ID   LRAT_MOUSE              Reviewed;         231 AA.
AC   Q9JI60;
DT   26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   14-OCT-2015, entry version 110.
DE   RecName: Full=Lecithin retinol acyltransferase;
DE            EC=2.3.1.135;
DE   AltName: Full=Phosphatidylcholine--retinol O-acyltransferase;
DE   AltName: Full=Phosphatidylcholine-retinol-O-acyltransferase;
GN   Name=Lrat;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION BY RETINOIC ACID.
RC   STRAIN=BALB/c; TISSUE=Liver;
RX   PubMed=11108736;
RA   Zolfaghari R., Ross A.C.;
RT   "Lecithin:retinol acyltransferase from mouse and rat liver. cDNA
RT   cloning and liver-specific regulation by dietary vitamin A and
RT   retinoic acid.";
RL   J. Lipid Res. 41:2024-2034(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Liver;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   SUBCELLULAR LOCATION, AND TOPOLOGY.
RX   PubMed=17114808; DOI=10.1074/jbc.M608315200;
RA   Moise A.R., Golczak M., Imanishi Y., Palczewski K.;
RT   "Topology and membrane association of lecithin: retinol
RT   acyltransferase.";
RL   J. Biol. Chem. 282:2081-2090(2007).
RN   [4]
RP   TISSUE SPECIFICITY.
RX   PubMed=18544127; DOI=10.1111/j.1478-3231.2008.01773.x;
RA   Nagatsuma K., Hayashi Y., Hano H., Sagara H., Murakami K., Saito M.,
RA   Masaki T., Lu T., Tanaka M., Enzan H., Aizawa Y., Tajiri H.,
RA   Matsuura T.;
RT   "Lecithin: retinol acyltransferase protein is distributed in both
RT   hepatic stellate cells and endothelial cells of normal rodent and
RT   human liver.";
RL   Liver Int. 29:47-54(2009).
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and
RT   expression.";
RL   Cell 143:1174-1189(2010).
RN   [6]
RP   ACTIVE SITE, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=20628054; DOI=10.1074/jbc.M110.152314;
RA   Golczak M., Palczewski K.;
RT   "An acyl-covalent enzyme intermediate of lecithin:retinol
RT   acyltransferase.";
RL   J. Biol. Chem. 285:29217-29222(2010).
CC   -!- FUNCTION: Transfers the acyl group from the sn-1 position of
CC       phosphatidylcholine to all-trans retinol, producing all-trans
CC       retinyl esters. Retinyl esters are storage forms of vitamin A.
CC       LRAT plays a critical role in vision. It provides the all-trans
CC       retinyl ester substrates for the isomerohydrolase which processes
CC       the esters into 11-cis-retinol in the retinal pigment epithelium;
CC       due to a membrane-associated alcohol dehydrogenase, 11 cis-retinol
CC       is oxidized and converted into 11-cis-retinaldehyde which is the
CC       chromophore for rhodopsin and the cone photopigments (By
CC       similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY: Phosphatidylcholine + retinol--[cellular-
CC       retinol-binding-protein] = 2-acylglycerophosphocholine + retinyl-
CC       ester--[cellular-retinol-binding-protein].
CC   -!- ENZYME REGULATION: Inhibited by all-trans-retinyl alpha-
CC       bromoacetate and N-boc-L-biocytinyl-11-aminoundecane chloro-methyl
CC       ketone (BACMK). {ECO:0000250}.
CC   -!- PATHWAY: Cofactor metabolism; retinol metabolism.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000269|PubMed:17114808}; Single-pass membrane protein
CC       {ECO:0000269|PubMed:17114808}. Rough endoplasmic reticulum
CC       {ECO:0000250}. Endosome, multivesicular body {ECO:0000250}.
CC       Cytoplasm, perinuclear region {ECO:0000250}. Note=Present in the
CC       rough endoplasmic reticulum and multivesicular body in hepatic
CC       stellate cells. Present in the rough endoplasmic reticulum and
CC       perinuclear region in endothelial cells (By similarity).
CC       {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Hepatic stellate cells and endothelial cells
CC       (at protein level). {ECO:0000269|PubMed:18544127}.
CC   -!- INDUCTION: LRAT activity is up-regulated by dietary vitamin A (By
CC       similarity). Under conditions of vitamin A depletion, LRAT
CC       expression in the liver is induced by retinoic acid. {ECO:0000250,
CC       ECO:0000269|PubMed:11108736}.
CC   -!- SIMILARITY: Belongs to the H-rev107 family. {ECO:0000305}.
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DR   EMBL; AF255061; AAF97787.1; -; mRNA.
DR   EMBL; AK004953; BAB23696.1; -; mRNA.
DR   CCDS; CCDS17430.1; -.
DR   RefSeq; NP_076113.1; NM_023624.4.
DR   UniGene; Mm.33921; -.
DR   PDB; 4Q95; X-ray; 2.20 A; A/B=76-106.
DR   PDBsum; 4Q95; -.
DR   ProteinModelPortal; Q9JI60; -.
DR   SMR; Q9JI60; 48-177.
DR   STRING; 10090.ENSMUSP00000029632; -.
DR   PhosphoSite; Q9JI60; -.
DR   MaxQB; Q9JI60; -.
DR   PaxDb; Q9JI60; -.
DR   PRIDE; Q9JI60; -.
DR   GeneID; 79235; -.
DR   KEGG; mmu:79235; -.
DR   UCSC; uc012cqv.1; mouse.
DR   CTD; 9227; -.
DR   MGI; MGI:1891259; Lrat.
DR   eggNOG; NOG40588; -.
DR   HOGENOM; HOG000013187; -.
DR   HOVERGEN; HBG047861; -.
DR   InParanoid; Q9JI60; -.
DR   KO; K00678; -.
DR   OMA; IPFCLWM; -.
DR   OrthoDB; EOG7CZK6X; -.
DR   PhylomeDB; Q9JI60; -.
DR   TreeFam; TF330836; -.
DR   BRENDA; 2.3.1.135; 3474.
DR   Reactome; R-MMU-2453902; The canonical retinoid cycle in rods (twilight vision).
DR   Reactome; R-MMU-975634; Retinoid metabolism and transport.
DR   UniPathway; UPA00912; -.
DR   NextBio; 349895; -.
DR   PRO; PR:Q9JI60; -.
DR   Proteomes; UP000000589; Unplaced.
DR   Bgee; Q9JI60; -.
DR   ExpressionAtlas; Q9JI60; baseline and differential.
DR   Genevisible; Q9JI60; MM.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005771; C:multivesicular body; IEA:UniProtKB-SubCell.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005791; C:rough endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR   GO; GO:0008374; F:O-acyltransferase activity; IDA:MGI.
DR   GO; GO:0047173; F:phosphatidylcholine-retinol O-acyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0001972; F:retinoic acid binding; IEA:Ensembl.
DR   GO; GO:0019841; F:retinol binding; IEA:Ensembl.
DR   GO; GO:0006653; P:1,2-diacyl-sn-glycero-3-phosphocholine metabolic process; TAS:MGI.
DR   GO; GO:0032370; P:positive regulation of lipid transport; IGI:MGI.
DR   GO; GO:0050896; P:response to stimulus; IEA:UniProtKB-KW.
DR   GO; GO:0042573; P:retinoic acid metabolic process; IEA:Ensembl.
DR   GO; GO:0042572; P:retinol metabolic process; IMP:MGI.
DR   GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
DR   GO; GO:0006776; P:vitamin A metabolic process; IDA:MGI.
DR   InterPro; IPR007053; LRAT-like_dom.
DR   Pfam; PF04970; LRAT; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acyltransferase; Complete proteome; Cytoplasm;
KW   Endoplasmic reticulum; Endosome; Membrane; Reference proteome;
KW   Sensory transduction; Transferase; Transmembrane; Transmembrane helix;
KW   Vision.
FT   CHAIN         1    231       Lecithin retinol acyltransferase.
FT                                /FTId=PRO_0000152479.
FT   TOPO_DOM      1    194       Cytoplasmic.
FT                                {ECO:0000269|PubMed:17114808}.
FT   TRANSMEM    195    215       Helical. {ECO:0000255}.
FT   TOPO_DOM    216    231       Lumenal. {ECO:0000269|PubMed:17114808}.
FT   ACT_SITE    161    161       Acyl-thioester intermediate.
FT                                {ECO:0000269|PubMed:20628054}.
FT   STRAND       76     83       {ECO:0000244|PDB:4Q95}.
FT   HELIX        88     90       {ECO:0000244|PDB:4Q95}.
FT   STRAND       98    106       {ECO:0000244|PDB:4Q95}.
SQ   SEQUENCE   231 AA;  25820 MW;  A1AE72330ED972BC CRC64;
     MKNPMLEAAS LLLEKLLLIS NFKLFSVSVP GGGTGKNRPY EISSFVRGDV LEVSRTHFIH
     YGIYLGENRV AHLMPDILLA LTNDKERTQK VVSNKRLLLG VICKVASIRV DTVEDFAYGA
     DILVNHLDGT LKKKSLLNEE VARRAEQQLG LTPYSLLWNN CEHFVTYCRY GSRISPQAEK
     FYDTVKIIIR DQRSSLASAV LGLASIVYTG LASYMTLPAI CIPFCLWMMS G
//