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Q9JI60 (LRAT_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 89. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Lecithin retinol acyltransferase
EC=2.3.1.135
Alternative name(s):
Phosphatidylcholine--retinol O-acyltransferase
Phosphatidylcholine-retinol-O-acyltransferase
Gene names
Name:Lrat
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length231 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Catalytic activity

Phosphatidylcholine + retinol--[cellular-retinol-binding-protein] = 2-acylglycerophosphocholine + retinyl-ester--[cellular-retinol-binding-protein].

Enzyme regulation

Inhibited by all-trans-retinyl alpha-bromoacetate and N-boc-L-biocytinyl-11-aminoundecane chloro-methyl ketone (BACMK) By similarity.

Pathway

Cofactor metabolism; retinol metabolism.

Subcellular location

Endoplasmic reticulum membrane; Single-pass membrane protein. Rough endoplasmic reticulum By similarity. Endosome › multivesicular body By similarity. Cytoplasm › perinuclear 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. Ref.3

Tissue specificity

Hepatic stellate cells and endothelial cells (at protein level). Ref.4

Induction

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. Ref.1

Sequence similarities

Belongs to the H-rev107 family.

Ontologies

Keywords
   Biological processSensory transduction
Vision
   Cellular componentCytoplasm
Endoplasmic reticulum
Endosome
Membrane
   DomainTransmembrane
Transmembrane helix
   Molecular functionAcyltransferase
Transferase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_process1,2-diacyl-sn-glycero-3-phosphocholine metabolic process

Traceable author statement Ref.1. Source: MGI

embryo development

Inferred from genetic interaction PubMed 18093970. Source: MGI

response to stimulus

Inferred from electronic annotation. Source: UniProtKB-KW

retinoic acid metabolic process

Inferred from electronic annotation. Source: Compara

retinol metabolic process

Inferred from mutant phenotype PubMed 18093970. Source: MGI

visual perception

Inferred from electronic annotation. Source: UniProtKB-KW

vitamin A metabolic process

Inferred from direct assay Ref.1. Source: MGI

   Cellular_componentendoplasmic reticulum membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral to membrane

Inferred from electronic annotation. Source: UniProtKB-KW

multivesicular body

Inferred from electronic annotation. Source: UniProtKB-SubCell

perinuclear region of cytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

rough endoplasmic reticulum

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionO-acyltransferase activity

Inferred from direct assay Ref.1. Source: MGI

phosphatidylcholine-retinol O-acyltransferase activity

Inferred from electronic annotation. Source: EC

retinoic acid binding

Inferred from electronic annotation. Source: Compara

retinol binding

Inferred from electronic annotation. Source: Compara

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 231231Lecithin retinol acyltransferase
PRO_0000152479

Regions

Topological domain1 – 194194Cytoplasmic Ref.3
Transmembrane195 – 21521Helical; Potential
Topological domain216 – 23116Lumenal Ref.3

Sites

Active site1611Acyl-thioester intermediate Ref.5

Sequences

Sequence LengthMass (Da)Tools
Q9JI60 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: A1AE72330ED972BC

FASTA23125,820
        10         20         30         40         50         60 
MKNPMLEAAS LLLEKLLLIS NFKLFSVSVP GGGTGKNRPY EISSFVRGDV LEVSRTHFIH 

        70         80         90        100        110        120 
YGIYLGENRV AHLMPDILLA LTNDKERTQK VVSNKRLLLG VICKVASIRV DTVEDFAYGA 

       130        140        150        160        170        180 
DILVNHLDGT LKKKSLLNEE VARRAEQQLG LTPYSLLWNN CEHFVTYCRY GSRISPQAEK 

       190        200        210        220        230 
FYDTVKIIIR DQRSSLASAV LGLASIVYTG LASYMTLPAI CIPFCLWMMS G

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF255061 mRNA. Translation: AAF97787.1.
AK004953 mRNA. Translation: BAB23696.1.
IPIIPI00119943.
RefSeqNP_076113.1. NM_023624.4.
UniGeneMm.33921.

3D structure databases

ProteinModelPortalQ9JI60.
SMRQ9JI60. Positions 48-171.
ModBaseSearch...

PTM databases

PhosphoSiteQ9JI60.

Proteomic databases

PaxDbQ9JI60.
PRIDEQ9JI60.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000029632; ENSMUSP00000029632; ENSMUSG00000028003.
GeneID79235.
KEGGmmu:79235.

Organism-specific databases

CTD9227.
MGIMGI:1891259. Lrat.

Phylogenomic databases

eggNOGNOG40588.
GeneTreeENSGT00510000047351.
HOGENOMHOG000013187.
HOVERGENHBG047861.
InParanoidQ9JI60.
KOK00678.
OMAIPFCLWM.
OrthoDBEOG49S67G.

Enzyme and pathway databases

UniPathwayUPA00912.

Gene expression databases

ArrayExpressQ9JI60.
BgeeQ9JI60.
GenevestigatorQ9JI60.
GermOnlineENSMUSG00000028003. Mus musculus.

Family and domain databases

InterProIPR007053. LRAT-like_dom.
[Graphical view]
PfamPF04970. LRAT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio349895.
SOURCESearch...

Entry information

Entry nameLRAT_MOUSE
AccessionPrimary (citable) accession number: Q9JI60
Entry history
Integrated into UniProtKB/Swiss-Prot: April 26, 2004
Last sequence update: October 1, 2000
Last modified: May 1, 2013
This is version 89 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents