Names & Taxonomy

Uniprot ID:
P00918
Entry Name:
CAH2_HUMAN
Status:
reviewed
Protein Names:
Carbonic anhydrase 2 (EC 4.2.1.1) (Carbonate dehydratase II) (Carbonic anhydrase C) (CAC) (Carbonic anhydrase II) (CA-II)
Gene Names:
CA2
Gene Names Primary:
CA2
Organism:
Homo sapiens (Human)

Structure

Length:
260
Sequence:
MSHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLKGGPLDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVVDVLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLLECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELMVDNWRPAQPLKNRQIKASFK
Proteomes:
UP000005640

Subcellular location

Subcellular Location:
Cytoplasm

Function

Function:
Essential for bone resorption and osteoclast differentiation (By similarity). Reversible hydration of carbon dioxide. Can hydrate cyanamide to urea. Involved in the regulation of fluid secretion into the anterior chamber of the eye. Contributes to intracellular pH regulation in the duodenal upper villous epithelium during proton-coupled peptide absorption. Stimulates the chloride-bicarbonate exchange activity of SLC26A6.
Catalytic Activity:
H(2)CO(3) = CO(2) + H(2)O.
Cofactor:
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Kinetics:
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=10 mM for CO(2)
Enzyme Regulation:
ENZYME REGULATION: Activated by X-ray, histamine, L-adrenaline, L- and D-phenylalanine, L- and D-histidine, L-His-OMe and beta-Ala-His (carnosine). Competitively inhibited by saccharin, thioxolone, coumarins, 667-coumate, celecoxib (Celebrex), valdecoxib (Bextra), SC-125, SC-560, diclofenac, acetate, azide, bromide, sulfonamide derivatives such as acetazolamide (AZA), methazolamide (MZA), ethoxzolamide (EZA), dichlorophenamide (DCP), brinzolamide, dansylamide, thiabendazole-5-sulfonamide, trifluoromethane sulfonamide and N-hydroxysulfamide, fructose-based sugar sulfamate RWJ-37497, and Foscarnet (phosphonoformate trisodium salt). Repressed strongly by hydrogen sulfide(HS) and weakly by nitrate (NO(3)). Esterase activity weakly reduced by cyanamide. N-hydroxyurea interfers with zinc binding and inhibit activity.
Active Site:
ACT_SITE 64 64 Proton acceptor.
Cross Reference Drug Bank:
DB00819 DB00436 DB00562 DB01194 DB00880 DB00606 DB01119 DB01144 DB00869 DB01031 DB00695 DB00999 DB00774 DB00703 DB00232 DB01325 DB00273 DB01021 DB03904 DB00909
Gene Ontology Go:
apical part of cell
axon
basolateral plasma membrane
cytoplasm
cytosol
extracellular exosome
extracellular space
microvillus
myelin sheath
plasma membrane
arylesterase activity
carbonate dehydratase activity
zinc ion binding
angiotensin-activated signaling pathway
bicarbonate transport
carbon dioxide transport
cellular response to fluid shear stress
kidney development
morphogenesis of an epithelium
odontogenesis of dentin-containing tooth
one-carbon metabolic process
positive regulation of bone resorption
positive regulation of cellular pH reduction
positive regulation of dipeptide transmembrane transport
positive regulation of osteoclast differentiation
positive regulation of synaptic transmission, GABAergic
regulation of anion transport
regulation of chloride transport
regulation of intracellular pH
response to estrogen
response to pH
response to zinc ion
secretion
small molecule metabolic process
Gene Ontology Biological Process:
angiotensin-activated signaling pathway
bicarbonate transport
carbon dioxide transport
cellular response to fluid shear stress
kidney development
morphogenesis of an epithelium
odontogenesis of dentin-containing tooth
one-carbon metabolic process
positive regulation of bone resorption
positive regulation of cellular pH reduction
positive regulation of dipeptide transmembrane transport
positive regulation of osteoclast differentiation
positive regulation of synaptic transmission, GABAergic
regulation of anion transport
regulation of chloride transport
regulation of intracellular pH
response to estrogen
response to pH
response to zinc ion
secretion
small molecule metabolic process
Gene Ontology Molecular Function:
arylesterase activity
carbonate dehydratase activity
zinc ion binding
Gene Ontology Cellular Component:
apical part of cell
axon
basolateral plasma membrane
cytoplasm
cytosol
extracellular exosome
extracellular space
microvillus
myelin sheath
plasma membrane
Keywords:
3D-structure
Acetylation
Cell membrane
Complete proteome
Cytoplasm
Direct protein sequencing
Disease mutation
Lyase
Membrane
Metal-binding
Osteopetrosis
Phosphoprotein
Polymorphism
Reference proteome
Zinc

Publication

PubMed ID:
3108857 3121496 14702039 15489334 4207120 823150 3000449 14567693 14736710 15218065 15990874 17314045 18618712 21269460 24275569 4621826 3151019 3151020 1909891 1932029 1910042 1336460 1433293 1474587 8431430 8485129 8399159 8218160 8482389 8262987 8331673 8451242 7901850 15299481 15299482 7803386 8070585 8142888 7696263 7608893 7761440 8639494 8987974 8557623 9265618 9398308 9541386 9865942 10550681 11015219 11076507 11327835 11572683 11802772 12056894 12171926 11831900 12166932 11818565 12499545 14736236 15453828 15667203 15865431 16214338 16134940 16106378 16511248 16820676 16290146 16759856 17000110 16807956 16506782 16787097 16686544 16942027 17125255 17181151 17705204 17319692 17330962 17127057 17251017 17346964 17540563 17588751 17071654 17407288 18266323 18942852 18024029 18162396 18374572 18359629 18640037 18161740 18461940 18768466 18260615 18481843 18723489 19170619 19583303 19186056 19206230 19115843 19731956 19827837 19778001 19520834 6817747 6407977 1928091 1542674 8834238 9143915 15300855