Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q9JI60

- LRAT_MOUSE

UniProt

Q9JI60 - LRAT_MOUSE

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Lecithin retinol acyltransferase

Gene

Lrat

Organism
Mus musculus (Mouse)
Status
Reviewed - 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

ReactomeiREACT_188277. The canonical retinoid cycle in rods (twilight vision).
REACT_198569. 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: 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. integral component of membrane Source: UniProtKB-KW
  2. multivesicular body Source: Ensembl
  3. perinuclear region of cytoplasm Source: Ensembl
  4. rough endoplasmic reticulum Source: Ensembl
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

3D structure databases

ProteinModelPortaliQ9JI60.
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.
OMAiAIFIPFC.
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 .
CCDSi CCDS17430.1.
RefSeqi NP_076113.1. NM_023624.4.
UniGenei Mm.33921.

3D structure databases

ProteinModelPortali Q9JI60.
SMRi Q9JI60. Positions 48-171.
ModBasei Search...
MobiDBi Search...

PTM databases

PhosphoSitei Q9JI60.

Proteomic databases

PaxDbi Q9JI60.
PRIDEi Q9JI60.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000029632 ; ENSMUSP00000029632 ; ENSMUSG00000028003 .
GeneIDi 79235.
KEGGi mmu:79235.
UCSCi uc012cqv.1. mouse.

Organism-specific databases

CTDi 9227.
MGIi MGI:1891259. Lrat.

Phylogenomic databases

eggNOGi NOG40588.
GeneTreei ENSGT00510000047351.
HOGENOMi HOG000013187.
HOVERGENi HBG047861.
InParanoidi Q9JI60.
KOi K00678.
OMAi AIFIPFC.
OrthoDBi EOG7CZK6X.
PhylomeDBi Q9JI60.
TreeFami TF330836.

Enzyme and pathway databases

UniPathwayi UPA00912 .
Reactomei REACT_188277. The canonical retinoid cycle in rods (twilight vision).
REACT_198569. Retinoid metabolism and transport.

Miscellaneous databases

NextBioi 349895.
PROi Q9JI60.
SOURCEi Search...

Gene expression databases

Bgeei Q9JI60.
ExpressionAtlasi Q9JI60. baseline and differential.
Genevestigatori Q9JI60.

Family and domain databases

InterProi IPR007053. LRAT-like_dom.
[Graphical view ]
Pfami PF04970. LRAT. 1 hit.
[Graphical view ]
ProtoNeti Search...

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(2000) [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(2005) [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(2007) [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(2009) [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(2010) [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: October 29, 2014
This is version 102 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3