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Protein

Carnitine O-palmitoyltransferase 1, liver isoform

Gene

Cpt1a

Organism
Rattus norvegicus (Rat)
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.1 Publication

Catalytic activityi

Palmitoyl-CoA + L-carnitine = CoA + L-palmitoylcarnitine.2 Publications

Enzyme regulationi

Inhibited by malonyl-CoA.2 Publications

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)DescriptionActionsGraphical viewLength
Active sitei473Proton acceptor1
Binding sitei589CarnitineBy similarity1
Binding sitei602CarnitineBy similarity1

GO - Molecular functioni

  • carnitine O-palmitoyltransferase activity Source: UniProtKB
  • identical protein binding Source: RGD
  • palmitoleoyltransferase activity Source: Ensembl

GO - Biological processi

  • carnitine metabolic process Source: UniProtKB
  • cellular response to fatty acid Source: RGD
  • eating behavior Source: RGD
  • epithelial cell differentiation Source: Ensembl
  • fatty acid beta-oxidation Source: UniProtKB-UniPathway
  • glucose metabolic process Source: RGD
  • long-chain fatty acid metabolic process Source: UniProtKB
  • positive regulation of fatty acid beta-oxidation Source: RGD
  • protein homooligomerization Source: RGD
  • regulation of fatty acid beta-oxidation Source: RGD
  • regulation of fatty acid oxidation Source: RGD
  • regulation of insulin secretion Source: RGD
  • response to drug Source: RGD
  • response to organic cyclic compound Source: RGD
  • transport Source: UniProtKB-KW
  • triglyceride metabolic process Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Fatty acid metabolism, Lipid metabolism, Transport

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-14439.
BRENDAi2.3.1.21. 5301.
ReactomeiR-RNO-200425. Import of palmitoyl-CoA into the mitochondrial matrix.
R-RNO-5362517. Signaling by Retinoic Acid.
SABIO-RKP32198.
UniPathwayiUPA00659.

Chemistry databases

SwissLipidsiSLP:000000777.

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
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 1

Organism-specific databases

RGDi2396. Cpt1a.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini2 – 47CytoplasmicSequence analysisAdd BLAST46
Transmembranei48 – 73HelicalSequence analysisAdd BLAST26
Topological domaini74 – 102Mitochondrial intermembraneSequence analysisAdd BLAST29
Transmembranei103 – 122HelicalSequence analysisAdd BLAST20
Topological domaini123 – 773CytoplasmicSequence analysisAdd BLAST651

GO - Cellular componenti

  • integral component of membrane Source: RGD
  • integral component of mitochondrial outer membrane Source: UniProtKB
  • intracellular membrane-bounded organelle Source: RGD
  • mitochondrial inner membrane Source: Ensembl
  • mitochondrial outer membrane Source: RGD
  • mitochondrion Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion outer membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi3E → R: Decreases susceptibility to inhibition by malonyl-CoA. 1 Publication1
Mutagenesisi9A → G: Increases susceptibility to inhibition by malonyl-CoA. 1 Publication1
Mutagenesisi18G → A: Increases susceptibility to inhibition by malonyl-CoA. 1 Publication1
Mutagenesisi381A → D: Reduces activity by 86%. No effect on inhibition by malonyl-coenzyme A. 1 Publication1
Mutagenesisi473H → A: Loss of activity. 1 Publication1
Mutagenesisi477D → A: Reduces activity by 98%. 1 Publication1
Mutagenesisi560K → A: Reduces activity by 50%. 1 Publication1
Mutagenesisi567D → A: Reduces activity by 97%. 1
Mutagenesisi590E → D: Reduces activity by over 60%. 1 Publication1
Mutagenesisi593M → A, E or S: Almost abolishes inhibition by malonyl-coenzyme A. 1 Publication1
Mutagenesisi608C → A: Slightly lowers inhibition by malonyl-coenzyme A. 1 Publication1
Mutagenesisi685S → A: Reduces activity by 50%. 1 Publication1
Mutagenesisi686T → A: Loss of activity. 1 Publication1
Mutagenesisi687S → A: Loss of activity. 1 Publication1

Chemistry databases

ChEMBLiCHEMBL3858.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00002101612 – 773Carnitine O-palmitoyltransferase 1, liver isoformAdd BLAST772

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanine1 Publication1
Modified residuei282Nitrated tyrosine1 Publication1
Modified residuei588Phosphothreonine1 Publication1
Modified residuei589Nitrated tyrosine1 Publication1
Modified residuei604Phosphothreonine1 Publication1
Modified residuei741Phosphoserine1 Publication1
Modified residuei747Phosphoserine1 Publication1

Keywords - PTMi

Acetylation, Nitration, Phosphoprotein

Proteomic databases

PaxDbiP32198.
PRIDEiP32198.

PTM databases

iPTMnetiP32198.
PhosphoSitePlusiP32198.

Expressioni

Tissue specificityi

Liver and kidney.

Gene expression databases

BgeeiENSRNOG00000014254.
GenevisibleiP32198. RN.

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 VDAC3.2 Publications

GO - Molecular functioni

  • identical protein binding Source: RGD

Protein-protein interaction databases

IntActiP32198. 1 interactor.
MINTiMINT-4590667.
STRINGi10116.ENSRNOP00000019652.

Chemistry databases

BindingDBiP32198.

Structurei

3D structure databases

ProteinModelPortaliP32198.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni555 – 567Coenzyme A bindingBy similarityAdd BLAST13

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.1 Publication

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3717. Eukaryota.
ENOG410XNZ9. LUCA.
GeneTreeiENSGT00760000119220.
HOGENOMiHOG000233542.
HOVERGENiHBG003458.
InParanoidiP32198.
KOiK08765.
OMAiHIVVFHK.
OrthoDBiEOG091G026C.
PhylomeDBiP32198.
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.

P32198-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAEAHQAVAF QFTVTPDGID LRLSHEALKQ ICLSGLHSWK KKFIRFKNGI
60 70 80 90 100
ITGVFPANPS SWLIVVVGVI SSMHAKVDPS LGMIAKISRT LDTTGRMSSQ
110 120 130 140 150
TKNIVSGVLF GTGLWVAVIM TMRYSLKVLL SYHGWMFAEH GKMSRSTKIW
160 170 180 190 200
MAMVKVLSGR KPMLYSFQTS LPRLPVPAVK DTVSRYLESV RPLMKEEDFQ
210 220 230 240 250
RMTALAQDFA VNLGPKLQWY LKLKSWWATN YVSDWWEEYI YLRGRGPLMV
260 270 280 290 300
NSNYYAMEML YITPTHIQAA RAGNTIHAIL LYRRTLDREE LKPIRLLGST
310 320 330 340 350
IPLCSAQWER LFNTSRIPGE ETDTIQHIKD SRHIVVYHRG RYFKVWLYHD
360 370 380 390 400
GRLLRPRELE QQMQQILDDP SEPQPGEAKL AALTAADRVP WAKCRQTYFA
410 420 430 440 450
RGKNKQSLDA VEKAAFFVTL DESEQGYREE DPEASIDSYA KSLLHGRCFD
460 470 480 490 500
RWFDKSITFV VFKNSKIGIN AEHSWADAPV VGHLWEYVMA TDVFQLGYSE
510 520 530 540 550
DGHCKGDTNP NIPKPTRLQW DIPGECQEVI DASLSSASLL ANDVDLHSFP
560 570 580 590 600
FDSFGKGLIK KCRTSPDAFI QLALQLAHYK DMGKFCLTYE ASMTRLFREG
610 620 630 640 650
RTETVRSCTM ESCNFVQAMM DPKSTAEQRL KLFKIACEKH QHLYRLAMTG
660 670 680 690 700
AGIDRHLFCL YVVSKYLAVD SPFLKEVLSE PWRLSTSQTP QQQVELFDFE
710 720 730 740 750
KNPDYVSCGG GFGPVADDGY GVSYIIVGEN FIHFHISSKF SSPETDSHRF
760 770
GKHLRQAMMD IITLFGLTIN SKK
Length:773
Mass (Da):88,125
Last modified:May 1, 2007 - v2
Checksum:i8C15594D45430CB8
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti266H → D AA sequence (PubMed:8348957).Curated1
Sequence conflicti374 – 375QP → NG AA sequence (PubMed:8348957).Curated2
Sequence conflicti480V → I in AAA40876 (PubMed:8449948).Curated1
Sequence conflicti531D → Y AA sequence (PubMed:8348957).Curated1
Sequence conflicti708C → R AA sequence (PubMed:8348957).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L07736 mRNA. Translation: AAA40876.1.
U88294 mRNA. Translation: AAB48046.1.
BC072522 mRNA. Translation: AAH72522.1.
PIRiA46627.
RefSeqiNP_113747.2. NM_031559.2.
XP_006230757.1. XM_006230695.2.
XP_017444326.1. XM_017588837.1.
UniGeneiRn.2856.

Genome annotation databases

EnsembliENSRNOT00000019652; ENSRNOP00000019652; ENSRNOG00000014254.
GeneIDi25757.
KEGGirno:25757.
UCSCiRGD:2396. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L07736 mRNA. Translation: AAA40876.1.
U88294 mRNA. Translation: AAB48046.1.
BC072522 mRNA. Translation: AAH72522.1.
PIRiA46627.
RefSeqiNP_113747.2. NM_031559.2.
XP_006230757.1. XM_006230695.2.
XP_017444326.1. XM_017588837.1.
UniGeneiRn.2856.

3D structure databases

ProteinModelPortaliP32198.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP32198. 1 interactor.
MINTiMINT-4590667.
STRINGi10116.ENSRNOP00000019652.

Chemistry databases

BindingDBiP32198.
ChEMBLiCHEMBL3858.
SwissLipidsiSLP:000000777.

PTM databases

iPTMnetiP32198.
PhosphoSitePlusiP32198.

Proteomic databases

PaxDbiP32198.
PRIDEiP32198.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000019652; ENSRNOP00000019652; ENSRNOG00000014254.
GeneIDi25757.
KEGGirno:25757.
UCSCiRGD:2396. rat.

Organism-specific databases

CTDi1374.
RGDi2396. Cpt1a.

Phylogenomic databases

eggNOGiKOG3717. Eukaryota.
ENOG410XNZ9. LUCA.
GeneTreeiENSGT00760000119220.
HOGENOMiHOG000233542.
HOVERGENiHBG003458.
InParanoidiP32198.
KOiK08765.
OMAiHIVVFHK.
OrthoDBiEOG091G026C.
PhylomeDBiP32198.
TreeFamiTF313836.

Enzyme and pathway databases

UniPathwayiUPA00659.
BioCyciMetaCyc:MONOMER-14439.
BRENDAi2.3.1.21. 5301.
ReactomeiR-RNO-200425. Import of palmitoyl-CoA into the mitochondrial matrix.
R-RNO-5362517. Signaling by Retinoic Acid.
SABIO-RKP32198.

Miscellaneous databases

PROiP32198.

Gene expression databases

BgeeiENSRNOG00000014254.
GenevisibleiP32198. RN.

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...

Entry informationi

Entry nameiCPT1A_RAT
AccessioniPrimary (citable) accession number: P32198
Secondary accession number(s): P97780, Q6IMZ4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: May 1, 2007
Last modified: November 30, 2016
This is version 140 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. 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.