CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-005199
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Carbonic anhydrase 5A, mitochondrial 
Protein Synonyms/Alias
 Carbonate dehydratase VA; CA Y; Carbonic anhydrase VA; CA-VA 
Gene Name
 Ca5a 
Gene Synonyms/Alias
 Ca5; Car5; Car5a 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
66SPINIQWKDSVYDPQacetylation[1, 2]
66SPINIQWKDSVYDPQsuccinylation[1]
162STKYENYKKASVGENacetylation[2]
189AHHQALQKLVDVLPEacetylation[3]
243SVTWIVQKTPVEVSPacetylation[4]
Reference
 [1] 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]
 [2] 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]
 [3] 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]
 [4] 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
Functional Description
 Reversible hydration of carbon dioxide. Low activity. 
Sequence Annotation
 REGION 229 230 Substrate binding (By similarity).
 ACT_SITE 94 94 Probable.
 ACT_SITE 158 158 By similarity.
 ACT_SITE 161 161 Probable.
 METAL 124 124 Zinc; catalytic.
 METAL 126 126 Zinc; catalytic.
 METAL 149 149 Zinc; catalytic.  
Keyword
 3D-structure; Complete proteome; Direct protein sequencing; Lyase; Metal-binding; Mitochondrion; Reference proteome; Transit peptide; Zinc. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 299 AA 
Protein Sequence
MLRRDPRKPL AILRHVGLLC ATGPQRWRFQ HSCAEEHSNC ARHPLWTGPV SSAEGTRQSP 60
INIQWKDSVY DPQLAPLRVS YDAASCRYLW NTGYFFQVEF DDSCEDSGIS GGPLGNHYRL 120
KQFHFHWGAT DEWGSEHAVD GHTYPAELHL VHWNSTKYEN YKKASVGENG LAVIGVFLKL 180
GAHHQALQKL VDVLPEVRHK DTQVAMGPFD PSCLLPACRD YWTYPGSLTT PPLAESVTWI 240
VQKTPVEVSP SQLSTFRTLL FSGRGEEEDV MVNNYRPLQP LRDRKLRSSF RLDRTKMRS 299 
Gene Ontology
 GO:0005739; C:mitochondrion; IDA:MGI.
 GO:0004089; F:carbonate dehydratase activity; IDA:MGI.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0006094; P:gluconeogenesis; TAS:MGI.
 GO:0006730; P:one-carbon metabolic process; IEA:InterPro. 
Interpro
 IPR018437; CA-V_mt.
 IPR001148; Carbonic_anhydrase_a.
 IPR023561; Carbonic_anhydrase_a-class.
 IPR018338; Carbonic_anhydrase_a-class_CS. 
Pfam
 PF00194; Carb_anhydrase 
SMART
 SM01057; Carb_anhydrase 
PROSITE
 PS00162; ALPHA_CA_1
 PS51144; ALPHA_CA_2 
PRINTS