglione G., Supuran C.T.; RT "Carbonic anhydrase catalyzes cyanamide hydration to urea: is it mimicking RT the physiological reaction?"; RL J. Biol. Inorg. Chem. 4:528-536(1999). RN [9] RP ACTIVITY REGULATION, FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=16807956; DOI=10.1002/chem.200600159; RA Temperini C., Scozzafava A., Vullo D., Supuran C.T.; RT "Carbonic anhydrase activators. Activation of isozymes I, II, IV, VA, VII, RT and XIV with l- and d-histidine and crystallographic analysis of their RT adducts with isoform II: engineering proton-transfer processes within the RT active site of an enzyme."; RL Chemistry 12:7057-7066(2006). RN [10] RP ACTIVITY REGULATION, FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=16686544; DOI=10.1021/jm0603320; RA Temperini C., Scozzafava A., Vullo D., Supuran C.T.; RT "Carbonic anhydrase activators. Activation of isoforms I, II, IV, VA, VII, RT and XIV with L- and D-phenylalanine and crystallographic analysis of their RT adducts with isozyme II: stereospecific recognition within the active site RT of an enzyme and its consequences for the drug design."; RL J. Med. Chem. 49:3019-3027(2006). RN [11] RP ACTIVITY REGULATION, FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=17127057; DOI=10.1016/j.bmcl.2006.11.027; RA Temperini C., Innocenti A., Scozzafava A., Mastrolorenzo A., Supuran C.T.; RT "Carbonic anhydrase activators: L-Adrenaline plugs the active site entrance RT of isozyme II, activating better isoforms I, IV, VA, VII, and XIV."; RL Bioorg. Med. Chem. Lett. 17:628-635(2007). RN [12] RP ACTIVITY REGULATION, FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=19186056; DOI=10.1016/j.bmcl.2009.01.038; RA Crocetti L., Maresca A., Temperini C., Hall R.A., Scozzafava A., RA Muehlschlegel F.A., Supuran C.T.; RT "A thiabendazole sulfonamide shows potent inhibitory activity against RT mammalian and nematode alpha-carbonic anhydrases."; RL Bioorg. Med. Chem. Lett. 19:1371-1375(2009). RN [13] RP ACTIVITY REGULATION, FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=19206230; DOI=10.1021/ja809683v; RA Maresca A., Temperini C., Vu H., Pham N.B., Poulsen S.-A., Scozzafava A., RA Quinn R.J., Supuran C.T.; RT "Non-zinc mediated inhibition of carbonic anhydrases: coumarins are a new RT class of suicide inhibitors."; RL J. Am. Chem. Soc. 131:3057-3062(2009). RN [14] RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY RP REGULATION. RX PubMed=18618712; DOI=10.1002/prot.22144; RA Di Fiore A., Monti S.M., Hilvo M., Parkkila S., Romano V., Scaloni A., RA Pedone C., Scozzafava A., Supuran C.T., De Simone G.; RT "Crystal structure of human carbonic anhydrase XIII and its complex with RT the inhibitor acetazolamide."; RL Proteins 74:164-175(2009). RN [15] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [16] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [17] RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 2-260. RX PubMed=4622589; DOI=10.1016/0022-2836(72)90452-4; RA Kannan K.K., Fridborg K., Bergsten P.C., Liljas A., Loevgren S., Petef M., RA Strandberg B., Waara I., Adler L., Falkbring S.O., Goethe P.O., Nyman P.O.; RT "Structure of human carbonic anhydrase B. I. Crystallization and heavy atom RT modifications."; RL J. Mol. Biol. 63:601-604(1972). RN [18] RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS). RX PubMed=804171; DOI=10.1073/pnas.72.1.51; RA Kannan K.K., Notstrand B., Fridborg K., Loevgren S., Ohlsson A., Petef M.; RT "Crystal structure of human erythrocyte carbonic anhydrase B. Three- RT dimensional structure at a nominal 2.2-A resolution."; RL Proc. Natl. Acad. Sci. U.S.A. 72:51-55(1975). RN [19] RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 2-260 IN COMPLEX WITH ZINC ION. RX PubMed=6430186; DOI=10.1111/j.1749-6632.1984.tb12314.x; RA Kannan K.K., Ramanadham M., Jones T.A.; RT "Structure, refinement, and function of carbonic anhydrase isozymes: RT refinement of human carbonic anhydrase I."; RL Ann. N. Y. Acad. Sci. 429:49-60(1984). RN [20] RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 2-260 IN COMPLEX WITH ZINC ION RP AND INHIBITORS. RX PubMed=15299369; DOI=10.1107/s0907444994001873; RA Kumar V., Kannan K.K., Sathyamurthi P.; RT "Differences in anionic inhibition of human carbonic anhydrase I revealed RT from the structures of iodide and gold cyanide inhibitor complexes."; RL Acta Crystallogr. D 50:731-738(1994). RN [21] RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 2-260 IN COMPLEX WITH ZINC ION RP AND BICARBONATE. RX PubMed=8057362; DOI=10.1006/jmbi.1994.1491; RA Kumar V., Kannan K.K.; RT "Enzyme-substrate interactions. Structure of human carbonic anhydrase I RT complexed with bicarbonate."; RL J. Mol. Biol. 241:226-232(1994). RN [22] RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 2-260 IN COMPLEX WITH ZINC ION RP AND INHIBITORS. RX PubMed=7932756; DOI=10.1006/jmbi.1994.1655; RA Chakravarty S., Kannan K.K.; RT "Drug-protein interactions. Refined structures of three sulfonamide drug RT complexes of human carbonic anhydrase I enzyme."; RL J. Mol. Biol. 243:298-309(1994). RN [23] RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 2-260 IN COMPLEX WITH ZINC ION, RP AND VARIANT MICHIGAN-1 ARG-68. RX PubMed=12009884; DOI=10.1021/bi0120446; RA Ferraroni M., Tilli S., Briganti F., Chegwidden W.R., Supuran C.T., RA Wiebauer K.E., Tashian R.E., Scozzafava A.; RT "Crystal structure of a zinc-activated variant of human carbonic anhydrase RT I, CA I Michigan 1: evidence for a second zinc binding site involving RT arginine coordination."; RL Biochemistry 41:6237-6244(2002). RN [24] RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 2-260 IN COMPLEX WITH ZINC ION RP AND ACTIVATORS, AND ACTIVATION BY IMIDAZOLE AND HISTIDINE. RX PubMed=16870440; DOI=10.1016/j.bmcl.2006.07.021; RA Temperini C., Scozzafava A., Supuran C.T.; RT "Carbonic anhydrase activators: the first X-ray crystallographic study of RT an adduct of isoform I."; RL Bioorg. Med. Chem. Lett. 16:5152-5156(2006). RN [25] RP X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 2-260 IN COMPLEX WITH ZINC ION RP AND INHIBITORS, ACTIVITY REGULATION, FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=16506782; DOI=10.1021/ja057257n; RA Jude K.M., Banerjee A.L., Haldar M.K., Manokaran S., Roy B., Mallik S., RA Srivastava D.K., Christianson D.W.; RT "Ultrahigh resolution crystal structures of human carbonic anhydrases I and RT II complexed with 'two-prong' inhibitors reveal the molecular basis of high RT affinity."; RL J. Am. Chem. Soc. 128:3011-3018(2006). RN [26] RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 6-260 IN COMPLEX WITH ZINC ION RP AND THE ANTIVIRAL FOSCARNET, ACTIVITY REGULATION, FUNCTION, AND CATALYTIC RP ACTIVITY. RX PubMed=17314045; DOI=10.1016/j.bmcl.2007.01.113; RA Temperini C., Innocenti A., Guerri A., Scozzafava A., Rusconi S., RA Supuran C.T.; RT "Phosph(on)ate as a zinc-binding group in metalloenzyme inhibitors: X-ray RT crystal structure of the antiviral drug foscarnet complexed to human RT carbonic anhydrase I."; RL Bioorg. Med. Chem. Lett. 17:2210-2215(2007). RN [27] RP X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 2-260 IN COMPLEX WITH ZINC ION RP AND INHIBITORS, ACTIVITY REGULATION, FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=17407288; DOI=10.1021/ja068359w; RA Srivastava D.K., Jude K.M., Banerjee A.L., Haldar M., Manokaran S., RA Kooren J., Mallik S., Christianson D.W.; RT "Structural analysis of charge discrimination in the binding of inhibitors RT to human carbonic anhydrases I and II."; RL J. Am. Chem. Soc. 129:5528-5537(2007). RN [28] RP VARIANT GUAM ARG-254. RX PubMed=6781336; RA Omoto K., Ueda S., Goriki K., Takahashi N., Misawa S., Pagaran I.G.; RT "Population genetic studies of the Philippine Negritos. III. Identification RT of the carbonic anhydrase-1 variant with CA1 Guam."; RL Am. J. Hum. Genet. 33:105-111(1981). RN [29] RP VARIANT MICHIGAN-1 ARG-68. RX PubMed=7866410; DOI=10.1002/humu.1380040411; RA Chegwidden W.R., Wagner L.E., Venta P.J., Bergenhem N.C.H., Yu Y.-S.L., RA Tashian R.E.; RT "Marked zinc activation of ester hydrolysis by a mutation, 67-His (CAT) to RT Arg (CGT), in the active site of human carbonic anhydrase I."; RL Hum. Mutat. 4:294-296(1994). CC -!- FUNCTION: Catalyzes the reversible hydration of carbon dioxide CC (PubMed:10550681, PubMed:18618712, PubMed:16807956, PubMed:16686544, CC PubMed:17127057, PubMed:19186056, PubMed:19206230, PubMed:16506782, CC PubMed:17314045, PubMed:17407288). Can hydrate cyanamide to urea CC (PubMed:10550681). {ECO:0000269|PubMed:10550681, CC ECO:0000269|PubMed:16506782, ECO:0000269|PubMed:16686544, CC ECO:0000269|PubMed:16807956, ECO:0000269|PubMed:17127057, CC ECO:0000269|PubMed:17314045, ECO:0000269|PubMed:17407288, CC ECO:0000269|PubMed:18618712, ECO:0000269|PubMed:19186056, CC ECO:0000269|PubMed:19206230}. 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:10550681, CC ECO:0000269|PubMed:16506782, ECO:0000269|PubMed:16686544, CC ECO:0000269|PubMed:16807956, ECO:0000269|PubMed:17127057, CC ECO:0000269|PubMed:17314045, ECO:0000269|PubMed:17407288, CC ECO:0000269|PubMed:18618712, ECO:0000269|PubMed:19186056, CC ECO:0000269|PubMed:19206230}; CC -!- CATALYTIC ACTIVITY: CC Reaction=urea = cyanamide + H2O; Xref=Rhea:RHEA:23056, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:16199, ChEBI:CHEBI:16698; EC=4.2.1.69; CC Evidence={ECO:0000269|PubMed:10550681}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000269|PubMed:12009884, ECO:0000269|PubMed:15299369, CC ECO:0000269|PubMed:16506782, ECO:0000269|PubMed:16870440, CC ECO:0000269|PubMed:17314045, ECO:0000269|PubMed:17407288, CC ECO:0000269|PubMed:6430186, ECO:0000269|PubMed:7932756, CC ECO:0000269|PubMed:804171, ECO:0000269|PubMed:8057362}; CC -!- ACTIVITY REGULATION: Activated by histamine, imidazole, L-adrenaline, CC L- and D-histidine, and L- and D-phenylalanine. Inhibited by coumarins, CC sulfonamide derivatives such as acetazolamide, benzenesulfonamide and CC derivatives (4-carboxyethylbenzene-sulfonamide, 4-carboxyethylbenzene- CC sulfonamide ethyl ester, 4-(acetyl-2-aminoethyl)benzene-sulfonamide, 4- CC aminoethylbenzene-sulfonamide), and 'prong inhibitors' BR15, BR17, BR22 CC and BR30. Activated by a short exposition to Foscarnet CC (phosphonoformate trisodium salt), but inhibited by a long one. CC Esterase activity weakly reduced by cyanamide. CC {ECO:0000269|PubMed:16506782, ECO:0000269|PubMed:16686544, CC ECO:0000269|PubMed:16807956, ECO:0000269|PubMed:17127057, CC ECO:0000269|PubMed:17314045, ECO:0000269|PubMed:17407288, CC ECO:0000269|PubMed:18618712, ECO:0000269|PubMed:19186056, CC ECO:0000269|PubMed:19206230}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=4 mM for CO(2) {ECO:0000269|PubMed:10550681, CC ECO:0000269|PubMed:18618712}; CC KM=15 mM for 4-nitrophenyl acetate {ECO:0000269|PubMed:10550681, CC ECO:0000269|PubMed:18618712}; CC -!- INTERACTION: CC P00915; Q12800: TFCP2; NbExp=6; IntAct=EBI-3912102, EBI-717422; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:B0BNN3}. CC -!- SIMILARITY: Belongs to the alpha-carbonic anhydrase family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X05014; CAA28663.1; -; mRNA. DR EMBL; M33987; AAA51910.1; -; mRNA. DR EMBL; BC027890; AAH27890.1; -; mRNA. DR CCDS; CCDS6237.1; -. DR PIR; JQ0786; CRHU1. DR RefSeq; NP_001122301.1; NM_001128829.3. DR RefSeq; NP_001122302.1; NM_001128830.3. DR RefSeq; NP_001122303.1; NM_001128831.3. DR RefSeq; NP_001158302.1; NM_001164830.1. DR RefSeq; NP_001729.1; NM_001738.4. DR PDB; 1AZM; X-ray; 2.00 A; A=2-261. DR PDB; 1BZM; X-ray; 2.00 A; A=2-261. DR PDB; 1CRM; X-ray; 2.00 A; A=2-261. DR PDB; 1CZM; X-ray; 2.00 A; A=2-261. DR PDB; 1HCB; X-ray; 1.60 A; A=2-261. DR PDB; 1HUG; X-ray; 2.00 A; A=2-261. DR PDB; 1HUH; X-ray; 2.20 A; A=2-261. DR PDB; 1J9W; X-ray; 2.60 A; A/B=2-261. DR PDB; 1JV0; X-ray; 2.00 A; A/B=2-261. DR PDB; 2CAB; X-ray; 2.00 A; A=2-261. DR PDB; 2FOY; X-ray; 1.55 A; A/B=2-261. DR PDB; 2FW4; X-ray; 2.00 A; A/B=2-261. DR PDB; 2IT4; X-ray; 2.00 A; A/B=6-261. DR PDB; 2NMX; X-ray; 1.55 A; A/B=2-261. DR PDB; 2NN1; X-ray; 1.65 A; A/B=2-261. DR PDB; 2NN7; X-ray; 1.85 A; A/B=2-261. DR PDB; 3LXE; X-ray; 1.90 A; A/B=2-261. DR PDB; 3W6H; X-ray; 2.96 A; A/B=2-261. DR PDB; 3W6I; X-ray; 2.69 A; A/E=2-261. DR PDB; 4WR7; X-ray; 1.50 A; A/B=3-261. DR PDB; 4WUP; X-ray; 1.75 A; A/B=3-261. DR PDB; 4WUQ; X-ray; 1.75 A; A/B=3-261. DR PDB; 5E2M; X-ray; 1.41 A; A/B=3-261. DR PDB; 5GMM; X-ray; 2.00 A; A/B=1-261. DR PDB; 6EVR; X-ray; 1.50 A; A/B=1-261. DR PDB; 6EX1; X-ray; 1.60 A; A/B=1-261. DR PDB; 6F3B; X-ray; 1.40 A; A/B=1-261. DR PDB; 6FAF; X-ray; 1.99 A; A/B=1-261. DR PDB; 6FAG; X-ray; 1.79 A; A/B=1-261. DR PDB; 6G3V; X-ray; 1.69 A; A/B=1-261. DR PDB; 6HWZ; X-ray; 1.64 A; A/B=1-261. DR PDB; 6I0J; X-ray; 1.35 A; A/B=1-261. DR PDB; 6I0L; X-ray; 1.40 A; A/B=1-261. DR PDB; 6SWM; X-ray; 2.77 A; A/B=1-261. DR PDB; 6XZE; X-ray; 1.54 A; A/B=1-261. DR PDB; 6XZO; X-ray; 1.44 A; A/B=1-261. DR PDB; 6XZS; X-ray; 1.53 A; A/B=1-261. DR PDB; 6XZX; X-ray; 1.55 A; A/B=1-261. DR PDB; 6XZY; X-ray; 1.66 A; A/B=1-261. DR PDB; 6Y00; X-ray; 1.37 A; A/B=1-261. DR PDB; 7PLF; X-ray; 1.46 A; AAA/BBB=1-261. DR PDB; 7Q0D; X-ray; 1.24 A; A/B=1-261. DR PDB; 7QOB; X-ray; 1.80 A; AAA/BBB=1-261. DR PDB; 7ZL5; X-ray; 1.48 A; AAA/BBB=1-261. DR PDBsum; 1AZM; -. DR PDBsum; 1BZM; -. DR PDBsum; 1CRM; -. DR PDBsum; 1CZM; -. DR PDBsum; 1HCB; -. DR PDBsum; 1HUG; -. DR PDBsum; 1HUH; -. DR PDBsum; 1J9W; -. DR PDBsum; 1JV0; -. DR PDBsum; 2CAB; -. DR PDBsum; 2FOY; -. DR PDBsum; 2FW4; -. DR PDBsum; 2IT4; -. DR PDBsum; 2NMX; -. DR PDBsum; 2NN1; -. DR PDBsum; 2NN7; -. DR PDBsum; 3LXE; -. DR PDBsum; 3W6H; -. DR PDBsum; 3W6I; -. DR PDBsum; 4WR7; -. DR PDBsum; 4WUP; -. DR PDBsum; 4WUQ; -. DR PDBsum; 5E2M; -. DR PDBsum; 5GMM; -. DR PDBsum; 6EVR; -. DR PDBsum; 6EX1; -. DR PDBsum; 6F3B; -. DR PDBsum; 6FAF; -. DR PDBsum; 6FAG; -. DR PDBsum; 6G3V; -. DR PDBsum; 6HWZ; -. DR PDBsum; 6I0J; -. DR PDBsum; 6I0L; -. DR PDBsum; 6SWM; -. DR PDBsum; 6XZE; -. DR PDBsum; 6XZO; -. DR PDBsum; 6XZS; -. DR PDBsum; 6XZX; -. DR PDBsum; 6XZY; -. DR PDBsum; 6Y00; -. DR PDBsum; 7PLF; -. DR PDBsum; 7Q0D; -. DR PDBsum; 7QOB; -. DR PDBsum; 7ZL5; -. DR AlphaFoldDB; P00915; -. DR BMRB; P00915; -. DR PCDDB; P00915; -. DR SMR; P00915; -. DR BioGRID; 107214; 11. DR IntAct; P00915; 5. DR MINT; P00915; -. DR STRING; 9606.ENSP00000430656; -. DR BindingDB; P00915; -. DR ChEMBL; CHEMBL261; -. DR DrugBank; DB08156; 3-[4-(AMINOSULFONYL)PHENYL]PROPANOIC ACID. DR DrugBank; DB00819; Acetazolamide. DR DrugBank; DB00381; Amlodipine. DR DrugBank; DB00436; Bendroflumethiazide. DR DrugBank; DB00562; Benzthiazide. DR DrugBank; DB01194; Brinzolamide. DR DrugBank; DB00880; Chlorothiazide. DR DrugBank; DB00310; Chlorthalidone. DR DrugBank; DB00606; Cyclothiazide. DR DrugBank; DB01119; Diazoxide. DR DrugBank; DB01144; Diclofenamide. DR DrugBank; DB00869; Dorzolamide. DR DrugBank; DB08846; Ellagic acid. DR DrugBank; DB01031; Ethinamate. DR DrugBank; DB00311; Ethoxzolamide. DR DrugBank; DB08157; ETHYL 3-[4-(AMINOSULFONYL)PHENYL]PROPANOATE. DR DrugBank; DB00774; Hydroflumethiazide. DR DrugBank; DB00703; Methazolamide. DR DrugBank; DB00423; Methocarbamol. DR DrugBank; DB00232; Methyclothiazide. DR DrugBank; DB08155; N-{2-[4-(AMINOSULFONYL)PHENYL]ETHYL}ACETAMIDE. DR DrugBank; DB01325; Quinethazone. DR DrugBank; DB09460; Sodium carbonate. DR DrugBank; DB09472; Sodium sulfate. DR DrugBank; DB00273; Topiramate. DR DrugBank; DB01021; Trichlormethiazide. DR DrugBank; DB01593; Zinc. DR DrugBank; DB14487; Zinc acetate. DR DrugBank; DB00909; Zonisamide. DR DrugCentral; P00915; -. DR GuidetoPHARMACOLOGY; 2597; -. DR GlyConnect; 2846; 1 O-GlcNAc glycan (2 sites). DR GlyCosmos; P00915; 2 sites, 1 glycan. DR GlyGen; P00915; 2 sites, 1 O-linked glycan (2 sites). DR iPTMnet; P00915; -. DR PhosphoSitePlus; P00915; -. DR BioMuta; CA1; -. DR DMDM; 115449; -. DR DOSAC-COBS-2DPAGE; P00915; -. DR REPRODUCTION-2DPAGE; IPI00215983; -. DR REPRODUCTION-2DPAGE; P00915; -. DR CPTAC; CPTAC-1302; -. DR CPTAC; non-CPTAC-1091; -. DR jPOST; P00915; -. DR MassIVE; P00915; -. DR PaxDb; 9606-ENSP00000430656; -. DR PeptideAtlas; P00915; -. DR ProteomicsDB; 51291; -. DR Pumba; P00915; -. DR TopDownProteomics; P00915; -. DR Antibodypedia; 1380; 719 antibodies from 41 providers. DR DNASU; 759; -. DR Ensembl; ENST00000431316.3; ENSP00000392338.1; ENSG00000133742.14. DR Ensembl; ENST00000523022.6; ENSP00000429798.1; ENSG00000133742.14. DR Ensembl; ENST00000523953.5; ENSP00000430656.1; ENSG00000133742.14. DR Ensembl; ENST00000542576.5; ENSP00000443517.1; ENSG00000133742.14. DR GeneID; 759; -. DR KEGG; hsa:759; -. DR MANE-Select; ENST00000523022.6; ENSP00000429798.1; NM_001128831.4; NP_001122303.1. DR AGR; HGNC:1368; -. DR CTD; 759; -. DR DisGeNET; 759; -. DR GeneCards; CA1; -. DR HGNC; HGNC:1368; CA1. DR HPA; ENSG00000133742; Group enriched (bone marrow, intestine). DR MIM; 114800; gene. DR neXtProt; NX_P00915; -. DR OpenTargets; ENSG00000133742; -. DR PharmGKB; PA25984; -. DR VEuPathDB; HostDB:ENSG00000133742; -. DR eggNOG; KOG0382; Eukaryota. DR GeneTree; ENSGT00940000161270; -. DR InParanoid; P00915; -. DR OMA; NGPEQWG; -. DR OrthoDB; 49814at2759; -. DR PhylomeDB; P00915; -. DR TreeFam; TF316425; -. DR BioCyc; MetaCyc:HS05785-MONOMER; -. DR BRENDA; 4.2.1.1; 2681. DR PathwayCommons; P00915; -. DR Reactome; R-HSA-1237044; Erythrocytes take up carbon dioxide and release oxygen. DR Reactome; R-HSA-1247673; Erythrocytes take up oxygen and release carbon dioxide. DR Reactome; R-HSA-1475029; Reversible hydration of carbon dioxide. DR Reactome; R-HSA-8950505; Gene and protein expression by JAK-STAT signaling after Interleukin-12 stimulation. DR SABIO-RK; P00915; -. DR SignaLink; P00915; -. DR BioGRID-ORCS; 759; 11 hits in 1160 CRISPR screens. DR ChiTaRS; CA1; human. DR EvolutionaryTrace; P00915; -. DR GeneWiki; CA1_(gene); -. DR GenomeRNAi; 759; -. DR Pharos; P00915; Tclin. DR PRO; PR:P00915; -. DR Proteomes; UP000005640; Chromosome 8. DR RNAct; P00915; Protein. DR Bgee; ENSG00000133742; Expressed in mucosa of transverse colon and 121 other cell types or tissues. DR ExpressionAtlas; P00915; baseline and differential. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0004064; F:arylesterase activity; IMP:CACAO. DR GO; GO:0004089; F:carbonate dehydratase activity; IDA:UniProtKB. DR GO; GO:0018820; F:cyanamide hydratase activity; IDA:UniProtKB. DR GO; GO:0016836; F:hydro-lyase activity; IDA:CACAO. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0006730; P:one-carbon metabolic process; IBA:GO_Central. DR Gene3D; 3.10.200.10; Alpha carbonic anhydrase; 1. DR InterPro; IPR001148; CA_dom. DR InterPro; IPR036398; CA_dom_sf. DR InterPro; IPR023561; Carbonic_anhydrase_a-class. DR InterPro; IPR018338; Carbonic_anhydrase_a-class_CS. DR PANTHER; PTHR18952; CARBONIC ANHYDRASE; 1. DR PANTHER; PTHR18952:SF271; CARBONIC ANHYDRASE 1; 1. DR Pfam; PF00194; Carb_anhydrase; 1. DR SMART; SM01057; Carb_anhydrase; 1. DR SUPFAM; SSF51069; Carbonic anhydrase; 1. DR PROSITE; PS00162; ALPHA_CA_1; 1. DR PROSITE; PS51144; ALPHA_CA_2; 1. DR UCD-2DPAGE; P00915; -. DR Genevisible; P00915; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Cytoplasm; Direct protein sequencing; Lyase; KW Metal-binding; Reference proteome; Zinc. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:4217196" FT CHAIN 2..261 FT /note="Carbonic anhydrase 1" FT /id="PRO_0000077409" FT DOMAIN 4..261 FT /note="Alpha-carbonic anhydrase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01134" FT REGION 1..31 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 241..261 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 65 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000250|UniProtKB:P00918" FT BINDING 65 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /note="in variant Michigan-1" FT /evidence="ECO:0000269|PubMed:12009884" FT BINDING 68 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /note="in variant Michigan-1" FT /evidence="ECO:0000269|PubMed:12009884" FT BINDING 95 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /ligand_note="catalytic" FT /evidence="ECO:0000269|PubMed:12009884, FT ECO:0000269|PubMed:15299369, ECO:0000269|PubMed:16506782, FT ECO:0000269|PubMed:16870440, ECO:0000269|PubMed:17314045, FT ECO:0000269|PubMed:17407288, ECO:0000269|PubMed:6430186, FT ECO:0000269|PubMed:7932756, ECO:0000269|PubMed:804171, FT ECO:0000269|PubMed:8057362" FT BINDING 97 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /ligand_note="catalytic" FT /evidence="ECO:0000269|PubMed:12009884, FT ECO:0000269|PubMed:15299369, ECO:0000269|PubMed:16506782, FT ECO:0000269|PubMed:16870440, ECO:0000269|PubMed:17314045, FT ECO:0000269|PubMed:17407288, ECO:0000269|PubMed:6430186, FT ECO:0000269|PubMed:7932756, ECO:0000269|PubMed:804171, FT ECO:0000269|PubMed:8057362" FT BINDING 120 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /ligand_note="catalytic" FT /evidence="ECO:0000269|PubMed:12009884, FT ECO:0000269|PubMed:15299369, ECO:0000269|PubMed:16506782, FT ECO:0000269|PubMed:16870440, ECO:0000269|PubMed:17314045, FT ECO:0000269|PubMed:17407288, ECO:0000269|PubMed:6430186, FT ECO:0000269|PubMed:7932756, ECO:0000269|PubMed:804171, FT ECO:0000269|PubMed:8057362" FT BINDING 200..201 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P00918" FT BINDING 200 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:8057362" FT BINDING 201 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /note="in variant Michigan-1" FT /evidence="ECO:0000269|PubMed:12009884" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0000269|PubMed:4207120, FT ECO:0000269|PubMed:4217196" FT VARIANT 68 FT /note="H -> R (in variant Michigan-1; confers enhanced FT esterase activity and an additional zinc binding site; FT dbSNP:rs990757234)" FT /evidence="ECO:0000269|PubMed:12009884, FT ECO:0000269|PubMed:7866410" FT /id="VAR_001378" FT VARIANT 143 FT /note="A -> V (in dbSNP:rs7821248)" FT /id="VAR_048679" FT VARIANT 254 FT /note="G -> R (in Guam; dbSNP:rs121909577)" FT /evidence="ECO:0000269|PubMed:6781336" FT /id="VAR_001379" FT CONFLICT 75..76 FT /note="DN -> ND (in Ref. 4; AA sequence and 5; AA FT sequence)" FT /evidence="ECO:0000305" FT TURN 10..12 FT /evidence="ECO:0007829|PDB:7Q0D" FT TURN 14..16 FT /evidence="ECO:0007829|PDB:7Q0D" FT HELIX 17..19 FT /evidence="ECO:0007829|PDB:7Q0D" FT HELIX 22..25 FT /evidence="ECO:0007829|PDB:7Q0D" FT STRAND 26..28 FT /evidence="ECO:0007829|PDB:7Q0D" FT STRAND 32..34 FT /evidence="ECO:0007829|PDB:1J9W" FT HELIX 36..38 FT /evidence="ECO:0007829|PDB:7Q0D" FT STRAND 48..51 FT /evidence="ECO:0007829|PDB:7Q0D" FT HELIX 54..56 FT /evidence="ECO:0007829|PDB:7Q0D" FT STRAND 57..62 FT /evidence="ECO:0007829|PDB:7Q0D" FT STRAND 64..71 FT /evidence="ECO:0007829|PDB:7Q0D" FT STRAND 74..82 FT /evidence="ECO:0007829|PDB:7Q0D" FT STRAND 89..98 FT /evidence="ECO:0007829|PDB:7Q0D" FT STRAND 100..104 FT /evidence="ECO:0007829|PDB:1HCB" FT STRAND 107..110 FT /evidence="ECO:0007829|PDB:7Q0D" FT STRAND 116..124 FT /evidence="ECO:0007829|PDB:7Q0D" FT TURN 126..128 FT /evidence="ECO:0007829|PDB:7Q0D" FT HELIX 132..135 FT /evidence="ECO:0007829|PDB:7Q0D" FT STRAND 141..153 FT /evidence="ECO:0007829|PDB:7Q0D" FT HELIX 156..158 FT /evidence="ECO:0007829|PDB:7Q0D" FT HELIX 159..164 FT /evidence="ECO:0007829|PDB:7Q0D" FT HELIX 165..167 FT /evidence="ECO:0007829|PDB:7Q0D" FT STRAND 174..176 FT /evidence="ECO:0007829|PDB:7Q0D" FT HELIX 182..185 FT /evidence="ECO:0007829|PDB:7Q0D" FT STRAND 192..197 FT /evidence="ECO:0007829|PDB:7Q0D" FT STRAND 208..215 FT /evidence="ECO:0007829|PDB:7Q0D" FT STRAND 217..219 FT /evidence="ECO:0007829|PDB:7Q0D" FT HELIX 221..228 FT /evidence="ECO:0007829|PDB:7Q0D" FT STRAND 230..233 FT /evidence="ECO:0007829|PDB:7Q0D" SQ SEQUENCE 261 AA; 28870 MW; 4959E5FA25E374F8 CRC64; MASPDWGYDD KNGPEQWSKL YPIANGNNQS PVDIKTSETK HDTSLKPISV SYNPATAKEI INVGHSFHVN FEDNDNRSVL KGGPFSDSYR LFQFHFHWGS TNEHGSEHTV DGVKYSAELH VAHWNSAKYS SLAEAASKAD GLAVIGVLMK VGEANPKLQK VLDALQAIKT KGKRAPFTNF DPSTLLPSSL DFWTYPGSLT HPPLYESVTW IICKESISVS SEQLAQFRSL LSNVEGDNAV PMQHNNRPTQ PLKGRTVRAS F //