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Database: UniProt
Entry: Q16790
LinkDB: Q16790
Original site: Q16790 
ID   CAH9_HUMAN              Reviewed;         459 AA.
AC   Q16790; Q5T4R1;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 2.
DT   07-APR-2021, entry version 195.
DE   RecName: Full=Carbonic anhydrase 9;
DE            EC=4.2.1.1;
DE   AltName: Full=Carbonate dehydratase IX;
DE   AltName: Full=Carbonic anhydrase IX;
DE            Short=CA-IX;
DE            Short=CAIX;
DE   AltName: Full=Membrane antigen MN;
DE   AltName: Full=P54/58N;
DE   AltName: Full=Renal cell carcinoma-associated antigen G250;
DE            Short=RCC-associated antigen G250;
DE   AltName: Full=pMW1;
DE   Flags: Precursor;
GN   Name=CA9; Synonyms=G250, MN;
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], CHARACTERIZATION, AND VARIANT MET-33.
RC   TISSUE=Carcinoma;
RX   PubMed=8084592;
RA   Pastorek J., Pastorekova S., Callebaut I., Mornon J.-P., Zelnik V.,
RA   Opavsky R., Zat'Ovicova M., Liao S., Portetelle D., Stanbridge E.J.,
RA   Zavada J., Burny A., Kettmann R.;
RT   "Cloning and characterization of MN, a human tumor-associated protein with
RT   a domain homologous to carbonic anhydrase and a putative helix-loop-helix
RT   DNA binding segment.";
RL   Oncogene 9:2877-2888(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Renal cell carcinoma;
RX   PubMed=10709109;
RX   DOI=10.1002/(sici)1097-0215(20000315)85:6<865::aid-ijc21>3.0.co;2-q;
RA   Grabmaier K., Vissers J.L.M., De Weijert M.C.A., Oosterwijk-Wakka J.C.,
RA   Van Bokhoven A., Brakenhoff R.H., Noessner E., Mulders P.A., Merkx G.,
RA   Figdor C.G., Adema G.J., Oosterwijk E.;
RT   "Molecular cloning and immunogenicity of renal cell carcinoma-associated
RT   antigen G250.";
RL   Int. J. Cancer 85:865-870(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15164053; DOI=10.1038/nature02465;
RA   Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA   Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA   Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA   Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA   Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA   Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA   Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA   Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA   Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA   Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA   Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA   Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA   Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA   Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA   Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA   Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA   Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA   Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA   McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA   Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA   Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA   Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA   Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA   West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA   Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA   Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA   Dunham I.;
RT   "DNA sequence and analysis of human chromosome 9.";
RL   Nature 429:369-374(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT MET-33.
RC   TISSUE=Colon;
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   [6]
RP   PROTEIN SEQUENCE OF 38-52.
RX   PubMed=15340161; DOI=10.1110/ps.04682504;
RA   Zhang Z., Henzel W.J.;
RT   "Signal peptide prediction based on analysis of experimentally verified
RT   cleavage sites.";
RL   Protein Sci. 13:2819-2824(2004).
RN   [7]
RP   CHARACTERIZATION.
RX   PubMed=1312272; DOI=10.1016/0042-6822(92)90464-z;
RA   Pastorekova S., Zavadova Z., Kostal M., Babusikova O., Zavada J.;
RT   "A novel quasi-viral agent, MaTu, is a two-component system.";
RL   Virology 187:620-626(1992).
RN   [8]
RP   SUBCELLULAR LOCATION.
RX   PubMed=8486430; DOI=10.1002/ijc.2910540218;
RA   Zavada J., Zavadova Z., Pastorekova S., Ciampor F., Pastorek J., Zelnik V.;
RT   "Expression of MaTu-MN protein in human tumor cultures and in clinical
RT   specimens.";
RL   Int. J. Cancer 54:268-274(1993).
RN   [9]
RP   PHOSPHORYLATION AT TYR-449.
RX   PubMed=16310354; DOI=10.1016/j.ejca.2005.09.011;
RA   Dorai T., Sawczuk I.S., Pastorek J., Wiernik P.H., Dutcher J.P.;
RT   "The role of carbonic anhydrase IX overexpression in kidney cancer.";
RL   Eur. J. Cancer 41:2935-2947(2005).
RN   [10]
RP   ACTIVITY REGULATION.
RX   PubMed=17705204; DOI=10.1002/anie.200701189;
RA   Koehler K., Hillebrecht A., Schulze Wischeler J., Innocenti A., Heine A.,
RA   Supuran C.T., Klebe G.;
RT   "Saccharin inhibits carbonic anhydrases: possible explanation for its
RT   unpleasant metallic aftertaste.";
RL   Angew. Chem. Int. Ed. Engl. 46:7697-7699(2007).
RN   [11]
RP   ACTIVITY REGULATION.
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   [12]
RP   FUNCTION, SUBUNIT, INDUCTION, GLYCOSYLATION AT THR-115 AND ASN-346, AND
RP   DISULFIDE BONDS.
RX   PubMed=18703501; DOI=10.1074/jbc.m800938200;
RA   Hilvo M., Baranauskiene L., Salzano A.M., Scaloni A., Matulis D.,
RA   Innocenti A., Scozzafava A., Monti S.M., Di Fiore A., De Simone G.,
RA   Lindfors M., Janis J., Valjakka J., Pastorekova S., Pastorek J.,
RA   Kulomaa M.S., Nordlund H.R., Supuran C.T., Parkkila S.;
RT   "Biochemical characterization of CA IX, one of the most active carbonic
RT   anhydrase isozymes.";
RL   J. Biol. Chem. 283:27799-27809(2008).
RN   [13]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [14]
RP   ACTIVITY REGULATION.
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   [15]
RP   ACTIVITY REGULATION.
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   [16]
RP   X-RAY CRYSTALLOGRAPHY (2.01 ANGSTROMS) OF 83-91 IN COMPLEX WITH SPECIFIC
RP   ANTIBODIES.
RX   PubMed=18041760; DOI=10.1002/prot.21821;
RA   Kral V., Mader P., Collard R., Fabry M., Horejsi M., Rezacova P.,
RA   Kozisek M., Zavada J., Sedlacek J., Rulisek L., Brynda J.;
RT   "Stabilization of antibody structure upon association to a human carbonic
RT   anhydrase IX epitope studied by X-ray crystallography, microcalorimetry,
RT   and molecular dynamics simulations.";
RL   Proteins 71:1275-1287(2008).
RN   [17]
RP   X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 137-391 IN COMPLEX WITH ZINC ION
RP   AND THE INHIBITOR ACETAZOLAMIDE, GLYCOSYLATION AT ASN-346, DISULFIDE BOND,
RP   SUBUNIT, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=19805286; DOI=10.1073/pnas.0908301106;
RA   Alterio V., Hilvo M., Di Fiore A., Supuran C.T., Pan P., Parkkila S.,
RA   Scaloni A., Pastorek J., Pastorekova S., Pedone C., Scozzafava A.,
RA   Monti S.M., De Simone G.;
RT   "Crystal structure of the catalytic domain of the tumor-associated human
RT   carbonic anhydrase IX.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:16233-16238(2009).
CC   -!- FUNCTION: Reversible hydration of carbon dioxide. Participates in pH
CC       regulation. May be involved in the control of cell proliferation and
CC       transformation. Appears to be a novel specific biomarker for a cervical
CC       neoplasia. {ECO:0000269|PubMed:18703501}.
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;
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000269|PubMed:19805286};
CC   -!- ACTIVITY REGULATION: Inhibited by coumarins, saccharin, sulfonamide
CC       derivatives such as acetazolamide (AZA) and Foscarnet (phosphonoformate
CC       trisodium salt). {ECO:0000269|PubMed:17314045,
CC       ECO:0000269|PubMed:17705204, ECO:0000269|PubMed:19186056,
CC       ECO:0000269|PubMed:19206230}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 6.5. {ECO:0000269|PubMed:19805286};
CC   -!- SUBUNIT: Forms oligomers linked by disulfide bonds.
CC       {ECO:0000269|PubMed:18041760, ECO:0000269|PubMed:18703501,
CC       ECO:0000269|PubMed:19805286}.
CC   -!- INTERACTION:
CC       Q16790; P21291: CSRP1; NbExp=3; IntAct=EBI-12259996, EBI-3959636;
CC       Q16790; O76003: GLRX3; NbExp=9; IntAct=EBI-12259996, EBI-374781;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:8486430}. Nucleus,
CC       nucleolus {ECO:0000269|PubMed:8486430}. Cell membrane
CC       {ECO:0000269|PubMed:8486430}; Single-pass type I membrane protein
CC       {ECO:0000269|PubMed:8486430}. Cell projection, microvillus membrane
CC       {ECO:0000269|PubMed:8486430}; Single-pass type I membrane protein
CC       {ECO:0000269|PubMed:8486430}. Note=Found on the surface microvilli and
CC       in the nucleus, particularly in nucleolus.
CC   -!- TISSUE SPECIFICITY: Expressed primarily in carcinoma cells lines.
CC       Expression is restricted to very few normal tissues and the most
CC       abundant expression is found in the epithelial cells of gastric mucosa.
CC   -!- INDUCTION: By hypoxia. {ECO:0000269|PubMed:18703501}.
CC   -!- PTM: Asn-346 bears high-mannose type glycan structures.
CC   -!- SIMILARITY: Belongs to the alpha-carbonic anhydrase family.
CC       {ECO:0000305}.
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DR   EMBL; X66839; CAA47315.1; -; mRNA.
DR   EMBL; AJ010588; CAB82444.1; -; mRNA.
DR   EMBL; AL133410; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL357874; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471071; EAW58359.1; -; Genomic_DNA.
DR   EMBL; BC014950; AAH14950.1; -; mRNA.
DR   CCDS; CCDS6585.1; -.
DR   PIR; I38013; I38013.
DR   RefSeq; NP_001207.2; NM_001216.2.
DR   PDB; 2HKF; X-ray; 2.01 A; P=83-91.
DR   PDB; 3IAI; X-ray; 2.20 A; A/B/C/D=137-391.
DR   PDB; 5DVX; X-ray; 1.60 A; A/B=140-399.
DR   PDB; 5FL4; X-ray; 1.82 A; A/B/C/D=137-391.
DR   PDB; 5FL5; X-ray; 2.05 A; A/B/C/D=137-391.
DR   PDB; 5FL6; X-ray; 1.95 A; A/B/C/D=137-391.
DR   PDB; 6FE0; X-ray; 1.91 A; A/B/C/D=137-391.
DR   PDB; 6FE1; X-ray; 1.95 A; A/B/C/D=137-391.
DR   PDB; 6FE2; X-ray; 1.87 A; A/B/C/D=137-391.
DR   PDB; 6G98; X-ray; 2.47 A; A/B/C/D=135-391.
DR   PDB; 6G9U; X-ray; 1.75 A; A/B/C/D=137-391.
DR   PDB; 6QN2; X-ray; 1.95 A; A/B/C/D=137-391.
DR   PDB; 6QN5; X-ray; 1.96 A; A/B/C/D=137-391.
DR   PDB; 6QN6; X-ray; 2.25 A; A/B/C/D=137-391.
DR   PDB; 6QUT; X-ray; 1.96 A; A/B/C/D=141-391.
DR   PDB; 6RQN; X-ray; 1.78 A; A=140-395.
DR   PDB; 6RQQ; X-ray; 1.28 A; A/C=140-395.
DR   PDB; 6RQU; X-ray; 1.39 A; A=140-395.
DR   PDB; 6RQW; X-ray; 1.49 A; A=140-395.
DR   PDB; 6TL5; X-ray; 2.21 A; A/B/C/D=135-391.
DR   PDB; 6TL6; X-ray; 2.15 A; A/B/C/D=135-391.
DR   PDB; 6Y74; X-ray; 1.53 A; A/B=137-394.
DR   PDBsum; 2HKF; -.
DR   PDBsum; 3IAI; -.
DR   PDBsum; 5DVX; -.
DR   PDBsum; 5FL4; -.
DR   PDBsum; 5FL5; -.
DR   PDBsum; 5FL6; -.
DR   PDBsum; 6FE0; -.
DR   PDBsum; 6FE1; -.
DR   PDBsum; 6FE2; -.
DR   PDBsum; 6G98; -.
DR   PDBsum; 6G9U; -.
DR   PDBsum; 6QN2; -.
DR   PDBsum; 6QN5; -.
DR   PDBsum; 6QN6; -.
DR   PDBsum; 6QUT; -.
DR   PDBsum; 6RQN; -.
DR   PDBsum; 6RQQ; -.
DR   PDBsum; 6RQU; -.
DR   PDBsum; 6RQW; -.
DR   PDBsum; 6TL5; -.
DR   PDBsum; 6TL6; -.
DR   PDBsum; 6Y74; -.
DR   SASBDB; Q16790; -.
DR   SMR; Q16790; -.
DR   BioGRID; 107223; 214.
DR   DIP; DIP-48973N; -.
DR   IntAct; Q16790; 2.
DR   STRING; 9606.ENSP00000367608; -.
DR   BindingDB; Q16790; -.
DR   ChEMBL; CHEMBL3594; -.
DR   DrugBank; DB00562; Benzthiazide.
DR   DrugBank; DB00606; Cyclothiazide.
DR   DrugBank; DB08846; Ellagic acid.
DR   DrugBank; DB05304; Girentuximab.
DR   DrugBank; DB00774; Hydroflumethiazide.
DR   DrugBank; DB09460; Sodium carbonate.
DR   DrugBank; DB00909; Zonisamide.
DR   DrugCentral; Q16790; -.
DR   GuidetoPHARMACOLOGY; 3055; -.
DR   GlyGen; Q16790; 2 sites, 2 O-linked glycans (1 site).
DR   iPTMnet; Q16790; -.
DR   PhosphoSitePlus; Q16790; -.
DR   BioMuta; CA9; -.
DR   DMDM; 83300925; -.
DR   EPD; Q16790; -.
DR   jPOST; Q16790; -.
DR   MassIVE; Q16790; -.
DR   MaxQB; Q16790; -.
DR   PaxDb; Q16790; -.
DR   PeptideAtlas; Q16790; -.
DR   PRIDE; Q16790; -.
DR   ProteomicsDB; 61071; -.
DR   ABCD; Q16790; 17 sequenced antibodies.
DR   Antibodypedia; 3915; 1258 antibodies.
DR   DNASU; 768; -.
DR   Ensembl; ENST00000378357; ENSP00000367608; ENSG00000107159.
DR   GeneID; 768; -.
DR   KEGG; hsa:768; -.
DR   UCSC; uc003zxo.5; human.
DR   CTD; 768; -.
DR   DisGeNET; 768; -.
DR   GeneCards; CA9; -.
DR   HGNC; HGNC:1383; CA9.
DR   HPA; ENSG00000107159; Group enriched (gallbladder, pancreas, stomach).
DR   MIM; 603179; gene.
DR   neXtProt; NX_Q16790; -.
DR   OpenTargets; ENSG00000107159; -.
DR   PharmGKB; PA25998; -.
DR   VEuPathDB; HostDB:ENSG00000107159.12; -.
DR   eggNOG; KOG0382; Eukaryota.
DR   GeneTree; ENSGT00940000161646; -.
DR   HOGENOM; CLU_039326_1_1_1; -.
DR   InParanoid; Q16790; -.
DR   OMA; VQMRRQQ; -.
DR   OrthoDB; 1377476at2759; -.
DR   PhylomeDB; Q16790; -.
DR   TreeFam; TF316425; -.
DR   BRENDA; 4.2.1.1; 2681.
DR   PathwayCommons; Q16790; -.
DR   Reactome; R-HSA-1234158; Regulation of gene expression by Hypoxia-inducible Factor.
DR   Reactome; R-HSA-1475029; Reversible hydration of carbon dioxide.
DR   SIGNOR; Q16790; -.
DR   BioGRID-ORCS; 768; 17 hits in 995 CRISPR screens.
DR   ChiTaRS; CA9; human.
DR   EvolutionaryTrace; Q16790; -.
DR   GeneWiki; Carbonic_anhydrase_9; -.
DR   GenomeRNAi; 768; -.
DR   Pharos; Q16790; Tclin.
DR   PRO; PR:Q16790; -.
DR   Proteomes; UP000005640; Chromosome 9.
DR   RNAct; Q16790; protein.
DR   Bgee; ENSG00000107159; Expressed in body of stomach and 133 other tissues.
DR   ExpressionAtlas; Q16790; baseline and differential.
DR   Genevisible; Q16790; HS.
DR   GO; GO:0016323; C:basolateral plasma membrane; IEA:Ensembl.
DR   GO; GO:0016021; C:integral component of membrane; TAS:ProtInc.
DR   GO; GO:0031528; C:microvillus membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0004089; F:carbonate dehydratase activity; IBA:GO_Central.
DR   GO; GO:0016836; F:hydro-lyase activity; IBA:GO_Central.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0015701; P:bicarbonate transport; TAS:Reactome.
DR   GO; GO:0002009; P:morphogenesis of an epithelium; IEA:Ensembl.
DR   GO; GO:0006730; P:one-carbon metabolic process; IBA:GO_Central.
DR   GO; GO:0061418; P:regulation of transcription from RNA polymerase II promoter in response to hypoxia; TAS:Reactome.
DR   GO; GO:0042493; P:response to drug; IEA:Ensembl.
DR   GO; GO:0033574; P:response to testosterone; IEA:Ensembl.
DR   GO; GO:0046903; P:secretion; IEA:Ensembl.
DR   Gene3D; 3.10.200.10; -; 1.
DR   InterPro; IPR018429; CA9.
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; PTHR18952; 1.
DR   PANTHER; PTHR18952:SF18; PTHR18952:SF18; 1.
DR   Pfam; PF00194; Carb_anhydrase; 1.
DR   SMART; SM01057; Carb_anhydrase; 1.
DR   SUPFAM; SSF51069; SSF51069; 1.
DR   PROSITE; PS00162; ALPHA_CA_1; 1.
DR   PROSITE; PS51144; ALPHA_CA_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cell membrane; Cell projection; Direct protein sequencing;
KW   Disulfide bond; Glycoprotein; Lyase; Membrane; Metal-binding; Nucleus;
KW   Phosphoprotein; Reference proteome; Signal; Transmembrane;
KW   Transmembrane helix; Zinc.
FT   SIGNAL          1..37
FT                   /evidence="ECO:0000269|PubMed:15340161"
FT   CHAIN           38..459
FT                   /note="Carbonic anhydrase 9"
FT                   /id="PRO_0000004243"
FT   TOPO_DOM        38..414
FT                   /note="Extracellular"
FT   TRANSMEM        415..435
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        436..459
FT                   /note="Cytoplasmic"
FT   DOMAIN          139..390
FT                   /note="Alpha-carbonic anhydrase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01134"
FT   REGION          38..112
FT                   /note="Proteoglycan-like (PG)"
FT   REGION          113..414
FT                   /note="Catalytic"
FT   REGION          332..333
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000250|UniProtKB:P00918"
FT   ACT_SITE        200
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P00918"
FT   METAL           226
FT                   /note="Zinc; catalytic"
FT                   /evidence="ECO:0000269|PubMed:19805286"
FT   METAL           228
FT                   /note="Zinc; catalytic"
FT                   /evidence="ECO:0000269|PubMed:19805286"
FT   METAL           251
FT                   /note="Zinc; catalytic"
FT                   /evidence="ECO:0000269|PubMed:19805286"
FT   MOD_RES         449
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000269|PubMed:16310354"
FT   CARBOHYD        115
FT                   /note="O-linked (GlcNAc...) threonine"
FT                   /evidence="ECO:0000269|PubMed:18703501"
FT   CARBOHYD        346
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:18703501,
FT                   ECO:0000269|PubMed:19805286"
FT   DISULFID        156..336
FT                   /evidence="ECO:0000269|PubMed:19805286"
FT   DISULFID        174
FT                   /note="Interchain"
FT                   /evidence="ECO:0000305|PubMed:19805286"
FT   VARIANT         33
FT                   /note="V -> M (in dbSNP:rs2071676)"
FT                   /evidence="ECO:0000269|PubMed:15489334,
FT                   ECO:0000269|PubMed:8084592"
FT                   /id="VAR_010787"
FT   VARIANT         326
FT                   /note="Q -> R (in dbSNP:rs3829078)"
FT                   /id="VAR_020049"
FT   TURN            137..139
FT                   /evidence="ECO:0007744|PDB:3IAI"
FT   STRAND          143..147
FT                   /evidence="ECO:0007744|PDB:6RQQ"
FT   TURN            150..152
FT                   /evidence="ECO:0007744|PDB:6RQQ"
FT   HELIX           154..157
FT                   /evidence="ECO:0007744|PDB:6RQQ"
FT   STRAND          164..166
FT                   /evidence="ECO:0007744|PDB:6G98"
FT   HELIX           168..170
FT                   /evidence="ECO:0007744|PDB:6RQQ"
FT   STRAND          171..173
FT                   /evidence="ECO:0007744|PDB:6RQQ"
FT   STRAND          181..184
FT                   /evidence="ECO:0007744|PDB:6RQQ"
FT   STRAND          193..197
FT                   /evidence="ECO:0007744|PDB:6RQQ"
FT   STRAND          202..205
FT                   /evidence="ECO:0007744|PDB:6RQQ"
FT   STRAND          211..215
FT                   /evidence="ECO:0007744|PDB:6RQQ"
FT   STRAND          218..229
FT                   /evidence="ECO:0007744|PDB:6RQQ"
FT   STRAND          238..241
FT                   /evidence="ECO:0007744|PDB:6RQQ"
FT   STRAND          247..256
FT                   /evidence="ECO:0007744|PDB:6RQQ"
FT   HELIX           262..265
FT                   /evidence="ECO:0007744|PDB:6RQQ"
FT   STRAND          271..281
FT                   /evidence="ECO:0007744|PDB:6RQQ"
FT   HELIX           287..293
FT                   /evidence="ECO:0007744|PDB:6RQQ"
FT   TURN            294..296
FT                   /evidence="ECO:0007744|PDB:5FL4"
FT   HELIX           297..299
FT                   /evidence="ECO:0007744|PDB:6RQQ"
FT   STRAND          305..308
FT                   /evidence="ECO:0007744|PDB:6RQQ"
FT   HELIX           313..316
FT                   /evidence="ECO:0007744|PDB:6RQQ"
FT   STRAND          324..330
FT                   /evidence="ECO:0007744|PDB:6RQQ"
FT   STRAND          338..347
FT                   /evidence="ECO:0007744|PDB:6RQQ"
FT   STRAND          349..351
FT                   /evidence="ECO:0007744|PDB:6RQQ"
FT   HELIX           353..361
FT                   /evidence="ECO:0007744|PDB:6RQQ"
FT   STRAND          366..370
FT                   /evidence="ECO:0007744|PDB:6QN6"
FT   STRAND          387..390
FT                   /evidence="ECO:0007744|PDB:6RQQ"
SQ   SEQUENCE   459 AA;  49698 MW;  BA67195483F0F5CE CRC64;
     MAPLCPSPWL PLLIPAPAPG LTVQLLLSLL LLVPVHPQRL PRMQEDSPLG GGSSGEDDPL
     GEEDLPSEED SPREEDPPGE EDLPGEEDLP GEEDLPEVKP KSEEEGSLKL EDLPTVEAPG
     DPQEPQNNAH RDKEGDDQSH WRYGGDPPWP RVSPACAGRF QSPVDIRPQL AAFCPALRPL
     ELLGFQLPPL PELRLRNNGH SVQLTLPPGL EMALGPGREY RALQLHLHWG AAGRPGSEHT
     VEGHRFPAEI HVVHLSTAFA RVDEALGRPG GLAVLAAFLE EGPEENSAYE QLLSRLEEIA
     EEGSETQVPG LDISALLPSD FSRYFQYEGS LTTPPCAQGV IWTVFNQTVM LSAKQLHTLS
     DTLWGPGDSR LQLNFRATQP LNGRVIEASF PAGVDSSPRA AEPVQLNSCL AAGDILALVF
     GLLFAVTSVA FLVQMRRQHR RGTKGGVSYR PAEVAETGA
//
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