Carbonic anhydrase 13

Human protein
CA13
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

3CZV, 3D0N, 3DA2, 4HU1, 4KNM, 4KNN, 4QIZ, 4QJP, 4QJX, 4QSJ

Identifiers
AliasesCA13, CAXIII, carbonic anhydrase 13
External IDsOMIM: 611436 MGI: 1931322 HomoloGene: 75207 GeneCards: CA13
Gene location (Human)
Chromosome 8 (human)
Chr.Chromosome 8 (human)[1]
Chromosome 8 (human)
Genomic location for CA13
Genomic location for CA13
Band8q21.2Start85,220,587 bp[1]
End85,284,073 bp[1]
Gene location (Mouse)
Chromosome 3 (mouse)
Chr.Chromosome 3 (mouse)[2]
Chromosome 3 (mouse)
Genomic location for CA13
Genomic location for CA13
Band3|3 A1Start14,706,787 bp[2]
End14,728,062 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • jejunal mucosa

  • palpebral conjunctiva

  • pancreatic epithelial cell

  • amniotic fluid

  • endothelial cell

  • duodenum

  • oral cavity

  • pancreatic ductal cell

  • parietal pleura

  • germinal epithelium
Top expressed in
  • meninges

  • esophagus

  • membranous bone

  • human mandible

  • lip

  • jejunum

  • gastric mucosa

  • epithelium of stomach

  • stria vascularis

  • duodenum
More reference expression data
BioGPS
n/a
Gene ontology
Molecular function
  • zinc ion binding
  • lyase activity
  • metal ion binding
  • carbonate dehydratase activity
  • carbonic anhydrase
Cellular component
  • myelin sheath
  • cytosol
  • intracellular membrane-bounded organelle
Biological process
  • bicarbonate transport
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

377677

71934

Ensembl

ENSG00000185015

ENSMUSG00000027555

UniProt

Q8N1Q1

Q9D6N1

RefSeq (mRNA)

NM_198584

NM_024495

RefSeq (protein)

NP_940986

NP_078771

Location (UCSC)Chr 8: 85.22 – 85.28 MbChr 3: 14.71 – 14.73 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Carbonic anhydrase 13 is a protein that in humans is encoded by the CA13 gene.[5]

Function

Carbonic anhydrases (CAs) are a family of zinc metalloenzymes that catalyze the interconversion between carbon dioxide and water and the dissociated ions of carbonic acid (i.e. bicarbonate and hydrogen ions).[6][7]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000185015 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000027555 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ "Entrez Gene: Carbonic anhydrase 13". Retrieved 2019-12-31.
  6. ^ Badger MR, Price GD (1994). "The role of carbonic anhydrase in photosynthesis". Annu. Rev. Plant Physiol. Plant Mol. Biol. 45: 369–392. doi:10.1146/annurev.pp.45.060194.002101.
  7. ^ Lindskog S (1997). "Structure and mechanism of carbonic anhydrase". Pharmacology & Therapeutics. 74 (1): 1–20. doi:10.1016/S0163-7258(96)00198-2. PMID 9336012.

Further reading

  • Lehtonen J, Shen B, Vihinen M, Casini A, Scozzafava A, Supuran CT, et al. (January 2004). "Characterization of CA XIII, a novel member of the carbonic anhydrase isozyme family". The Journal of Biological Chemistry. 279 (4): 2719–27. doi:10.1074/jbc.M308984200. PMID 14600151.
  • Kummola L, Hämäläinen JM, Kivelä J, Kivelä AJ, Saarnio J, Karttunen T, Parkkila S (April 2005). "Expression of a novel carbonic anhydrase, CA XIII, in normal and neoplastic colorectal mucosa". BMC Cancer. 5: 41. doi:10.1186/1471-2407-5-41. PMC 1097719. PMID 15836783.
  • Hilvo M, Innocenti A, Monti SM, De Simone G, Supuran CT, Parkkila S (2008). "Recent advances in research on the most novel carbonic anhydrases, CA XIII and XV". Current Pharmaceutical Design. 14 (7): 672–8. doi:10.2174/138161208783877811. PMID 18336313.

External links

  • Overview of all the structural information available in the PDB for UniProt: Q8N1Q1 (Human Carbonic anhydrase 13) at the PDBe-KB.
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This article incorporates text from the United States National Library of Medicine, which is in the public domain.