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Protein

Lecithin retinol acyltransferase

Gene

Lrat

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

Functioni

Transfers the acyl group from the sn-1 position of phosphatidylcholine to all-trans retinol, producing all-trans retinyl esters. Retinyl esters are storage forms of vitamin A. LRAT plays a critical role in vision. It provides the all-trans retinyl ester substrates for the isomerohydrolase which processes the esters into 11-cis-retinol in the retinal pigment epithelium; due to a membrane-associated alcohol dehydrogenase, 11 cis-retinol is oxidized and converted into 11-cis-retinaldehyde which is the chromophore for rhodopsin and the cone photopigments (By similarity).By similarity

Catalytic activityi

Phosphatidylcholine + retinol--[cellular-retinol-binding-protein] = 2-acylglycerophosphocholine + retinyl-ester--[cellular-retinol-binding-protein].

Enzyme regulationi

Inhibited by all-trans-retinyl alpha-bromoacetate and N-boc-L-biocytinyl-11-aminoundecane chloro-methyl ketone (BACMK).By similarity

Pathwayi: retinol metabolism

This protein is involved in the pathway retinol metabolism, which is part of Cofactor metabolism.
View all proteins of this organism that are known to be involved in the pathway retinol metabolism and in Cofactor metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei161Acyl-thioester intermediate1 Publication1

GO - Molecular functioni

GO - Biological processi

  • 1,2-diacyl-sn-glycero-3-phosphocholine metabolic process Source: MGI
  • cellular response to leukemia inhibitory factor Source: MGI
  • positive regulation of lipid transport Source: MGI
  • retinoic acid metabolic process Source: Ensembl
  • retinol metabolic process Source: MGI
  • visual perception Source: UniProtKB-KW
  • vitamin A metabolic process Source: MGI

Keywordsi

Molecular functionAcyltransferase, Transferase
Biological processSensory transduction, Vision

Enzyme and pathway databases

BRENDAi2.3.1.135 3474
ReactomeiR-MMU-2453902 The canonical retinoid cycle in rods (twilight vision)
R-MMU-975634 Retinoid metabolism and transport
UniPathwayiUPA00912

Names & Taxonomyi

Protein namesi
Recommended name:
Lecithin retinol acyltransferase (EC:2.3.1.135)
Alternative name(s):
Phosphatidylcholine--retinol O-acyltransferase
Phosphatidylcholine-retinol-O-acyltransferase
Gene namesi
Name:Lrat
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 3

Organism-specific databases

MGIiMGI:1891259 Lrat

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 194Cytoplasmic1 PublicationAdd BLAST194
Transmembranei195 – 215HelicalSequence analysisAdd BLAST21
Topological domaini216 – 231Lumenal1 PublicationAdd BLAST16

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum, Endosome, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001524791 – 231Lecithin retinol acyltransferaseAdd BLAST231

Proteomic databases

MaxQBiQ9JI60
PaxDbiQ9JI60
PRIDEiQ9JI60

PTM databases

iPTMnetiQ9JI60
PhosphoSitePlusiQ9JI60

Expressioni

Tissue specificityi

Hepatic stellate cells and endothelial cells (at protein level).1 Publication

Inductioni

LRAT activity is up-regulated by dietary vitamin A (By similarity). Under conditions of vitamin A depletion, LRAT expression in the liver is induced by retinoic acid.By similarity1 Publication

Gene expression databases

BgeeiENSMUSG00000028003
ExpressionAtlasiQ9JI60 baseline and differential
GenevisibleiQ9JI60 MM

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000029632

Structurei

Secondary structure

1231
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi76 – 83Combined sources8
Helixi88 – 90Combined sources3
Beta strandi98 – 106Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4Q95X-ray2.20A/B76-106[»]
ProteinModelPortaliQ9JI60
SMRiQ9JI60
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the H-rev107 family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410IRMW Eukaryota
ENOG4111M0Q LUCA
GeneTreeiENSGT00510000047351
HOGENOMiHOG000013187
HOVERGENiHBG047861
InParanoidiQ9JI60
KOiK00678
OMAiIPFCLWM
OrthoDBiEOG091G0J9E
PhylomeDBiQ9JI60
TreeFamiTF330836

Family and domain databases

InterProiView protein in InterPro
IPR007053 LRAT-like_dom
PfamiView protein in Pfam
PF04970 LRAT, 1 hit

Sequencei

Sequence statusi: Complete.

Q9JI60-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKNPMLEAAS LLLEKLLLIS NFKLFSVSVP GGGTGKNRPY EISSFVRGDV
60 70 80 90 100
LEVSRTHFIH YGIYLGENRV AHLMPDILLA LTNDKERTQK VVSNKRLLLG
110 120 130 140 150
VICKVASIRV DTVEDFAYGA DILVNHLDGT LKKKSLLNEE VARRAEQQLG
160 170 180 190 200
LTPYSLLWNN CEHFVTYCRY GSRISPQAEK FYDTVKIIIR DQRSSLASAV
210 220 230
LGLASIVYTG LASYMTLPAI CIPFCLWMMS G
Length:231
Mass (Da):25,820
Last modified:October 1, 2000 - v1
Checksum:iA1AE72330ED972BC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF255061 mRNA Translation: AAF97787.1
AK004953 mRNA Translation: BAB23696.1
CCDSiCCDS17430.1
RefSeqiNP_076113.1, NM_023624.4
UniGeneiMm.33921

Genome annotation databases

EnsembliENSMUST00000029632; ENSMUSP00000029632; ENSMUSG00000028003
GeneIDi79235
KEGGimmu:79235
UCSCiuc012cqv.1 mouse

Similar proteinsi

Entry informationi

Entry nameiLRAT_MOUSE
AccessioniPrimary (citable) accession number: Q9JI60
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 26, 2004
Last sequence update: October 1, 2000
Last modified: December 20, 2017
This is version 123 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome