LOCUS NP_000746 626 aa linear PRI 22-OCT-2008
DEFINITION carnitine acetyltransferase isoform 1 precursor [Homo sapiens].
ACCESSION NP_000746
VERSION NP_000746.2 GI:21618331
DBSOURCE REFSEQ: accession NM_000755.2
KEYWORDS .
SOURCE Homo sapiens (human)
ORGANISM Homo sapiens
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
REFERENCE 1 (residues 1 to 626)
AUTHORS Govindasamy,L., Kukar,T., Lian,W., Pedersen,B., Gu,Y.,
Agbandje-McKenna,M., Jin,S., McKenna,R. and Wu,D.
TITLE Structural and mutational characterization of L-carnitine binding
to human carnitine acetyltransferase
JOURNAL J. Struct. Biol. 146 (3), 416-424 (2004)
PUBMED 15099582
REMARK GeneRIF: structure of a binary complex of human peroxisomal
carnitine acetyltransferase and the substrate l-carnitine, refined
to a resolution of 1.8; site-directed mutagenesis and kinetic
characterization
REFERENCE 2 (residues 1 to 626)
AUTHORS Wu,D., Govindasamy,L., Lian,W., Gu,Y., Kukar,T.,
Agbandje-McKenna,M. and McKenna,R.
TITLE Structure of human carnitine acetyltransferase. Molecular basis for
fatty acyl transfer
JOURNAL J. Biol. Chem. 278 (15), 13159-13165 (2003)
PUBMED 12562770
REMARK GeneRIF: The structure and reactions of this enzyme are examined.
REFERENCE 3 (residues 1 to 626)
AUTHORS Jogl,G. and Tong,L.
TITLE Crystal structure of carnitine acetyltransferase and implications
for the catalytic mechanism and fatty acid transport
JOURNAL Cell 112 (1), 113-122 (2003)
PUBMED 12526798
REFERENCE 4 (residues 1 to 626)
AUTHORS Lian,W., Govindasamy,L., Gu,Y., Kukar,T., Agbandje-McKenna,M.,
McKenna,R. and Wu,D.
TITLE Crystallization and preliminary X-ray crystallographic studies on
recombinant human carnitine acetyltransferase
JOURNAL Acta Crystallogr. D Biol. Crystallogr. 58 (PT 7), 1193-1194 (2002)
PUBMED 12077440
REMARK GeneRIF: the purification, crystallization and preliminary X-ray
crystallographic studies of human carnitine acetyltransferase are
reported
REFERENCE 5 (residues 1 to 626)
AUTHORS van der Leij,F.R., Huijkman,N.C., Boomsma,C., Kuipers,J.R. and
Bartelds,B.
TITLE Genomics of the human carnitine acyltransferase genes
JOURNAL Mol. Genet. Metab. 71 (1-2), 139-153 (2000)
PUBMED 11001805
REMARK GeneRIF: Human CPT1A, CPT1B, CPT2, CROT and CRAT are known to
encode active carnitine acyltransferases. Earlier pfam annotations
refer to the non-existing compound CARNITATE. In 2000 this has been
changed to CARNITINE.
Review article
REFERENCE 6 (residues 1 to 626)
AUTHORS Corti,O., DiDonato,S. and Finocchiaro,G.
TITLE Divergent sequences in the 5' region of cDNA suggest alternative
splicing as a mechanism for the generation of carnitine
acetyltransferases with different subcellular localizations
JOURNAL Biochem. J. 303 (PT 1), 37-41 (1994)
PUBMED 7945262
REFERENCE 7 (residues 1 to 626)
AUTHORS Corti,O., Finocchiaro,G., Rossi,E., Zuffardi,O. and DiDonato,S.
TITLE Molecular cloning of cDNAs encoding human carnitine
acetyltransferase and mapping of the corresponding gene to
chromosome 9q34.1
JOURNAL Genomics 23 (1), 94-99 (1994)
PUBMED 7829107
REFERENCE 8 (residues 1 to 626)
AUTHORS Kalaria,R.N. and Harik,S.I.
TITLE Carnitine acetyltransferase activity in the human brain and its
microvessels is decreased in Alzheimer's disease
JOURNAL Ann. Neurol. 32 (4), 583-586 (1992)
PUBMED 1456745
COMMENT REVIEWED REFSEQ: This record has been curated by NCBI staff. The
reference sequence was derived from BC000723.2, BQ068230.1 and
X78706.1.
On Jun 27, 2002 this sequence version replaced gi:4557487.
Summary: Carnitine acetyltransferase (CRAT) is a key enzyme in the
metabolic pathway in mitochondria, peroxisomes and endoplasmic
reticulum. CRAT catalyzes the reversible transfer of acyl groups
from an acyl-CoA thioester to carnitine and regulates the ratio of
acylCoA/CoA in the subcellular compartments. Different subcellular
localizations of the CRAT mRNAs are thought to result from
alternative splicing of the CRAT gene suggested by the divergent
sequences in the 5' region of peroxisomal and mitochondrial CRAT
cDNAs and the location of an intron where the sequences diverge.
The alternatively splicing of this gene results in three distinct
isoforms, one of which contains an N-terminial mitochondrial
transit peptide, and has been shown to be located in mitochondria.
[provided by RefSeq].
Transcript Variant: This variant (1) is also known as the
mitochondrial transcript variant. It encodes the longest isoform
(1) that contains a mitochondrial leader peptide.
FEATURES Location/Qualifiers
source 1..626
/organism="Homo sapiens"
/db_xref="taxon:9606"
/chromosome="9"
/map="9q34.1"
Protein 1..626
/product="carnitine acetyltransferase isoform 1 precursor"
/EC_number="2.3.1.7"
transit_peptide 1..11
/calculated_mol_wt=1207
mat_peptide 12..544
/product="carnitine acetyltransferase, isoform 1"
/calculated_mol_wt=60623
CDS 1..626
/gene="CRAT"
/gene_synonym="CAT1"
/coded_by="NM_000755.2:296..2176"
/note="isoform 1 precursor is encoded by transcript
variant 1"
/db_xref="CCDS:CCDS6919.1"
/db_xref="GeneID:1384"
/db_xref="HGNC:2342"
/db_xref="HPRD:08971"
/db_xref="MIM:600184"
ORIGIN
1 mlafaartvv kplgflkpfs lmkassrfka hqdalprlpv pplqqsldhy lkalqpivse
61 eewahtkqlv defqasggvg erlqkglerr arktenwlse wwlktaylqy rqpvviyssp
121 gvmlpkqdfv dlqgqlrfaa kliegvldfk vmidnetlpv eylggkplcm nqyyqilssc
181 rvpgpkqdtv snfsktkkpp thitvvhnyq ffeldvyhsd gtpltadqif vqlekiwnss
241 lqtnkepvgi ltsnhrnswa kayntlikdk vnrdsvrsiq ksiftvclda tmprvsedvy
301 rshvagqmlh gggsrlnsgn rwfdktlqfi vaedgscglv yehaaaegpp ivtlldyvie
361 ytkkpelvrs pmvplpmpkk lrfnitpeik sdiekakqnl simiqdldit vmvfhhfgkd
421 fpkseklspd afiqmalqla yyriygqaca tyesaslrmf hlgrtdtirs asmdsltfvk
481 amddssvteh qkvellrkav qahrgytdra irgeafdrhl lglklqaied lvsmpdifmd
541 tsyaiamhfh lstsqvpakt dcvmffgpvv pdgygvcynp meahinfsls aynscaetna
601 arlahyleka lldmrallqs hprakl
//