CAH9_HUMAN
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 03-AUG-2022, entry version 200.
DE RecName: Full=Carbonic anhydrase 9;
DE EC=4.2.1.1 {ECO:0000269|PubMed:17314045, ECO:0000269|PubMed:17705204, ECO:0000269|PubMed:18703501, ECO:0000269|PubMed:19186056, ECO:0000269|PubMed:19206230, ECO:0000269|PubMed:19805286};
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, FUNCTION, AND CATALYTIC ACTIVITY.
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, FUNCTION, AND CATALYTIC 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 [12]
RP FUNCTION, SUBUNIT, INDUCTION, GLYCOSYLATION AT THR-115 AND ASN-346,
RP DISULFIDE BONDS, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES,
RP COFACTOR, AND ACTIVITY REGULATION.
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, 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 [15]
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 [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, BIOPHYSICOCHEMICAL PROPERTIES, FUNCTION, CATALYTIC ACTIVITY,
RP COFACTOR, ZINC-BINDING SITES, AND ACTIVITY REGULATION.
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: Catalyzes the interconversion between carbon dioxide and
CC water and the dissociated ions of carbonic acid (i.e. bicarbonate and
CC hydrogen ions). {ECO:0000269|PubMed:17314045,
CC ECO:0000269|PubMed:17705204, ECO:0000269|PubMed:18703501,
CC ECO:0000269|PubMed:19186056, ECO:0000269|PubMed:19206230,
CC ECO:0000269|PubMed:19805286}.
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:17314045,
CC ECO:0000269|PubMed:17705204, ECO:0000269|PubMed:18703501,
CC ECO:0000269|PubMed:19186056, ECO:0000269|PubMed:19206230,
CC ECO:0000269|PubMed:19805286};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10749;
CC Evidence={ECO:0000305|PubMed:18703501};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:10750;
CC Evidence={ECO:0000305|PubMed:18703501};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:18703501, 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:18703501,
CC ECO:0000269|PubMed:19186056, ECO:0000269|PubMed:19206230,
CC ECO:0000269|PubMed:19805286}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=7.5 mM for CO(2) {ECO:0000269|PubMed:18703501};
CC KM=7.3 mM for CO(2) (in the presence of ZnCl2)
CC {ECO:0000269|PubMed:18703501};
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:18703501, 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 {ECO:0000269|PubMed:19805286}.
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 PDB; 7POM; X-ray; 1.98 A; A/B/C/D=137-391.
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 PDBsum; 7POM; -.
DR AlphaFoldDB; Q16790; -.
DR SASBDB; Q16790; -.
DR SMR; Q16790; -.
DR BioGRID; 107223; 215.
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 TCDB; 8.A.164.1.1; the integral membrane carbonic anhydrase xi (ca9) family.
DR GlyGen; Q16790; 3 sites, 3 O-linked glycans (2 sites).
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; 1240 antibodies from 45 providers.
DR DNASU; 768; -.
DR Ensembl; ENST00000378357.9; ENSP00000367608.4; ENSG00000107159.14.
DR GeneID; 768; -.
DR KEGG; hsa:768; -.
DR MANE-Select; ENST00000378357.9; ENSP00000367608.4; NM_001216.3; NP_001207.2.
DR UCSC; uc003zxo.5; human.
DR CTD; 768; -.
DR DisGeNET; 768; -.
DR GeneCards; CA9; -.
DR HGNC; HGNC:1383; CA9.
DR HPA; ENSG00000107159; Tissue enriched (stomach).
DR MIM; 603179; gene.
DR neXtProt; NX_Q16790; -.
DR OpenTargets; ENSG00000107159; -.
DR PharmGKB; PA25998; -.
DR VEuPathDB; HostDB:ENSG00000107159; -.
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 SignaLink; Q16790; -.
DR SIGNOR; Q16790; -.
DR BioGRID-ORCS; 768; 22 hits in 1082 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 127 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; IDA:UniProtKB.
DR GO; GO:0016836; F:hydro-lyase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
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:0001666; P:response to hypoxia; IEA:Ensembl.
DR GO; GO:0033574; P:response to testosterone; IEA:Ensembl.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
DR GO; GO:0046903; P:secretion; IEA:Ensembl.
DR DisProt; DP02538; -.
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 42..154
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 138..391
FT /note="Catalytic"
FT /evidence="ECO:0000269|PubMed:19805286"
FT COMPBIAS 57..93
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 94..111
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 126..141
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 200
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P00918"
FT BINDING 226
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:19805286"
FT BINDING 228
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:19805286"
FT BINDING 251
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:19805286"
FT BINDING 332..333
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00918"
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:0007829|PDB:3IAI"
FT STRAND 143..147
FT /evidence="ECO:0007829|PDB:6RQQ"
FT TURN 150..152
FT /evidence="ECO:0007829|PDB:6RQQ"
FT HELIX 154..157
FT /evidence="ECO:0007829|PDB:6RQQ"
FT STRAND 164..166
FT /evidence="ECO:0007829|PDB:6G98"
FT HELIX 168..170
FT /evidence="ECO:0007829|PDB:6RQQ"
FT STRAND 171..173
FT /evidence="ECO:0007829|PDB:6RQQ"
FT STRAND 181..184
FT /evidence="ECO:0007829|PDB:6RQQ"
FT STRAND 193..197
FT /evidence="ECO:0007829|PDB:6RQQ"
FT STRAND 202..205
FT /evidence="ECO:0007829|PDB:6RQQ"
FT STRAND 211..215
FT /evidence="ECO:0007829|PDB:6RQQ"
FT STRAND 218..229
FT /evidence="ECO:0007829|PDB:6RQQ"
FT STRAND 238..241
FT /evidence="ECO:0007829|PDB:6RQQ"
FT STRAND 247..256
FT /evidence="ECO:0007829|PDB:6RQQ"
FT HELIX 262..265
FT /evidence="ECO:0007829|PDB:6RQQ"
FT STRAND 271..281
FT /evidence="ECO:0007829|PDB:6RQQ"
FT HELIX 287..293
FT /evidence="ECO:0007829|PDB:6RQQ"
FT TURN 294..296
FT /evidence="ECO:0007829|PDB:5FL4"
FT HELIX 297..299
FT /evidence="ECO:0007829|PDB:6RQQ"
FT STRAND 305..308
FT /evidence="ECO:0007829|PDB:6RQQ"
FT HELIX 313..316
FT /evidence="ECO:0007829|PDB:6RQQ"
FT STRAND 324..330
FT /evidence="ECO:0007829|PDB:6RQQ"
FT STRAND 338..347
FT /evidence="ECO:0007829|PDB:6RQQ"
FT STRAND 349..351
FT /evidence="ECO:0007829|PDB:6RQQ"
FT HELIX 353..361
FT /evidence="ECO:0007829|PDB:6RQQ"
FT HELIX 366..368
FT /evidence="ECO:0007829|PDB:6Y74"
FT STRAND 387..390
FT /evidence="ECO:0007829|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
