| General information | | DisProt: | DP00305 | | Name: | Carnitine O-acetyltransferase [Isoform 1] | | Synonym(s): | CACP_HUMAN
Carnitine acetylase
Carnitine acetyltransferase
CrAT
CAT
SM-1400
EC=2.3.1.7
| | First appeared in release: | Release 3.0 (02/17/2006) | | UniProt: | P43155-1 | | UniGene: | Hs.12068 | | SwissProt: | CACP_HUMAN | | TrEMBL: | | | NCBI (GI): | 215274265 | | Source organism: | Homo sapiens (Human) | | Sequence length: | 626 | | Percent disordered: | 1% | | Homologues: | |
| Native sequence |
10 20 30 40 50 60
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MLAFAARTVV KPLGFLKPFS LMKASSRFKA HQDALPRLPV PPLQQSLDHY LKALQPIVSE - 60
EEWAHTKQLV DEFQASGGVG ERLQKGLERR ARKTENWLSE WWLKTAYLQY RQPVVIYSSP - 120
GVMLPKQDFV DLQGQLRFAA KLIEGVLDFK VMIDNETLPV EYLGGKPLCM NQYYQILSSC - 180
RVPGPKQDTV SNFSKTKKPP THITVVHNYQ FFELDVYHSD GTPLTADQIF VQLEKIWNSS - 240
LQTNKEPVGI LTSNHRNSWA KAYNTLIKDK VNRDSVRSIQ KSIFTVCLDA TMPRVSEDVY - 300
RSHVAGQMLH GGGSRLNSGN RWFDKTLQFI VAEDGSCGLV YEHAAAEGFP IVTLLDYVIE - 360
YTKKPELVRS PMVPLPMPKK LRFNITPEIK SDIEKAKQNL SIMIQDLDIT VMVFHHFGKD - 420
FPKSEKLSPD AFIQMALQLA YYRIYGQACA TYESASLRMF HLGRTDTIRS ASMDSLTFVK - 480
AMDDSSVTEH QKVELLRKAV QAHRGYTDRA IRGEAFDRHL LGLKLQAIED LVSMPDIFMD - 540
TSYAIAMHFH LSTSQVPAKT DCVMFFGPVV PDGYGVCYNP MEAHINFSLS AYNSCAETNA - 600
ARLAHYLEKA LLDMRALLQS HPRAKL
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| Functional narrative |
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.
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| Map of ordered and disordered regions |
Note: 'Mouse' over a region to see the start and stop residues. Click on a region to see detailed information.
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| Region 1 | | Type: | Disordered | | Name: | | | Location: | 621 - 626 | | Length: | 6 | | Region sequence: |
HPRAKL | | Modification type: | | | PDB: | 1NM8:A | | Structural/functional type: | | | Functional classes: | | | Functional subclasses: | | Detection methods:
| References:
- Wu D, Govindasamy L, Lian W, Gu Y, Kukar T, Agbandje-McKenna M, McKenna R. "Structure of human carnitine acetyltransferase. Molecular basis for fatty acyl transfer." J Biol Chem. 2003; 278(15): 13159-65. PubMed: 12562770
| Comments:The PDB file has an additional sequence of missing residues at the C terminus of this disordered region. It consists of the following residues: ISEEDLSLISG.
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| Comments |
This disordered protein entry is based solely on missing electron density in the Protein Data Bank.
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| If you have any comments or wish to provide additional references to this protein or its disordered region(s), please click here to e-mail us. |
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