CAH7_MOUSE
ID CAH7_MOUSE Reviewed; 264 AA.
AC Q9ERQ8; Q811X4;
DT 09-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2005, sequence version 2.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Carbonic anhydrase 7;
DE EC=4.2.1.1;
DE AltName: Full=Carbonate dehydratase VII;
DE AltName: Full=Carbonic anhydrase VII;
DE Short=CA-VII;
GN Name=Ca7; Synonyms=Car7;
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].
RA Chen Y., Huang C.-H.;
RT "Molecular identification of carbonic anhydrases (CA) and CA-related (CAR)
RT genes.";
RL Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 10-264.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Ling B., Bergenhem N.C.H., Tashian R.E.;
RT "Conservation of the deduced amino acid sequences of human and mouse
RT carbonic anhydrase VII cDNAs.";
RL Isozyme Bull. 28:32-32(1995).
RN [4]
RP CHARACTERIZATION.
RX PubMed=9692974; DOI=10.1021/bi980046t;
RA Earnhardt J.N., Qian M., Tu C., Lakkis M.M., Bergenhem N.C., Laipis P.J.,
RA Tashian R.E., Silverman D.N.;
RT "The catalytic properties of murine carbonic anhydrase VII.";
RL Biochemistry 37:10837-10845(1998).
CC -!- FUNCTION: Reversible hydration of carbon dioxide.
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:P43166};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the alpha-carbonic anhydrase family.
CC {ECO:0000305}.
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DR EMBL; AY075021; AAL78169.1; -; mRNA.
DR EMBL; BC094913; AAH94913.1; -; mRNA.
DR EMBL; AF291660; AAG16230.1; -; mRNA.
DR CCDS; CCDS22581.1; -.
DR RefSeq; NP_001288093.1; NM_001301164.1.
DR RefSeq; NP_001288094.1; NM_001301165.1.
DR RefSeq; NP_444300.1; NM_053070.3.
DR AlphaFoldDB; Q9ERQ8; -.
DR SMR; Q9ERQ8; -.
DR STRING; 10090.ENSMUSP00000052136; -.
DR BindingDB; Q9ERQ8; -.
DR ChEMBL; CHEMBL2216; -.
DR DrugCentral; Q9ERQ8; -.
DR PhosphoSitePlus; Q9ERQ8; -.
DR CPTAC; non-CPTAC-3421; -.
DR CPTAC; non-CPTAC-3693; -.
DR PaxDb; Q9ERQ8; -.
DR PRIDE; Q9ERQ8; -.
DR ProteomicsDB; 265502; -.
DR Antibodypedia; 29327; 135 antibodies from 27 providers.
DR DNASU; 12354; -.
DR Ensembl; ENSMUST00000056051; ENSMUSP00000052136; ENSMUSG00000031883.
DR GeneID; 12354; -.
DR KEGG; mmu:12354; -.
DR UCSC; uc009nat.2; mouse.
DR CTD; 12354; -.
DR MGI; MGI:103100; Car7.
DR VEuPathDB; HostDB:ENSMUSG00000031883; -.
DR eggNOG; KOG0382; Eukaryota.
DR GeneTree; ENSGT00940000159757; -.
DR InParanoid; Q9ERQ8; -.
DR OMA; RMRMENN; -.
DR OrthoDB; 1377476at2759; -.
DR PhylomeDB; Q9ERQ8; -.
DR TreeFam; TF316425; -.
DR Reactome; R-MMU-1475029; Reversible hydration of carbon dioxide.
DR BioGRID-ORCS; 12354; 2 hits in 72 CRISPR screens.
DR PRO; PR:Q9ERQ8; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q9ERQ8; protein.
DR Bgee; ENSMUSG00000031883; Expressed in yolk sac and 122 other tissues.
DR ExpressionAtlas; Q9ERQ8; baseline and differential.
DR Genevisible; Q9ERQ8; MM.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0004089; F:carbonate dehydratase activity; IMP:MGI.
DR GO; GO:0016836; F:hydro-lyase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0070050; P:neuron cellular homeostasis; IMP:MGI.
DR GO; GO:0006730; P:one-carbon metabolic process; IBA:GO_Central.
DR GO; GO:0032849; P:positive regulation of cellular pH reduction; IMP:MGI.
DR GO; GO:0032230; P:positive regulation of synaptic transmission, GABAergic; IGI:MGI.
DR GO; GO:2001225; P:regulation of chloride transport; IMP:MGI.
DR GO; GO:0051453; P:regulation of intracellular pH; IBA:GO_Central.
DR CDD; cd03149; alpha_CA_VII; 1.
DR Gene3D; 3.10.200.10; -; 1.
DR InterPro; IPR041890; Alpha_CA_VII.
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 PANTHER; PTHR18952; PTHR18952; 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 Cytoplasm; Lyase; Metal-binding; Reference proteome; Zinc.
FT CHAIN 1..264
FT /note="Carbonic anhydrase 7"
FT /id="PRO_0000077432"
FT DOMAIN 5..262
FT /note="Alpha-carbonic anhydrase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01134"
FT ACT_SITE 66
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P00918"
FT BINDING 96
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P43166"
FT BINDING 98
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P43166"
FT BINDING 121
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P43166"
FT BINDING 201..202
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00918"
SQ SEQUENCE 264 AA; 29915 MW; B58E0E20CB840FA5 CRC64;
MTGHHCWGYG QDDGPSNWHK LYPIAQGDRQ SPINIISSQA VYSPSLQPLE LFYEACMSLS
ITNNGHSVQV DFNDSDDRTV VSGGPLEGPY RLKQLHFHWG KKRDMGSEHT VDGKSFPSEL
HLVHWNAKKY STFGEAAAAP DGLAVVGVFL ETGDEHPSMN RLTDALYMVR FKDTKAQFSC
FNPKCLLPTS RHYWTYPGSL TTPPLSESVT WIVLREPIRI SERQMEKFRS LLFTSEDDER
IHMVDNFRPP QPLKGRVVKA SFQA
