CAH3_MOUSE
ID CAH3_MOUSE Reviewed; 260 AA.
AC P16015; Q9ERN8;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Carbonic anhydrase 3;
DE EC=4.2.1.1 {ECO:0000250|UniProtKB:P07451};
DE AltName: Full=Carbonate dehydratase III {ECO:0000303|PubMed:2496681};
DE AltName: Full=Carbonic anhydrase III {ECO:0000303|PubMed:2496681};
DE Short=CA-III {ECO:0000303|PubMed:2496681};
GN Name=Ca3 {ECO:0000312|MGI:MGI:88270}; Synonyms=Car3;
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].
RX PubMed=2496681; DOI=10.1007/bf00563015;
RA Tweedie S., Edwards Y.;
RT "Mouse carbonic anhydrase III: nucleotide sequence and expression
RT studies.";
RL Biochem. Genet. 27:17-30(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/SvJ;
RX PubMed=11255005; DOI=10.1016/s0378-1119(01)00355-9;
RA Kim G., Lee T.-H., Wynshaw-Boris A., Levine R.L.;
RT "Nucleotide sequence and structure of the mouse carbonic anhydrase III
RT gene.";
RL Gene 265:37-44(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver;
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 [4]
RP PROTEIN SEQUENCE OF 79-96, AND TISSUE SPECIFICITY.
RX PubMed=1922100; DOI=10.1210/mend-5-6-860;
RA Stanton L.W., Ponte P.A., Coleman R.T., Snyder M.A.;
RT "Expression of CA III in rodent models of obesity.";
RL Mol. Endocrinol. 5:860-866(1991).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-176, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Reversible hydration of carbon dioxide.
CC {ECO:0000250|UniProtKB:P07451}.
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 Evidence={ECO:0000250|UniProtKB:P07451};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P07451};
CC -!- ACTIVITY REGULATION: Inhibited by acetazolamide.
CC {ECO:0000250|UniProtKB:P07451}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P07451}.
CC -!- TISSUE SPECIFICITY: Expressed at lower levels in adipose tissue from
CC animals that were either genetically obese or had experimentally
CC induced obesity. {ECO:0000269|PubMed:1922100}.
CC -!- PTM: S-thiolated both by thiol-disulfide exchange with glutathione
CC disulfide and by oxyradical-initiated S-thiolation with reduced
CC glutathione. {ECO:0000250|UniProtKB:P14141}.
CC -!- PTM: S-glutathionylated in hepatocytes under oxidative stress.
CC {ECO:0000250|UniProtKB:P14141}.
CC -!- SIMILARITY: Belongs to the alpha-carbonic anhydrase family.
CC {ECO:0000305}.
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DR EMBL; M27796; AAA37355.1; -; mRNA.
DR EMBL; AF294988; AAG22029.1; -; Genomic_DNA.
DR EMBL; AF294983; AAG22029.1; JOINED; Genomic_DNA.
DR EMBL; AF294984; AAG22029.1; JOINED; Genomic_DNA.
DR EMBL; AF294985; AAG22029.1; JOINED; Genomic_DNA.
DR EMBL; AF294986; AAG22029.1; JOINED; Genomic_DNA.
DR EMBL; AF294987; AAG22029.1; JOINED; Genomic_DNA.
DR EMBL; BC011129; AAH11129.1; -; mRNA.
DR CCDS; CCDS17250.1; -.
DR PIR; A43641; A43641.
DR RefSeq; NP_031632.2; NM_007606.3.
DR AlphaFoldDB; P16015; -.
DR SMR; P16015; -.
DR BioGRID; 198484; 4.
DR IntAct; P16015; 2.
DR MINT; P16015; -.
DR STRING; 10090.ENSMUSP00000029076; -.
DR iPTMnet; P16015; -.
DR PhosphoSitePlus; P16015; -.
DR SwissPalm; P16015; -.
DR SWISS-2DPAGE; P16015; -.
DR CPTAC; non-CPTAC-3694; -.
DR jPOST; P16015; -.
DR MaxQB; P16015; -.
DR PaxDb; P16015; -.
DR PeptideAtlas; P16015; -.
DR PRIDE; P16015; -.
DR ProteomicsDB; 265324; -.
DR Antibodypedia; 3326; 454 antibodies from 35 providers.
DR DNASU; 12350; -.
DR Ensembl; ENSMUST00000029076; ENSMUSP00000029076; ENSMUSG00000027559.
DR GeneID; 12350; -.
DR KEGG; mmu:12350; -.
DR UCSC; uc008oqs.1; mouse.
DR CTD; 12350; -.
DR MGI; MGI:88270; Car3.
DR VEuPathDB; HostDB:ENSMUSG00000027559; -.
DR eggNOG; KOG0382; Eukaryota.
DR GeneTree; ENSGT00940000159435; -.
DR HOGENOM; CLU_039326_2_1_1; -.
DR InParanoid; P16015; -.
DR OMA; ERWHENY; -.
DR OrthoDB; 1377476at2759; -.
DR PhylomeDB; P16015; -.
DR TreeFam; TF316425; -.
DR BRENDA; 4.2.1.1; 3474.
DR Reactome; R-MMU-1475029; Reversible hydration of carbon dioxide.
DR BioGRID-ORCS; 12350; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Car3; mouse.
DR PRO; PR:P16015; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; P16015; protein.
DR Bgee; ENSMUSG00000027559; Expressed in intercostal muscle and 216 other tissues.
DR Genevisible; P16015; MM.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0004089; F:carbonate dehydratase activity; ISO:MGI.
DR GO; GO:0016836; F:hydro-lyase activity; IBA:GO_Central.
DR GO; GO:0016151; F:nickel cation binding; IDA:MGI.
DR GO; GO:0016791; F:phosphatase activity; ISO:MGI.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006730; P:one-carbon metabolic process; IBA:GO_Central.
DR GO; GO:0009617; P:response to bacterium; IEP:MGI.
DR GO; GO:0045471; P:response to ethanol; IEA:Ensembl.
DR GO; GO:0006979; P:response to oxidative stress; ISO:MGI.
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; IPR018441; Carbonic_anhydrase_CA3.
DR PANTHER; PTHR18952; PTHR18952; 1.
DR PANTHER; PTHR18952:SF127; PTHR18952:SF127; 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 Acetylation; Cytoplasm; Direct protein sequencing; Glutathionylation;
KW Lyase; Metal-binding; Phosphoprotein; Reference proteome; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P07450"
FT CHAIN 2..260
FT /note="Carbonic anhydrase 3"
FT /id="PRO_0000077427"
FT DOMAIN 3..259
FT /note="Alpha-carbonic anhydrase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01134"
FT REGION 64..67
FT /note="Involved in proton transfer"
FT /evidence="ECO:0000250|UniProtKB:P07451"
FT BINDING 94
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
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:P00918"
FT BINDING 119
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P00918"
FT BINDING 198..199
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00918"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P07450"
FT MOD_RES 29
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P14141"
FT MOD_RES 43
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P14141"
FT MOD_RES 48
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P14141"
FT MOD_RES 50
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P14141"
FT MOD_RES 55
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P14141"
FT MOD_RES 73
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P14141"
FT MOD_RES 127
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P14141"
FT MOD_RES 129
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P14141"
FT MOD_RES 176
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 182
FT /note="S-glutathionyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P14141"
FT MOD_RES 187
FT /note="S-glutathionyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P14141"
FT MOD_RES 216
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P14141"
FT MOD_RES 219
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P14141"
FT CONFLICT 9
FT /note="S -> R (in Ref. 1; AAA37355)"
FT /evidence="ECO:0000305"
FT CONFLICT 86
FT /note="G -> R (in Ref. 1; AAA37355)"
FT /evidence="ECO:0000305"
FT CONFLICT 126
FT /note="K -> R (in Ref. 1; AAA37355)"
FT /evidence="ECO:0000305"
FT CONFLICT 146
FT /note="F -> L (in Ref. 1; AAA37355)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 260 AA; 29366 MW; F4E9FE69A3C324BB CRC64;
MAKEWGYASH NGPDHWHELY PIAKGDNQSP IELHTKDIKH DPSLQPWSAS YDPGSAKTIL
NNGKTCRVVF DDTYDRSMLR GGPLSGPYRL RQFHLHWGSS DDHGSEHTVD GVKYAAELHL
VHWNPKYNTF GEALKQPDGI AVVGIFLKIG REKGEFQILL DALDKIKTKG KEAPFTHFDP
SCLFPACRDY WTYHGSFTTP PCEECIVWLL LKEPMTVSSD QMAKLRSLFS SAENEPPVPL
VGNWRPPQPV KGRVVRASFK
