ID CAH6_SHEEP Reviewed; 307 AA. AC P08060; DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1988, sequence version 1. DT 25-NOV-2008, entry version 61. DE RecName: Full=Carbonic anhydrase 6; DE EC=4.2.1.1; DE AltName: Full=Carbonic anhydrase VI; DE Short=CA-VI; DE AltName: Full=Carbonate dehydratase VI; DE AltName: Full=Secreted carbonic anhydrase; DE AltName: Full=Salivary carbonic anhydrase; GN Name=CA6; OS Ovis aries (Sheep). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia; OC Pecora; Bovidae; Caprinae; Ovis. OX NCBI_TaxID=9940; RN [1] RP PROTEIN SEQUENCE. RC TISSUE=Saliva; RX MEDLINE=88294021; PubMed=3135834; DOI=10.1021/bi00408a023; RA Fernley R.T., Wright R.D., Coghlan J.P.; RT "Complete amino acid sequence of ovine salivary carbonic anhydrase."; RL Biochemistry 27:2815-2820(1988). CC -!- FUNCTION: Reversible hydration of carbon dioxide. Its role in CC saliva is unknown. CC -!- CATALYTIC ACTIVITY: H(2)CO(3) = CO(2) + H(2)O. CC -!- COFACTOR: Zinc (By similarity). CC -!- SUBCELLULAR LOCATION: Secreted. CC -!- TISSUE SPECIFICITY: Major constituent of saliva. CC -!- SIMILARITY: Belongs to the alpha-carbonic anhydrase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR PIR; A29993; A29993. DR HSSP; O43570; 1JD0. DR HOVERGEN; P08060; -. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW. DR GO; GO:0004089; F:carbonate dehydratase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0006730; P:one-carbon compound metabolic process; IEA:InterPro. DR InterPro; IPR001148; Euk_COanhd. DR Gene3D; G3DSA:3.10.200.10; Euk_COanhd; 1. DR PANTHER; PTHR18952; Euk_COanhd; 1. DR Pfam; PF00194; Carb_anhydrase; 1. DR ProDom; PD000865; Euk_COanhd; 1. DR PROSITE; PS00162; ALPHA_CA_1; 1. DR PROSITE; PS51144; ALPHA_CA_2; 1. PE 1: Evidence at protein level; KW Direct protein sequencing; Glycoprotein; Lyase; Metal-binding; KW Secreted; Zinc. FT CHAIN 1 307 Carbonic anhydrase 6. FT /FTId=PRO_0000077430. FT METAL 94 94 Zinc; catalytic (By similarity). FT METAL 96 96 Zinc; catalytic (By similarity). FT METAL 121 121 Zinc; catalytic (By similarity). FT CARBOHYD 50 50 N-linked (GlcNAc...). FT CARBOHYD 239 239 N-linked (GlcNAc...). FT DISULFID 25 207 Potential. FT VARIANT 63 63 V -> M. FT VARIANT 297 297 I -> M. SQ SEQUENCE 307 AA; 35555 MW; 338682C2D45E5D6C CRC64; GHGVEWTYSE GMLDEAHWPL EYPKCGGRRQ SPIDLQMKKV QYNPSLRALN LTGYGLWHGE FPVTNNGHTV QISLPSTMSM TTSDGTQYLA KQMHFHWGGA SSEISGSEHT VDGMRYVIEI HVVHYNSKYN SYEEAQKEPD GLAVLAALVE VKDYTENAYY SKFISHLEDI RYAGQSTVLR GLDIEDMLPG DLRYYYSYLG SLTTPPCTEN VHWFVVADTV KLSKTQVEKL ENSLLNHQNK TIQNDYRRTQ PLNHRVVEAN FMSRPHQEYT LASKLHFYLN NIDQTLEYLR RFIEQKIPKR KKQENWP //