CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-006070
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Carnitine O-palmitoyltransferase 1, liver isoform 
Protein Synonyms/Alias
 CPT1-L; Carnitine O-palmitoyltransferase I, liver isoform; CPT I; CPTI-L; Carnitine palmitoyltransferase 1A 
Gene Name
 Cpt1a 
Gene Synonyms/Alias
 Cpt-1; Cpt1 
Created Date
 July 27, 2013 
Organism
 Rattus norvegicus (Rat) 
NCBI Taxa ID
 10116 
Lysine Modification
Position
Peptide
Type
References
195ESVRPLMKEEDFQRMacetylation[1]
292TLDREELKPIRLLGSacetylation[1]
329TDTIQHIKDSRHIVVacetylation[1]
Reference
 [1] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns.
 Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV.
 Cell Rep. 2012 Aug 30;2(2):419-31. [PMID: 22902405] 
Functional Description
 Catalyzes the transfer of the acyl group of long-chain fatty acid-CoA conjugates onto carnitine, an essential step for the mitochondrial uptake of long-chain fatty acids and their subsequent beta-oxidation in the mitochondrion. Plays an important role in triglyceride metabolism. 
Sequence Annotation
 REGION 555 567 Coenzyme A binding (By similarity).
 ACT_SITE 473 473 Proton acceptor.
 BINDING 589 589 Carnitine (By similarity).
 BINDING 602 602 Carnitine (By similarity).
 MOD_RES 2 2 N-acetylalanine.
 MOD_RES 282 282 Nitrated tyrosine.
 MOD_RES 588 588 Phosphothreonine.
 MOD_RES 589 589 Nitrated tyrosine.
 MOD_RES 604 604 Phosphothreonine.
 MOD_RES 741 741 Phosphoserine.
 MOD_RES 747 747 Phosphoserine.  
Keyword
 Acetylation; Acyltransferase; Complete proteome; Direct protein sequencing; Fatty acid metabolism; Lipid metabolism; Membrane; Mitochondrion; Mitochondrion outer membrane; Nitration; Phosphoprotein; Reference proteome; Transferase; Transmembrane; Transmembrane helix; Transport. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 773 AA 
Protein Sequence
MAEAHQAVAF QFTVTPDGID LRLSHEALKQ ICLSGLHSWK KKFIRFKNGI ITGVFPANPS 60
SWLIVVVGVI SSMHAKVDPS LGMIAKISRT LDTTGRMSSQ TKNIVSGVLF GTGLWVAVIM 120
TMRYSLKVLL SYHGWMFAEH GKMSRSTKIW MAMVKVLSGR KPMLYSFQTS LPRLPVPAVK 180
DTVSRYLESV RPLMKEEDFQ RMTALAQDFA VNLGPKLQWY LKLKSWWATN YVSDWWEEYI 240
YLRGRGPLMV NSNYYAMEML YITPTHIQAA RAGNTIHAIL LYRRTLDREE LKPIRLLGST 300
IPLCSAQWER LFNTSRIPGE ETDTIQHIKD SRHIVVYHRG RYFKVWLYHD GRLLRPRELE 360
QQMQQILDDP SEPQPGEAKL AALTAADRVP WAKCRQTYFA RGKNKQSLDA VEKAAFFVTL 420
DESEQGYREE DPEASIDSYA KSLLHGRCFD RWFDKSITFV VFKNSKIGIN AEHSWADAPV 480
VGHLWEYVMA TDVFQLGYSE DGHCKGDTNP NIPKPTRLQW DIPGECQEVI DASLSSASLL 540
ANDVDLHSFP FDSFGKGLIK KCRTSPDAFI QLALQLAHYK DMGKFCLTYE ASMTRLFREG 600
RTETVRSCTM ESCNFVQAMM DPKSTAEQRL KLFKIACEKH QHLYRLAMTG AGIDRHLFCL 660
YVVSKYLAVD SPFLKEVLSE PWRLSTSQTP QQQVELFDFE KNPDYVSCGG GFGPVADDGY 720
GVSYIIVGEN FIHFHISSKF SSPETDSHRF GKHLRQAMMD IITLFGLTIN SKK 773 
Gene Ontology
 GO:0031307; C:integral to mitochondrial outer membrane; IDA:UniProtKB.
 GO:0005743; C:mitochondrial inner membrane; IEA:Compara.
 GO:0004095; F:carnitine O-palmitoyltransferase activity; IDA:UniProtKB.
 GO:0042802; F:identical protein binding; IDA:RGD.
 GO:0009437; P:carnitine metabolic process; IDA:UniProtKB.
 GO:0071398; P:cellular response to fatty acid; IEP:RGD.
 GO:0042755; P:eating behavior; IMP:RGD.
 GO:0006635; P:fatty acid beta-oxidation; IEA:UniProtKB-UniPathway.
 GO:0006006; P:glucose metabolic process; IMP:RGD.
 GO:0001676; P:long-chain fatty acid metabolic process; IDA:UniProtKB.
 GO:0032000; P:positive regulation of fatty acid beta-oxidation; IMP:RGD.
 GO:0051260; P:protein homooligomerization; IDA:RGD.
 GO:0050796; P:regulation of insulin secretion; IMP:RGD.
 GO:0042493; P:response to drug; IEP:RGD.
 GO:0014070; P:response to organic cyclic compound; IEP:RGD.
 GO:0006810; P:transport; IEA:UniProtKB-KW.
 GO:0006641; P:triglyceride metabolic process; IMP:RGD. 
Interpro
 IPR000542; Carn_acyl_trans. 
Pfam
 PF00755; Carn_acyltransf 
SMART
  
PROSITE
 PS00439; ACYLTRANSF_C_1
 PS00440; ACYLTRANSF_C_2 
PRINTS