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Q9JI60

- LRAT_MOUSE

UniProt

Q9JI60 - LRAT_MOUSE

Protein

Lecithin retinol acyltransferase

Gene

Lrat

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 101 (01 Oct 2014)
      Sequence version 1 (01 Oct 2000)
      Previous versions | rss
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    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. response to stimulus Source: UniProtKB-KW
    3. retinoic acid metabolic process Source: Ensembl
    4. retinol metabolic process Source: MGI
    5. visual perception Source: UniProtKB-KW
    6. vitamin A metabolic process Source: MGI

    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

    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

    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

    ArrayExpressiQ9JI60.
    BgeeiQ9JI60.
    GenevestigatoriQ9JI60.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9JI60.
    SMRiQ9JI60. Positions 48-171.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

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

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei195 – 21521HelicalSequence AnalysisAdd
    BLAST

    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

    MKNPMLEAAS LLLEKLLLIS NFKLFSVSVP GGGTGKNRPY EISSFVRGDV    50
    LEVSRTHFIH YGIYLGENRV AHLMPDILLA LTNDKERTQK VVSNKRLLLG 100
    VICKVASIRV DTVEDFAYGA DILVNHLDGT LKKKSLLNEE VARRAEQQLG 150
    LTPYSLLWNN CEHFVTYCRY GSRISPQAEK FYDTVKIIIR DQRSSLASAV 200
    LGLASIVYTG LASYMTLPAI CIPFCLWMMS G 231
    Length:231
    Mass (Da):25,820
    Last modified:October 1, 2000 - v1
    Checksum:iA1AE72330ED972BC
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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

    ArrayExpressi Q9JI60.
    Bgeei Q9JI60.
    Genevestigatori Q9JI60.

    Family and domain databases

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

    Publicationsi

    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 1, 2014
    This is version 101 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