ID CAH1_HORSE Reviewed; 261 AA. AC P00917; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 02-SEP-2026, entry version 131. DE RecName: Full=Carbonic anhydrase 1; DE EC=4.2.1.1 {ECO:0000250|UniProtKB:P00915}; DE AltName: Full=Carbonate dehydratase I; DE AltName: Full=Carbonic anhydrase I; DE Short=CA-I; DE AltName: Full=Cyanamide hydratase CA1; DE EC=4.2.1.69 {ECO:0000250|UniProtKB:P00915}; GN Name=CA1; OS Equus caballus (Horse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus. OX NCBI_TaxID=9796; RN [1] RP PROTEIN SEQUENCE OF 2-261, AND VARIANTS ASP-55; GLY-66; GLY-82; PHE-84; RP HIS-116; GLY-158; ARG-184; TYR-213; ARG-223 AND ALA-225. RX PubMed=6773961; DOI=10.1016/s0021-9258(19)70546-8; RA Jabusch J.R., Bray R.P., Deutsch H.F.; RT "Sequence of the low activity equine erythrocyte carbonic anhydrase and RT delineation of the amino acid substitutions in various polymorphic forms."; RL J. Biol. Chem. 255:9196-9204(1980). CC -!- FUNCTION: Catalyzes the reversible hydration of carbon dioxide. Can CC hydrate cyanamide to urea. {ECO:0000250|UniProtKB:P00915}. 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:P00915}; 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:P00915}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000250|UniProtKB:P00915}; CC -!- ACTIVITY REGULATION: Inhibited by acetazolamide. CC {ECO:0000250|UniProtKB:P00915}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:B0BNN3}. CC -!- POLYMORPHISM: The sequence shown is that of the electrophoretically CC homogeneous D isozyme. {ECO:0000269|PubMed:6773961}. 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 PIR; A01140; CRHO1D. DR FunCoup; P00917; 349. DR STRING; 9796.ENSECAP00000007854; -. DR BindingDB; P00917; -. DR ChEMBL; CHEMBL4105955; -. DR PaxDb; 9796-ENSECAP00000007854; -. DR PeptideAtlas; P00917; -. DR InParanoid; P00917; -. DR Proteomes; UP000002281; Unplaced. DR GO; GO:0005737; C:cytoplasm; 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 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:SF282; CARBONIC ANHYDRASE 1; 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; Cytoplasm; Direct protein sequencing; Lyase; Metal-binding; KW Reference proteome; Zinc. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000250|UniProtKB:P00915, FT ECO:0000269|PubMed:6773961" FT CHAIN 2..261 FT /note="Carbonic anhydrase 1" FT /id="PRO_0000077408" FT DOMAIN 4..261 FT /note="Alpha-carbonic anhydrase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01134" FT ACT_SITE 65 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000250|UniProtKB:P00918" FT BINDING 95 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000250|UniProtKB:P00915" FT BINDING 97 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000250|UniProtKB:P00915" FT BINDING 120 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000250|UniProtKB:P00915" FT BINDING 200..201 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P00918" FT BINDING 200 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P00915" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0000250|UniProtKB:P00915" FT VARIANT 55 FT /note="A -> D (in isozyme T)" FT /evidence="ECO:0000269|PubMed:6773961" FT VARIANT 66 FT /note="S -> G (in homogeneous D isozyme)" FT /evidence="ECO:0000269|PubMed:6773961" FT VARIANT 82 FT /note="D -> G (in isozyme A2)" FT /evidence="ECO:0000269|PubMed:6773961" FT VARIANT 84 FT /note="P -> F (in isozyme A2)" FT /evidence="ECO:0000269|PubMed:6773961" FT VARIANT 116 FT /note="S -> H (in homogeneous D isozyme)" FT /evidence="ECO:0000269|PubMed:6773961" FT VARIANT 158 FT /note="L -> G (in homogeneous D isozyme)" FT /evidence="ECO:0000269|PubMed:6773961" FT VARIANT 184 FT /note="S -> R (in isozyme A1 and isozyme B)" FT /evidence="ECO:0000269|PubMed:6773961" FT VARIANT 213 FT /note="C -> Y (in homogeneous D isozyme)" FT /evidence="ECO:0000269|PubMed:6773961" FT VARIANT 223 FT /note="Q -> R (in isozyme B)" FT /evidence="ECO:0000269|PubMed:6773961" FT VARIANT 225 FT /note="S -> A (in homogeneous D isozyme)" FT /evidence="ECO:0000269|PubMed:6773961" FT UNSURE 12 FT /note="N or D" FT UNSURE 25 FT /note="N or D" FT UNSURE 27 FT /note="N or D" FT UNSURE 28 FT /note="N or D" SQ SEQUENCE 261 AA; 29025 MW; E2DD4D1BDAE62353 CRC64; MAHSDWGYDS PNGPZEWVKL YPIANGNNQS PIDIKTSETK HDTSLKPFSV SYDPATAKEI VNVGHSFQVK FEDSDNRSVL KDGPLPGSYR LVQFHFHWGS TDDYGSEHTV DGVKYSAELH LVHWNSSKYS SFDEASSQAD GLAILGVLMK VGEANPKLQK VLDALNEVKT KGKKAPFKNF DPSSLLPSSP DYWTYSGSLT HPPLYESVTW IVCKENISIS SQQLSQFRSL LSNVEGGKAV PIQHNNRPPQ PLKGRTVRAF F //