ID A0A3B3IRX9_HUMAN Unreviewed; 300 AA. AC A0A3B3IRX9; DT 05-DEC-2018, integrated into UniProtKB/TrEMBL. DT 05-DEC-2018, sequence version 1. DT 14-DEC-2022, entry version 19. DE RecName: Full=Carbonic anhydrase {ECO:0000256|RuleBase:RU367011}; DE EC=4.2.1.1 {ECO:0000256|RuleBase:RU367011}; GN Name=CA5A {ECO:0000313|Ensembl:ENSP00000496993.1}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000496993.1, ECO:0000313|Proteomes:UP000005640}; RN [1] {ECO:0000313|Ensembl:ENSP00000496993.1, ECO:0000313|Proteomes:UP000005640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15616553; DOI=10.1038/nature03187; RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M., RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., RA Myers R.M., Rubin E.M., Pennacchio L.A.; RT "The sequence and analysis of duplication-rich human chromosome 16."; RL Nature 432:988-994(2004). RN [2] {ECO:0000313|Ensembl:ENSP00000496993.1} RP IDENTIFICATION. RG Ensembl; RL Submitted (AUG-2022) to UniProtKB. CC -!- FUNCTION: Reversible hydration of carbon dioxide. CC {ECO:0000256|RuleBase:RU367011}. 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:0000256|RuleBase:RU367011}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|RuleBase:RU367011}; CC -!- SIMILARITY: Belongs to the alpha-carbonic anhydrase family. CC {ECO:0000256|ARBA:ARBA00010718, ECO:0000256|RuleBase:RU367011}. 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; AC127455; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC133539; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR AlphaFoldDB; A0A3B3IRX9; -. DR SMR; A0A3B3IRX9; -. DR PeptideAtlas; A0A3B3IRX9; -. DR Antibodypedia; 55888; 146 antibodies from 23 providers. DR Ensembl; ENST00000649158.1; ENSP00000496993.1; ENSG00000174990.8. DR HGNC; HGNC:1377; CA5A. DR VEuPathDB; HostDB:ENSG00000174990; -. DR GeneTree; ENSGT00940000162066; -. DR ChiTaRS; CA5A; human. DR Proteomes; UP000005640; Chromosome 16. DR Bgee; ENSG00000174990; Expressed in right lobe of liver and 67 other tissues. DR ExpressionAtlas; A0A3B3IRX9; baseline and differential. DR GO; GO:0004089; F:carbonate dehydratase activity; IEA:UniProtKB-UniRule. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule. DR Gene3D; 3.10.200.10; -; 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 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 Lyase {ECO:0000256|RuleBase:RU367011}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, KW ECO:0000256|RuleBase:RU367011}; KW Proteomics identification {ECO:0007829|PeptideAtlas:A0A3B3IRX9, KW ECO:0007829|ProteomicsDB:A0A3B3IRX9}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}; KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU367011}. FT DOMAIN 39..294 FT /note="Alpha-carbonic anhydrase" FT /evidence="ECO:0000259|PROSITE:PS51144" SQ SEQUENCE 300 AA; 34125 MW; 172A50234058FC34 CRC64; MLGRNTWKTS AFSFLVEQMW APLWSRSMRP GRWCSQRSCA WQTSNNTLHP LWTVPVSVPG GTRQSPINIQ WRDSVYDPQL KPLRVSYEAA SCLYIWNTGY LFQVEFDDAT EASGISGGPL ENHYRLKQFH FHWGAVNEGG SEHTVDGHAY PAELHLVHWN SVKYQNYKEA VVGENGLAVI GVFLKLGAHH QTLQRLVDIL PEIKHKDARA AMRPFDPSTL LPTCWDYWTY AGSLTTPPLT ESVTWIIQKE PVEVAPSQGA LCTHQHLCLL KNGLCQLFLK TGANPETRRY SREAIRAWTH //