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Database: UniProt
Entry: P18915
LinkDB: P18915
Original site: P18915 
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   22-JAN-2014, entry version 105.
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;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
OC   Pecora; Bovidae; Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Submandibular gland;
RX   PubMed=8761494;
RA   Jiang W., Woitach J.T., Gupta D.;
RT   "Sequence of bovine carbonic anhydrase VI: potential recognition sites
RT   for N-acetylgalactosaminyltransferase.";
RL   Biochem. J. 318:291-296(1996).
RN   [2]
RP   PROTEIN SEQUENCE OF 15-39.
RX   PubMed=2497732;
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
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.
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DR   EMBL; X96503; CAA65357.1; -; mRNA.
DR   PIR; S71877; S71877.
DR   RefSeq; NP_776323.1; NM_173898.2.
DR   UniGene; Bt.47; -.
DR   ProteinModelPortal; P18915; -.
DR   STRING; 9913.ENSBTAP00000012525; -.
DR   BindingDB; P18915; -.
DR   ChEMBL; CHEMBL2096971; -.
DR   PRIDE; P18915; -.
DR   GeneID; 280742; -.
DR   KEGG; bta:280742; -.
DR   CTD; 765; -.
DR   eggNOG; COG3338; -.
DR   HOGENOM; HOG000112637; -.
DR   HOVERGEN; HBG002837; -.
DR   InParanoid; P18915; -.
DR   KO; K01672; -.
DR   NextBio; 20804913; -.
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; Carbonic_anhydrase_a.
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:SF17; PTHR18952:SF17; 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   Complete proteome; Direct protein sequencing; Disulfide bond;
KW   Glycoprotein; Lyase; Metal-binding; Reference proteome; Secreted;
KW   Signal; Zinc.
FT   SIGNAL        1     14
FT   CHAIN        15    319       Carbonic anhydrase 6.
FT                                /FTId=PRO_0000004239.
FT   REGION      215    216       Substrate binding (By similarity).
FT   ACT_SITE     80     80       Proton acceptor (By similarity).
FT   ACT_SITE    141    141       By similarity.
FT   METAL       106    106       Zinc; catalytic (By similarity).
FT   METAL       108    108       Zinc; catalytic (By similarity).
FT   METAL       133    133       Zinc; catalytic (By similarity).
FT   CARBOHYD     62     62       N-linked (GlcNAc...).
FT   CARBOHYD    251    251       N-linked (GlcNAc...).
FT   DISULFID     37    219       Potential.
FT   CONFLICT     16     16       H -> S (in Ref. 2; AA sequence).
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
//
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