[1]	NUCLEOTIDE SEQUENCE [MRNA] OF 3-626 (ISOFORM 1), AND PARTIAL PROTEIN SEQUENCE. DOI=10.1006/geno.1994.1463; PubMed=7829107 [NCBI, ExPASy, EBI, Israel, Japan] Corti O., Finocchiaro G., Rossi E., Zuffardi O., Didonato S.; "Molecular cloning of cDNAs encoding human carnitine acetyltransferase and mapping of the corresponding gene to chromosome 9q34.1."; Genomics 23:94-99(1994).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). TISSUE=Placenta; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.; "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."; Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[4]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-52, AND ALTERNATIVE SPLICING. PubMed=7945262 [NCBI, ExPASy, EBI, Israel, Japan] Corti O., DiDonato S., Finocchiaro G.; "Divergent sequences in the 5' region of cDNA suggest alternative splicing as a mechanism for the generation of carnitine acetyltransferases with different subcellular localizations."; Biochem. J. 303:37-41(1994).
[5]	X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 35-626, AND SUBUNIT. DOI=10.1074/jbc.M212356200; PubMed=12562770 [NCBI, ExPASy, EBI, Israel, Japan] 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. 278:13159-13165(2003).
[6]	X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 35-626 IN COMPLEX WITH CARNITINE, AND MUTAGENESIS OF TYR-452; THR-465; ARG-518 AND PHE-566. DOI=10.1016/j.jsb.2004.01.011; PubMed=15099582 [NCBI, ExPASy, EBI, Israel, Japan] Govindasamy L., Kukar T., Lian W., Pedersen B., Gu Y., Agbandje-McKenna M., Jin S., McKenna R., Wu D.; "Structural and mutational characterization of L-carnitine binding to human carnitine acetyltransferase."; J. Struct. Biol. 146:416-424(2004).

Comments

FUNCTION: 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.
CATALYTIC ACTIVITY: Acetyl-CoA + carnitine = CoA + O-acetylcarnitine.
SUBUNIT: Monomer.
SUBCELLULAR LOCATION: Endoplasmic reticulum (Potential). Peroxisome (Potential). Mitochondrion inner membrane; Peripheral membrane protein; Matrix side (Potential).

ALTERNATIVE PRODUCTS: 3 named isoforms [FASTA] produced by alternative splicing.

Name	1
Isoform ID	P43155-1
Note: May be mitochondrial.
This is the isoform sequence displayed in this entry.

Name	2
Isoform ID	P43155-2
Note: May be peroxisomal. No experimental confirmation available.
Features which should be applied to build the isoform sequence: VSP_000792.

Name	3
Isoform ID	P43155-3
Features which should be applied to build the isoform sequence: VSP_012798.

TISSUE SPECIFICITY: Mostly in skeletal muscle, less in heart, liver and pancreas, only weakly detectable in brain, placenta, lung and kidney.
SIMILARITY: Belongs to the carnitine/choline acetyltransferase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

X78706; CAA55359.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC000723; AAH00723.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BT006801; AAP35447.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X79825; -; NOT_ANNOTATED_CDS; Genomic_DNA.	[EMBL / GenBank / DDBJ]

PIR

A55720; A55720.

RefSeq

NP_000746.2; -.
NP_003994.2; -.

UniGene

Hs.12068

3D structure databases

PDB

1NM8; X-ray; 1.60 A; A=31-626.	[ExPASy / RCSB / EBI]
1S5O; X-ray; 1.80 A; A=31-626.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

1NM8; -.
1S5O; -.

DP00305; -.

Organism-specific databases

HIX0008446; -.

HGNC:2342; CRAT.

600184; gene. [NCBI / EBI]

PharmGKB

PA26862; -.

GeneCards

P43155.

Gene expression databases

ArrayExpress

P43155; -.

CleanEx

HS_CRAT; -.

GermOnline

ENSG00000095321; Homo sapiens.

Ontologies

GO:0005783;	Cellular component: endoplasmic reticulum (non-traceable author statement from ProtInc).
GO:0005777;	Cellular component: peroxisome (non-traceable author statement from ProtInc).
GO:0015980;	Biological process: energy derivation by oxidation of organic compounds (traceable author statement from ProtInc).
QuickGo view.

Family and domain databases

InterPro

IPR000542; Carn_acyl_trans.
Graphical view of domain structure.

PANTHER

PTHR22589; Carn_acyl_trans; 1.

Pfam

PF00755; Carn_acyltransf; 1.
Pfam graphical view of domain structure.

PROSITE

PS00439; ACYLTRANSF_C_1; 1.
PS00440; ACYLTRANSF_C_2; 1.

BLOCKS

P43155.

Genome annotation databases

Ensembl

ENSG00000095321; Homo sapiens. [Contig view]

GeneID

1384; -.

KEGG

hsa:1384; -.

Phylogenomic databases

HOGENOM

P43155; -.

HOVERGEN

P43155; -.

Other

DrugBank

DB00583; L-Carnitine.

CRAT; Homo sapiens.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Acyltransferase; Alternative splicing; Direct protein sequencing; Endoplasmic reticulum; Fatty acid metabolism; Lipid metabolism; Membrane; Mitochondrion; Mitochondrion inner membrane; Peroxisome; Transferase; Transport.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 626`	`626`	`Carnitine O-acetyltransferase.`	`PRO_0000210172`
`REGION`	`418 430`	`13`	`Coenzyme A binding (By similarity).`
`MOTIF`	`624 626`	`3`	`Microbody targeting signal (Potential).`
`ACT_SITE`	`343 343`		`Proton acceptor (Probable).`
`BINDING`	`452 452`		`Carnitine.`
`BINDING`	`454 454`		`Carnitine.`
`BINDING`	`465 465`		`Carnitine.`
`VAR_SEQ`	`1 21`		`Missing (in isoform 2).`	`VSP_000792`
`VAR_SEQ`	`281 362`		`Missing (in isoform 3).`	`VSP_012798`
`MUTAGEN`	`452 452`		`Y->A: Increases the KM for carnitine 100-fold.`
`MUTAGEN`	`452 452`		`Y->F: Increases the KM for carnitine 320-fold and reduces enzyme activity 10000-fold.`
`MUTAGEN`	`465 465`		`T->A: Increases the KM for carnitine almost 70-fold and reduces enzyme activity 450-fold.`
`MUTAGEN`	`518 518`		`R->Q: Increases the KM for carnitine 230-fold and reduces enzyme activity almost 100-fold.`
`MUTAGEN`	`566 566`		`F->A: Increases the KM for carnitine 18-fold and reduces enzyme activity 100-fold.`
`MUTAGEN`	`566 566`		`F->Y: No effect.`
`CONFLICT`	`88 88`		`E -> G (in Ref. 1; CAA55359).`
`CONFLICT`	`517 517`		`D -> G (in Ref. 1; CAA55359).`
`CONFLICT`	`534 534`		`M -> T (in Ref. 1; CAA55359).`
`HELIX`	`43 54`	`12`
`TURN`	`55 57`	`3`
`HELIX`	`60 74`	`15`
`HELIX`	`79 93`	`15`
`STRAND`	`94 96`	`3`
`HELIX`	`99 106`	`8`
`TURN`	`107 109`	`3`
`TURN`	`116 118`	`3`
`STRAND`	`121 123`	`3`
`HELIX`	`132 154`	`23`
`HELIX`	`171 175`	`5`
`STRAND`	`179 182`	`4`
`STRAND`	`185 187`	`3`
`STRAND`	`189 192`	`4`
`STRAND`	`196 198`	`3`
`STRAND`	`202 207`	`6`
`STRAND`	`210 215`	`6`
`HELIX`	`226 238`	`13`
`HELIX`	`248 253`	`6`
`HELIX`	`256 266`	`11`
`HELIX`	`270 281`	`12`
`STRAND`	`285 289`	`5`
`HELIX`	`300 310`	`11`
`TURN`	`314 319`	`6`
`STRAND`	`325 332`	`8`
`STRAND`	`337 341`	`5`
`HELIX`	`348 363`	`16`
`STRAND`	`379 381`	`3`
`HELIX`	`387 406`	`20`
`STRAND`	`407 414`	`8`
`HELIX`	`420 424`	`5`
`HELIX`	`429 445`	`17`
`STRAND`	`451 456`	`6`
`STRAND`	`465 469`	`5`
`HELIX`	`473 482`	`10`
`HELIX`	`489 511`	`23`
`HELIX`	`517 529`	`13`
`HELIX`	`536 539`	`4`
`HELIX`	`541 546`	`6`
`STRAND`	`550 555`	`6`
`STRAND`	`559 561`	`3`
`STRAND`	`563 565`	`3`
`STRAND`	`574 580`	`7`
`STRAND`	`585 592`	`8`
`HELIX`	`600 619`	`20`

Sequence information

Length: 626 AA [This is the length of the unprocessed precursor]

Molecular weight: 70926 Da [This is the MW of the unprocessed precursor]

CRC64: BFBE740B34E27F46 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MLAFAARTVV KPLGFLKPFS LMKASSRFKA HQDALPRLPV PPLQQSLDHY LKALQPIVSE 

        70         80         90        100        110        120 
EEWAHTKQLV DEFQASGGVG ERLQKGLERR ARKTENWLSE WWLKTAYLQY RQPVVIYSSP 

       130        140        150        160        170        180 
GVMLPKQDFV DLQGQLRFAA KLIEGVLDFK VMIDNETLPV EYLGGKPLCM NQYYQILSSC 

       190        200        210        220        230        240 
RVPGPKQDTV SNFSKTKKPP THITVVHNYQ FFELDVYHSD GTPLTADQIF VQLEKIWNSS 

       250        260        270        280        290        300 
LQTNKEPVGI LTSNHRNSWA KAYNTLIKDK VNRDSVRSIQ KSIFTVCLDA TMPRVSEDVY 

       310        320        330        340        350        360 
RSHVAGQMLH GGGSRLNSGN RWFDKTLQFI VAEDGSCGLV YEHAAAEGFP IVTLLDYVIE 

       370        380        390        400        410        420 
YTKKPELVRS PMVPLPMPKK LRFNITPEIK SDIEKAKQNL SIMIQDLDIT VMVFHHFGKD 

       430        440        450        460        470        480 
FPKSEKLSPD AFIQMALQLA YYRIYGQACA TYESASLRMF HLGRTDTIRS ASMDSLTFVK 

       490        500        510        520        530        540 
AMDDSSVTEH QKVELLRKAV QAHRGYTDRA IRGEAFDRHL LGLKLQAIED LVSMPDIFMD 

       550        560        570        580        590        600 
TSYAIAMHFH LSTSQVPAKT DCVMFFGPVV PDGYGVCYNP MEAHINFSLS AYNSCAETNA 

       610        620 
ARLAHYLEKA LLDMRALLQS HPRAKL

P43155 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools