CA2
entrez
760
canonical
uniprot
P00918
canonical
ensembl
ENSG00000104267
resolver
ensp
ENSP00000285379
resolver
enst
ENST00000285379
resolver
genesymbol
CA2
resolver
genesymbol
HEL-76
resolver
hgnc
HGNC:1373
resolver
uniprot
B2R7G8
resolver
uniprot
Q6FI12
resolver
uniprot
Q96ET9
resolver
uniprot
V9HW21
resolver
uniprot_entry
CAH2_HUMAN
resolver
uniprot_entry
V9HW21_HUMAN
resolver
uniprot_sec
B2R7G8
resolver
uniprot_sec
Q6FI12
resolver
uniprot_sec
Q96ET9
resolver
activity_regulation
ACTIVITY 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 interferes with zinc binding and inhibit activity. {ECO:0000269|PubMed:11802772, ECO:0000269|PubMed:1336460, ECO:0000269|PubMed:14736236, ECO:0000269|PubMed:16214338, ECO:0000269|PubMed:16290146, ECO:0000269|PubMed:16686544, ECO:0000269|PubMed:16759856, ECO:0000269|PubMed:16807956, ECO:0000269|PubMed:17127057, ECO:0000269|PubMed:17314045, ECO:0000269|PubMed:17540563, ECO:0000269|PubMed:17588751, ECO:0000269|PubMed:17705204, ECO:0000269|PubMed:18024029, ECO:0000269|PubMed:18162396, ECO:0000269|PubMed:18266323, ECO:0000269|PubMed:18374572, ECO:0000269|PubMed:18481843, ECO:0000269|PubMed:18640037, ECO:0000269|PubMed:1910042, ECO:0000269|PubMed:19170619, ECO:0000269|PubMed:19186056, ECO:0000269|PubMed:19206230, ECO:0000269|PubMed:19520834, ECO:0000269|PubMed:19778001, ECO:0000269|PubMed:9265618}.
uniprot
proteins
amino_acid_sequence
MSHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLKGGPLDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVVDVLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLLECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELMVDNWRPAQPLKNRQIKASFK
uniprot
proteins
disease_involvement
DISEASE: Osteopetrosis, autosomal recessive 3 (OPTB3) [MIM:259730]: A rare genetic disease characterized by abnormally dense bone, due to defective resorption of immature bone. Osteopetrosis occurs in two forms: a severe autosomal recessive form occurring in utero, infancy, or childhood, and a benign autosomal dominant form occurring in adolescence or adulthood. Recessive osteopetrosis commonly manifests in early infancy with macrocephaly, feeding difficulties, evolving blindness and deafness, bone marrow failure, severe anemia, and hepatosplenomegaly. Deafness and blindness are generally thought to represent effects of pressure on nerves. OPTB3 is associated with renal tubular acidosis, cerebral calcification (marble brain disease) and in some cases with intellectual disability. {ECO:0000269|PubMed:15300855, ECO:0000269|PubMed:1542674, ECO:0000269|PubMed:1928091, ECO:0000269|PubMed:8834238, ECO:0000269|PubMed:9143915}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
4.2.1.1
uniprot
proteins
ec_number
4.2.1.69
uniprot
proteins
function
FUNCTION: Catalyzes the reversible hydration of carbon dioxide (PubMed:11327835, PubMed:11802772, PubMed:11831900, PubMed:12056894, PubMed:12171926, PubMed:1336460, PubMed:14736236, PubMed:15300855, PubMed:15453828, PubMed:15667203, PubMed:15865431, PubMed:16106378, PubMed:16214338, PubMed:16290146, PubMed:16686544, PubMed:16759856, PubMed:16807956, PubMed:17127057, PubMed:17251017, PubMed:17314045, PubMed:17330962, PubMed:17346964, PubMed:17540563, PubMed:17588751, PubMed:17705204, PubMed:18024029, PubMed:18162396, PubMed:18266323, PubMed:18374572, PubMed:18481843, PubMed:18640037, PubMed:18942852, PubMed:1909891, PubMed:1910042, PubMed:19170619, PubMed:19186056, PubMed:19206230, PubMed:19520834, PubMed:19778001, PubMed:7761440, PubMed:7901850, PubMed:8218160, PubMed:8262987, PubMed:8399159, PubMed:8451242, PubMed:8485129, PubMed:8639494, PubMed:9265618, PubMed:9398308, PubMed:4994926). Can also hydrate cyanamide to urea (PubMed:10550681, PubMed:11015219). Stimulates the chloride-bicarbonate exchange activity of SLC26A6 (PubMed:15990874). Essential for bone resorption and osteoclast differentiation (PubMed:15300855). 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. {ECO:0000269|PubMed:10550681, ECO:0000269|PubMed:11015219, ECO:0000269|PubMed:11327835, ECO:0000269|PubMed:11802772, ECO:0000269|PubMed:11831900, ECO:0000269|PubMed:12056894, ECO:0000269|PubMed:12171926, ECO:0000269|PubMed:1336460, ECO:0000269|PubMed:14736236, ECO:0000269|PubMed:15300855, ECO:0000269|PubMed:15453828, ECO:0000269|PubMed:15667203, ECO:0000269|PubMed:15865431, ECO:0000269|PubMed:15990874, ECO:0000269|PubMed:16106378, ECO:0000269|PubMed:16214338, ECO:0000269|PubMed:16290146, ECO:0000269|PubMed:16686544, ECO:0000269|PubMed:16759856, ECO:0000269|PubMed:16807956, ECO:0000269|PubMed:17127057, ECO:0000269|PubMed:17251017, ECO:0000269|PubMed:17314045, ECO:0000269|PubMed:17330962, ECO:0000269|PubMed:17346964, ECO:0000269|PubMed:17540563, ECO:0000269|PubMed:17588751, ECO:0000269|PubMed:17705204, ECO:0000269|PubMed:18024029, ECO:0000269|PubMed:18162396, ECO:0000269|PubMed:18266323, ECO:0000269|PubMed:18374572, ECO:0000269|PubMed:18481843, ECO:0000269|PubMed:18640037, ECO:0000269|PubMed:18942852, ECO:0000269|PubMed:1909891, ECO:0000269|PubMed:1910042, ECO:0000269|PubMed:19170619, ECO:0000269|PubMed:19186056, ECO:0000269|PubMed:19206230, ECO:0000269|PubMed:19520834, ECO:0000269|PubMed:19778001, ECO:0000269|PubMed:4994926, ECO:0000269|PubMed:7761440, ECO:0000269|PubMed:7901850, ECO:0000269|PubMed:8218160, ECO:0000269|PubMed:8262987, ECO:0000269|PubMed:8399159, ECO:0000269|PubMed:8451242, ECO:0000269|PubMed:8485129, ECO:0000269|PubMed:8639494, ECO:0000269|PubMed:9265618, ECO:0000269|PubMed:9398308}.
uniprot
proteins
mass_dalton
29246
uniprot
proteins
mutagenesis
MUTAGEN 5; /note="W->A: Impaired activity, not rescued by 4-methylimidazole (4-MI); when associated with W-64."; /evidence="ECO:0000269|PubMed:17071654"; MUTAGEN 7; /note="Y->F: Enhanced activity."; /evidence="ECO:0000269|PubMed:12171926, ECO:0000269|PubMed:17330962"; MUTAGEN 7; /note="Y->H: Reduced proton transfer rate."; /evidence="ECO:0000269|PubMed:12171926, ECO:0000269|PubMed:17330962"; MUTAGEN 62; /note="N->A: Reduced activity."; /evidence="ECO:0000269|PubMed:18942852"; MUTAGEN 62; /note="N->D: Strongly reduced activity."; /evidence="ECO:0000269|PubMed:18942852"; MUTAGEN 62; /note="N->H: Reduced proton transfer; when associated with A-64."; /evidence="ECO:0000269|PubMed:15667203, ECO:0000269|PubMed:17330962, ECO:0000269|PubMed:18942852"; MUTAGEN 62; /note="N->L: Reduced activity."; /evidence="ECO:0000269|PubMed:17330962, ECO:0000269|PubMed:18942852"; MUTAGEN 62; /note="N->T: Reduced activity."; /evidence="ECO:0000269|PubMed:18942852"; MUTAGEN 62; /note="N->V: Reduced activity."; /evidence="ECO:0000269|PubMed:18942852"; MUTAGEN 64; /note="H->A: Reduced CO(2) hydrase activity, rescued by 4-methylimidazole (4-MI). Reduced proton transfer; when associated with H-62. Enhanced proton transfer; when associated with H-67. Enhanced proton transfer capacity; when associated with H-99."; /evidence="ECO:0000269|PubMed:11327835, ECO:0000269|PubMed:15667203, ECO:0000269|PubMed:16106378, ECO:0000269|PubMed:17071654"; MUTAGEN 64; /note="H->G: Impaired activity, not rescued by 4-methylimidazole (4-MI)."; /evidence="ECO:0000269|PubMed:11327835, ECO:0000269|PubMed:16106378, ECO:0000269|PubMed:17071654"; MUTAGEN 64; /note="H->W: Impaired activity, rescued by 4-methylimidazole (4-MI). Impaired activity, not rescued by 4-methylimidazole (4-MI); when associated with A-5."; /evidence="ECO:0000269|PubMed:11327835, ECO:0000269|PubMed:16106378, ECO:0000269|PubMed:17071654"; MUTAGEN 65; /note="A->F: Reduced activity."; MUTAGEN 65; /note="A->S: 2-fold decrease in enzyme efficiency, as determined by kcat/KM ratio, and efficiently inhibited by chlorzolamide; when associated with Q-67."; /evidence="ECO:0000269|PubMed:19170619"; MUTAGEN 67; /note="N->H: Enhanced proton transfer; when associated with A-64."; /evidence="ECO:0000269|PubMed:15667203"; MUTAGEN 67; /note="N->L: Reduced activity."; /evidence="ECO:0000269|PubMed:17330962"; MUTAGEN 67; /note="N->Q: 2-fold decrease in enzyme efficiency, as determined by kcat/KM ratio, and efficiently inhibited by chlorzolamide; when associated with S-65."; /evidence="ECO:0000269|PubMed:19170619"; MUTAGEN 94; /note="H->C,D,E,N,Q: Strongly reduced CO(2) hydrase and p-nitrophenyl acetate esterase activities, impaired stability of zinc binding."; /evidence="ECO:0000269|PubMed:8431430, ECO:0000269|PubMed:9398308"; MUTAGEN 106; /note="E->A,Q: Strongly reduced CO(2) hydrase activity."; /evidence="ECO:0000269|PubMed:15299482, ECO:0000269|PubMed:7901850"; MUTAGEN 106; /note="E->D: Normal CO(2) hydrase activity."; /evidence="ECO:0000269|PubMed:15299482, ECO:0000269|PubMed:7901850"; MUTAGEN 117; /note="E->Q: Strongly reduced activity and sulfonamide affinity."; /evidence="ECO:0000269|PubMed:8639494"; MUTAGEN 119; /note="H->D,N,Q: Reduced activity."; /evidence="ECO:0000269|PubMed:9398308"; MUTAGEN 119; /note="H->E: Strongly reduced activity."; /evidence="ECO:0000269|PubMed:9398308"; MUTAGEN 121; /note="V->A,G,I,L,S: Reduced CO(2) hydrase and p-nitrophenyl acetate esterase activities."; /evidence="ECO:0000269|PubMed:1910042"; MUTAGEN 121; /note="V->K,R: Strongly reduced CO(2) hydrase and p-nitrophenyl acetate esterase activities."; /evidence="ECO:0000269|PubMed:1910042"; MUTAGEN 142; /note="V->F,Y: Strongly impaired activity."; /evidence="ECO:0000269|PubMed:1932029"; MUTAGEN 142; /note="V->G: Weakly impaired activity."; /evidence="ECO:0000269|PubMed:1932029"; MUTAGEN 142; /note="V->H: Impaired activity."; /evidence="ECO:0000269|PubMed:1932029"; MUTAGEN 197; /note="L->A: Reduced CO(2) hydrase activity."; /evidence="ECO:0000269|PubMed:8485129"; MUTAGEN 197; /note="L->E,H,R: Strongly reduced CO(2) hydrase activity."; /evidence="ECO:0000269|PubMed:8485129"; MUTAGEN 197; /note="L->F: Normal activity."; /evidence="ECO:0000269|PubMed:8485129"; MUTAGEN 198; /note="T->A,C,H,P: Strongly reduced activity."; /evidence="ECO:0000269|PubMed:12056894, ECO:0000269|PubMed:7761440, ECO:0000269|PubMed:7901850, ECO:0000269|PubMed:8262987, ECO:0000269|PubMed:8399159"; MUTAGEN 198; /note="T->D,E: Strongly reduced activity, but enhanced zinc affinity."; /evidence="ECO:0000269|PubMed:12056894, ECO:0000269|PubMed:7761440, ECO:0000269|PubMed:7901850, ECO:0000269|PubMed:8262987, ECO:0000269|PubMed:8399159"; MUTAGEN 198; /note="T->S,V: Reduced activity."; /evidence="ECO:0000269|PubMed:12056894, ECO:0000269|PubMed:7761440, ECO:0000269|PubMed:7901850, ECO:0000269|PubMed:8262987, ECO:0000269|PubMed:8399159"; MUTAGEN 199; /note="T->H: Higher affinity for bicarbonate. Enhanced proton transfer capacity; when associated with A-64."; /evidence="ECO:0000269|PubMed:16106378, ECO:0000269|PubMed:1909891, ECO:0000269|PubMed:8451242"; MUTAGEN 199; /note="T->S: Enhanced p-nitrophenyl acetate esterase activity, but normal CO(2) hydrase activity."; /evidence="ECO:0000269|PubMed:16106378, ECO:0000269|PubMed:1909891, ECO:0000269|PubMed:8451242"; MUTAGEN 201; /note="P->A: Normal CO(2) hydrase activity, but impaired stability."; /evidence="ECO:0000269|PubMed:8218160
uniprot
proteins
protein_family
Alpha-carbonic anhydrase family
uniprot
proteins
pubmed
10550681
uniprot
proteins
pubmed
11015219
uniprot
proteins
pubmed
11076507
uniprot
proteins
pubmed
11327835
uniprot
proteins
pubmed
11572683
uniprot
proteins
pubmed
11802772
uniprot
proteins
pubmed
11818565
uniprot
proteins
pubmed
11831900
uniprot
proteins
pubmed
12056894
uniprot
proteins
pubmed
12166932
uniprot
proteins
pubmed
12171926
uniprot
proteins
pubmed
12499545
uniprot
proteins
pubmed
1336460
uniprot
proteins
pubmed
1433293
uniprot
proteins
pubmed
14567693
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
14736236
uniprot
proteins
pubmed
14736710
uniprot
proteins
pubmed
1474587
uniprot
proteins
pubmed
15218065
uniprot
proteins
pubmed
15299481
uniprot
proteins
pubmed
15299482
uniprot
proteins
pubmed
15300855
uniprot
proteins
pubmed
1542674
uniprot
proteins
pubmed
15453828
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15667203
uniprot
proteins
pubmed
15865431
uniprot
proteins
pubmed
15990874
uniprot
proteins
pubmed
16106378
uniprot
proteins
pubmed
16134940
uniprot
proteins
pubmed
16214338
uniprot
proteins
pubmed
16290146
uniprot
proteins
pubmed
16506782
uniprot
proteins
pubmed
16511248
uniprot
proteins
pubmed
16686544
uniprot
proteins
pubmed
16759856
uniprot
proteins
pubmed
16787097
uniprot
proteins
pubmed
16807956
uniprot
proteins
pubmed
16820676
uniprot
proteins
pubmed
16942027
uniprot
proteins
pubmed
17000110
uniprot
proteins
pubmed
17071654
uniprot
proteins
pubmed
17125255
uniprot
proteins
pubmed
17127057
uniprot
proteins
pubmed
17181151
uniprot
proteins
pubmed
17251017
uniprot
proteins
pubmed
17314045
uniprot
proteins
pubmed
17319692
uniprot
proteins
pubmed
17330962
uniprot
proteins
pubmed
17346964
uniprot
proteins
pubmed
17407288
uniprot
proteins
pubmed
17540563
uniprot
proteins
pubmed
17588751
uniprot
proteins
pubmed
17705204
uniprot
proteins
pubmed
18024029
uniprot
proteins
pubmed
18161740
uniprot
proteins
pubmed
18162396
uniprot
proteins
pubmed
18260615
uniprot
proteins
pubmed
18266323
uniprot
proteins
pubmed
18359629
uniprot
proteins
pubmed
18374572
uniprot
proteins
pubmed
18461940
uniprot
proteins
pubmed
18481843
uniprot
proteins
pubmed
18640037
uniprot
proteins
pubmed
18723489
uniprot
proteins
pubmed
18768466
uniprot
proteins
pubmed
18942852
uniprot
proteins
pubmed
1909891
uniprot
proteins
pubmed
1910042
uniprot
proteins
pubmed
19115843
uniprot
proteins
pubmed
19170619
uniprot
proteins
pubmed
19186056
uniprot
proteins
pubmed
19206230
uniprot
proteins
pubmed
1928091
uniprot
proteins
pubmed
1932029
uniprot
proteins
pubmed
19520834
uniprot
proteins
pubmed
19583303
uniprot
proteins
pubmed
19731956
uniprot
proteins
pubmed
19778001
uniprot
proteins
pubmed
19827837
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
3000449
uniprot
proteins
pubmed
3108857
uniprot
proteins
pubmed
3121496
uniprot
proteins
pubmed
3151019
uniprot
proteins
pubmed
3151020
uniprot
proteins
pubmed
4207120
uniprot
proteins
pubmed
4621826
uniprot
proteins
pubmed
4994926
uniprot
proteins
pubmed
6407977
uniprot
proteins
pubmed
6817747
uniprot
proteins
pubmed
7608893
uniprot
proteins
pubmed
7696263
uniprot
proteins
pubmed
7761440
uniprot
proteins
pubmed
7803386
uniprot
proteins
pubmed
7901850
uniprot
proteins
pubmed
8070585
uniprot
proteins
pubmed
8142888
uniprot
proteins
pubmed
8218160
uniprot
proteins
pubmed
823150
uniprot
proteins
pubmed
8262987
uniprot
proteins
pubmed
8331673
uniprot
proteins
pubmed
8399159
uniprot
proteins
pubmed
8431430
uniprot
proteins
pubmed
8451242
uniprot
proteins
pubmed
8482389
uniprot
proteins
pubmed
8485129
uniprot
proteins
pubmed
8557623
uniprot
proteins
pubmed
8639494
uniprot
proteins
pubmed
8834238
uniprot
proteins
pubmed
8987974
uniprot
proteins
pubmed
9143915
uniprot
proteins
pubmed
9265618
uniprot
proteins
pubmed
9398308
uniprot
proteins
pubmed
9541386
uniprot
proteins
pubmed
9865942
uniprot
proteins
sequence_length
260
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15990874}. Cell membrane {ECO:0000269|PubMed:15990874}. Note=Colocalized with SLC26A6 at the surface of the cell membrane in order to form a bicarbonate transport metabolon. Displaced from the cytosolic surface of the cell membrane by PKC in phorbol myristate acetate (PMA)-induced cells. {ECO:0000269|PubMed:15990874}.
uniprot
proteins