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Q16790

- CAH9_HUMAN

UniProt

Q16790 - CAH9_HUMAN

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Protein
Carbonic anhydrase 9
Gene
CA9, G250, MN
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Reversible hydration of carbon dioxide. Participates in pH regulation. May be involved in the control of cell proliferation and transformation. Appears to be a novel specific biomarker for a cervical neoplasia.1 Publication

Catalytic activityi

H2CO3 = CO2 + H2O.

Cofactori

Zinc.

Enzyme regulationi

Inhibited by coumarins, saccharin, sulfonamide derivatives such as acetazolamide (AZA) and Foscarnet (phosphonoformate trisodium salt).4 Publications

pH dependencei

Optimum pH is 6.5.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei200 – 2001Proton acceptor By similarity
Metal bindingi226 – 2261Zinc; catalytic
Metal bindingi228 – 2281Zinc; catalytic
Metal bindingi251 – 2511Zinc; catalytic

GO - Molecular functioni

  1. carbonate dehydratase activity Source: ProtInc
  2. zinc ion binding Source: InterPro
Complete GO annotation...

GO - Biological processi

  1. bicarbonate transport Source: Reactome
  2. cellular response to hypoxia Source: Reactome
  3. morphogenesis of an epithelium Source: Ensembl
  4. one-carbon metabolic process Source: InterPro
  5. regulation of transcription from RNA polymerase II promoter in response to hypoxia Source: Reactome
  6. response to drug Source: Ensembl
  7. response to testosterone Source: Ensembl
  8. secretion Source: Ensembl
  9. small molecule metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BRENDAi4.2.1.1. 2681.
ReactomeiREACT_121092. Regulation of gene expression by Hypoxia-inducible Factor.
REACT_121123. Reversible hydration of carbon dioxide.

Names & Taxonomyi

Protein namesi
Recommended name:
Carbonic anhydrase 9 (EC:4.2.1.1)
Alternative name(s):
Carbonate dehydratase IX
Carbonic anhydrase IX
Short name:
CA-IX
Short name:
CAIX
Membrane antigen MN
P54/58N
Renal cell carcinoma-associated antigen G250
Short name:
RCC-associated antigen G250
pMW1
Gene namesi
Name:CA9
Synonyms:G250, MN
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 9

Organism-specific databases

HGNCiHGNC:1383. CA9.

Subcellular locationi

Nucleus. Nucleusnucleolus. Cell membrane; Single-pass type I membrane protein. Cell projectionmicrovillus membrane; Single-pass type I membrane protein
Note: Found on the surface microvilli and in the nucleus, particularly in nucleolus.1 Publication

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini38 – 414377Extracellular
Add
BLAST
Transmembranei415 – 43521Helical; Reviewed prediction
Add
BLAST
Topological domaini436 – 45924Cytoplasmic
Add
BLAST

GO - Cellular componenti

  1. basolateral plasma membrane Source: Ensembl
  2. integral component of membrane Source: ProtInc
  3. microvillus membrane Source: UniProtKB-SubCell
  4. nucleolus Source: UniProtKB-SubCell
  5. plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell projection, Membrane, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA25998.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 37371 Publication
Add
BLAST
Chaini38 – 459422Carbonic anhydrase 9
PRO_0000004243Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi115 – 1151O-linked (GlcNAc...)1 Publication
Disulfide bondi156 ↔ 3362 Publications
Disulfide bondi174 – 174Interchain Inferred
Glycosylationi346 – 3461N-linked (GlcNAc...)2 Publications
Modified residuei449 – 4491Phosphotyrosine1 Publication

Post-translational modificationi

Asn-346 bears high-mannose type glycan structures.

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiQ16790.
PaxDbiQ16790.
PRIDEiQ16790.

PTM databases

PhosphoSiteiQ16790.

Expressioni

Tissue specificityi

Expressed primarily in carcinoma cells lines. Expression is restricted to very few normal tissues and the most abundant expression is found in the epithelial cells of gastric mucosa.

Inductioni

By hypoxia.5 Publications

Gene expression databases

BgeeiQ16790.
CleanExiHS_CA9.
GenevestigatoriQ16790.

Organism-specific databases

HPAiCAB005100.
CAB017107.

Interactioni

Subunit structurei

Forms oligomers linked by disulfide bonds.2 Publications

Protein-protein interaction databases

BioGridi107223. 31 interactions.
DIPiDIP-48973N.
STRINGi9606.ENSP00000367608.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni137 – 1393
Beta strandi143 – 1475
Helixi149 – 1524
Helixi154 – 1574
Helixi168 – 1703
Beta strandi171 – 1733
Beta strandi181 – 1844
Beta strandi193 – 1975
Beta strandi202 – 2054
Beta strandi211 – 2155
Beta strandi218 – 22912
Beta strandi238 – 2414
Beta strandi247 – 25610
Helixi262 – 2654
Beta strandi271 – 28111
Helixi287 – 2937
Helixi294 – 2996
Beta strandi305 – 3084
Helixi313 – 3164
Beta strandi324 – 3307
Beta strandi338 – 34710
Beta strandi349 – 3513
Helixi353 – 3619
Beta strandi387 – 3893

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2HKFX-ray2.01P83-91[»]
3IAIX-ray2.20A/B/C/D137-391[»]
ProteinModelPortaliQ16790.
SMRiQ16790. Positions 139-391.

Miscellaneous databases

EvolutionaryTraceiQ16790.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni38 – 11275Proteoglycan-like (PG)
Add
BLAST
Regioni113 – 414302Catalytic
Add
BLAST
Regioni332 – 3332Substrate binding By similarity

Sequence similaritiesi

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG3338.
HOGENOMiHOG000112637.
HOVERGENiHBG002837.
InParanoidiQ16790.
KOiK01672.
OMAiSRYFRYE.
OrthoDBiEOG7WMCK7.
PhylomeDBiQ16790.
TreeFamiTF316425.

Family and domain databases

Gene3Di3.10.200.10. 1 hit.
InterProiIPR018429. CA9.
IPR001148. Carbonic_anhydrase_a.
IPR023561. Carbonic_anhydrase_a-class.
IPR018338. Carbonic_anhydrase_a-class_CS.
[Graphical view]
PANTHERiPTHR18952. PTHR18952. 1 hit.
PTHR18952:SF18. PTHR18952:SF18. 1 hit.
PfamiPF00194. Carb_anhydrase. 1 hit.
[Graphical view]
SMARTiSM01057. Carb_anhydrase. 1 hit.
[Graphical view]
SUPFAMiSSF51069. SSF51069. 1 hit.
PROSITEiPS00162. ALPHA_CA_1. 1 hit.
PS51144. ALPHA_CA_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q16790-1 [UniParc]FASTAAdd to Basket

« Hide

MAPLCPSPWL PLLIPAPAPG LTVQLLLSLL LLVPVHPQRL PRMQEDSPLG    50
GGSSGEDDPL GEEDLPSEED SPREEDPPGE EDLPGEEDLP GEEDLPEVKP 100
KSEEEGSLKL EDLPTVEAPG DPQEPQNNAH RDKEGDDQSH WRYGGDPPWP 150
RVSPACAGRF QSPVDIRPQL AAFCPALRPL ELLGFQLPPL PELRLRNNGH 200
SVQLTLPPGL EMALGPGREY RALQLHLHWG AAGRPGSEHT VEGHRFPAEI 250
HVVHLSTAFA RVDEALGRPG GLAVLAAFLE EGPEENSAYE QLLSRLEEIA 300
EEGSETQVPG LDISALLPSD FSRYFQYEGS LTTPPCAQGV IWTVFNQTVM 350
LSAKQLHTLS DTLWGPGDSR LQLNFRATQP LNGRVIEASF PAGVDSSPRA 400
AEPVQLNSCL AAGDILALVF GLLFAVTSVA FLVQMRRQHR RGTKGGVSYR 450
PAEVAETGA 459
Length:459
Mass (Da):49,698
Last modified:December 6, 2005 - v2
Checksum:iBA67195483F0F5CE
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti33 – 331V → M.2 Publications
Corresponds to variant rs2071676 [ dbSNP | Ensembl ].
VAR_010787
Natural varianti326 – 3261Q → R.
Corresponds to variant rs3829078 [ dbSNP | Ensembl ].
VAR_020049

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X66839 mRNA. Translation: CAA47315.1.
AJ010588 mRNA. Translation: CAB82444.1.
AL133410, AL357874 Genomic DNA. Translation: CAI10985.1.
AL357874, AL133410 Genomic DNA. Translation: CAI13455.1.
CH471071 Genomic DNA. Translation: EAW58359.1.
BC014950 mRNA. Translation: AAH14950.1.
CCDSiCCDS6585.1.
PIRiI38013.
RefSeqiNP_001207.2. NM_001216.2.
UniGeneiHs.63287.

Genome annotation databases

EnsembliENST00000378357; ENSP00000367608; ENSG00000107159.
GeneIDi768.
KEGGihsa:768.
UCSCiuc003zxo.4. human.

Polymorphism databases

DMDMi83300925.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X66839 mRNA. Translation: CAA47315.1 .
AJ010588 mRNA. Translation: CAB82444.1 .
AL133410 , AL357874 Genomic DNA. Translation: CAI10985.1 .
AL357874 , AL133410 Genomic DNA. Translation: CAI13455.1 .
CH471071 Genomic DNA. Translation: EAW58359.1 .
BC014950 mRNA. Translation: AAH14950.1 .
CCDSi CCDS6585.1.
PIRi I38013.
RefSeqi NP_001207.2. NM_001216.2.
UniGenei Hs.63287.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2HKF X-ray 2.01 P 83-91 [» ]
3IAI X-ray 2.20 A/B/C/D 137-391 [» ]
ProteinModelPortali Q16790.
SMRi Q16790. Positions 139-391.
ModBasei Search...

Protein-protein interaction databases

BioGridi 107223. 31 interactions.
DIPi DIP-48973N.
STRINGi 9606.ENSP00000367608.

Chemistry

BindingDBi Q16790.
ChEMBLi CHEMBL3594.

PTM databases

PhosphoSitei Q16790.

Polymorphism databases

DMDMi 83300925.

Proteomic databases

MaxQBi Q16790.
PaxDbi Q16790.
PRIDEi Q16790.

Protocols and materials databases

DNASUi 768.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000378357 ; ENSP00000367608 ; ENSG00000107159 .
GeneIDi 768.
KEGGi hsa:768.
UCSCi uc003zxo.4. human.

Organism-specific databases

CTDi 768.
GeneCardsi GC09P035673.
H-InvDB HIX0008019.
HGNCi HGNC:1383. CA9.
HPAi CAB005100.
CAB017107.
MIMi 603179. gene.
neXtProti NX_Q16790.
PharmGKBi PA25998.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG3338.
HOGENOMi HOG000112637.
HOVERGENi HBG002837.
InParanoidi Q16790.
KOi K01672.
OMAi SRYFRYE.
OrthoDBi EOG7WMCK7.
PhylomeDBi Q16790.
TreeFami TF316425.

Enzyme and pathway databases

BRENDAi 4.2.1.1. 2681.
Reactomei REACT_121092. Regulation of gene expression by Hypoxia-inducible Factor.
REACT_121123. Reversible hydration of carbon dioxide.

Miscellaneous databases

EvolutionaryTracei Q16790.
GeneWikii Carbonic_anhydrase_9.
GenomeRNAii 768.
NextBioi 3106.
PROi Q16790.
SOURCEi Search...

Gene expression databases

Bgeei Q16790.
CleanExi HS_CA9.
Genevestigatori Q16790.

Family and domain databases

Gene3Di 3.10.200.10. 1 hit.
InterProi IPR018429. CA9.
IPR001148. Carbonic_anhydrase_a.
IPR023561. Carbonic_anhydrase_a-class.
IPR018338. Carbonic_anhydrase_a-class_CS.
[Graphical view ]
PANTHERi PTHR18952. PTHR18952. 1 hit.
PTHR18952:SF18. PTHR18952:SF18. 1 hit.
Pfami PF00194. Carb_anhydrase. 1 hit.
[Graphical view ]
SMARTi SM01057. Carb_anhydrase. 1 hit.
[Graphical view ]
SUPFAMi SSF51069. SSF51069. 1 hit.
PROSITEi PS00162. ALPHA_CA_1. 1 hit.
PS51144. ALPHA_CA_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and characterization of MN, a human tumor-associated protein with a domain homologous to carbonic anhydrase and a putative helix-loop-helix DNA binding segment."
    Pastorek J., Pastorekova S., Callebaut I., Mornon J.-P., Zelnik V., Opavsky R., Zat'Ovicova M., Liao S., Portetelle D., Stanbridge E.J., Zavada J., Burny A., Kettmann R.
    Oncogene 9:2877-2888(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION, VARIANT MET-33.
    Tissue: Carcinoma.
  2. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Renal cell carcinoma.
  3. "DNA sequence and analysis of human chromosome 9."
    Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
    , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
    Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT MET-33.
    Tissue: Colon.
  6. "Signal peptide prediction based on analysis of experimentally verified cleavage sites."
    Zhang Z., Henzel W.J.
    Protein Sci. 13:2819-2824(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 38-52.
  7. "A novel quasi-viral agent, MaTu, is a two-component system."
    Pastorekova S., Zavadova Z., Kostal M., Babusikova O., Zavada J.
    Virology 187:620-626(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  8. "Expression of MaTu-MN protein in human tumor cultures and in clinical specimens."
    Zavada J., Zavadova Z., Pastorekova S., Ciampor F., Pastorek J., Zelnik V.
    Int. J. Cancer 54:268-274(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  9. "The role of carbonic anhydrase IX overexpression in kidney cancer."
    Dorai T., Sawczuk I.S., Pastorek J., Wiernik P.H., Dutcher J.P.
    Eur. J. Cancer 41:2935-2947(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT TYR-449.
  10. "Saccharin inhibits carbonic anhydrases: possible explanation for its unpleasant metallic aftertaste."
    Koehler K., Hillebrecht A., Schulze Wischeler J., Innocenti A., Heine A., Supuran C.T., Klebe G.
    Angew. Chem. Int. Ed. Engl. 46:7697-7699(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION.
  11. "Phosph(on)ate as a zinc-binding group in metalloenzyme inhibitors: X-ray crystal structure of the antiviral drug foscarnet complexed to human carbonic anhydrase I."
    Temperini C., Innocenti A., Guerri A., Scozzafava A., Rusconi S., Supuran C.T.
    Bioorg. Med. Chem. Lett. 17:2210-2215(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION.
  12. Cited for: FUNCTION, SUBUNIT, INDUCTION, GLYCOSYLATION AT THR-115 AND ASN-346, DISULFIDE BONDS.
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. "A thiabendazole sulfonamide shows potent inhibitory activity against mammalian and nematode alpha-carbonic anhydrases."
    Crocetti L., Maresca A., Temperini C., Hall R.A., Scozzafava A., Muehlschlegel F.A., Supuran C.T.
    Bioorg. Med. Chem. Lett. 19:1371-1375(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION.
  15. "Non-zinc mediated inhibition of carbonic anhydrases: coumarins are a new class of suicide inhibitors."
    Maresca A., Temperini C., Vu H., Pham N.B., Poulsen S.-A., Scozzafava A., Quinn R.J., Supuran C.T.
    J. Am. Chem. Soc. 131:3057-3062(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION.
  16. "Stabilization of antibody structure upon association to a human carbonic anhydrase IX epitope studied by X-ray crystallography, microcalorimetry, and molecular dynamics simulations."
    Kral V., Mader P., Collard R., Fabry M., Horejsi M., Rezacova P., Kozisek M., Zavada J., Sedlacek J., Rulisek L., Brynda J.
    Proteins 71:1275-1287(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.01 ANGSTROMS) OF 83-91 IN COMPLEX WITH SPECIFIC ANTIBODIES.
  17. Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 137-391 IN COMPLEX WITH ZINC ION AND THE INHIBITOR ACETAZOLAMIDE, GLYCOSYLATION AT ASN-346, DISULFIDE BOND, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES.

Entry informationi

Entry nameiCAH9_HUMAN
AccessioniPrimary (citable) accession number: Q16790
Secondary accession number(s): Q5T4R1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: December 6, 2005
Last modified: September 3, 2014
This is version 141 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 9
    Human chromosome 9: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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