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Protein

Carnitine O-palmitoyltransferase 1, liver isoform

Gene

Cpt1a

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.2 Publications

Catalytic activityi

Palmitoyl-CoA + L-carnitine = CoA + L-palmitoylcarnitine.1 Publication

Enzyme regulationi

Inhibited by malonyl-CoA.

Pathwayi: fatty acid beta-oxidation

This protein is involved in the pathway fatty acid beta-oxidation, which is part of Lipid metabolism.
View all proteins of this organism that are known to be involved in the pathway fatty acid beta-oxidation and in Lipid metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei473 – 4731Proton acceptorBy similarity
Binding sitei589 – 5891CarnitineBy similarity
Binding sitei602 – 6021CarnitineBy similarity

GO - Molecular functioni

  • carnitine O-palmitoyltransferase activity Source: UniProtKB
  • palmitoleoyltransferase activity Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Fatty acid metabolism, Lipid metabolism, Transport

Enzyme and pathway databases

ReactomeiR-MMU-1368092. Rora activates gene expression.
R-MMU-200425. Import of palmitoyl-CoA into the mitochondrial matrix.
R-MMU-5362517. Signaling by Retinoic Acid.
UniPathwayiUPA00659.

Names & Taxonomyi

Protein namesi
Recommended name:
Carnitine O-palmitoyltransferase 1, liver isoform (EC:2.3.1.21)
Short name:
CPT1-L
Alternative name(s):
Carnitine O-palmitoyltransferase I, liver isoform
Short name:
CPT I
Short name:
CPTI-L
Carnitine palmitoyltransferase 1A
Gene namesi
Name:Cpt1a
Synonyms:Cpt-1, Cpt1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 19

Organism-specific databases

MGIiMGI:1098296. Cpt1a.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini2 – 4746CytoplasmicSequence analysisAdd
BLAST
Transmembranei48 – 7326HelicalSequence analysisAdd
BLAST
Topological domaini74 – 10229Mitochondrial intermembraneSequence analysisAdd
BLAST
Transmembranei103 – 12220HelicalSequence analysisAdd
BLAST
Topological domaini123 – 773651CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • integral component of mitochondrial outer membrane Source: UniProtKB
  • membrane Source: MGI
  • mitochondrial inner membrane Source: MGI
  • mitochondrial outer membrane Source: Reactome
  • mitochondrion Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion outer membrane

Pathology & Biotechi

Disruption phenotypei

Complete lethality during early embryogenesis. Heterozygous mice are prone to liver steatosis. Compared to wild-type, heterozygotes show minor differences in blood glucose levels and in serum free fatty acid levels after fasting.2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 773772Carnitine O-palmitoyltransferase 1, liver isoformPRO_0000210160Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei282 – 2821Nitrated tyrosineBy similarity
Modified residuei588 – 5881PhosphothreonineBy similarity
Modified residuei589 – 5891Nitrated tyrosineBy similarity
Modified residuei604 – 6041PhosphothreonineBy similarity
Modified residuei741 – 7411PhosphoserineBy similarity
Modified residuei747 – 7471PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Nitration, Phosphoprotein

Proteomic databases

EPDiP97742.
PaxDbiP97742.
PeptideAtlasiP97742.
PRIDEiP97742.

PTM databases

iPTMnetiP97742.
PhosphoSiteiP97742.
SwissPalmiP97742.

Expressioni

Gene expression databases

BgeeiP97742.
CleanExiMM_CPT1A.
ExpressionAtlasiP97742. baseline and differential.
GenevisibleiP97742. MM.

Interactioni

Subunit structurei

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 (By similarity).By similarity

Protein-protein interaction databases

BioGridi198863. 1 interaction.
MINTiMINT-1845420.
STRINGi10090.ENSMUSP00000025835.

Structurei

3D structure databases

ProteinModelPortaliP97742.
SMRiP97742. Positions 1-42, 168-761.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni555 – 56713Coenzyme A bindingBy similarityAdd
BLAST

Domaini

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.By similarity

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3717. Eukaryota.
ENOG410XNZ9. LUCA.
HOGENOMiHOG000233542.
HOVERGENiHBG003458.
InParanoidiP97742.
KOiK08765.
OMAiHIVVFHK.
OrthoDBiEOG7J17ZQ.
PhylomeDBiP97742.
TreeFamiTF313836.

Family and domain databases

InterProiIPR000542. Carn_acyl_trans.
IPR032476. CPT_N.
[Graphical view]
PANTHERiPTHR22589. PTHR22589. 1 hit.
PfamiPF00755. Carn_acyltransf. 1 hit.
PF16484. CPT_N. 1 hit.
[Graphical view]
PROSITEiPS00439. ACYLTRANSF_C_1. 1 hit.
PS00440. ACYLTRANSF_C_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P97742-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAEAHQAVAF QFTVTPDGID LRLSHEALKQ ICLSGLHSWK KKFIRFKNGI
60 70 80 90 100
ITGVFPASPS SWLIVVVGVI SSMHTKVDPS LGMIAKINRT LDTTGRMSSQ
110 120 130 140 150
TKNIVSGVLF GTGLWVAIIM TMRYSLKVLL SYHGWMFAEH GKMSRSTRIW
160 170 180 190 200
MAMVKVFSGR KPMLYSFQTS LPRLPVPAVK DTVSRYLESV RPLMKEGDFQ
210 220 230 240 250
RMTALAQDFA VNLGPKLQWY LKLKSWWATN YVSDWWEEYI YLRGRGPIMV
260 270 280 290 300
NSNYYAMEML YITPTHIQAA RAGNTIHAIL LYRRTVDREE LKPIRLLGST
310 320 330 340 350
IPLCSAQWER LFNTSRIPGE ETDTIQHVKD SRHIVVYHRG RYFKVWLYHD
360 370 380 390 400
GRLLRPRELE QQMQQILDDT SEPQPGEAKL AALTAADRVP WAKCRQTYFA
410 420 430 440 450
RGKNKQSLDA VEKAAFFVTL DESEQGYREE DPEASIDSYA KSLLHGRCFD
460 470 480 490 500
RWFDKSITFV VFKNSKIGIN AEHSWADAPI VGHLWEYVMA TDVFQLGYSE
510 520 530 540 550
DGHCKGDKNP NIPKPTRLQW DIPGECQEVI ETSLSSASFL ANDVDLHSFP
560 570 580 590 600
FDTFGKGLIK KCRTSPDAFI QLALQLAHYK DMGKFCLTYE ASMTRLFREG
610 620 630 640 650
RTETVRSCTT ESCNFVLAMM DPTTTAEQRF KLFKIACEKH QHLYRLAMTG
660 670 680 690 700
AGIDRHLFCL YVVSKYLAVD SPFLKEVLSE PWRLSTSQTP QQQVELFDFE
710 720 730 740 750
KYPDYVSCGG GFGPVADDGY GVSYIIVGEN FIHFHISSKF SSPETDSHRF
760 770
GKHLRQAMMD IITLFGLTAN SKK
Length:773
Mass (Da):88,251
Last modified:July 5, 2004 - v4
Checksum:i85C3D386FFD97C5E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti145 – 1451R → C in AAH38395 (PubMed:15489334).Curated
Sequence conflicti145 – 1451R → C in AAH46383 (PubMed:15489334).Curated
Sequence conflicti398 – 3981Y → C in AAC31641 (PubMed:9680378).Curated
Sequence conflicti531 – 5311E → D in BAC36808 (PubMed:16141072).Curated
Sequence conflicti630 – 6301F → L in AAC31641 (PubMed:9680378).Curated
Sequence conflicti732 – 7321I → T in AAC31641 (PubMed:9680378).Curated
Sequence conflicti760 – 7601D → A in AAC31641 (PubMed:9680378).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK050213 mRNA. Translation: BAC34126.2.
AK077454 mRNA. Translation: BAC36808.1.
BC038395 mRNA. Translation: AAH38395.1.
BC046383 mRNA. Translation: AAH46383.1.
AF017175 mRNA. Translation: AAC31641.1.
S82796 mRNA. Translation: AAB39370.1.
CCDSiCCDS29395.1.
RefSeqiNP_038523.2. NM_013495.2.
XP_006531717.1. XM_006531654.1.
XP_006531718.1. XM_006531655.1.
XP_006531719.1. XM_006531656.2.
XP_006531720.1. XM_006531657.2.
XP_006531721.1. XM_006531658.2.
XP_006531722.1. XM_006531659.2.
UniGeneiMm.18522.

Genome annotation databases

EnsembliENSMUST00000025835; ENSMUSP00000025835; ENSMUSG00000024900.
GeneIDi12894.
KEGGimmu:12894.
UCSCiuc008fwf.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK050213 mRNA. Translation: BAC34126.2.
AK077454 mRNA. Translation: BAC36808.1.
BC038395 mRNA. Translation: AAH38395.1.
BC046383 mRNA. Translation: AAH46383.1.
AF017175 mRNA. Translation: AAC31641.1.
S82796 mRNA. Translation: AAB39370.1.
CCDSiCCDS29395.1.
RefSeqiNP_038523.2. NM_013495.2.
XP_006531717.1. XM_006531654.1.
XP_006531718.1. XM_006531655.1.
XP_006531719.1. XM_006531656.2.
XP_006531720.1. XM_006531657.2.
XP_006531721.1. XM_006531658.2.
XP_006531722.1. XM_006531659.2.
UniGeneiMm.18522.

3D structure databases

ProteinModelPortaliP97742.
SMRiP97742. Positions 1-42, 168-761.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi198863. 1 interaction.
MINTiMINT-1845420.
STRINGi10090.ENSMUSP00000025835.

PTM databases

iPTMnetiP97742.
PhosphoSiteiP97742.
SwissPalmiP97742.

Proteomic databases

EPDiP97742.
PaxDbiP97742.
PeptideAtlasiP97742.
PRIDEiP97742.

Protocols and materials databases

DNASUi12894.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000025835; ENSMUSP00000025835; ENSMUSG00000024900.
GeneIDi12894.
KEGGimmu:12894.
UCSCiuc008fwf.2. mouse.

Organism-specific databases

CTDi1374.
MGIiMGI:1098296. Cpt1a.

Phylogenomic databases

eggNOGiKOG3717. Eukaryota.
ENOG410XNZ9. LUCA.
HOGENOMiHOG000233542.
HOVERGENiHBG003458.
InParanoidiP97742.
KOiK08765.
OMAiHIVVFHK.
OrthoDBiEOG7J17ZQ.
PhylomeDBiP97742.
TreeFamiTF313836.

Enzyme and pathway databases

UniPathwayiUPA00659.
ReactomeiR-MMU-1368092. Rora activates gene expression.
R-MMU-200425. Import of palmitoyl-CoA into the mitochondrial matrix.
R-MMU-5362517. Signaling by Retinoic Acid.

Miscellaneous databases

PROiP97742.
SOURCEiSearch...

Gene expression databases

BgeeiP97742.
CleanExiMM_CPT1A.
ExpressionAtlasiP97742. baseline and differential.
GenevisibleiP97742. MM.

Family and domain databases

InterProiIPR000542. Carn_acyl_trans.
IPR032476. CPT_N.
[Graphical view]
PANTHERiPTHR22589. PTHR22589. 1 hit.
PfamiPF00755. Carn_acyltransf. 1 hit.
PF16484. CPT_N. 1 hit.
[Graphical view]
PROSITEiPS00439. ACYLTRANSF_C_1. 1 hit.
PS00440. ACYLTRANSF_C_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Embryo and Liver.
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: FVB/N.
    Tissue: Liver and Mammary gland.
  3. "Chromosomal locations of the mouse fatty acid oxidation genes Cpt1a, Cpt1b, Cpt2, Acadvl, and metabolically related Crat gene."
    Cox K.B., Johnson K.R., Wood P.A.
    Mamm. Genome 9:608-610(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 10-773.
    Strain: ICR.
    Tissue: Liver.
  4. "Increased expression of carnitine palmitoyltransferase I gene is repressed by administering L-carnitine in the hearts of carnitine-deficient juvenile visceral steatosis mice."
    Uenaka R., Kuwajima M., Ono A., Matsuzawa Y., Hayakawa J., Inohara N., Kagawa Y., Ohta S.
    J. Biochem. 119:533-540(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 734-773.
    Tissue: Heart.
  5. "Homozygous carnitine palmitoyltransferase 1a (liver isoform) deficiency is lethal in the mouse."
    Nyman L.R., Cox K.B., Hoppel C.L., Kerner J., Barnoski B.L., Hamm D.A., Tian L., Schoeb T.R., Wood P.A.
    Mol. Genet. Metab. 86:179-187(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE, FUNCTION, CATALYTIC ACTIVITY.
  6. "Phosphatidylinositol 3-kinase-dependent modulation of carnitine palmitoyltransferase 1A expression regulates lipid metabolism during hematopoietic cell growth."
    Deberardinis R.J., Lum J.J., Thompson C.B.
    J. Biol. Chem. 281:37372-37380(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  8. "Long term effects of high fat or high carbohydrate diets on glucose tolerance in mice with heterozygous carnitine palmitoyltransferase-1a (CPT-1a) deficiency: Diet influences on CPT1a deficient mice."
    Nyman L.R., Tian L., Hamm D.A., Schoeb T.R., Gower B.A., Nagy T.R., Wood P.A.
    Nutr. Diabetes 1:E14-E14(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE.

Entry informationi

Entry nameiCPT1A_MOUSE
AccessioniPrimary (citable) accession number: P97742
Secondary accession number(s): O35288
, Q80SW3, Q8BP98, Q8C7H8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 5, 2004
Last modified: July 6, 2016
This is version 142 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.