CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-013117
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Methylcrotonoyl-CoA carboxylase beta chain, mitochondrial 
Protein Synonyms/Alias
 MCCase subunit beta; 3-methylcrotonyl-CoA carboxylase 2; 3-methylcrotonyl-CoA carboxylase non-biotin-containing subunit; 3-methylcrotonyl-CoA:carbon dioxide ligase subunit beta 
Gene Name
 Mccc2 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
50QENYEQMKALVSQLHacetylation[1, 2, 3]
70VRLGGSEKARARHTSacetylation[2, 3, 4, 5]
70VRLGGSEKARARHTSsuccinylation[5]
141VANDATVKGGTYYPVacetylation[5]
141VANDATVKGGTYYPVsuccinylation[5]
433VAAVACAKVPKITVIacetylation[5]
433VAAVACAKVPKITVIsuccinylation[5]
495DQKAREGKQFSSAEEacetylation[2, 3, 4, 5]
495DQKAREGKQFSSAEEsuccinylation[5]
506SAEEAALKEPIIKRFacetylation[2]
511ALKEPIIKRFEEEGNacetylation[2, 4]
Reference
 [1] 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]
 [2] 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]
 [3] 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]
 [4] Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways.
 Rardin MJ, Newman JC, Held JM, Cusack MP, Sorensen DJ, Li B, Schilling B, Mooney SD, Kahn CR, Verdin E, Gibson BW.
 Proc Natl Acad Sci U S A. 2013 Apr 16;110(16):6601-6. [PMID: 23576753]
 [5] 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
Functional Description
 Carboxyltransferase subunit of the 3-methylcrotonyl-CoA carboxylase, an enzyme that catalyzes the conversion of 3- methylcrotonyl-CoA to 3-methylglutaconyl-CoA, a critical step for leucine and isovaleric acid catabolism (By similarity). 
Sequence Annotation
 DOMAIN 55 557 Carboxyltransferase.
 REGION 343 372 Acyl-CoA binding (Potential).  
Keyword
 ATP-binding; Complete proteome; Ligase; Mitochondrion; Nucleotide-binding; Reference proteome; Transit peptide. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 563 AA 
Protein Sequence
MWGALRSALR PCCRAAVPPQ RAYHGDSVAR LGTQPDSASS TYQENYEQMK ALVSQLHERA 60
QYVRLGGSEK ARARHTSRGK LLPRDRIDNL IDPGSPFLEF SQFAGYQLYG DEEVPAGGII 120
TGIGRVSGVE CMIVANDATV KGGTYYPVTV KKHVRAQEIA LQNRLPCIYL VDSGGANLPR 180
QADTFPDRDH FGRIFYNQAI MSSKNITQIA VVMGSCTAGG AYVPAMADEN IIVQKQGTIF 240
LAGPPLVKAA TGEEVSAEDL GGADLHCRKS GVTDHYALDD HHALHLTRKV VRSLNYQKKM 300
DVTIEPSEEP LFPADELYGI VGANLKRSFD VREVIARIVD GSRFNEFKAL YGDTLVTGFA 360
RIFGYPVGII GNNGVLFSES AKKGAHFVQL CCQRNIPLLF LQNITGFMVG RDYEAEGIAK 420
DGAKMVAAVA CAKVPKITVI IGGSYGAGNY GMCGRAYSPR FLYMWPNARI SVMGGEQAAT 480
VLATVARDQK AREGKQFSSA EEAALKEPII KRFEEEGNPY YSSARLWDDG IIDPVDTRLV 540
LGLSLSAALN APIQRTDFGI FRM 563 
Gene Ontology
 GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
 GO:0005739; C:mitochondrion; IDA:MGI.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0004485; F:methylcrotonoyl-CoA carboxylase activity; ISS:UniProtKB.
 GO:0015936; P:coenzyme A metabolic process; IEA:Compara.
 GO:0006552; P:leucine catabolic process; IEA:UniProtKB-UniPathway. 
Interpro
 IPR000022; Carboxyl_trans.
 IPR011763; COA_CT_C.
 IPR011762; COA_CT_N. 
Pfam
 PF01039; Carboxyl_trans 
SMART
  
PROSITE
 PS50989; COA_CT_CTER
 PS50980; COA_CT_NTER 
PRINTS