CAH3_RAT
ID CAH3_RAT Reviewed; 260 AA.
AC P14141; O54961; Q9QV77;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 187.
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:2852973};
DE AltName: Full=Carbonic anhydrase III {ECO:0000303|PubMed:2852973};
DE Short=CA-III {ECO:0000303|PubMed:2852973};
GN Name=Ca3;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2852973; DOI=10.1007/bf01121636;
RA Kelly C.D., Carter N.D., Jeffery S., Edwards Y.H.;
RT "Characterisation of cDNA clones for rat muscle carbonic anhydrase III.";
RL Biosci. Rep. 8:401-406(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION.
RC STRAIN=Wistar; TISSUE=Liver, and Soleus muscle;
RX PubMed=10900145; DOI=10.1006/abbi.2000.1911;
RA Ikeda M., Ishii Y., Kato H., Akazawa D., Hatsumura M., Ishida T.,
RA Matsusue K., Yamada H., Oguri K.;
RT "Suppression of carbonic anhydrase III in rat liver by a dioxin-related
RT toxic compound, coplanar polychlorinated biphenyl, 3,3',4,4',5-
RT pentachlorobiphenyl.";
RL Arch. Biochem. Biophys. 380:159-164(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN
RP COMPLEX WITH ZINC ION AND GLUTATHIONE, GLUTATHIONYLATION AT CYS-182 AND
RP CYS-187, AND COFACTOR.
RC TISSUE=Liver;
RX PubMed=11024467; DOI=10.1016/s0014-5793(00)02022-6;
RA Mallis R.J., Poland B.W., Chatterjee T.K., Fisher R.A., Darmawan S.,
RA Honzatko R.B., Thomas J.A.;
RT "Crystal structure of S-glutathiolated carbonic anhydrase III.";
RL FEBS Lett. 482:237-241(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate;
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 [5]
RP PROTEIN SEQUENCE OF 19-45 AND 120-142, AND TISSUE SPECIFICITY.
RC STRAIN=Zucker;
RX PubMed=8476041; DOI=10.1152/ajpendo.1993.264.4.e621;
RA Lynch C.J., Brennan W.A. Jr., Vary T.C., Carter N., Dodgson S.J.;
RT "Carbonic anhydrase III in obese Zucker rats.";
RL Am. J. Physiol. 264:E621-E630(1993).
RN [6]
RP PROTEIN SEQUENCE OF 19-33.
RC TISSUE=Liver;
RX PubMed=1659965; DOI=10.1016/0305-0491(91)90029-d;
RA Nagase T., Sugiyama T., Kawata S., Tarui S., Deutsch H.F., Taniguchi N.;
RT "Analyses of polypeptides in the liver of a novel mutant (LEC rats) to
RT hereditary hepatitis and hepatoma by two-dimensional gel electrophoresis:
RT identification of P29/6.8 as carbonic anhydrase III and triosephosphate
RT isomerase.";
RL Comp. Biochem. Physiol. 99B:193-201(1991).
RN [7]
RP PROTEIN SEQUENCE OF 25-35; 40-57; 68-76; 81-89; 114-135; 189-201 AND
RP 225-239.
RC TISSUE=Liver;
RX PubMed=1899179; DOI=10.1016/0003-9861(91)90295-t;
RA Chai Y.-C., Jung C.-H., Lii C.-K., Ashraf S.S., Hendrich S., Wolf B.,
RA Sies H., Thomas J.A.;
RT "Identification of an abundant S-thiolated rat liver protein as carbonic
RT anhydrase III; characterization of S-thiolation and dethiolation
RT reactions.";
RL Arch. Biochem. Biophys. 284:270-278(1991).
RN [8]
RP PROTEIN SEQUENCE OF 113-125 AND 136-148, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Spinal cord;
RA Lubec G., Afjehi-Sadat L.;
RL Submitted (DEC-2006) to UniProtKB.
RN [9]
RP INDUCTION.
RX PubMed=15930751; DOI=10.1248/bpb.28.1087;
RA Ishii Y., Akazawa D., Aoki Y., Yamada H., Oguri K.;
RT "Suppression of carbonic anhydrase III mRNA level by an aryl hydrocarbon
RT receptor ligand in primary cultured hepatocytes of rat.";
RL Biol. Pharm. Bull. 28:1087-1090(2005).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-29; SER-43; SER-48; SER-50;
RP SER-55; THR-73; TYR-127; THR-129; THR-216 AND SER-219, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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:0000269|PubMed:11024467};
CC -!- ACTIVITY REGULATION: Inhibited by acetazolamide.
CC {ECO:0000250|UniProtKB:P07451}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P07451}.
CC -!- TISSUE SPECIFICITY: Expressed in liver and muscle.
CC {ECO:0000269|PubMed:8476041}.
CC -!- INDUCTION: Repressed by 3,3',4,4',5-pentachlorobiphenyl (PenCB) and 3-
CC methylchlantherene (3MC). {ECO:0000269|PubMed:10900145,
CC ECO:0000269|PubMed:15930751}.
CC -!- PTM: S-thiolated both by thiol-disulfide exchange with glutathione
CC disulfide and by oxyradical-initiated S-thiolation with reduced
CC glutathione. {ECO:0000269|PubMed:11024467}.
CC -!- PTM: S-glutathionylated in hepatocytes under oxidative stress.
CC {ECO:0000269|PubMed:11024467}.
CC -!- MISCELLANEOUS: Expressed at much higher levels in the adipocytes of
CC lean Zucker rats than in obese Zucker rats. Expression is higher is the
CC adipocytes of male Zucker rats than in female Zucker rats.
CC {ECO:0000269|PubMed:8476041}.
CC -!- SIMILARITY: Belongs to the alpha-carbonic anhydrase family.
CC {ECO:0000305}.
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DR EMBL; M22413; AAA40846.1; -; mRNA.
DR EMBL; AB030829; BAB08111.1; -; mRNA.
DR EMBL; AB030830; BAB20673.1; -; mRNA.
DR EMBL; AF037072; AAB92558.1; -; mRNA.
DR EMBL; BC061980; AAH61980.1; -; mRNA.
DR PIR; I52551; I52551.
DR RefSeq; NP_062165.2; NM_019292.4.
DR RefSeq; XP_006232178.1; XM_006232116.1.
DR PDB; 1FLJ; X-ray; 1.80 A; A=2-259.
DR PDBsum; 1FLJ; -.
DR AlphaFoldDB; P14141; -.
DR SMR; P14141; -.
DR IntAct; P14141; 2.
DR STRING; 10116.ENSRNOP00000014177; -.
DR CarbonylDB; P14141; -.
DR iPTMnet; P14141; -.
DR PhosphoSitePlus; P14141; -.
DR PaxDb; P14141; -.
DR PRIDE; P14141; -.
DR Ensembl; ENSRNOT00000105296; ENSRNOP00000083954; ENSRNOG00000010079.
DR GeneID; 54232; -.
DR KEGG; rno:54232; -.
DR UCSC; RGD:2241; rat.
DR CTD; 761; -.
DR RGD; 2241; Ca3.
DR eggNOG; KOG0382; Eukaryota.
DR GeneTree; ENSGT00940000159435; -.
DR HOGENOM; CLU_039326_2_1_1; -.
DR InParanoid; P14141; -.
DR OMA; ERWHENY; -.
DR OrthoDB; 1377476at2759; -.
DR PhylomeDB; P14141; -.
DR TreeFam; TF316425; -.
DR BRENDA; 4.2.1.1; 5301.
DR Reactome; R-RNO-1475029; Reversible hydration of carbon dioxide.
DR EvolutionaryTrace; P14141; -.
DR PRO; PR:P14141; -.
DR Proteomes; UP000002494; Chromosome 2.
DR Bgee; ENSRNOG00000010079; Expressed in esophagus and 20 other tissues.
DR Genevisible; P14141; RN.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
DR GO; GO:0004089; F:carbonate dehydratase activity; ISO:RGD.
DR GO; GO:0016836; F:hydro-lyase activity; IBA:GO_Central.
DR GO; GO:0016151; F:nickel cation binding; ISO:RGD.
DR GO; GO:0016791; F:phosphatase activity; IDA:CACAO.
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; ISO:RGD.
DR GO; GO:0045471; P:response to ethanol; IEP:RGD.
DR GO; GO:0006979; P:response to oxidative stress; IMP:RGD.
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 3D-structure; Acetylation; Cytoplasm; Direct protein sequencing;
KW Disulfide bond; Glutathionylation; Lyase; Metal-binding; Phosphoprotein;
KW 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_0000077429"
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:0000269|PubMed:11024467"
FT BINDING 96
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:11024467"
FT BINDING 119
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:11024467"
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:0007744|PubMed:22673903"
FT MOD_RES 43
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 48
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 50
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 55
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 73
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 127
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 129
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 182
FT /note="S-glutathionyl cysteine"
FT /evidence="ECO:0000269|PubMed:11024467"
FT MOD_RES 187
FT /note="S-glutathionyl cysteine"
FT /evidence="ECO:0000269|PubMed:11024467"
FT MOD_RES 216
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 219
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT CONFLICT 8
FT /note="A -> G (in Ref. 1; AAA40846)"
FT /evidence="ECO:0000305"
FT CONFLICT 34
FT /note="H -> HI (in Ref. 7; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 57
FT /note="K -> R (in Ref. 7; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 126
FT /note="K -> DR (in Ref. 7; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 130..131
FT /note="FG -> SE (in Ref. 1; AAA40846)"
FT /evidence="ECO:0000305"
FT CONFLICT 135
FT /note="K -> R (in Ref. 7; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 189..191
FT /note="DYW -> QYP (in Ref. 7; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 224..225
FT /note="KL -> NV (in Ref. 1; AAA40846)"
FT /evidence="ECO:0000305"
FT CONFLICT 225..226
FT /note="LR -> DE (in Ref. 7; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 230
FT /note="A -> G (in Ref. 7; AA sequence)"
FT /evidence="ECO:0000305"
FT TURN 9..11
FT /evidence="ECO:0007829|PDB:1FLJ"
FT HELIX 13..18
FT /evidence="ECO:0007829|PDB:1FLJ"
FT HELIX 21..24
FT /evidence="ECO:0007829|PDB:1FLJ"
FT STRAND 25..27
FT /evidence="ECO:0007829|PDB:1FLJ"
FT HELIX 35..37
FT /evidence="ECO:0007829|PDB:1FLJ"
FT STRAND 38..40
FT /evidence="ECO:0007829|PDB:1FLJ"
FT STRAND 47..50
FT /evidence="ECO:0007829|PDB:1FLJ"
FT HELIX 53..55
FT /evidence="ECO:0007829|PDB:1FLJ"
FT STRAND 56..61
FT /evidence="ECO:0007829|PDB:1FLJ"
FT STRAND 66..70
FT /evidence="ECO:0007829|PDB:1FLJ"
FT STRAND 73..81
FT /evidence="ECO:0007829|PDB:1FLJ"
FT STRAND 88..97
FT /evidence="ECO:0007829|PDB:1FLJ"
FT STRAND 106..109
FT /evidence="ECO:0007829|PDB:1FLJ"
FT STRAND 115..123
FT /evidence="ECO:0007829|PDB:1FLJ"
FT HELIX 125..127
FT /evidence="ECO:0007829|PDB:1FLJ"
FT HELIX 130..133
FT /evidence="ECO:0007829|PDB:1FLJ"
FT STRAND 139..151
FT /evidence="ECO:0007829|PDB:1FLJ"
FT HELIX 154..162
FT /evidence="ECO:0007829|PDB:1FLJ"
FT HELIX 163..166
FT /evidence="ECO:0007829|PDB:1FLJ"
FT STRAND 172..174
FT /evidence="ECO:0007829|PDB:1FLJ"
FT HELIX 180..183
FT /evidence="ECO:0007829|PDB:1FLJ"
FT STRAND 190..195
FT /evidence="ECO:0007829|PDB:1FLJ"
FT STRAND 206..213
FT /evidence="ECO:0007829|PDB:1FLJ"
FT STRAND 215..217
FT /evidence="ECO:0007829|PDB:1FLJ"
FT HELIX 219..225
FT /evidence="ECO:0007829|PDB:1FLJ"
FT STRAND 229..231
FT /evidence="ECO:0007829|PDB:1FLJ"
FT STRAND 255..258
FT /evidence="ECO:0007829|PDB:1FLJ"
SQ SEQUENCE 260 AA; 29431 MW; C3C7DA7DA8793F18 CRC64;
MAKEWGYASH NGPEHWHELY PIAKGDNQSP IELHTKDIRH DPSLQPWSVS YDPGSAKTIL
NNGKTCRVVF DDTFDRSMLR GGPLSGPYRL RQFHLHWGSS DDHGSEHTVD GVKYAAELHL
VHWNPKYNTF GEALKQPDGI AVVGIFLKIG REKGEFQILL DALDKIKTKG KEAPFNHFDP
SCLFPACRDY WTYHGSFTTP PCEECIVWLL LKEPMTVSSD QMAKLRSLFA SAENEPPVPL
VGNWRPPQPI KGRVVRASFK
