CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-004404
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Carbonic anhydrase 3 
Protein Synonyms/Alias
 Carbonate dehydratase III; Carbonic anhydrase III; CA-III 
Gene Name
 Ca3 
Gene Synonyms/Alias
 Car3 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
3*****MAKEWGYASHacetylation[1]
3*****MAKEWGYASHubiquitination[2]
24HELYPIAKGDNQSPIubiquitination[2]
36SPIELHTKDIKHDPSacetylation[1, 3, 4, 5]
36SPIELHTKDIKHDPSubiquitination[2]
39ELHTKDIKHDPSLQPacetylation[3, 4, 5, 6]
39ELHTKDIKHDPSLQPubiquitination[2]
57SYDPGSAKTILNNGKacetylation[5]
57SYDPGSAKTILNNGKubiquitination[2]
64KTILNNGKTCRVVFDacetylation[3, 7]
64KTILNNGKTCRVVFDphosphoglycerylation[8]
64KTILNNGKTCRVVFDsuccinylation[7]
64KTILNNGKTCRVVFDubiquitination[2]
126HLVHWNPKYNTFGEAacetylation[3]
126HLVHWNPKYNTFGEAubiquitination[2]
135NTFGEALKQPDGIAVacetylation[3, 6]
135NTFGEALKQPDGIAVubiquitination[2]
153FLKIGREKGEFQILLacetylation[3]
153FLKIGREKGEFQILLubiquitination[2]
165ILLDALDKIKTKGKEacetylation[3]
165ILLDALDKIKTKGKEubiquitination[2]
171DKIKTKGKEAPFTHFacetylation[4]
171DKIKTKGKEAPFTHFubiquitination[2]
212CIVWLLLKEPMTVSSacetylation[3, 4]
224VSSDQMAKLRSLFSSubiquitination[2]
251WRPPQPVKGRVVRASubiquitination[2]
Reference
 [1] Circadian acetylome reveals regulation of mitochondrial metabolic pathways.
 Masri S, Patel VR, Eckel-Mahan KL, Peleg S, Forne I, Ladurner AG, Baldi P, Imhof A, Sassone-Corsi P.
 Proc Natl Acad Sci U S A. 2013 Feb 26;110(9):3339-44. [PMID: 23341599]
 [2] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]
 [3] Quantitative assessment of the impact of the gut microbiota on lysine epsilon-acetylation of host proteins using gnotobiotic mice.
 Simon GM, Cheng J, Gordon JI.
 Proc Natl Acad Sci U S A. 2012 Jul 10;109(28):11133-8. [PMID: 22733758]
 [4] Calorie restriction and SIRT3 trigger global reprogramming of the mitochondrial protein acetylome.
 Hebert AS, Dittenhafer-Reed KE, Yu W, Bailey DJ, Selen ES, Boersma MD, Carson JJ, Tonelli M, Balloon AJ, Higbee AJ, Westphall MS, Pagliarini DJ, Prolla TA, Assadi-Porter F, Roy S, Denu JM, Coon JJ.
 Mol Cell. 2013 Jan 10;49(1):186-99. [PMID: 23201123]
 [5] Quantification of mitochondrial acetylation dynamics highlights prominent sites of metabolic regulation.
 Still AJ, Floyd BJ, Hebert AS, Bingman CA, Carson JJ, Gunderson DR, Dolan BK, Grimsrud PA, Dittenhafer-Reed KE, Stapleton DS, Keller MP, Westphall MS, Denu JM, Attie AD, Coon JJ, Pagliarini DJ.
 J Biol Chem. 2013 Jul 17;. [PMID: 23864654]
 [6] The fasted/fed mouse metabolic acetylome: N6-acetylation differences suggest acetylation coordinates organ-specific fuel switching.
 Yang L, Vaitheesvaran B, Hartil K, Robinson AJ, Hoopmann MR, Eng JK, Kurland IJ, Bruce JE.
 J Proteome Res. 2011 Sep 2;10(9):4134-49. [PMID: 21728379]
 [7] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
 Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
 Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337]
 [8] Functional lysine modification by an intrinsically reactive primary glycolytic metabolite.
 Moellering RE, Cravatt BF.
 Science. 2013 Aug 2;341(6145):549-53. [PMID: 23908237
Functional Description
 Reversible hydration of carbon dioxide. 
Sequence Annotation
 REGION 64 67 Involved in proton transfer (By
 REGION 198 199 Substrate binding (By similarity).
 ACT_SITE 127 127 By similarity.
 METAL 94 94 Zinc; catalytic.
 METAL 96 96 Zinc; catalytic.
 METAL 119 119 Zinc; catalytic.
 MOD_RES 2 2 N-acetylalanine (By similarity).
 MOD_RES 182 182 S-glutathionyl cysteine (By similarity).
 MOD_RES 187 187 S-glutathionyl cysteine (By similarity).  
Keyword
 Acetylation; Complete proteome; Cytoplasm; Direct protein sequencing; Glutathionylation; Lyase; Metal-binding; Reference proteome; Zinc. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 260 AA 
Protein Sequence
MAKEWGYASH NGPDHWHELY PIAKGDNQSP IELHTKDIKH DPSLQPWSAS YDPGSAKTIL 60
NNGKTCRVVF DDTYDRSMLR GGPLSGPYRL RQFHLHWGSS DDHGSEHTVD GVKYAAELHL 120
VHWNPKYNTF GEALKQPDGI AVVGIFLKIG REKGEFQILL DALDKIKTKG KEAPFTHFDP 180
SCLFPACRDY WTYHGSFTTP PCEECIVWLL LKEPMTVSSD QMAKLRSLFS SAENEPPVPL 240
VGNWRPPQPV KGRVVRASFK 260 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0004089; F:carbonate dehydratase activity; IEA:EC.
 GO:0016151; F:nickel cation binding; IDA:MGI.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0006730; P:one-carbon metabolic process; IEA:InterPro.
 GO:0006979; P:response to oxidative stress; IEA:Compara. 
Interpro
 IPR001148; Carbonic_anhydrase_a.
 IPR023561; Carbonic_anhydrase_a-class.
 IPR018338; Carbonic_anhydrase_a-class_CS.
 IPR018441; Carbonic_anhydrase_CA3. 
Pfam
 PF00194; Carb_anhydrase 
SMART
 SM01057; Carb_anhydrase 
PROSITE
 PS00162; ALPHA_CA_1
 PS51144; ALPHA_CA_2 
PRINTS