ID   CAH6_BOVIN              Reviewed;         319 AA.
AC   P18915; Q95322;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1999, sequence version 2.
DT   03-AUG-2022, entry version 130.
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;
DE   Flags: Precursor;
GN   Name=CA6;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Submandibular gland;
RX   PubMed=8761494; DOI=10.1042/bj3180291;
RA   Jiang W., Woitach J.T., Gupta D.;
RT   "Sequence of bovine carbonic anhydrase VI: potential recognition sites for
RT   N-acetylgalactosaminyltransferase.";
RL   Biochem. J. 318:291-296(1996).
RN   [2]
RP   PROTEIN SEQUENCE OF 15-39.
RX   PubMed=2497732; DOI=10.1042/bj2590091;
RA   Fernley R.T., Darling P., Aldred P., Wright R.D., Coghlan J.P.;
RT   "Tissue and species distribution of the secreted carbonic anhydrase
RT   isoenzyme.";
RL   Biochem. J. 259:91-96(1989).
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   EMBL; X96503; CAA65357.1; -; mRNA.
DR   PIR; S71877; S71877.
DR   RefSeq; NP_776323.1; NM_173898.2.
DR   AlphaFoldDB; P18915; -.
DR   SMR; P18915; -.
DR   STRING; 9913.ENSBTAP00000012525; -.
DR   BindingDB; P18915; -.
DR   ChEMBL; CHEMBL2096971; -.
DR   DrugCentral; P18915; -.
DR   PaxDb; P18915; -.
DR   GeneID; 280742; -.
DR   KEGG; bta:280742; -.
DR   CTD; 765; -.
DR   eggNOG; KOG0382; Eukaryota.
DR   InParanoid; P18915; -.
DR   OrthoDB; 1377476at2759; -.
DR   Proteomes; UP000009136; 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; Signal; Zinc.
FT   SIGNAL          1..14
FT                   /evidence="ECO:0000269|PubMed:2497732"
FT   CHAIN           15..319
FT                   /note="Carbonic anhydrase 6"
FT                   /id="PRO_0000004239"
FT   DOMAIN          16..273
FT                   /note="Alpha-carbonic anhydrase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01134"
FT   ACT_SITE        80
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P00918"
FT   BINDING         106
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P23280"
FT   BINDING         108
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P23280"
FT   BINDING         133
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P23280"
FT   BINDING         215..216
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P00918"
FT   CARBOHYD        62
FT                   /note="N-linked (GlcNAc...) asparagine"
FT   CARBOHYD        251
FT                   /note="N-linked (GlcNAc...) asparagine"
FT   DISULFID        37..219
FT                   /evidence="ECO:0000255"
FT   CONFLICT        16
FT                   /note="H -> S (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   319 AA;  37007 MW;  179884A7A9083AED CRC64;
     MITLLFLLVV GAQAQHEWTY SEGVLDEKHW RLQYPDCGGT RQSPIDLKMK KVRYNPSLRA
     LNLTGYGLRQ GEFPMTNNGH TVQISLPSSM RMTTSDGSQY LAKQMHFHWG GDSSEISGSE
     HTVDGMRYII EIHVVHYHSK YGSYEEAQNE PDGLAVLAAL VEVKDYAENT YYSNFISHLE
     DIRYAGQSTV LRDLDIQDML PGDLRYYYSY LGSLTTPSCT ENVHWFVVAD TVKLSKTQIE
     KLENSLLNHQ NETIQNNYRS TQPLNHRVVE ANFVSHPHQE YTLGSKLHFY LNNIDQNLEY
     LRRFIEQKIT KRKKEKYWP