ID   CAH6_CANLF              Reviewed;         320 AA.
AC   Q865C0;
DT   12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 95.
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   Flags: Precursor;
GN   Name=CA6;
OS   Canis lupus familiaris (Dog) (Canis familiaris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX   NCBI_TaxID=9615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Parotid gland;
RA   Murakami M.;
RT   "Canine carbonic anhydrase VI (CA6), mRNA.";
RL   Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Reversible hydration of carbon dioxide. Its role in saliva is
CC       unknown (By similarity). {ECO:0000250}.
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   -!- SIMILARITY: Belongs to the alpha-carbonic anhydrase family.
CC       {ECO:0000305}.
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DR   EMBL; AB080972; BAC65098.1; -; mRNA.
DR   RefSeq; NP_001002999.1; NM_001002999.1.
DR   AlphaFoldDB; Q865C0; -.
DR   SMR; Q865C0; -.
DR   STRING; 9612.ENSCAFP00000029168; -.
DR   PaxDb; Q865C0; -.
DR   GeneID; 403503; -.
DR   KEGG; cfa:403503; -.
DR   CTD; 765; -.
DR   eggNOG; KOG0382; Eukaryota.
DR   InParanoid; Q865C0; -.
DR   OrthoDB; 1377476at2759; -.
DR   Proteomes; UP000002254; 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   2: Evidence at transcript level;
KW   Disulfide bond; Glycoprotein; Lyase; Metal-binding; Reference proteome;
KW   Secreted; Signal; Zinc.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000255"
FT   CHAIN           18..320
FT                   /note="Carbonic anhydrase 6"
FT                   /id="PRO_0000004240"
FT   DOMAIN          21..278
FT                   /note="Alpha-carbonic anhydrase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01134"
FT   ACT_SITE        85
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P00918"
FT   BINDING         111
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P23280"
FT   BINDING         113
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P23280"
FT   BINDING         138
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P23280"
FT   BINDING         220..221
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P00918"
FT   CARBOHYD        256
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        42..224
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   320 AA;  36705 MW;  6E00A8D08AA0D23F CRC64;
     MRALALLLAL PLLGARAQHG SLWTYSEGAL DQVHWPREYP TCGGTRQSPI DLQRRKVQYN
     PSLKALKLTG YRIQVGEFPM INNGHTVQIS LPPTMRMMAS DGTEYIAQQM HFHWGGASSE
     ISGSEHTIDG IRFVAEIHIV HYNSKYKSYD IAQHEPDGLA VLAALVKVED YGENTYYSNF
     ISHLNNIRYP GQSTVLSGLD IEDMLPENTH HYYTYRGSLT TPPCTENVHW FVLVHHVRLS
     SIQTWKLENS ILDHQNKTLH SDYRRIQPLN GRVVESNFVN LPSQGSEFQF YVNKLNNKLE
     YLRRLLEKTK VEKKPHIHQA