CAH6_MOUSE
ID CAH6_MOUSE Reviewed; 317 AA.
AC P18761; B1ARR5; O88625;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 168.
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; Synonyms=Car6;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=CD-1; TISSUE=Salivary gland;
RX PubMed=9858573; DOI=10.1128/mcb.19.1.495;
RA Sok J., Wang X.Z., Batchvarova N., Kuroda M., Harding H., Ron D.;
RT "CHOP-dependent stress-inducible expression of a novel form of carbonic
RT anhydrase VI.";
RL Mol. Cell. Biol. 19:495-504(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP PROTEIN SEQUENCE OF 18-38.
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; AF079835; AAD12540.1; -; mRNA.
DR EMBL; AL606903; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466594; EDL14887.1; -; Genomic_DNA.
DR CCDS; CCDS51386.1; -.
DR PIR; S03863; S03863.
DR RefSeq; NP_033932.2; NM_009802.2.
DR AlphaFoldDB; P18761; -.
DR SMR; P18761; -.
DR STRING; 10090.ENSMUSP00000030817; -.
DR GlyGen; P18761; 1 site.
DR MaxQB; P18761; -.
DR PaxDb; P18761; -.
DR PeptideAtlas; P18761; -.
DR PRIDE; P18761; -.
DR ProteomicsDB; 281757; -.
DR Antibodypedia; 27596; 354 antibodies from 29 providers.
DR DNASU; 12353; -.
DR Ensembl; ENSMUST00000030817; ENSMUSP00000030817; ENSMUSG00000028972.
DR GeneID; 12353; -.
DR KEGG; mmu:12353; -.
DR UCSC; uc008vxm.1; mouse.
DR CTD; 12353; -.
DR MGI; MGI:1333786; Car6.
DR VEuPathDB; HostDB:ENSMUSG00000028972; -.
DR eggNOG; KOG0382; Eukaryota.
DR GeneTree; ENSGT00940000160409; -.
DR InParanoid; P18761; -.
DR OMA; RAVEANF; -.
DR OrthoDB; 1377476at2759; -.
DR PhylomeDB; P18761; -.
DR TreeFam; TF316425; -.
DR Reactome; R-MMU-1475029; Reversible hydration of carbon dioxide.
DR BioGRID-ORCS; 12353; 4 hits in 74 CRISPR screens.
DR ChiTaRS; Car6; mouse.
DR PRO; PR:P18761; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; P18761; protein.
DR Bgee; ENSMUSG00000028972; Expressed in submandibular gland and 38 other tissues.
DR ExpressionAtlas; P18761; baseline and differential.
DR Genevisible; P18761; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0005615; C:extracellular space; IDA:MGI.
DR GO; GO:0004089; F:carbonate dehydratase activity; IBA:GO_Central.
DR GO; GO:0016836; F:hydro-lyase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0001580; P:detection of chemical stimulus involved in sensory perception of bitter taste; ISO:MGI.
DR GO; GO:0006730; P:one-carbon metabolic process; IBA:GO_Central.
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; 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; 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..17
FT /evidence="ECO:0000269|PubMed:2497732"
FT CHAIN 18..317
FT /note="Carbonic anhydrase 6"
FT /id="PRO_0000004242"
FT DOMAIN 19..277
FT /note="Alpha-carbonic anhydrase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01134"
FT ACT_SITE 84
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P00918"
FT BINDING 110
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P23280"
FT BINDING 112
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P23280"
FT BINDING 137
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P23280"
FT BINDING 219..220
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00918"
FT CARBOHYD 255
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 41..223
FT /evidence="ECO:0000255"
FT CONFLICT 18
FT /note="H -> G (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 35
FT /note="S -> T (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 185
FT /note="N -> D (in Ref. 1; AAD12540)"
FT /evidence="ECO:0000305"
FT CONFLICT 202
FT /note="N -> D (in Ref. 1; AAD12540)"
FT /evidence="ECO:0000305"
FT CONFLICT 235
FT /note="K -> R (in Ref. 1; AAD12540)"
FT /evidence="ECO:0000305"
FT CONFLICT 281
FT /note="Q -> P (in Ref. 1; AAD12540)"
FT /evidence="ECO:0000305"
FT CONFLICT 291
FT /note="L -> P (in Ref. 1; AAD12540)"
FT /evidence="ECO:0000305"
FT CONFLICT 314
FT /note="W -> G (in Ref. 1; AAD12540)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 317 AA; 36495 MW; 6A933F9551954240 CRC64;
MRALVSVVSL FFLGIQAHSD WSYSGDDGVG ESQWSEQYPS CGGERQSPID VKTEEVMFNP
SLKPLSLVNY EKENLEFTMT NNGHTVSIDL PPSMYLETSD GTEFISKAFH FHWGGRDWEL
SGSEHTIDGI RSIMEAHFVH FNKEYGTYEN AKDQKNGLAV LAVLFKIDEY AENTYYSDII
SALKNIEKPG ETTTLKDTTI RNLLPKDVHH YYTYPGSLTT PPCTENVQWF VLRDKVTLSK
AQVVTIENSV MDHNNNTIQN GYRSTQPNNH RVVEANFLNV QDMYSSYHLY LKNMQKEILQ
PKKQKKTKKN RHFWSRK
