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Protein

Lecithin retinol acyltransferase

Gene

LRAT

Organism
Homo sapiens (Human)
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.1 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).1 Publication

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

GO - Biological processi

Keywordsi

Molecular functionAcyltransferase, Transferase
Biological processSensory transduction, Vision

Enzyme and pathway databases

BioCyciMetaCyc:HS04474-MONOMER
BRENDAi2.3.1.135 2681
ReactomeiR-HSA-2453864 Retinoid cycle disease events
R-HSA-2453902 The canonical retinoid cycle in rods (twilight vision)
R-HSA-975634 Retinoid metabolism and transport
UniPathwayiUPA00912

Chemistry databases

SwissLipidsiSLP:000000686

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
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 4

Organism-specific databases

EuPathDBiHostDB:ENSG00000121207.11
HGNCiHGNC:6685 LRAT
MIMi604863 gene
neXtProtiNX_O95237

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 – 230LumenalBy similarityAdd BLAST15

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum, Endosome, Membrane

Pathology & Biotechi

Involvement in diseasei

Leber congenital amaurosis 14 (LCA14)3 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA severe dystrophy of the retina, typically becoming evident in the first years of life. Visual function is usually poor and often accompanied by nystagmus, sluggish or near-absent pupillary responses, photophobia, high hyperopia and keratoconus.
See also OMIM:613341
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_018386175S → R in LCA14; loss of function. 1 PublicationCorresponds to variant dbSNP:rs104893848EnsemblClinVar.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi161C → A or S: Loss of activity. 1 Publication1
Mutagenesisi168C → A: Loss of activity. 1 Publication1
Mutagenesisi168C → S: Does not affect activity. 1 Publication1
Mutagenesisi182C → A: Does not affect activity. 1 Publication1
Mutagenesisi208C → A: Does not affect activity. 1 Publication1

Keywords - Diseasei

Disease mutation, Leber congenital amaurosis

Organism-specific databases

DisGeNETi9227
GeneReviewsiLRAT
MalaCardsiLRAT
MIMi613341 phenotype
OpenTargetsiENSG00000121207
Orphaneti65 Leber congenital amaurosis
791 Retinitis pigmentosa
364055 Severe early-childhood-onset retinal dystrophy
PharmGKBiPA30443

Chemistry databases

ChEMBLiCHEMBL2202
DrugBankiDB00162 Vitamin A

Polymorphism and mutation databases

BioMutaiLRAT

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001524781 – 230Lecithin retinol acyltransferaseAdd BLAST230

Proteomic databases

EPDiO95237
MaxQBiO95237
PaxDbiO95237
PeptideAtlasiO95237
PRIDEiO95237
ProteomicsDBi50736

PTM databases

iPTMnetiO95237
PhosphoSitePlusiO95237

Expressioni

Tissue specificityi

Hepatic stellate cells and endothelial cells (at protein level). Found at high levels in testis and liver, followed by retinal pigment epithelium, small intestine, prostate, pancreas and colon. Low expression observed in brain. In fetal tissues, expressed in retinal pigment epithelium and liver, and barely in the brain.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 (By similarity).By similarity

Gene expression databases

BgeeiENSG00000121207
CleanExiHS_LRAT
ExpressionAtlasiO95237 baseline and differential
GenevisibleiO95237 HS

Organism-specific databases

HPAiHPA070726

Interactioni

Protein-protein interaction databases

BioGridi114658, 2 interactors
STRINGi9606.ENSP00000337224

Chemistry databases

BindingDBiO95237

Structurei

3D structure databases

ProteinModelPortaliO95237
SMRiO95237
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
InParanoidiO95237
KOiK00678
OMAiIPFCLWM
OrthoDBiEOG091G0J9E
PhylomeDBiO95237
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.

O95237-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKNPMLEVVS LLLEKLLLIS NFTLFSSGAA GEDKGRNSFY ETSSFHRGDV
60 70 80 90 100
LEVPRTHLTH YGIYLGDNRV AHMMPDILLA LTDDMGRTQK VVSNKRLILG
110 120 130 140 150
VIVKVASIRV DTVEDFAYGA NILVNHLDES LQKKALLNEE VARRAEKLLG
160 170 180 190 200
FTPYSLLWNN CEHFVTYCRY GTPISPQSDK FCETVKIIIR DQRSVLASAV
210 220 230
LGLASIVCTG LVSYTTLPAI FIPFFLWMAG
Length:230
Mass (Da):25,703
Last modified:April 26, 2004 - v2
Checksum:iDCB7F5A1C3FF7689
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti32E → K in AAD13529 (PubMed:9920938).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_063559173P → L1 Publication1
Natural variantiVAR_018386175S → R in LCA14; loss of function. 1 PublicationCorresponds to variant dbSNP:rs104893848EnsemblClinVar.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF071510 mRNA Translation: AAD13529.1
AY546085 mRNA Translation: AAS49412.1
AY546086 mRNA Translation: AAS49413.1
AK292598 mRNA Translation: BAF85287.1
CH471056 Genomic DNA Translation: EAX04904.1
BC031053 mRNA Translation: AAH31053.1
CCDSiCCDS3789.1
RefSeqiNP_001288574.1, NM_001301645.1
NP_004735.2, NM_004744.4
UniGeneiHs.658427
Hs.736130

Genome annotation databases

EnsembliENST00000336356; ENSP00000337224; ENSG00000121207
ENST00000507827; ENSP00000426761; ENSG00000121207
GeneIDi9227
KEGGihsa:9227
UCSCiuc003ion.2 human

Keywords - Coding sequence diversityi

Polymorphism

Similar proteinsi

Entry informationi

Entry nameiLRAT_HUMAN
AccessioniPrimary (citable) accession number: O95237
Secondary accession number(s): A8K983, Q8N716
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 26, 2004
Last sequence update: April 26, 2004
Last modified: June 20, 2018
This is version 142 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 4
    Human chromosome 4: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. SIMILARITY comments
    Index of protein domains and families

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