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Showing Protein Carbonic anhydrase 9 (HMDBP03173)

IdentificationBiological propertiesGene propertiesProtein propertiesExternal linksReferencesXMLShow 7 metabolites
Identification
HMDB Protein ID HMDBP03173
Secondary Accession Numbers
  • 8732
  • HMDBP04949
Name Carbonic anhydrase 9
Synonyms
  1. CA-IX
  2. CAIX
  3. Carbonate dehydratase IX
  4. Carbonic anhydrase IX
  5. Membrane antigen MN
  6. P54/58N
  7. RCC-associated antigen G250
  8. Renal cell carcinoma-associated antigen G250
  9. pMW1
Gene Name CA9
Protein Type Unknown
Biological Properties
General Function Involved in carbonate dehydratase activity
Specific Function 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.
Pathways Not Available
Reactions
Hydrogen carbonate → CO(2) + Water details
Hydrogen carbonate → Carbon dioxide + Water details
GO Classification
Biological Process
small molecule metabolic process
bicarbonate transport
morphogenesis of an epithelium
secretion
regulation of transcription from RNA polymerase II promoter in response to hypoxia
one-carbon metabolic process
Cellular Component
microvillus membrane
nucleolus
plasma membrane
integral to membrane
Function
ion binding
cation binding
metal ion binding
binding
catalytic activity
carbonate dehydratase activity
transition metal ion binding
zinc ion binding
lyase activity
carbon-oxygen lyase activity
hydro-lyase activity
Molecular Function
metal ion binding
zinc ion binding
carbonate dehydratase activity
Process
metabolic process
cellular metabolic process
one-carbon metabolic process
Cellular Location
  1. Cell membrane
  2. Nucleus
  3. Nucleus
  4. nucleolus
  5. Single-pass type I membrane protein
  6. Single-pass type I membrane protein
  7. Cell projection
  8. microvillus membrane
Gene Properties
Chromosome Location 9
Locus 9p13.3
SNPs CA9
Gene Sequence 
>1380 bp
ATGGCTCCCCTGTGCCCCAGCCCCTGGCTCCCTCTGTTGATCCCGGCCCCTGCTCCAGGC
CTCACTGTGCAACTGCTGCTGTCACTGCTGCTTCTGATGCCTGTCCATCCCCAGAGGTTG
CCCCGGATGCAGGAGGATTCCCCCTTGGGAGGAGGCTCTTCTGGGGAAGATGACCCACTG
GGCGAGGAGGATCTGCCCAGTGAAGAGGATTCACCCAGAGAGGAGGATCCACCCGGAGAG
GAGGATCTACCTGGAGAGGAGGATCTACCTGGAGAGGAGGATCTACCTGAAGTTAAGCCT
AAATCAGAAGAAGAGGGCTCCCTGAAGTTAGAGGATCTACCTACTGTTGAGGCTCCTGGA
GATCCTCAAGAACCCCAGAATAATGCCCACAGGGACAAAGAAGGGGATGACCAGAGTCAT
TGGCGCTATGGAGGCGACCCGCCCTGGCCCCGGGTGTCCCCAGCCTGCGCGGGCCGCTTC
CAGTCCCCGGTGGATATCCGCCCCCAGCTCGCCGCCTTCTGCCCGGCCCTGCGCCCCCTG
GAACTCCTGGGCTTCCAGCTCCCGCCGCTCCCAGAACTGCGCCTGCGCAACAATGGCCAC
AGTGTGCAACTGACCCTGCCTCCTGGGCTAGAGATGGCTCTGGGTCCCGGGCGGGAGTAC
CGGGCTCTGCAGCTGCATCTGCACTGGGGGGCTGCAGGTCGTCCGGGCTCGGAGCACACT
GTGGAAGGCCACCGTTTCCCTGCCGAGATCCACGTGGTTCACCTCAGCACCGCCTTTGCC
AGAGTTGACGAGGCCTTGGGGCGCCCGGGAGGCCTGGCCGTGTTGGCCGCCTTTCTGGAG
GAGGGCCCGGAAGAAAACAGTGCCTATGAGCAGTTGCTGTCTCGCTTGGAAGAAATCGCT
GAGGAAGGCTCAGAGACTCAGGTCCCAGGACTGGACATATCTGCACTCCTGCCCTCTGAC
TTCAGCCGCTACTTCCAATATGAGGGGTCTCTGACTACACCGCCCTGTGCCCAGGGTGTC
ATCTGGACTGTGTTTAACCAGACAGTGATGCTGAGTGCTAAGCAGCTCCACACCCTCTCT
GACACCCTGTGGGGACCTGGTGACTCTCGGCTACAGCTGAACTTCCGAGCGACGCAGCCT
TTGAATGGGCGAGTGATTGAGGCCTCCTTCCCTGCTGGAGTGGACAGCAGTCCTCGGGCT
GCTGAGCCAGTCCAGCTGAATTCCTGCCTGGCTGCTGGTGACATCCTAGCCCTGGTTTTT
GGCCTCCTTTTTGCTGTCACCAGCGTCGCGTTCCTTGTGCAGATGAGAAGGCAGCACAGA
AGGGGAACCAAAGGGGGTGTGAGCTACCGCCCAGCAGAGGTAGCCGAGACTGGAGCCTAG
Protein Properties
Number of Residues 459
Molecular Weight 49697.36
Theoretical pI 4.715
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence 
>Carbonic anhydrase 9
MAPLCPSPWLPLLIPAPAPGLTVQLLLSLLLLVPVHPQRLPRMQEDSPLGGGSSGEDDPL
GEEDLPSEEDSPREEDPPGEEDLPGEEDLPGEEDLPEVKPKSEEEGSLKLEDLPTVEAPG
DPQEPQNNAHRDKEGDDQSHWRYGGDPPWPRVSPACAGRFQSPVDIRPQLAAFCPALRPL
ELLGFQLPPLPELRLRNNGHSVQLTLPPGLEMALGPGREYRALQLHLHWGAAGRPGSEHT
VEGHRFPAEIHVVHLSTAFARVDEALGRPGGLAVLAAFLEEGPEENSAYEQLLSRLEEIA
EEGSETQVPGLDISALLPSDFSRYFQYEGSLTTPPCAQGVIWTVFNQTVMLSAKQLHTLS
DTLWGPGDSRLQLNFRATQPLNGRVIEASFPAGVDSSPRAAEPVQLNSCLAAGDILALVF
GLLFAVTSVAFLVQMRRQHRRGTKGGVSYRPAEVAETGA
GenBank ID Protein 1000702
UniProtKB/Swiss-Prot ID Q16790
UniProtKB/Swiss-Prot Entry Name CAH9_HUMAN
PDB IDs
GenBank Gene ID X66839
GeneCard ID CA9
GenAtlas ID CA9
HGNC ID HGNC:1383
References
General References
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  5. Maresca A, Temperini C, Vu H, Pham NB, Poulsen SA, Scozzafava A, Quinn RJ, Supuran CT: Non-zinc mediated inhibition of carbonic anhydrases: coumarins are a new class of suicide inhibitors. J Am Chem Soc. 2009 Mar 4;131(8):3057-62. doi: 10.1021/ja809683v. [PubMed:19206230 ]
  6. Temperini C, Innocenti A, Guerri A, Scozzafava A, Rusconi S, Supuran CT: 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. Bioorg Med Chem Lett. 2007 Apr 15;17(8):2210-5. Epub 2007 Feb 8. [PubMed:17314045 ]
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  8. Pastorek J, Pastorekova S, Callebaut I, Mornon JP, Zelnik V, Opavsky R, Zat'ovicova M, Liao S, Portetelle D, Stanbridge EJ, et al.: 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. Oncogene. 1994 Oct;9(10):2877-88. [PubMed:8084592 ]
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  15. Alterio V, Hilvo M, Di Fiore A, Supuran CT, Pan P, Parkkila S, Scaloni A, Pastorek J, Pastorekova S, Pedone C, Scozzafava A, Monti SM, De Simone G: Crystal structure of the catalytic domain of the tumor-associated human carbonic anhydrase IX. Proc Natl Acad Sci U S A. 2009 Sep 22;106(38):16233-8. doi: 10.1073/pnas.0908301106. Epub 2009 Sep 14. [PubMed:19805286 ]