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Carnitine O-palmitoyltransferase 1, liver isoform (CPT1-L) (EC 2.3.1.21) (Carnitine O-palmitoyltransferase I, liver isoform) (CPT I) (CPTI-L) (Carnitine palmitoyltransferase 1A)

 CPT1A_RAT               Reviewed;         773 AA.
P32198; P97780; Q6IMZ4;
01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
01-MAY-2007, sequence version 2.
23-MAY-2018, entry version 151.
RecName: Full=Carnitine O-palmitoyltransferase 1, liver isoform;
Short=CPT1-L;
EC=2.3.1.21;
AltName: Full=Carnitine O-palmitoyltransferase I, liver isoform;
Short=CPT I;
Short=CPTI-L;
AltName: Full=Carnitine palmitoyltransferase 1A;
Name=Cpt1a; Synonyms=Cpt-1, Cpt1;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Liver;
PubMed=8449948;
Esser V., Britton C.H., Weis B.C., Foster D.W., McGarry J.D.;
"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.";
J. Biol. Chem. 268:5817-5822(1993).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Sprague-Dawley; TISSUE=Liver;
PubMed=9136891; DOI=10.1021/bi962875p;
de Vries Y., Arvidson D.N., Waterham H.R., Cregg J.M.,
Woldegiorgis G.;
"Functional characterization of mitochondrial carnitine
palmitoyltransferases I and II expressed in the yeast Pichia
pastoris.";
Biochemistry 36:5285-5292(1997).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Heart;
PubMed=15489334; DOI=10.1101/gr.2596504;
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).
[4]
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, AND IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Liver;
PubMed=17478130; DOI=10.1016/j.bbapap.2007.03.012;
Distler A.M., Kerner J., Hoppel C.L.;
"Post-translational modifications of rat liver mitochondrial outer
membrane proteins identified by mass spectrometry.";
Biochim. Biophys. Acta 1774:628-636(2007).
[5]
PROTEIN SEQUENCE OF 4-21; 259-276; 361-379; 529-543 AND 696-717.
TISSUE=Liver;
PubMed=8348957; DOI=10.1016/0014-5793(93)81007-M;
Kolodziej M.P., Zammit V.A.;
"Mature carnitine palmitoyltransferase I retains the N-terminus of the
nascent protein in rat liver.";
FEBS Lett. 327:294-296(1993).
[6]
PARTIAL PROTEIN SEQUENCE.
PubMed=8449947;
Esser V., Kuwajima M., Britton C.H., Krishnan K., Foster D.W.,
McGarry J.D.;
"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.";
J. Biol. Chem. 268:5810-5816(1993).
[7]
CHARACTERIZATION.
STRAIN=Sprague-Dawley; TISSUE=Heart;
PubMed=8636126; DOI=10.1074/jbc.271.12.6972;
Esser V., Brown N.F., Cowan A.T., Foster D.W., McGarry J.D.;
"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.";
J. Biol. Chem. 271:6972-6977(1996).
[8]
TOPOLOGY.
PubMed=9169604; DOI=10.1042/bj3230711;
Fraser F., Corstorphine C.G., Zammit V.A.;
"Topology of carnitine palmitoyltransferase I in the mitochondrial
outer membrane.";
Biochem. J. 323:711-718(1997).
[9]
MUTAGENESIS OF ALA-381 AND HIS-473, AND 3D-STRUCTURE MODELING.
PubMed=11553629; DOI=10.1074/jbc.M106920200;
Morillas M., Gomez-Puertas P., Roca R., Serra D., Asins G.,
Valencia A., Hegardt F.G.;
"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.";
J. Biol. Chem. 276:45001-45008(2001).
[10]
MUTAGENESIS OF MET-593 AND CYS-608.
PubMed=12499375; DOI=10.1074/jbc.M209999200;
Morillas M., Gomez-Puertas P., Bentebibel A., Selles E., Casals N.,
Valencia A., Hegardt F.G., Asins G., Serra D.;
"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.";
J. Biol. Chem. 278:9058-9063(2003).
[11]
MUTAGENESIS OF ASP-477; LYS-560; GLU-590; SER-685; THR-686 AND
SER-687, AND 3D-STRUCTURE MODELING.
PubMed=14711372; DOI=10.1042/BJ20031373;
Morillas M., Lopez-Vinas E., Valencia A., Serra D., Gomez-Puertas P.,
Hegardt F.G., Asins G.;
"Structural model of carnitine palmitoyltransferase I based on the
carnitine acetyltransferase crystal.";
Biochem. J. 379:777-784(2004).
[12]
SUBCELLULAR LOCATION, CATALYTIC ACTIVITY, AND ENZYME REGULATION.
PubMed=16908527; DOI=10.1074/jbc.M600843200;
Borthwick K., Jackson V.N., Price N.T., Zammit V.A.;
"The mitochondrial intermembrane loop region of rat carnitine
palmitoyltransferase 1A is a major determinant of its malonyl-CoA
sensitivity.";
J. Biol. Chem. 281:32946-32952(2006).
[13]
FUNCTION.
PubMed=18349115; DOI=10.1152/ajpendo.00497.2007;
Stefanovic-Racic M., Perdomo G., Mantell B.S., Sipula I.J.,
Brown N.F., O'Doherty R.M.;
"A moderate increase in carnitine palmitoyltransferase 1a activity is
sufficient to substantially reduce hepatic triglyceride levels.";
Am. J. Physiol. 294:E969-E977(2008).
[14]
SUBUNIT, AND SUBCELLULAR LOCATION.
PubMed=19136561; DOI=10.1074/jbc.M808487200;
Jenei Z.A., Borthwick K., Zammit V.A., Dixon A.M.;
"Self-association of transmembrane domain 2 (TM2), but not TM1, in
carnitine palmitoyltransferase 1A: role of GXXXG(A) motifs.";
J. Biol. Chem. 284:6988-6997(2009).
[15]
SUBCELLULAR LOCATION, IDENTIFICATION IN A COMPLEX WITH ACSL1 AND
VDAC1; IDENTIFICATION IN COMPLEXES WITH ACSL1; VDAC2 AND VDAC3, AND
IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=21622568; DOI=10.1074/jbc.M111.228692;
Lee K., Kerner J., Hoppel C.L.;
"Mitochondrial carnitine palmitoyltransferase 1a (CPT1a) is part of an
outer membrane fatty acid transfer complex.";
J. Biol. Chem. 286:25655-25662(2011).
[16]
CATALYTIC ACTIVITY, ENZYME REGULATION, DOMAIN, AND MUTAGENESIS OF
GLU-3; ALA-9 AND GLY-18.
PubMed=21990363; DOI=10.1074/jbc.M111.306951;
Rao J.N., Warren G.Z., Estolt-Povedano S., Zammit V.A., Ulmer T.S.;
"An environment-dependent structural switch underlies the regulation
of carnitine palmitoyltransferase 1A.";
J. Biol. Chem. 286:42545-42554(2011).
-!- FUNCTION: Catalyzes the transfer of the acyl group of long-chain
fatty acid-CoA conjugates onto carnitine, an essential step for
the mitochondrial uptake of long-chain fatty acids and their
subsequent beta-oxidation in the mitochondrion. Plays an important
role in triglyceride metabolism. {ECO:0000269|PubMed:18349115}.
-!- CATALYTIC ACTIVITY: Palmitoyl-CoA + L-carnitine = CoA + L-
palmitoylcarnitine. {ECO:0000269|PubMed:16908527,
ECO:0000269|PubMed:21990363}.
-!- ENZYME REGULATION: Inhibited by malonyl-CoA.
{ECO:0000269|PubMed:16908527, ECO:0000269|PubMed:21990363}.
-!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
-!- SUBUNIT: Homohexamer and homotrimer. Identified in a complex that
contains at least CPT1A, ACSL1 and VDAC1. Also identified in
complexes with ACSL1 and VDAC2 and VDAC3.
{ECO:0000269|PubMed:19136561, ECO:0000269|PubMed:21622568}.
-!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
{ECO:0000269|PubMed:16908527, ECO:0000269|PubMed:19136561,
ECO:0000269|PubMed:21622568}; Multi-pass membrane protein
{ECO:0000269|PubMed:16908527, ECO:0000269|PubMed:19136561,
ECO:0000269|PubMed:21622568}.
-!- TISSUE SPECIFICITY: Liver and kidney.
-!- DOMAIN: A conformation change in the N-terminal region spanning
the first 42 residues plays an important role in the regulation of
enzyme activity by malonyl-CoA. {ECO:0000269|PubMed:21990363}.
-!- SIMILARITY: Belongs to the carnitine/choline acetyltransferase
family. {ECO:0000305}.
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EMBL; L07736; AAA40876.1; -; mRNA.
EMBL; U88294; AAB48046.1; -; mRNA.
EMBL; BC072522; AAH72522.1; -; mRNA.
PIR; A46627; A46627.
RefSeq; NP_113747.2; NM_031559.2.
RefSeq; XP_006230757.1; XM_006230695.2.
RefSeq; XP_017444326.1; XM_017588837.1.
UniGene; Rn.2856; -.
ProteinModelPortal; P32198; -.
SMR; P32198; -.
CORUM; P32198; -.
IntAct; P32198; 1.
MINT; P32198; -.
STRING; 10116.ENSRNOP00000019652; -.
BindingDB; P32198; -.
ChEMBL; CHEMBL3858; -.
SwissLipids; SLP:000000777; -.
iPTMnet; P32198; -.
PhosphoSitePlus; P32198; -.
PaxDb; P32198; -.
PRIDE; P32198; -.
Ensembl; ENSRNOT00000019652; ENSRNOP00000019652; ENSRNOG00000014254.
GeneID; 25757; -.
KEGG; rno:25757; -.
UCSC; RGD:2396; rat.
CTD; 1374; -.
RGD; 2396; Cpt1a.
eggNOG; KOG3717; Eukaryota.
eggNOG; ENOG410XNZ9; LUCA.
GeneTree; ENSGT00760000119220; -.
HOGENOM; HOG000233542; -.
HOVERGEN; HBG003458; -.
InParanoid; P32198; -.
KO; K08765; -.
OMA; ASHMWEN; -.
OrthoDB; EOG091G026C; -.
PhylomeDB; P32198; -.
TreeFam; TF313836; -.
BioCyc; MetaCyc:MONOMER-14439; -.
BRENDA; 2.3.1.21; 5301.
Reactome; R-RNO-200425; Import of palmitoyl-CoA into the mitochondrial matrix.
Reactome; R-RNO-5362517; Signaling by Retinoic Acid.
SABIO-RK; P32198; -.
UniPathway; UPA00659; -.
PRO; PR:P32198; -.
Proteomes; UP000002494; Chromosome 1.
Bgee; ENSRNOG00000014254; -.
Genevisible; P32198; RN.
GO; GO:0016021; C:integral component of membrane; IDA:RGD.
GO; GO:0031307; C:integral component of mitochondrial outer membrane; IDA:UniProtKB.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:RGD.
GO; GO:0005741; C:mitochondrial outer membrane; IDA:RGD.
GO; GO:0005739; C:mitochondrion; IDA:RGD.
GO; GO:0004095; F:carnitine O-palmitoyltransferase activity; IDA:UniProtKB.
GO; GO:0042802; F:identical protein binding; IDA:RGD.
GO; GO:1990698; F:palmitoleoyltransferase activity; IEA:Ensembl.
GO; GO:0009437; P:carnitine metabolic process; IDA:UniProtKB.
GO; GO:0071398; P:cellular response to fatty acid; IEP:RGD.
GO; GO:0042755; P:eating behavior; IMP:RGD.
GO; GO:0030855; P:epithelial cell differentiation; IEA:Ensembl.
GO; GO:0006635; P:fatty acid beta-oxidation; IEA:UniProtKB-UniPathway.
GO; GO:0006006; P:glucose metabolic process; IMP:RGD.
GO; GO:0001676; P:long-chain fatty acid metabolic process; IDA:UniProtKB.
GO; GO:0032000; P:positive regulation of fatty acid beta-oxidation; IMP:RGD.
GO; GO:0051260; P:protein homooligomerization; IDA:RGD.
GO; GO:0031998; P:regulation of fatty acid beta-oxidation; TAS:RGD.
GO; GO:0046320; P:regulation of fatty acid oxidation; IMP:RGD.
GO; GO:0050796; P:regulation of insulin secretion; IMP:RGD.
GO; GO:0042493; P:response to drug; IEP:RGD.
GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
GO; GO:0006641; P:triglyceride metabolic process; IMP:RGD.
InterPro; IPR000542; Carn_acyl_trans.
InterPro; IPR032476; CPT_N.
PANTHER; PTHR22589; PTHR22589; 1.
Pfam; PF00755; Carn_acyltransf; 1.
Pfam; PF16484; CPT_N; 1.
PROSITE; PS00439; ACYLTRANSF_C_1; 1.
PROSITE; PS00440; ACYLTRANSF_C_2; 1.
1: Evidence at protein level;
Acetylation; Acyltransferase; Complete proteome;
Direct protein sequencing; Fatty acid metabolism; Lipid metabolism;
Membrane; Mitochondrion; Mitochondrion outer membrane; Nitration;
Phosphoprotein; Reference proteome; Transferase; Transmembrane;
Transmembrane helix; Transport.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:17478130}.
CHAIN 2 773 Carnitine O-palmitoyltransferase 1, liver
isoform.
/FTId=PRO_0000210161.
TOPO_DOM 2 47 Cytoplasmic. {ECO:0000255}.
TRANSMEM 48 73 Helical. {ECO:0000255}.
TOPO_DOM 74 102 Mitochondrial intermembrane.
{ECO:0000255}.
TRANSMEM 103 122 Helical. {ECO:0000255}.
TOPO_DOM 123 773 Cytoplasmic. {ECO:0000255}.
REGION 555 567 Coenzyme A binding. {ECO:0000250}.
ACT_SITE 473 473 Proton acceptor.
BINDING 589 589 Carnitine. {ECO:0000250}.
BINDING 602 602 Carnitine. {ECO:0000250}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000269|PubMed:17478130}.
MOD_RES 282 282 Nitrated tyrosine.
{ECO:0000269|PubMed:17478130}.
MOD_RES 588 588 Phosphothreonine.
{ECO:0000269|PubMed:17478130}.
MOD_RES 589 589 Nitrated tyrosine.
{ECO:0000269|PubMed:17478130}.
MOD_RES 604 604 Phosphothreonine.
{ECO:0000269|PubMed:17478130}.
MOD_RES 741 741 Phosphoserine.
{ECO:0000269|PubMed:17478130}.
MOD_RES 747 747 Phosphoserine.
{ECO:0000269|PubMed:17478130}.
MUTAGEN 3 3 E->R: Decreases susceptibility to
inhibition by malonyl-CoA.
{ECO:0000269|PubMed:21990363}.
MUTAGEN 9 9 A->G: Increases susceptibility to
inhibition by malonyl-CoA.
{ECO:0000269|PubMed:21990363}.
MUTAGEN 18 18 G->A: Increases susceptibility to
inhibition by malonyl-CoA.
{ECO:0000269|PubMed:21990363}.
MUTAGEN 381 381 A->D: Reduces activity by 86%. No effect
on inhibition by malonyl-coenzyme A.
{ECO:0000269|PubMed:11553629}.
MUTAGEN 473 473 H->A: Loss of activity.
{ECO:0000269|PubMed:11553629}.
MUTAGEN 477 477 D->A: Reduces activity by 98%.
{ECO:0000269|PubMed:14711372}.
MUTAGEN 560 560 K->A: Reduces activity by 50%.
{ECO:0000269|PubMed:14711372}.
MUTAGEN 567 567 D->A: Reduces activity by 97%.
MUTAGEN 590 590 E->D: Reduces activity by over 60%.
{ECO:0000269|PubMed:14711372}.
MUTAGEN 593 593 M->A,E,S: Almost abolishes inhibition by
malonyl-coenzyme A.
{ECO:0000269|PubMed:12499375}.
MUTAGEN 608 608 C->A: Slightly lowers inhibition by
malonyl-coenzyme A.
{ECO:0000269|PubMed:12499375}.
MUTAGEN 685 685 S->A: Reduces activity by 50%.
{ECO:0000269|PubMed:14711372}.
MUTAGEN 686 686 T->A: Loss of activity.
{ECO:0000269|PubMed:14711372}.
MUTAGEN 687 687 S->A: Loss of activity.
{ECO:0000269|PubMed:14711372}.
CONFLICT 266 266 H -> D (in Ref. 5; AA sequence).
{ECO:0000305}.
CONFLICT 374 375 QP -> NG (in Ref. 5; AA sequence).
{ECO:0000305}.
CONFLICT 480 480 V -> I (in Ref. 1; AAA40876).
{ECO:0000305}.
CONFLICT 531 531 D -> Y (in Ref. 5; AA sequence).
{ECO:0000305}.
CONFLICT 708 708 C -> R (in Ref. 5; AA sequence).
{ECO:0000305}.
SEQUENCE 773 AA; 88125 MW; 8C15594D45430CB8 CRC64;
MAEAHQAVAF QFTVTPDGID LRLSHEALKQ ICLSGLHSWK KKFIRFKNGI ITGVFPANPS
SWLIVVVGVI SSMHAKVDPS LGMIAKISRT LDTTGRMSSQ TKNIVSGVLF GTGLWVAVIM
TMRYSLKVLL SYHGWMFAEH GKMSRSTKIW MAMVKVLSGR KPMLYSFQTS LPRLPVPAVK
DTVSRYLESV RPLMKEEDFQ RMTALAQDFA VNLGPKLQWY LKLKSWWATN YVSDWWEEYI
YLRGRGPLMV NSNYYAMEML YITPTHIQAA RAGNTIHAIL LYRRTLDREE LKPIRLLGST
IPLCSAQWER LFNTSRIPGE ETDTIQHIKD SRHIVVYHRG RYFKVWLYHD GRLLRPRELE
QQMQQILDDP SEPQPGEAKL AALTAADRVP WAKCRQTYFA RGKNKQSLDA VEKAAFFVTL
DESEQGYREE DPEASIDSYA KSLLHGRCFD RWFDKSITFV VFKNSKIGIN AEHSWADAPV
VGHLWEYVMA TDVFQLGYSE DGHCKGDTNP NIPKPTRLQW DIPGECQEVI DASLSSASLL
ANDVDLHSFP FDSFGKGLIK KCRTSPDAFI QLALQLAHYK DMGKFCLTYE ASMTRLFREG
RTETVRSCTM ESCNFVQAMM DPKSTAEQRL KLFKIACEKH QHLYRLAMTG AGIDRHLFCL
YVVSKYLAVD SPFLKEVLSE PWRLSTSQTP QQQVELFDFE KNPDYVSCGG GFGPVADDGY
GVSYIIVGEN FIHFHISSKF SSPETDSHRF GKHLRQAMMD IITLFGLTIN SKK


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