ID CAH2_CHICK Reviewed; 260 AA. AC P07630; DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 24-JAN-2024, entry version 179. 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 Gallus gallus (Chicken). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae; OC Phasianinae; Gallus. OX NCBI_TaxID=9031; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=Hubbard White Mountain; TISSUE=Testis; RX PubMed=7926806; DOI=10.1016/0378-1119(94)90072-8; RA Mezquita J., Pau M., Mezquita C.; RT "A novel carbonic anhydrase II mRNA isolated from mature chicken testis RT displays a TATA box and other promoter sequences in a leader 5' RT untranslated region not present in somatic tissues."; RL Gene 147:231-235(1994). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. RC STRAIN=White leghorn; RX PubMed=3029691; DOI=10.1093/nar/15.2.753; RA Yoshihara C.M., Lee J.-D., Dodgson J.B.; RT "The chicken carbonic anhydrase II gene: evidence for a recent shift in RT intron position."; RL Nucleic Acids Res. 15:753-770(1987). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] OF 5-260. RC STRAIN=White leghorn; TISSUE=Retina; RX PubMed=3102231; DOI=10.1111/j.1432-1033.1987.tb10550.x; RA Rogers J.H.; RT "Sequence of carbonic anhydrase II cDNA from chick retina."; RL Eur. J. Biochem. 162:119-122(1987). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] OF 222-260. RC TISSUE=Retina; RX PubMed=1969140; DOI=10.1093/nar/18.4.1049; RA Godbout R., Andison R., Upton C., Day R.; RT "Utilization of the second polyadenylation signal at the 3' end of the RT chicken carbonic anhydrase II gene."; RL Nucleic Acids Res. 18:1049-1049(1990). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] OF 8-87. RX PubMed=6331256; DOI=10.1111/j.1749-6632.1984.tb12357.x; RA Yoshihara C.M., Federspiel M., Dodgson J.B.; RT "Isolation of the chicken carbonic anhydrase II gene."; RL Ann. N. Y. Acad. Sci. 429:332-334(1984). CC -!- FUNCTION: Catalyzes the reversible hydration of carbon dioxide. Can CC also hydrate cyanamide to urea. {ECO:0000250|UniProtKB:P00918}. CC -!- CATALYTIC ACTIVITY: CC Reaction=H(+) + hydrogencarbonate = 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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P00918}. Cell CC membrane {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; Z14957; CAA78681.1; -; mRNA. DR EMBL; X12639; CAA31175.1; -; mRNA. DR EMBL; X06000; CAA29417.1; -; Genomic_DNA. DR EMBL; X06001; CAA29417.1; JOINED; Genomic_DNA. DR EMBL; X06002; CAA29417.1; JOINED; Genomic_DNA. DR EMBL; X06003; CAA29417.1; JOINED; Genomic_DNA. DR EMBL; X06004; CAA29417.1; JOINED; Genomic_DNA. DR EMBL; X06005; CAA29417.1; JOINED; Genomic_DNA. DR EMBL; X04810; CAA28501.1; -; mRNA. DR EMBL; X17378; CAA35250.1; -; mRNA. DR EMBL; M25943; AAA48646.1; -; mRNA. DR PIR; JC2580; JC2580. DR RefSeq; NP_990648.1; NM_205317.1. DR AlphaFoldDB; P07630; -. DR SMR; P07630; -. DR STRING; 9031.ENSGALP00000056391; -. DR PaxDb; 9031-ENSGALP00000025525; -. DR Ensembl; ENSGALT00000140805; ENSGALP00000087022; ENSGALG00000030781. DR Ensembl; ENSGALT00010032073.1; ENSGALP00010018863.1; ENSGALG00010013325.1. DR Ensembl; ENSGALT00015009157; ENSGALP00015005133; ENSGALG00015003949. DR GeneID; 396257; -. DR KEGG; gga:396257; -. DR CTD; 760; -. DR VEuPathDB; HostDB:geneid_396257; -. DR eggNOG; KOG0382; Eukaryota. DR GeneTree; ENSGT00940000160385; -. DR HOGENOM; CLU_039326_2_1_1; -. DR InParanoid; P07630; -. DR OMA; WADSFPI; -. DR OrthoDB; 49814at2759; -. DR PhylomeDB; P07630; -. DR TreeFam; TF316425; -. DR Reactome; R-GGA-1237044; Erythrocytes take up carbon dioxide and release oxygen. DR Reactome; R-GGA-1247673; Erythrocytes take up oxygen and release carbon dioxide. DR Reactome; R-GGA-1475029; Reversible hydration of carbon dioxide. DR PRO; PR:P07630; -. DR Proteomes; UP000000539; Chromosome 2. DR Bgee; ENSGALG00000030781; Expressed in lung and 13 other cell types or tissues. DR GO; GO:0045177; C:apical part of cell; IBA:GO_Central. DR GO; GO:0005737; C:cytoplasm; IDA:AgBase. DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB. DR GO; GO:0004089; F:carbonate dehydratase activity; IDA:AgBase. DR GO; GO:0018820; F:cyanamide hydratase activity; IEA:RHEA. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0015670; P:carbon dioxide transport; IBA:GO_Central. DR GO; GO:0071244; P:cellular response to carbon dioxide; IDA:AgBase. DR GO; GO:0006730; P:one-carbon metabolic process; IBA:GO_Central. DR GO; GO:0051453; P:regulation of intracellular pH; IBA:GO_Central. DR CDD; cd03119; alpha_CA_I_II_III_XIII; 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 2: Evidence at transcript level; KW Cell membrane; Cytoplasm; Lyase; Membrane; Metal-binding; KW Reference proteome; Zinc. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000250|UniProtKB:P00918" FT CHAIN 2..260 FT /note="Carbonic anhydrase 2" FT /id="PRO_0000077423" 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 CONFLICT 5 FT /note="W -> L (in Ref. 3; CAA28501)" FT /evidence="ECO:0000305" FT CONFLICT 8 FT /note="D -> G (in Ref. 5; AAA48646)" FT /evidence="ECO:0000305" FT CONFLICT 87 FT /note="V -> S (in Ref. 5; AAA48646)" FT /evidence="ECO:0000305" FT CONFLICT 250 FT /note="L -> V (in Ref. 2; CAA31175/CAA29417)" FT /evidence="ECO:0000305" SQ SEQUENCE 260 AA; 29008 MW; 6723309BC77A4950 CRC64; MSHHWGYDSH NGPAHWHEHF PIANGERQSP IAISTKAARY DPALKPLSFS YDAGTAKAIV NNGHSFNVEF DDSSDKSVLQ GGALDGVYRL VQFHIHWGSC EGQGSEHTVD GVKYDAELHI VHWNVKYGKF AEALKHPDGL AVVGIFMKVG NAKPEIQKVV DALNSIQTKG KQASFTNFDP TGLLPPCRDY WTYPGSLTTP PLHECVIWHV LKEPITVSSE QMCKLRGLCF SAENEPVCRM VDNWRPCQPL KSREVRASFQ //