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Protein

Lecithin retinol acyltransferase

Gene

Lrat

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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 (By similarity). 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 similarity1 Publication

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 intermediateBy similarity1

GO - Molecular functioni

  • lecithin:11-cis retinol acyltransferase activity Source: UniProtKB-EC
  • O-acyltransferase activity Source: RGD
  • phosphatidylcholine-retinol O-acyltransferase activity Source: RGD
  • retinoic acid binding Source: RGD
  • retinol binding Source: RGD

GO - Biological processi

Keywordsi

Molecular functionAcyltransferase, Transferase
Biological processSensory transduction, Vision

Enzyme and pathway databases

BRENDAi2.3.1.135. 5301.
ReactomeiR-RNO-2453902. The canonical retinoid cycle in rods (twilight vision).
R-RNO-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
Gene namesi
Name:Lrat
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 2

Organism-specific databases

RGDi68362. 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 – 194CytoplasmicBy similarityAdd BLAST194
Transmembranei195 – 215HelicalSequence analysisAdd BLAST21
Topological domaini216 – 231LumenalBy similarityAdd BLAST16

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum, Endosome, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001524801 – 231Lecithin retinol acyltransferaseAdd BLAST231

Proteomic databases

PaxDbiQ9JI61.
PRIDEiQ9JI61.

Expressioni

Tissue specificityi

Hepatic stellate cells and endothelial cells (at protein level). Highly expressed in adrenal gland, small intestine, testis and eye. Lower levels of expression are observed in liver, heart, lung, skin, mammary tissue and skeletal muscle.2 Publications

Inductioni

LRAT activity is up-regulated by dietary vitamin A. Under conditions of vitamin A depletion, LRAT expression in the liver is induced by retinoic acid.2 Publications

Gene expression databases

BgeeiENSRNOG00000025608.
ExpressionAtlasiQ9JI61. baseline and differential.

Interactioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000035053.

Structurei

3D structure databases

SMRiQ9JI61.
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.
InParanoidiQ9JI61.
KOiK00678.
OMAiIPFCLWM.
OrthoDBiEOG091G0J9E.
PhylomeDBiQ9JI61.
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.

Q9JI61-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKNSMLEAAS LLLEKLLLIS NFKIFSVCAP GGGTGKKHPY EINSFLRGDV
60 70 80 90 100
LEVSRTHFTH YGIYLGDNRV AHLMPDILLA LTSDKERTQK VVSNKRLLPG
110 120 130 140 150
VICKVASIRV DTVEDFAYGA DILVNHLDET LKKKSLLNEE VARRAEQQLG
160 170 180 190 200
LTPYSLLWNN CEHFVTYCRY GSPISPQAEK FHETVKILIR DQRSCLASAV
210 220 230
LGLVSIIYTG LASYMTLPAV CIPFCLWMMS G
Length:231
Mass (Da):25,810
Last modified:October 1, 2000 - v1
Checksum:i61583C82D76A28A6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF255060 mRNA. Translation: AAF97786.1.
RefSeqiNP_071616.1. NM_022280.2.
UniGeneiRn.137431.

Genome annotation databases

EnsembliENSRNOT00000035411; ENSRNOP00000035053; ENSRNOG00000025608.
GeneIDi64047.
KEGGirno:64047.

Similar proteinsi

Entry informationi

Entry nameiLRAT_RAT
AccessioniPrimary (citable) accession number: Q9JI61
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 26, 2004
Last sequence update: October 1, 2000
Last modified: November 22, 2017
This is version 99 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

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families