CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-024346
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Acyl-coenzyme A amino acid N-acyltransferase 1 
Protein Synonyms/Alias
  
Gene Name
 Acnat1 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
38VTIKATVKDENDNVFacetylation[1, 2]
38VTIKATVKDENDNVFubiquitination[3]
138WFVGPGVKREQIQEGacetylation[2]
138WFVGPGVKREQIQEGubiquitination[3]
312KNILPVEKAQGKILFubiquitination[3]
331NDELLDSKLHAQRAMubiquitination[3]
403HSWREIQKFFRKHLLacetylation[1, 2]
407EIQKFFRKHLLQSGSacetylation[4]
Reference
 [1] 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]
 [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] 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]
 [4] Substrate and functional diversity of lysine acetylation revealed by a proteomics survey.
 Kim SC, Sprung R, Chen Y, Xu Y, Ball H, Pei J, Cheng T, Kho Y, Xiao H, Xiao L, Grishin NV, White M, Yang XJ, Zhao Y.
 Mol Cell. 2006 Aug;23(4):607-18. [PMID: 16916647] 
Functional Description
 Acyltransferase which efficiently conjugates very long- chain and long-chain fatty acids to taurine. Shows no conjugation activity in the presence of glycine. 
Sequence Annotation
 MOTIF 414 416 Microbody targeting signal.
 ACT_SITE 235 235 Charge relay system (By similarity).
 ACT_SITE 325 325 Charge relay system (By similarity).
 ACT_SITE 359 359 Charge relay system (By similarity).
 MOD_RES 407 407 N6-acetyllysine.  
Keyword
 Acetylation; Acyltransferase; Alternative splicing; Complete proteome; Fatty acid metabolism; Lipid metabolism; Peroxisome; Reference proteome; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 416 AA 
Protein Sequence
MMIKLIATPS NALVDEPVSI RATGLPPSQI VTIKATVKDE NDNVFQSQAF YKTNEAGEVD 60
LEKTPALGGD YVGVHPMGLF FSLKPKKAFH RLMKKDVMNS PFCICLDLYD SVNWLETVRI 120
PSKASQRVQR WFVGPGVKRE QIQEGRVRGA LFLPPGKGPF PGIIDLFGVI GGLVEFRASL 180
LASHGFAVLA LAYFAYKDLP EKLQEVDLEY FEEAANFLLS HPKIQQPGIG VISTSKGAEI 240
GLAMACYLKQ VIATVCINGA TTTTAVPLRY QDLVVTPIQQ ALERMEVHVS GAVCFRHTTQ 300
YLQNKNILPV EKAQGKILFI VGENDELLDS KLHAQRAMDR LRRHGRSSGR MLAYPGAGHL 360
IEPPYSPLCF ASWQPVLGRP MCFGGDLMAH AAAQEHSWRE IQKFFRKHLL QSGSKL 416 
Gene Ontology
 GO:0005777; C:peroxisome; IDA:UniProtKB.
 GO:0016410; F:N-acyltransferase activity; IDA:UniProtKB.
 GO:0016790; F:thiolester hydrolase activity; IEA:InterPro.
 GO:0006637; P:acyl-CoA metabolic process; IEA:InterPro.
 GO:0006631; P:fatty acid metabolic process; IDA:UniProtKB. 
Interpro
 IPR016662; Acyl-CoA_thioEstase_long-chain.
 IPR014940; BAAT_C.
 IPR006862; Thio_Ohase/aa_AcTrfase. 
Pfam
 PF08840; BAAT_C
 PF04775; Bile_Hydr_Trans 
SMART
  
PROSITE
  
PRINTS