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Protein

Lecithin retinol acyltransferase

Gene

Lrat

Organism
Mus musculus (Mouse)
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. 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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei161 – 1611Acyl-thioester intermediate1 Publication

GO - Molecular functioni

  1. O-acyltransferase activity Source: MGI
  2. phosphatidylcholine-retinol O-acyltransferase activity Source: UniProtKB-EC
  3. retinoic acid binding Source: Ensembl
  4. retinol binding Source: Ensembl

GO - Biological processi

  1. 1,2-diacyl-sn-glycero-3-phosphocholine metabolic process Source: MGI
  2. positive regulation of lipid transport Source: MGI
  3. response to stimulus Source: UniProtKB-KW
  4. retinoic acid metabolic process Source: Ensembl
  5. retinol metabolic process Source: MGI
  6. visual perception Source: UniProtKB-KW
  7. vitamin A metabolic process Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Sensory transduction, Vision

Enzyme and pathway databases

BRENDAi2.3.1.135. 3474.
ReactomeiREACT_280597. The canonical retinoid cycle in rods (twilight vision).
REACT_295031. 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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 3

Organism-specific databases

MGIiMGI:1891259. Lrat.

Subcellular locationi

Endoplasmic reticulum membrane 1 Publication; Single-pass membrane protein 1 Publication. Rough endoplasmic reticulum By similarity. Endosomemultivesicular body By similarity. Cytoplasmperinuclear region By similarity
Note: Present in the rough endoplasmic reticulum and multivesicular body in hepatic stellate cells. Present in the rough endoplasmic reticulum and perinuclear region in endothelial cells (By similarity).By similarity

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 194194Cytoplasmic1 PublicationAdd
BLAST
Transmembranei195 – 21521HelicalSequence AnalysisAdd
BLAST
Topological domaini216 – 23116Lumenal1 PublicationAdd
BLAST

GO - Cellular componenti

  1. endoplasmic reticulum membrane Source: UniProtKB-SubCell
  2. integral component of membrane Source: UniProtKB-KW
  3. multivesicular body Source: UniProtKB-SubCell
  4. perinuclear region of cytoplasm Source: UniProtKB-SubCell
  5. rough endoplasmic reticulum Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum, Endosome, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 231231Lecithin retinol acyltransferasePRO_0000152479Add
BLAST

Proteomic databases

PaxDbiQ9JI60.
PRIDEiQ9JI60.

PTM databases

PhosphoSiteiQ9JI60.

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

BgeeiQ9JI60.
ExpressionAtlasiQ9JI60. baseline and differential.
GenevestigatoriQ9JI60.

Structurei

Secondary structure

1
231
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi76 – 838Combined sources
Helixi88 – 903Combined sources
Beta strandi98 – 1069Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4Q95X-ray2.20A/B76-106[»]
SMRiQ9JI60. Positions 48-171.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the H-rev107 family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG40588.
GeneTreeiENSGT00510000047351.
HOGENOMiHOG000013187.
HOVERGENiHBG047861.
InParanoidiQ9JI60.
KOiK00678.
OMAiIPFCLWM.
OrthoDBiEOG7CZK6X.
PhylomeDBiQ9JI60.
TreeFamiTF330836.

Family and domain databases

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

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.

Cross-referencesi

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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4Q95X-ray2.20A/B76-106[»]
SMRiQ9JI60. Positions 48-171.
ModBaseiSearch...
MobiDBiSearch...

PTM databases

PhosphoSiteiQ9JI60.

Proteomic databases

PaxDbiQ9JI60.
PRIDEiQ9JI60.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi9227.
MGIiMGI:1891259. Lrat.

Phylogenomic databases

eggNOGiNOG40588.
GeneTreeiENSGT00510000047351.
HOGENOMiHOG000013187.
HOVERGENiHBG047861.
InParanoidiQ9JI60.
KOiK00678.
OMAiIPFCLWM.
OrthoDBiEOG7CZK6X.
PhylomeDBiQ9JI60.
TreeFamiTF330836.

Enzyme and pathway databases

UniPathwayiUPA00912.
BRENDAi2.3.1.135. 3474.
ReactomeiREACT_280597. The canonical retinoid cycle in rods (twilight vision).
REACT_295031. Retinoid metabolism and transport.

Miscellaneous databases

NextBioi349895.
PROiQ9JI60.
SOURCEiSearch...

Gene expression databases

BgeeiQ9JI60.
ExpressionAtlasiQ9JI60. baseline and differential.
GenevestigatoriQ9JI60.

Family and domain databases

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

Publicationsi

« Hide 'large scale' publications
  1. "Lecithin:retinol acyltransferase from mouse and rat liver. cDNA cloning and liver-specific regulation by dietary vitamin A and retinoic acid."
    Zolfaghari R., Ross A.C.
    J. Lipid Res. 41:2024-2034(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], INDUCTION BY RETINOIC ACID.
    Strain: BALB/c.
    Tissue: Liver.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Liver.
  3. "Topology and membrane association of lecithin: retinol acyltransferase."
    Moise A.R., Golczak M., Imanishi Y., Palczewski K.
    J. Biol. Chem. 282:2081-2090(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, TOPOLOGY.
  4. "Lecithin: retinol acyltransferase protein is distributed in both hepatic stellate cells and endothelial cells of normal rodent and human liver."
    Nagatsuma K., Hayashi Y., Hano H., Sagara H., Murakami K., Saito M., Masaki T., Lu T., Tanaka M., Enzan H., Aizawa Y., Tajiri H., Matsuura T.
    Liver Int. 29:47-54(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  5. "An acyl-covalent enzyme intermediate of lecithin:retinol acyltransferase."
    Golczak M., Palczewski K.
    J. Biol. Chem. 285:29217-29222(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACTIVE SITE, IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiLRAT_MOUSE
AccessioniPrimary (citable) accession number: Q9JI60
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 26, 2004
Last sequence update: October 1, 2000
Last modified: April 1, 2015
This is version 106 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.