Q704S8 (CACP_RAT) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Carnitine O-acetyltransferase
Short name=Carnitine acetylase
EC=2.3.1.7

Alternative name(s):
Carnitine acetyltransferase
Short name=CAT
Short name=CrAT

Gene names

Name:

Crat

Organism

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	626 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (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 By similarity. Ref.1
Catalytic activity	Acetyl-CoA + carnitine = CoA + O-acetylcarnitine.
Subunit structure	Monomer By similarity.
Subcellular location	Endoplasmic reticulum Potential. Peroxisome Potential. Mitochondrion inner membrane; Peripheral membrane protein; Matrix side Potential.
Tissue specificity	Expressed in flagella of epididymal sperm. Ref.3
Sequence similarities	Belongs to the carnitine/choline acetyltransferase family.

Ontologies

Keywords
Biological process	Fatty acid metabolism Lipid metabolism Transport
Cellular component	Endoplasmic reticulum Membrane Mitochondrion Mitochondrion inner membrane Peroxisome
Molecular function	Acyltransferase Transferase
PTM	Acetylation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	fatty acid metabolic process Inferred from direct assay Ref.1. Source: RGD transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	endoplasmic reticulum Traceable author statement Ref.1. Source: RGD mitochondrial inner membrane Inferred from electronic annotation. Source: UniProtKB-SubCell peroxisome Traceable author statement Ref.1. Source: RGD
Molecular function	carnitine O-acetyltransferase activity Inferred from direct assay Ref.1. Source: RGD
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 626	626	Carnitine O-acetyltransferase		PRO_0000210174
Regions
	Region	418 – 430	13	Coenzyme A binding By similarity
	Motif	624 – 626	3	Microbody targeting signal Potential
Sites
	Active site	343	1	Proton acceptor
	Binding site	452	1	Carnitine By similarity
	Binding site	454	1	Carnitine By similarity
	Binding site	455	1	Coenzyme A By similarity
	Binding site	465	1	Carnitine By similarity
Amino acid modifications
	Modified residue	261	1	N6-acetyllysine By similarity
	Modified residue	268	1	N6-acetyllysine By similarity
Experimental info
	Mutagenesis	343	1	H → A: Loss of enzyme activity. Ref.1
	Mutagenesis	347	1	E → A: Loss of enzyme activity. Ref.1
	Mutagenesis	564	1	M → A: Increases activity towards medium chain fatty acids. Ref.1
	Mutagenesis	564	1	M → G: Increases activity towards medium and long chain fatty acids. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q704S8 [UniParc]. Last modified July 5, 2004. Version 1. Checksum: 85B0D5DEF7EB0FF1	FASTA	626	70,801
	10 20 30 40 50 60 MLAFAARTVV KPLGLLKPSS LMKVSGRFKA HQDALPRLPV PPLQQSLDHY LKALQPIVSE 70 80 90 100 110 120 EEWAHTKQLV DEFQTSGGVG ERLQKGLERR AKKMENWLSE WWLKTAYLQF RQPVVIYSSP 130 140 150 160 170 180 GVLLPKQDFM DLQGQLRFAA KLIEGVLDFK SMIDNETLPV EFLGGQPLCM NQYYQILSSC 190 200 210 220 230 240 RVPGLKQDSV VNFLKSKKPP THITVVHNYQ FFELDVYHSD GTPLTSDQIF VQLEKIWNSS 250 260 270 280 290 300 LQSNKEPVGI LTSNHRNSWA KAYSSLIKDK VNRESVNSIQ KSIFTVCLDK QVPRVSDDVY 310 320 330 340 350 360 RSHVAGQMLH GGGSKFNSGN RWFDKTLQFI VAEDGSCGMV YEHAAAEGPP IVALVDHVME 370 380 390 400 410 420 YTKKPELVRS PMVPLPMPKK LRFNITPEIK NDIEKAKQNI SIMIQDLDIM MLVFHHFGKD 430 440 450 460 470 480 FPKSQKLSPD AFIQIALQLA YYRIYGQACA TYESASLRMF HLGRTDTIRS ASTDSLAFVK 490 500 510 520 530 540 GMDDPKVPEQ QRVELLRKAV QAHRAYTDRA IRGEAFDRHL LGLKLQAIED LVSMPDIFMD 550 560 570 580 590 600 TSYAIAMHFN LSTSQVPAKT DCVMSFGPVV PDGYGICYNP MEAHINFSVS AYNSCAETNA 610 620 ARMAHYLEKA LLDMRTLLQN HPRAKL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Redesign of carnitine acetyltransferase specificity by protein engineering." Cordente A.G., Lopez-Vinas E., Vazquez M.I., Swiegers J.H., Pretorius I.S., Gomez-Puertas P., Hegardt F.G., Asins G., Serra D. J. Biol. Chem. 279:33899-33908(2004) [PubMed: 15155769] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, MUTAGENESIS OF HIS-343; GLU-347 AND MET-564, 3D-STRUCTURE MODELING. Strain: Sprague-Dawley. Tissue: Testis.
[2]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Testis.
[3]	"Identification of novel immunodominant epididymal sperm proteins using combinatorial approach." Khan S.A., Suryawanshi A.R., Ranpura S.A., Jadhav S.V., Khole V.V. Reproduction 138:81-93(2009) [PubMed: 19423663] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY, TISSUE SPECIFICITY.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AJ620886 mRNA. Translation: CAF06525.1. BC083616 mRNA. Translation: AAH83616.1.
IPI	IPI00949645.
RefSeq	NP_001004085.1. NM_001004085.2.
UniGene	Rn.6249.
3D structure databases
ProteinModelPortal	Q704S8.
SMR	Q704S8. Positions 30-625.
ModBase	Search...
Protein-protein interaction databases
STRING	Q704S8.
Proteomic databases
PRIDE	Q704S8.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSRNOT00000065128; ENSRNOP00000063089; ENSRNOG00000018145.
GeneID	311849.
KEGG	rno:311849.
UCSC	NM_001004085. rat.
Organism-specific databases
CTD	1384.
RGD	1303031. Crat.
Phylogenomic databases
eggNOG	roNOG07896.
GeneTree	ENSGT00550000074345.
HOVERGEN	HBG107717.
InParanoid	Q704S8.
PhylomeDB	Q704S8.
Enzyme and pathway databases
BioCyc	MetaCyc:MONOMER-14440.
Gene expression databases
ArrayExpress	Q704S8.
Genevestigator	Q704S8.
GermOnline	ENSRNOG00000018145. Rattus norvegicus.
Family and domain databases
InterPro	IPR000542. Carn_acyl_trans. [Graphical view]
KO	K00624.
PANTHER	PTHR22589. Carn_acyl_trans. 1 hit.
Pfam	PF00755. Carn_acyltransf. 1 hit. [Graphical view]
PROSITE	PS00439. ACYLTRANSF_C_1. 1 hit. PS00440. ACYLTRANSF_C_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	664307.

Entry information

Entry name

CACP_RAT

Accession

Primary (citable) accession number: Q704S8

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 15, 2005
Last sequence update:	July 5, 2004
Last modified:	November 16, 2011
This is version 60 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program