Carnitine O-palmitoyltransferase 1, liver isoform

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Reviewed, UniProtKB/Swiss-Prot P32198 (CPT1A_RAT)

Last modified January 19, 2010. Version 86. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Carnitine O-palmitoyltransferase 1, liver isoform
      Short name=CPT1-L
    EC=2.3.1.21
Alternative name(s):
    Carnitine O-palmitoyltransferase I, liver isoform
      Short name=CPTI-L
      Short name=CPT I
    Carnitine palmitoyltransferase 1A

Gene names

Name:	Cpt1a
Synonyms:	Cpt-1, Cpt1

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

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Protein attributes

Sequence length	773 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Catalytic activity	Palmitoyl-CoA + L-carnitine = CoA + L-palmitoylcarnitine.
Enzyme regulation	Inhibitors such as malonyl-CoA interact with its catalytic domain and not with an associated regulatory component.
Pathway	Lipid metabolism; fatty acid beta-oxidation.
Subcellular location	Mitochondrion outer membrane; Multi-pass membrane protein.
Tissue specificity	Liver and kidney.
Sequence similarities	Belongs to the carnitine/choline acetyltransferase family.

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Ontologies

Keywords
Biological process	Fatty acid metabolism Lipid metabolism Transport
Cellular component	Membrane Mitochondrion Mitochondrion outer membrane
Domain	Transmembrane
Molecular function	Acyltransferase Transferase
PTM	Acetylation Nitration Phosphoprotein
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	carnitine metabolic process Traceable author statement. Source: RGD eating behavior Inferred from mutant phenotype. Source: RGD glucose metabolic process Inferred from mutant phenotype. Source: RGD long-chain fatty acid metabolic process Inferred from mutant phenotype. Source: RGD positive regulation of fatty acid beta-oxidation Inferred from mutant phenotype. Source: RGD protein homooligomerization Inferred from direct assay. Source: RGD regulation of insulin secretion Inferred from mutant phenotype. Source: RGD response to drug Inferred from expression pattern. Source: RGD response to organic cyclic substance Inferred from expression pattern. Source: RGD transport Inferred from electronic annotation. Source: UniProtKB-KW triglyceride metabolic process Inferred from mutant phenotype. Source: RGD
Cellular component	integral to membrane Inferred from direct assay. Source: RGD microsome Inferred from direct assay. Source: RGD mitochondrial outer membrane Ref.8 Inferred from direct assay. Source: RGD
Molecular function	carnitine O-palmitoyltransferase activity Ref.8 Ref.10 Ref.11 Inferred from direct assay. Source: RGD identical protein binding Inferred from direct assay. Source: RGD
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed Ref.4

Chain

2 – 773

772

Carnitine O-palmitoyltransferase 1, liver isoform

PRO_0000210161

Regions

Topological domain

2 – 47

Cytoplasmic Potential

Transmembrane

48 – 73

Potential

Topological domain

74 – 102

Mitochondrial intermembrane Potential

Transmembrane

103 – 122

Potential

Topological domain

123 – 773

651

Cytoplasmic Potential

Region

555 – 567

Coenzyme A binding By similarity

Sites

Active site

473

Proton acceptor

Binding site

589

Carnitine By similarity

Binding site

602

Carnitine By similarity

Amino acid modifications

Modified residue

N-acetylalanine Ref.4

Modified residue

282

Nitrated tyrosine Ref.4

Modified residue

588

Phosphothreonine Ref.4

Modified residue

589

Nitrated tyrosine Ref.4

Modified residue

604

Phosphothreonine Ref.4

Modified residue

741

Phosphoserine Ref.4

Modified residue

747

Phosphoserine Ref.4

Experimental info

Mutagenesis

381

A → D: Reduces activity by 86%. No effect on inhibition by malonyl-coenzyme A. Ref.9

Mutagenesis

473

H → A: Loss of activity. Ref.9

Mutagenesis

477

D → A: Reduces activity by 98%. Ref.11

Mutagenesis

560

K → A: Reduces activity by 50%. Ref.11

Mutagenesis

567

D → A: Reduces activity by 97%.

Mutagenesis

590

E → D: Reduces activity by over 60%. Ref.11

Mutagenesis

593

M → A, E or S: Almost abolishes inhibition by malonyl-coenzyme A. Ref.10

Mutagenesis

608

C → A: Slightly lowers inhibition by malonyl-coenzyme A. Ref.10

Mutagenesis

685

S → A: Reduces activity by 50%. Ref.11

Mutagenesis

686

T → A: Loss of activity. Ref.11

Mutagenesis

687

S → A: Loss of activity. Ref.11

Sequence conflict

266

H → D AA sequence Ref.5

Sequence conflict

374 – 375

QP → NG AA sequence Ref.5

Sequence conflict

480

V → I in AAA40876. Ref.1

Sequence conflict

531

D → Y AA sequence Ref.5

Sequence conflict

708

C → R AA sequence Ref.5

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Sequences

Sequence

Length

Mass (Da)

Tools

P32198-1 [UniParc].

Last modified May 1, 2007. Version 2.
Checksum: 8C15594D45430CB8
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FASTA

773

88,125

        10         20         30         40         50         60 
MAEAHQAVAF QFTVTPDGID LRLSHEALKQ ICLSGLHSWK KKFIRFKNGI ITGVFPANPS 

        70         80         90        100        110        120 
SWLIVVVGVI SSMHAKVDPS LGMIAKISRT LDTTGRMSSQ TKNIVSGVLF GTGLWVAVIM 

       130        140        150        160        170        180 
TMRYSLKVLL SYHGWMFAEH GKMSRSTKIW MAMVKVLSGR KPMLYSFQTS LPRLPVPAVK 

       190        200        210        220        230        240 
DTVSRYLESV RPLMKEEDFQ RMTALAQDFA VNLGPKLQWY LKLKSWWATN YVSDWWEEYI 

       250        260        270        280        290        300 
YLRGRGPLMV NSNYYAMEML YITPTHIQAA RAGNTIHAIL LYRRTLDREE LKPIRLLGST 

       310        320        330        340        350        360 
IPLCSAQWER LFNTSRIPGE ETDTIQHIKD SRHIVVYHRG RYFKVWLYHD GRLLRPRELE 

       370        380        390        400        410        420 
QQMQQILDDP SEPQPGEAKL AALTAADRVP WAKCRQTYFA RGKNKQSLDA VEKAAFFVTL 

       430        440        450        460        470        480 
DESEQGYREE DPEASIDSYA KSLLHGRCFD RWFDKSITFV VFKNSKIGIN AEHSWADAPV 

       490        500        510        520        530        540 
VGHLWEYVMA TDVFQLGYSE DGHCKGDTNP NIPKPTRLQW DIPGECQEVI DASLSSASLL 

       550        560        570        580        590        600 
ANDVDLHSFP FDSFGKGLIK KCRTSPDAFI QLALQLAHYK DMGKFCLTYE ASMTRLFREG 

       610        620        630        640        650        660 
RTETVRSCTM ESCNFVQAMM DPKSTAEQRL KLFKIACEKH QHLYRLAMTG AGIDRHLFCL 

       670        680        690        700        710        720 
YVVSKYLAVD SPFLKEVLSE PWRLSTSQTP QQQVELFDFE KNPDYVSCGG GFGPVADDGY 

       730        740        750        760        770 
GVSYIIVGEN FIHFHISSKF SSPETDSHRF GKHLRQAMMD IITLFGLTIN SKK

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning, sequencing, and expression of a cDNA encoding rat liver carnitine palmitoyltransferase I. Direct evidence that a single polypeptide is involved in inhibitor interaction and catalytic function." Esser V., Britton C.H., Weis B.C., Foster D.W., McGarry J.D. J. Biol. Chem. 268:5817-5822(1993) [PubMed: 8449948] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Liver.
[2]	"Functional characterization of mitochondrial carnitine palmitoyltransferases I and II expressed in the yeast Pichia pastoris." de Vries Y., Arvidson D.N., Waterham H.R., Cregg J.M., Woldegiorgis G. Biochemistry 36:5285-5292(1997) [PubMed: 9136891] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: Sprague-Dawley. Tissue: Liver.
[3]	"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: Heart.
[4]	"Post-translational modifications of rat liver mitochondrial outer membrane proteins identified by mass spectrometry." Distler A.M., Kerner J., Hoppel C.L. Biochim. Biophys. Acta 1774:628-636(2007) [PubMed: 17478130] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-22; 272-283; 585-595 AND 599-606, ACETYLATION AT ALA-2, NITRATION AT TYR-282 AND TYR-589, PHOSPHORYLATION AT THR-588; THR-604; SER-741 AND SER-747, MASS SPECTROMETRY. Tissue: Liver.
[5]	"Mature carnitine palmitoyltransferase I retains the N-terminus of the nascent protein in rat liver." Kolodziej M.P., Zammit V.A. FEBS Lett. 327:294-296(1993) [PubMed: 8348957] [Abstract] Cited for: PROTEIN SEQUENCE OF 4-21; 259-276; 361-379; 529-543 AND 696-717. Tissue: Liver.
[6]	"Inhibitors of mitochondrial carnitine palmitoyltransferase I limit the action of proteases on the enzyme. Isolation and partial amino acid analysis of a truncated form of the rat liver isozyme." Esser V., Kuwajima M., Britton C.H., Krishnan K., Foster D.W., McGarry J.D. J. Biol. Chem. 268:5810-5816(1993) [PubMed: 8449947] [Abstract] Cited for: PARTIAL PROTEIN SEQUENCE.
[7]	"Expression of a cDNA isolated from rat brown adipose tissue and heart identifies the product as the muscle isoform of carnitine palmitoyltransferase I (M-CPT I). M-CPT I is the predominant CPT I isoform expressed in both white (epididymal) and brown adipocytes." Esser V., Brown N.F., Cowan A.T., Foster D.W., McGarry J.D. J. Biol. Chem. 271:6972-6977(1996) [PubMed: 8636126] [Abstract] Cited for: CHARACTERIZATION. Strain: Sprague-Dawley. Tissue: Heart.
[8]	"Topology of carnitine palmitoyltransferase I in the mitochondrial outer membrane." Fraser F., Corstorphine C.G., Zammit V.A. Biochem. J. 323:711-718(1997) [PubMed: 9169604] [Abstract] Cited for: TOPOLOGY.
[9]	"Structural model of the catalytic core of carnitine palmitoyltransferase I and carnitine octanoyltransferase (COT): mutation of CPT I histidine 473 and alanine 381 and COT alanine 238 impairs the catalytic activity." Morillas M., Gomez-Puertas P., Roca R., Serra D., Asins G., Valencia A., Hegardt F.G. J. Biol. Chem. 276:45001-45008(2001) [PubMed: 11553629] [Abstract] Cited for: MUTAGENESIS OF ALA-381 AND HIS-473, 3D-STRUCTURE MODELING.
[10]	"Identification of conserved amino acid residues in rat liver carnitine palmitoyltransferase I critical for malonyl-CoA inhibition. Mutation of methionine 593 abolishes malonyl-CoA inhibition." Morillas M., Gomez-Puertas P., Bentebibel A., Selles E., Casals N., Valencia A., Hegardt F.G., Asins G., Serra D. J. Biol. Chem. 278:9058-9063(2003) [PubMed: 12499375] [Abstract] Cited for: MUTAGENESIS OF MET-593 AND CYS-608.
[11]	"Structural model of carnitine palmitoyltransferase I based on the carnitine acetyltransferase crystal." Morillas M., Lopez-Vinas E., Valencia A., Serra D., Gomez-Puertas P., Hegardt F.G., Asins G. Biochem. J. 379:777-784(2004) [PubMed: 14711372] [Abstract] Cited for: MUTAGENESIS OF ASP-477; LYS-560; GLU-590; SER-685; THR-686 AND SER-687, 3D-STRUCTURE MODELING.
+	Additional computationally mapped references.

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Cross-references

Sequence databases
EMBL GenBank DDBJ	L07736 mRNA. Translation: AAA40876.1. U88294 mRNA. Translation: AAB48046.1. BC072522 mRNA. Translation: AAH72522.1.
IPI	IPI00213538.
PIR	A46627.
RefSeq	NP_113747.2.
UniGene	Rn.2856
3D structure databases
SMR	P32198. Positions 167-765.
ModBase	Search...
Protein-protein interaction databases
STRING	P32198.
PTM databases
PhosphoSite	P32198.
Proteomic databases
PRIDE	P32198.
Genome annotation databases
Ensembl	ENSRNOT00000019652; ENSRNOP00000019652; ENSRNOG00000014254; Rattus norvegicus. [Genome view]
GeneID	25757.
KEGG	rno:25757.
UCSC	NM_031559. rat.
Organism-specific databases
CTD	25757.
RGD	2396. Cpt1a.
Phylogenomic databases
eggNOG	maNOG13702.
HOVERGEN	P32198.
InParanoid	P32198.
OMA	KGWMYES.
OrthoDB	EOG9PP124.
PhylomeDB	P32198.
Enzyme and pathway databases
BioCyc	MetaCyc:MONOMER-14439.
BRENDA	2.3.1.21. 248.
Gene expression databases
ArrayExpress	P32198.
Genevestigator	P32198.
GermOnline	ENSRNOG00000014254. Rattus norvegicus.
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...
Other Resources
NextBio	607961.

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Entry information

Entry name

CPT1A_RAT

Accession

Primary (citable) accession number: P32198
Secondary accession number(s): P97780, Q6IMZ4

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1993
Last sequence update:	May 1, 2007
Last modified:	January 19, 2010
This is version 86 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents