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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
  • phosphatidylcholine-retinol O-acyltransferase activity Source: RGD
  • retinoic acid binding Source: RGD
  • retinol binding Source: RGD

GO - Biological processi

  • positive regulation of lipid transport Source: Ensembl
  • response to stimulus Source: UniProtKB-KW
  • retinoic acid metabolic process Source: RGD
  • retinol metabolic process Source: RGD
  • visual perception Source: UniProtKB-KW
  • vitamin A metabolic process Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Sensory 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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 2

Organism-specific databases

RGDi68362. Lrat.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 194CytoplasmicBy similarityAdd BLAST194
Transmembranei195 – 215HelicalSequence analysisAdd BLAST21
Topological domaini216 – 231LumenalBy similarityAdd BLAST16

GO - Cellular componenti

  • endoplasmic reticulum membrane Source: UniProtKB-SubCell
  • integral component of membrane Source: UniProtKB-KW
  • intracellular membrane-bounded organelle Source: RGD
  • multivesicular body Source: UniProtKB
  • perinuclear region of cytoplasm Source: UniProtKB
  • rough endoplasmic reticulum Source: UniProtKB
Complete GO annotation...

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.

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

InterProiIPR007053. LRAT-like_dom.
[Graphical view]
PfamiPF04970. LRAT. 1 hit.
[Graphical view]

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.

Cross-referencesi

Sequence databases

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

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000035053.

Proteomic databases

PaxDbiQ9JI61.
PRIDEiQ9JI61.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi9227.
RGDi68362. Lrat.

Phylogenomic databases

eggNOGiENOG410IRMW. Eukaryota.
ENOG4111M0Q. LUCA.
GeneTreeiENSGT00510000047351.
HOGENOMiHOG000013187.
HOVERGENiHBG047861.
InParanoidiQ9JI61.
KOiK00678.
OMAiIPFCLWM.
OrthoDBiEOG091G0J9E.
PhylomeDBiQ9JI61.
TreeFamiTF330836.

Enzyme and pathway databases

UniPathwayiUPA00912.
BRENDAi2.3.1.135. 5301.
ReactomeiR-RNO-2453902. The canonical retinoid cycle in rods (twilight vision).
R-RNO-975634. Retinoid metabolism and transport.

Miscellaneous databases

PROiQ9JI61.

Gene expression databases

BgeeiENSRNOG00000025608.
ExpressionAtlasiQ9JI61. baseline and differential.

Family and domain databases

InterProiIPR007053. LRAT-like_dom.
[Graphical view]
PfamiPF04970. LRAT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiLRAT_RAT
AccessioniPrimary (citable) accession number: Q9JI61
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 26, 2004
Last sequence update: October 1, 2000
Last modified: September 7, 2016
This is version 94 of the entry and version 1 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. 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.