ID CAH2_RABIT Reviewed; 260 AA. AC P00919; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 02-SEP-2026, entry version 161. 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 Oryctolagus cuniculus (Rabbit). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus. OX NCBI_TaxID=9986; RN [1] RP PROTEIN SEQUENCE OF 2-260. RX PubMed=416851; DOI=10.1016/0005-2795(78)90541-x; RA Ferrell R.E., Stroup S.K., Tanis R.J., Tashian R.E.; RT "Amino acid sequence of rabbit carbonic anhydrase II."; RL Biochim. Biophys. Acta 533:1-11(1978). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] OF 8-239. RC STRAIN=New Zealand white; TISSUE=Kidney; RX PubMed=8285209; DOI=10.1152/ajprenal.1993.265.6.f764; RA Schwartz G.J., Winkler C.A., Zavilowitz B.J., Bargiello T.; RT "Carbonic anhydrase II mRNA is induced in rabbit kidney cortex during RT chronic metabolic acidosis."; RL Am. J. Physiol. 265:F764-F772(1993). CC -!- FUNCTION: Catalyzes the reversible hydration of carbon dioxide. Can CC also hydrate cyanamide to urea (By similarity). Involved in the CC regulation of fluid secretion into the anterior chamber of the eye. CC Essential for bone resorption and osteoclast differentiation. CC Contributes to intracellular pH regulation in the duodenal upper CC villous epithelium during proton-coupled peptide absorption. Stimulates CC the chloride-bicarbonate exchange activity of SLC26A6. 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:0000250|UniProtKB:P00921}; CC -!- ACTIVITY REGULATION: Inhibited by acetazolamide. CC {ECO:0000250|UniProtKB:P00918}. CC -!- SUBUNIT: Interacts with SLC4A4 and SLC26A6. Interaction with SLC4A7 CC regulates 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 (By CC similarity). {ECO:0000250|UniProtKB:P00918}. 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; M98395; AAA80531.1; -; mRNA. DR PIR; A01142; CRRB2. DR RefSeq; NP_001182637.1; NM_001195708.1. DR AlphaFoldDB; P00919; -. DR SMR; P00919; -. DR FunCoup; P00919; 143. DR STRING; 9986.ENSOCUP00000032692; -. DR PaxDb; 9986-ENSOCUP00000032692; -. DR Ensembl; ENSOCUT00000011742.4; ENSOCUP00000010096.2; ENSOCUG00000011742.4. DR GeneID; 100009156; -. DR KEGG; ocu:100009156; -. DR CTD; 760; -. DR eggNOG; KOG0382; Eukaryota. DR GeneTree; ENSGT00940000160385; -. DR HOGENOM; CLU_039326_2_1_1; -. DR InParanoid; P00919; -. DR OMA; INPHWKV; -. DR OrthoDB; 429145at2759; -. DR Proteomes; UP000001811; Chromosome 3. DR Bgee; ENSOCUG00000011742; Expressed in blood and 15 other cell types or tissues. DR ExpressionAtlas; P00919; baseline. DR GO; GO:0045177; C:apical part of cell; IEA:TreeGrafter. 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:0015670; P:carbon dioxide transport; IEA:TreeGrafter. 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. PE 1: Evidence at protein level; KW Acetylation; Cell membrane; Cytoplasm; Direct protein sequencing; Lyase; KW Membrane; Metal-binding; Phosphoprotein; Reference proteome; Zinc. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:416851" FT CHAIN 2..260 FT /note="Carbonic anhydrase 2" FT /id="PRO_0000077420" 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:0000250|UniProtKB:P00918" FT BINDING 96 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000250|UniProtKB:P00918" FT BINDING 119 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000250|UniProtKB:P00918" 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 204 FT /note="E -> Q" FT CONFLICT 24 FT /note="N -> D (in Ref. 1; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 36 FT /note="N -> D (in Ref. 1; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 50 FT /note="C -> S (in Ref. 1; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 77 FT /note="T -> S (in Ref. 1; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 103 FT /note="Q -> E (in Ref. 1; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 177 FT /note="D -> N (in Ref. 1; AA sequence)" FT /evidence="ECO:0000305" SQ SEQUENCE 260 AA; 29500 MW; 1601916B7D8A2828 CRC64; MSHHWGYGKH NGPEHWHKDF PIANGERQSP IDIDTNAAKH DPSLKPLRVC YEHPISRRII NNGHSFNVEF DDSHDKTVLK EGPLEGTYRL IQFHFHWGSS DGQGSEHTVN KKKYAAELHL VHWNTKYGDF GKAVKHPDGL AVLGIFLKIG SATPGLQKVV DTLSSIKTKG KSVDFTDFDP RGLLPESLDY WTYPGSLTTP PLLECVTWIV LKEPITVSSE QMLKFRNLNF NKEAEPEEPM VDNWRPTQPL KGRQVKASFV //