Tag | Content |
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CPLM ID | CPLM-015604 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Carnitine O-acetyltransferase |
Protein Synonyms/Alias | Carnitine acetylase; Carnitine acetyltransferase; CAT; CrAT |
Gene Name | Crat |
Gene Synonyms/Alias | |
Created Date | July 27, 2013 |
Organism | Rattus norvegicus (Rat) |
NCBI Taxa ID | 10116 |
Lysine Modification | Position | Peptide | Type | References |
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52 | QSLDHYLKALQPIVS | acetylation | [1] | 93 | GLERRAKKMENWLSE | acetylation | [1] | 186 | SCRVPGLKQDSVVNF | acetylation | [1] | 195 | DSVVNFLKSKKPPTH | acetylation | [1] | 245 | NSSLQSNKEPVGILT | acetylation | [1] | 261 | NHRNSWAKAYSSLIK | acetylation | [1] | 268 | KAYSSLIKDKVNRES | acetylation | [1] | 315 | MLHGGGSKFNSGNRW | acetylation | [1] | 390 | FNITPEIKNDIEKAK | acetylation | [1] | 395 | EIKNDIEKAKQNISI | acetylation | [1] | 480 | TDSLAFVKGMDDPKV | acetylation | [1] | 486 | VKGMDDPKVPEQQRV | acetylation | [1] | 609 | RMAHYLEKALLDMRT | acetylation | [1] |
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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 | Carnitine acetylase is specific for short chain fatty acids. Carnitine acetylase seems to affect the flux through the pyruvate dehydrogenase complex. It may be involved as well in the transport of acetyl-CoA into mitochondria (By similarity). |
Sequence Annotation | REGION 418 430 Coenzyme A binding (By similarity). MOTIF 624 626 Microbody targeting signal (Potential). ACT_SITE 343 343 Proton acceptor. BINDING 452 452 Carnitine (By similarity). BINDING 454 454 Carnitine (By similarity). BINDING 455 455 Coenzyme A (By similarity). BINDING 465 465 Carnitine (By similarity). MOD_RES 261 261 N6-acetyllysine (By similarity). MOD_RES 268 268 N6-acetyllysine (By similarity). |
Keyword | Acetylation; Acyltransferase; Complete proteome; Endoplasmic reticulum; Fatty acid metabolism; Lipid metabolism; Membrane; Mitochondrion; Mitochondrion inner membrane; Peroxisome; Reference proteome; Transferase; Transport. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 626 AA |
Protein Sequence | MLAFAARTVV KPLGLLKPSS LMKVSGRFKA HQDALPRLPV PPLQQSLDHY LKALQPIVSE 60 EEWAHTKQLV DEFQTSGGVG ERLQKGLERR AKKMENWLSE WWLKTAYLQF RQPVVIYSSP 120 GVLLPKQDFM DLQGQLRFAA KLIEGVLDFK SMIDNETLPV EFLGGQPLCM NQYYQILSSC 180 RVPGLKQDSV VNFLKSKKPP THITVVHNYQ FFELDVYHSD GTPLTSDQIF VQLEKIWNSS 240 LQSNKEPVGI LTSNHRNSWA KAYSSLIKDK VNRESVNSIQ KSIFTVCLDK QVPRVSDDVY 300 RSHVAGQMLH GGGSKFNSGN RWFDKTLQFI VAEDGSCGMV YEHAAAEGPP IVALVDHVME 360 YTKKPELVRS PMVPLPMPKK LRFNITPEIK NDIEKAKQNI SIMIQDLDIM MLVFHHFGKD 420 FPKSQKLSPD AFIQIALQLA YYRIYGQACA TYESASLRMF HLGRTDTIRS ASTDSLAFVK 480 GMDDPKVPEQ QRVELLRKAV QAHRAYTDRA IRGEAFDRHL LGLKLQAIED LVSMPDIFMD 540 TSYAIAMHFN LSTSQVPAKT DCVMSFGPVV PDGYGICYNP MEAHINFSVS AYNSCAETNA 600 ARMAHYLEKA LLDMRTLLQN HPRAKL 626 |
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