ID CAH2_BOVIN Reviewed; 260 AA. AC P00921; Q3ZBJ5; Q865Y7; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 02-SEP-2026, entry version 183. DE RecName: Full=Carbonic anhydrase 2; DE EC=4.2.1.1 {ECO:0000250|UniProtKB:P00918}; DE AltName: Full=Carbonate dehydratase II; DE AltName: Full=Carbonic anhydrase II; DE Short=CA-II; DE AltName: Full=Cyanamide hydratase CA2; DE EC=4.2.1.69 {ECO:0000250|UniProtKB:P00918}; GN Name=CA2; OS Bos taurus (Bovine). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae; OC Bovinae; Bos. OX NCBI_TaxID=9913; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Bone marrow; RA Daigle R., Castro I., Desrochers M., Charest P.-M.; RT "Full length cDNA of bovine carbonic anhydrase II."; RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=Hereford; TISSUE=Hypothalamus; RG NIH - Mammalian Gene Collection (MGC) project; RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases. RN [3] RP PROTEIN SEQUENCE OF 2-260. RC TISSUE=Erythrocyte; RX PubMed=826282; DOI=10.1016/s0300-9084(76)80085-5; RA Sciaky M., Limozin N., Filippi-Foveau D., Gulian J.M., Laurent-Tabusse G.; RT "Primary structure of bovine erythrocyte carbonic carbonic anhydrase CI. RT II. Complete sequence."; RL Biochimie 58:1071-1082(1976). RN [4] RP SEQUENCE REVISION. RX PubMed=19093; DOI=10.1016/s0300-9084(77)80146-6; RA Gulian J.M., Limozin N., Mallet B., di Costanzo J., Charrel M.; RT "Genetic independence of two forms of carbonic anhydrase from bovine RT erythrocytes."; RL Biochimie 59:293-302(1977). RN [5] RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 2-260 IN COMPLEX WITH ZINC ION. RX PubMed=15039588; DOI=10.1107/s0907444904003166; RA Saito R., Sato T., Ikai A., Tanaka N.; RT "Structure of bovine carbonic anhydrase II at 1.95 A resolution."; RL Acta Crystallogr. D 60:792-795(2004). RN [6] RP X-RAY CRYSTALLOGRAPHY (3.50 ANGSTROMS) OF 1-254 IN COMPLEX WITH ANTIBODY. RX PubMed=11342547; DOI=10.1074/jbc.m102107200; RA Desmyter A., Decanniere K., Muyldermans S., Wyns L.; RT "Antigen specificity and high affinity binding provided by one single loop RT of a camel single-domain antibody."; RL J. Biol. Chem. 276:26285-26290(2001). CC -!- FUNCTION: Catalyzes the reversible hydration of carbon dioxide (By CC similarity). Can also hydrate cyanamide to urea (By similarity). CC Involved in the regulation of fluid secretion into the anterior chamber CC of the eye (By similarity). Essential for bone resorption and CC osteoclast differentiation (By similarity). Contributes to CC intracellular pH regulation in the duodenal upper villous epithelium CC during proton-coupled peptide absorption (By similarity). Stimulates CC the chloride-bicarbonate exchange activity of SLC26A6 (By similarity). CC {ECO:0000250|UniProtKB:P00918}. CC -!- CATALYTIC ACTIVITY: CC Reaction=hydrogencarbonate + H(+) = CO2 + H2O; Xref=Rhea:RHEA:10748, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, CC ChEBI:CHEBI:17544; EC=4.2.1.1; CC Evidence={ECO:0000250|UniProtKB:P00918}; CC -!- CATALYTIC ACTIVITY: CC Reaction=urea = cyanamide + H2O; Xref=Rhea:RHEA:23056, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:16199, ChEBI:CHEBI:16698; EC=4.2.1.69; CC Evidence={ECO:0000250|UniProtKB:P00918}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000269|PubMed:15039588}; CC -!- ACTIVITY REGULATION: Inhibited by acetazolamide. CC {ECO:0000250|UniProtKB:P00918}. CC -!- SUBUNIT: Interacts with SLC4A4. Interaction with SLC4A7 regulates CC SLC4A7 transporter activity (By similarity). CC {ECO:0000250|UniProtKB:P00918}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P00918}. Cell CC membrane {ECO:0000250|UniProtKB:P00918}. Note=Colocalized with SLC26A6 CC at the surface of the cell membrane in order to form a bicarbonate CC transport metabolon. Displaced from the cytosolic surface of the cell CC membrane by PKC in phorbol myristate acetate (PMA)-induced cells. CC {ECO:0000250|UniProtKB:P00918}. CC -!- MISCELLANEOUS: One minor and two major forms were isolated CC chromatographically. CC -!- SIMILARITY: Belongs to the alpha-carbonic anhydrase family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AY240020; AAO85140.1; -; mRNA. DR EMBL; BC103260; AAI03261.1; -; mRNA. DR PIR; A01144; CRBO2. DR RefSeq; NP_848667.1; NM_178572.2. DR PDB; 1G6V; X-ray; 3.50 A; A=1-256. DR PDB; 1V9E; X-ray; 1.95 A; A/B=2-260. DR PDB; 1V9I; X-ray; 2.95 A; C=2-260. DR PDB; 23OM; X-ray; 1.70 A; A/B=2-260. DR PDB; 23ON; X-ray; 1.50 A; A/B=2-260. DR PDB; 4CNR; X-ray; 2.29 A; A/B/C/D=1-260. DR PDB; 4CNV; X-ray; 1.62 A; A=1-260. DR PDB; 4CNW; X-ray; 2.03 A; A/B=1-260. DR PDB; 4CNX; X-ray; 1.23 A; A=1-260. DR PDB; 5A25; X-ray; 1.90 A; A/B=1-260. DR PDB; 5EZT; X-ray; 1.54 A; X=4-260. DR PDB; 6SKS; X-ray; 1.75 A; A=1-260. DR PDB; 6SKT; X-ray; 1.90 A; A=1-260. DR PDB; 6SKV; X-ray; 1.75 A; A=1-260. DR AlphaFoldDB; P00921; -. DR MDposit; P00921; -. DR PCDDB; P00921; -. DR SASBDB; P00921; -. DR SMR; P00921; -. DR FunCoup; P00921; 690. DR IntAct; P00921; 1. DR MINT; P00921; -. DR STRING; 9913.ENSBTAP00000023581; -. DR BindingDB; P00921; -. DR ChEMBL; CHEMBL2283; -. DR DrugCentral; P00921; -. DR PaxDb; 9913-ENSBTAP00000023581; -. DR PeptideAtlas; P00921; -. DR ABCD; P00921; 1 sequenced antibody. DR Ensembl; ENSBTAT00085071118; ENSBTAP00085043143; ENSBTAG00085041460. DR Ensembl; ENSBTAT00090038916; ENSBTAP00090019973; ENSBTAG00090019115. DR GeneID; 280740; -. DR KEGG; bta:280740; -. DR CTD; 760; -. DR eggNOG; KOG0382; Eukaryota. DR InParanoid; P00921; -. DR OrthoDB; 429145at2759; -. DR BRENDA; 4.2.1.1; 908. DR EvolutionaryTrace; P00921; -. DR PRO; PR:P00921; -. DR Proteomes; UP000009136; Unplaced. DR GO; GO:0045177; C:apical part of cell; IBA:GO_Central. DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB. DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB. DR GO; GO:0004089; F:carbonate dehydratase activity; ISS:UniProtKB. DR GO; GO:0018820; F:cyanamide hydratase activity; ISS:UniProtKB. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0038166; P:angiotensin-activated signaling pathway; ISS:UniProtKB. DR GO; GO:2001150; P:positive regulation of dipeptide transmembrane transport; ISS:UniProtKB. DR GO; GO:0051453; P:regulation of intracellular pH; ISS:UniProtKB. DR GO; GO:0044070; P:regulation of monoatomic anion transport; ISS:UniProtKB. DR FunFam; 3.10.200.10:FF:000001; Carbonic anhydrase 2; 1. DR Gene3D; 3.10.200.10; Alpha carbonic anhydrase; 1. DR InterPro; IPR001148; CA_dom. DR InterPro; IPR036398; CA_dom_sf. DR InterPro; IPR023561; Carbonic_anhydrase_a-class. DR InterPro; IPR018338; Carbonic_anhydrase_a-class_CS. DR PANTHER; PTHR18952; CARBONIC ANHYDRASE; 1. DR PANTHER; PTHR18952:SF120; CARBONIC ANHYDRASE 2; 1. DR Pfam; PF00194; Carb_anhydrase; 1. DR SMART; SM01057; Carb_anhydrase; 1. DR SUPFAM; SSF51069; Carbonic anhydrase; 1. DR PROSITE; PS00162; ALPHA_CA_1; 1. DR PROSITE; PS51144; ALPHA_CA_2; 1. DR PDBsum; 1G6V; -. DR PDBsum; 1V9E; -. DR PDBsum; 1V9I; -. DR PDBsum; 23OM; -. DR PDBsum; 23ON; -. DR PDBsum; 4CNR; -. DR PDBsum; 4CNV; -. DR PDBsum; 4CNW; -. DR PDBsum; 4CNX; -. DR PDBsum; 5A25; -. DR PDBsum; 5EZT; -. DR PDBsum; 6SKS; -. DR PDBsum; 6SKT; -. DR PDBsum; 6SKV; -. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Cell membrane; Cytoplasm; KW Direct protein sequencing; Lyase; Membrane; Metal-binding; Phosphoprotein; KW Reference proteome; Zinc. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:19093, FT ECO:0000269|PubMed:826282" FT CHAIN 2..260 FT /note="Carbonic anhydrase 2" FT /id="PRO_0000077417" FT DOMAIN 3..259 FT /note="Alpha-carbonic anhydrase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01134" FT ACT_SITE 64 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000250|UniProtKB:P00918" FT BINDING 94 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000269|PubMed:15039588" FT BINDING 96 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000269|PubMed:15039588" FT BINDING 119 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000269|PubMed:15039588" FT BINDING 198..199 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P00918" FT SITE 7 FT /note="Fine-tunes the proton-transfer properties of H-64" FT /evidence="ECO:0000250|UniProtKB:P00918" FT SITE 62 FT /note="Fine-tunes the proton-transfer properties of H-64" FT /evidence="ECO:0000250|UniProtKB:P00918" FT SITE 67 FT /note="Fine-tunes the proton-transfer properties of H-64" FT /evidence="ECO:0000250|UniProtKB:P00918" FT MOD_RES 2 FT /note="N-acetylserine" FT /evidence="ECO:0000250|UniProtKB:P00918" FT MOD_RES 2 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P27139" FT MOD_RES 165 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P00918" FT MOD_RES 172 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P00918" FT VARIANT 57 FT /note="R -> Q (in one of the major forms)" FT TURN 9..11 FT /evidence="ECO:0007829|PDB:4CNX" FT HELIX 13..15 FT /evidence="ECO:0007829|PDB:4CNX" FT HELIX 16..19 FT /evidence="ECO:0007829|PDB:4CNX" FT HELIX 21..24 FT /evidence="ECO:0007829|PDB:4CNX" FT STRAND 25..27 FT /evidence="ECO:0007829|PDB:5EZT" FT STRAND 31..33 FT /evidence="ECO:0007829|PDB:1G6V" FT STRAND 35..37 FT /evidence="ECO:0007829|PDB:4CNX" FT STRAND 47..50 FT /evidence="ECO:0007829|PDB:4CNX" FT STRAND 56..61 FT /evidence="ECO:0007829|PDB:4CNX" FT STRAND 63..70 FT /evidence="ECO:0007829|PDB:4CNX" FT STRAND 73..81 FT /evidence="ECO:0007829|PDB:4CNX" FT STRAND 88..97 FT /evidence="ECO:0007829|PDB:4CNX" FT STRAND 99..102 FT /evidence="ECO:0007829|PDB:1G6V" FT STRAND 106..109 FT /evidence="ECO:0007829|PDB:4CNX" FT STRAND 115..124 FT /evidence="ECO:0007829|PDB:4CNX" FT HELIX 125..127 FT /evidence="ECO:0007829|PDB:4CNX" FT HELIX 130..133 FT /evidence="ECO:0007829|PDB:4CNX" FT STRAND 139..151 FT /evidence="ECO:0007829|PDB:4CNX" FT HELIX 154..160 FT /evidence="ECO:0007829|PDB:4CNX" FT HELIX 163..166 FT /evidence="ECO:0007829|PDB:4CNX" FT STRAND 167..169 FT /evidence="ECO:0007829|PDB:1G6V" FT STRAND 172..174 FT /evidence="ECO:0007829|PDB:4CNX" FT HELIX 180..183 FT /evidence="ECO:0007829|PDB:4CNX" FT STRAND 190..195 FT /evidence="ECO:0007829|PDB:4CNX" FT STRAND 206..213 FT /evidence="ECO:0007829|PDB:4CNX" FT STRAND 215..217 FT /evidence="ECO:0007829|PDB:4CNX" FT HELIX 219..225 FT /evidence="ECO:0007829|PDB:4CNX" FT STRAND 229..231 FT /evidence="ECO:0007829|PDB:4CNX" FT HELIX 245..247 FT /evidence="ECO:0007829|PDB:4CNX" FT HELIX 253..255 FT /evidence="ECO:0007829|PDB:4CNX" FT STRAND 256..258 FT /evidence="ECO:0007829|PDB:4CNX" SQ SEQUENCE 260 AA; 29114 MW; A89412C23FFD19A7 CRC64; MSHHWGYGKH NGPEHWHKDF PIANGERQSP VDIDTKAVVQ DPALKPLALV YGEATSRRMV NNGHSFNVEY DDSQDKAVLK DGPLTGTYRL VQFHFHWGSS DDQGSEHTVD RKKYAAELHL VHWNTKYGDF GTAAQQPDGL AVVGVFLKVG DANPALQKVL DALDSIKTKG KSTDFPNFDP GSLLPNVLDY WTYPGSLTTP PLLESVTWIV LKEPISVSSQ QMLKFRTLNF NAEGEPELLM LANWRPAQPL KNRQVRGFPK //