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   03-AUG-2022, entry version 110.
DE   RecName: Full=Carbonic anhydrase 6;
DE            EC=4.2.1.1;
DE   AltName: Full=Carbonate dehydratase VI;
DE   AltName: Full=Carbonic anhydrase VI;
DE            Short=CA-VI;
DE   AltName: Full=Salivary carbonic anhydrase;
DE   AltName: Full=Secreted carbonic anhydrase;
GN   Name=CA6;
OS   Ovis aries (Sheep).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Caprinae; Ovis.
OX   NCBI_TaxID=9940;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   TISSUE=Saliva;
RX   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 saliva is
CC       unknown.
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   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000250|UniProtKB:P23589};
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Major constituent of saliva.
CC   -!- SIMILARITY: Belongs to the alpha-carbonic anhydrase family.
CC       {ECO:0000305}.
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DR   PIR; A29993; A29993.
DR   AlphaFoldDB; P08060; -.
DR   SMR; P08060; -.
DR   STRING; 9940.ENSOARP00000009896; -.
DR   eggNOG; KOG0382; Eukaryota.
DR   Proteomes; UP000002356; Unplaced.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004089; F:carbonate dehydratase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006730; P:one-carbon metabolic process; IEA:InterPro.
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   InterPro; IPR018428; Carbonic_anhydrase_CA6.
DR   PANTHER; PTHR18952; PTHR18952; 1.
DR   PANTHER; PTHR18952:SF110; PTHR18952:SF110; 1.
DR   Pfam; PF00194; Carb_anhydrase; 1.
DR   SMART; SM01057; Carb_anhydrase; 1.
DR   SUPFAM; SSF51069; SSF51069; 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; Disulfide bond; Glycoprotein; Lyase;
KW   Metal-binding; Reference proteome; Secreted; Zinc.
FT   CHAIN           1..307
FT                   /note="Carbonic anhydrase 6"
FT                   /id="PRO_0000077430"
FT   DOMAIN          4..261
FT                   /note="Alpha-carbonic anhydrase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01134"
FT   ACT_SITE        68
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:P23280"
FT   BINDING         96
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P23280"
FT   BINDING         121
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P23280"
FT   BINDING         203..204
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P00918"
FT   CARBOHYD        50
FT                   /note="N-linked (GlcNAc...) asparagine"
FT   CARBOHYD        239
FT                   /note="N-linked (GlcNAc...) asparagine"
FT   DISULFID        25..207
FT                   /evidence="ECO:0000255"
FT   VARIANT         63
FT                   /note="V -> M"
FT   VARIANT         297
FT                   /note="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