Reviewed, UniProtKB/Swiss-Prot P52826 (CACP_COLLI)

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=CrAT
      Short name=CAT

Gene names

Name:

CRAT

Organism

Columba livia (Domestic pigeon)

Taxonomic identifier

8932 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Archosauria › Dinosauria › Saurischia › Theropoda › Coelurosauria › Aves › Neognathae › Columbiformes › Columbidae › Columba

Protein attributes

Sequence length	627 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
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 out of the mitochondria for fatty acid biosynthesis or urinary excretion.
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.
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
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	fatty acid metabolic process Inferred from electronic annotation. Source: UniProtKB-KW transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	endoplasmic reticulum Inferred from electronic annotation. Source: UniProtKB-SubCell extrinsic to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell mitochondrial inner membrane Inferred from electronic annotation. Source: UniProtKB-KW peroxisome Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	carnitine O-acetyltransferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Propeptide	1 – 30	30			PRO_0000004428
	Chain	31 – 627	597	Carnitine O-acetyltransferase		PRO_0000004429
Regions
	Region	419 – 431	13	Coenzyme A binding By similarity
	Motif	625 – 627	3	Microbody targeting signal Potential
Sites
	Active site	344	1	Proton acceptor By similarity
	Binding site	453	1	Carnitine By similarity
	Binding site	455	1	Carnitine By similarity
	Binding site	456	1	Coenzyme A By similarity
	Binding site	466	1	Carnitine By similarity

Sequences

	Sequence		Length	Mass (Da)
	P52826-1 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: DD42317336AF0D2A	FASTA	627	71,067
	10 20 30 40 50 60 MDRKQKQAEK ARPYGLLKPA ALGKIPGRFQ LHQEALPHLP VPPLQQTLDR YLLALQPIIS 70 80 90 100 110 120 EEELNHTQEL VAEFRKPGGV GERLQKGLER RAKKTDNWLS DWWLKTAYLE YRLPVVVHSS 130 140 150 160 170 180 PGVVLPKQDF QDRQGQLRFA AKLIEGILDF KTMIDNETLP VEYMGGKPLC MNQYYQILSS 190 200 210 220 230 240 CRIPGPKRDS IVNYAKGKKQ SRHITVVHNF QFFELDVYNS DGSPLTTDQL FIQLEKIWNT 250 260 270 280 290 300 SLQTNKEPVG ILTTNHRNSW AKAYNNLLKD KTNKESVRTI EKSICTICLD APMPRVSDDI 310 320 330 340 350 360 YKSPVAAQML HGGGSRWNSG NRWFDKTLQF IIAEDGSCGL VYEHAPAEGP PIVALLDHIV 370 380 390 400 410 420 EYTKKPELVR SPMIPLPMPK KLRFNITPEI KSDIEKAKQN LNIMVEDLDV IVLVFHQFGK 430 440 450 460 470 480 NYPKSEKISP DAFIQLALQL AYYRMYGHSC ATYESASLRM FRLGRTDTIR STSIESHKFV 490 500 510 520 530 540 QSMDSPDKSD QEKADLLRRA TQAHKEYTNM AIQGNAIDRH LLGLKLQAIE DLVSIPELFM 550 560 570 580 590 600 DTAYAVAMHF NLSTSQVPAK TDCVMCFGPV VPDGYGICYN PMGEHINFAI SAFNSCADTN 610 620 AARMAHYLEK ALLDMRSLLQ SAPKSKL

References

[1]

"Cloning, sequencing and heterologous expression of a cDNA encoding pigeon liver carnitine acetyltransferase." Johnson T.M., Kocher H.P., Anderson R.C., Nemecek G.M. Biochem. J. 305:439-444(1995) [PubMed: 7832757] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE. Tissue: Liver and Pectoralis muscle.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U08229 mRNA. Translation: AAA80570.1.
PIR	S53369.
3D structure databases
SMR	P52826. Positions 45-621.
ModBase	Search...
Phylogenomic databases
HOVERGEN	P52826.
Enzyme and pathway databases
BRENDA	2.3.1.7. 3625.
Family and domain databases
InterPro	IPR000542. Carn_acyl_trans. [Graphical view]
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...

Entry information

Entry name

CACP_COLLI

Accession

Primary (citable) accession number: P52826

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	February 9, 2010
This is version 57 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)