LRAT_RAT
ID LRAT_RAT Reviewed; 231 AA.
AC Q9JI61;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Lecithin retinol acyltransferase;
DE EC=2.3.1.135;
DE AltName: Full=Phosphatidylcholine--retinol O-acyltransferase;
GN Name=Lrat;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND INDUCTION BY RETINOIC
RP ACID AND VITAMIN A.
RC STRAIN=Lewis; TISSUE=Liver;
RX PubMed=11108736;
RA Zolfaghari R., Ross A.C.;
RT "Lecithin:retinol acyltransferase from mouse and rat liver. cDNA cloning
RT and liver-specific regulation by dietary vitamin A and retinoic acid.";
RL J. Lipid Res. 41:2024-2034(2000).
RN [2]
RP FUNCTION.
RX PubMed=3410848; DOI=10.1016/s0021-9258(18)37779-2;
RA MacDonald P.N., Ong D.E.;
RT "Evidence for a lecithin-retinol acyltransferase activity in the rat small
RT intestine.";
RL J. Biol. Chem. 263:12478-12482(1988).
RN [3]
RP INDUCTION BY VITAMIN A.
RX PubMed=1885578; DOI=10.1016/s0021-9258(18)55321-7;
RA Randolph R.K., Ross A.C.;
RT "Vitamin A status regulates hepatic lecithin:retinol acyltransferase
RT activity in rats.";
RL J. Biol. Chem. 266:16453-16457(1991).
RN [4]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=17158102; DOI=10.1074/jbc.m606369200;
RA Jin X.H., Okamoto Y., Morishita J., Tsuboi K., Tonai T., Ueda N.;
RT "Discovery and characterization of a Ca2+-independent
RT phosphatidylethanolamine N-acyltransferase generating the anandamide
RT precursor and its congeners.";
RL J. Biol. Chem. 282:3614-3623(2007).
RN [5]
RP SUBCELLULAR LOCATION, AND 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., Matsuura T.;
RT "Lecithin: retinol acyltransferase protein is distributed in both hepatic
RT stellate cells and endothelial cells of normal rodent and human liver.";
RL Liver Int. 29:47-54(2009).
CC -!- FUNCTION: Transfers the acyl group from the sn-1 position of
CC phosphatidylcholine to all-trans retinol, producing all-trans retinyl
CC esters (PubMed:3410848). Retinyl esters are storage forms of vitamin A
CC (By similarity). LRAT plays a critical role in vision (By similarity).
CC It provides the all-trans retinyl ester substrates for the
CC isomerohydrolase which processes the esters into 11-cis-retinol in the
CC retinal pigment epithelium; due to a membrane-associated alcohol
CC dehydrogenase, 11 cis-retinol is oxidized and converted into 11-cis-
CC retinaldehyde which is the chromophore for rhodopsin and the cone
CC photopigments (By similarity). Required for the survival of cone
CC photoreceptors and correct rod photoreceptor cell morphology (By
CC similarity). {ECO:0000250|UniProtKB:O95237,
CC ECO:0000250|UniProtKB:Q9JI60, ECO:0000269|PubMed:17158102,
CC ECO:0000269|PubMed:3410848}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + all-trans-retinol--
CC [retinol-binding protein] = a 2-acyl-sn-glycero-3-phosphocholine + an
CC all-trans-retinyl ester + apo--[retinol-binding protein];
CC Xref=Rhea:RHEA:17469, Rhea:RHEA-COMP:14426, Rhea:RHEA-COMP:14428,
CC ChEBI:CHEBI:17336, ChEBI:CHEBI:57643, ChEBI:CHEBI:57875,
CC ChEBI:CHEBI:63410, ChEBI:CHEBI:83228; EC=2.3.1.135;
CC Evidence={ECO:0000250|UniProtKB:Q9JI60};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17470;
CC Evidence={ECO:0000250|UniProtKB:Q9JI60};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-dihexadecanoyl-sn-glycero-3-phosphocholine + all-trans-
CC retinol = all-trans-retinyl hexadecanoate + hexadecanoyl-sn-glycero-
CC 3-phosphocholine; Xref=Rhea:RHEA:43904, ChEBI:CHEBI:17336,
CC ChEBI:CHEBI:17616, ChEBI:CHEBI:64563, ChEBI:CHEBI:72999;
CC Evidence={ECO:0000269|PubMed:17158102};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43905;
CC Evidence={ECO:0000305|PubMed:17158102};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-diheptanoyl-sn-glycero-3-phosphocholine + all-trans-
CC retinol--[retinol-binding protein] = 2-heptanoyl-sn-glycero-3-
CC phosphocholine + all-trans-retinyl heptanoate + apo--[retinol-binding
CC protein]; Xref=Rhea:RHEA:55320, Rhea:RHEA-COMP:14426, Rhea:RHEA-
CC COMP:14428, ChEBI:CHEBI:17336, ChEBI:CHEBI:83228, ChEBI:CHEBI:138195,
CC ChEBI:CHEBI:138266, ChEBI:CHEBI:138724;
CC Evidence={ECO:0000250|UniProtKB:Q9JI60};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55321;
CC Evidence={ECO:0000250|UniProtKB:Q9JI60};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-dioctanoyl-sn-glycero-3-phosphocholine + all-trans-
CC retinol--[retinol-binding protein] = 2-octanoyl-sn-glycero-3-
CC phosphocholine + all-trans-retinyl octanoate + apo--[retinol-binding
CC protein]; Xref=Rhea:RHEA:56240, Rhea:RHEA-COMP:14426, Rhea:RHEA-
CC COMP:14428, ChEBI:CHEBI:17336, ChEBI:CHEBI:78228, ChEBI:CHEBI:83228,
CC ChEBI:CHEBI:140082, ChEBI:CHEBI:140084;
CC Evidence={ECO:0000250|UniProtKB:Q9JI60};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56241;
CC Evidence={ECO:0000250|UniProtKB:Q9JI60};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-dihexadecanoyl-sn-glycero-3-phosphocholine + all-trans-
CC retinol--[retinol-binding protein] = 2-hexadecanoyl-sn-glycero-3-
CC phosphocholine + all-trans-retinyl hexadecanoate + apo--[retinol-
CC binding protein]; Xref=Rhea:RHEA:56244, Rhea:RHEA-COMP:14426,
CC Rhea:RHEA-COMP:14428, ChEBI:CHEBI:17336, ChEBI:CHEBI:17616,
CC ChEBI:CHEBI:72999, ChEBI:CHEBI:76078, ChEBI:CHEBI:83228;
CC Evidence={ECO:0000250|UniProtKB:Q9JI60};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56245;
CC Evidence={ECO:0000250|UniProtKB:Q9JI60};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-didodecanoyl-sn-glycero-3-phosphocholine + all-trans-
CC retinol--[retinol-binding protein] = 2-dodecanoyl-sn-glycero-3-
CC phosphocholine + all-trans-retinyl dodecanoate + apo--[retinol-
CC binding protein]; Xref=Rhea:RHEA:56248, Rhea:RHEA-COMP:14426,
CC Rhea:RHEA-COMP:14428, ChEBI:CHEBI:17336, ChEBI:CHEBI:65211,
CC ChEBI:CHEBI:83228, ChEBI:CHEBI:140088, ChEBI:CHEBI:140089;
CC Evidence={ECO:0000250|UniProtKB:Q9JI60};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56249;
CC Evidence={ECO:0000250|UniProtKB:Q9JI60};
CC -!- ACTIVITY REGULATION: Inhibited by all-trans-retinyl alpha-bromoacetate
CC and N-boc-L-biocytinyl-11-aminoundecane chloro-methyl ketone (BACMK).
CC {ECO:0000250}.
CC -!- PATHWAY: Cofactor metabolism; retinol metabolism.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Single-pass membrane protein {ECO:0000250}. Rough endoplasmic reticulum
CC {ECO:0000269|PubMed:18544127}. Endosome, multivesicular body
CC {ECO:0000269|PubMed:18544127}. Cytoplasm, perinuclear region
CC {ECO:0000269|PubMed:18544127}. Note=Present in the rough endoplasmic
CC reticulum and multivesicular body in hepatic stellate cells. Present in
CC the rough endoplasmic reticulum and perinuclear region in endothelial
CC cells.
CC -!- TISSUE SPECIFICITY: Hepatic stellate cells and endothelial cells (at
CC protein level). Highly expressed in adrenal gland, small intestine,
CC testis and eye. Lower levels of expression are observed in liver,
CC heart, lung, skin, mammary tissue and skeletal muscle.
CC {ECO:0000269|PubMed:11108736, ECO:0000269|PubMed:18544127}.
CC -!- INDUCTION: LRAT activity is up-regulated by dietary vitamin A. Under
CC conditions of vitamin A depletion, LRAT expression in the liver is
CC induced by retinoic acid. {ECO:0000269|PubMed:11108736,
CC ECO:0000269|PubMed:1885578}.
CC -!- SIMILARITY: Belongs to the H-rev107 family. {ECO:0000305}.
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DR EMBL; AF255060; AAF97786.1; -; mRNA.
DR RefSeq; NP_071616.1; NM_022280.2.
DR AlphaFoldDB; Q9JI61; -.
DR SMR; Q9JI61; -.
DR STRING; 10116.ENSRNOP00000035053; -.
DR ChEMBL; CHEMBL4523463; -.
DR SwissLipids; SLP:000001908; -.
DR PaxDb; Q9JI61; -.
DR Ensembl; ENSRNOT00000035411; ENSRNOP00000035053; ENSRNOG00000025608.
DR GeneID; 64047; -.
DR KEGG; rno:64047; -.
DR CTD; 9227; -.
DR RGD; 68362; Lrat.
DR eggNOG; ENOG502QWSA; Eukaryota.
DR GeneTree; ENSGT00510000047351; -.
DR HOGENOM; CLU_105262_0_0_1; -.
DR InParanoid; Q9JI61; -.
DR OMA; ADKFCEY; -.
DR OrthoDB; 1602481at2759; -.
DR PhylomeDB; Q9JI61; -.
DR TreeFam; TF330836; -.
DR BRENDA; 2.3.1.135; 5301.
DR Reactome; R-RNO-2453902; The canonical retinoid cycle in rods (twilight vision).
DR Reactome; R-RNO-975634; Retinoid metabolism and transport.
DR UniPathway; UPA00912; -.
DR PRO; PR:Q9JI61; -.
DR Proteomes; UP000002494; Chromosome 2.
DR Bgee; ENSRNOG00000025608; Expressed in liver and 15 other tissues.
DR ExpressionAtlas; Q9JI61; baseline and differential.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:RGD.
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:0043231; C:intracellular membrane-bounded organelle; IDA:RGD.
DR GO; GO:0005771; C:multivesicular body; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0005791; C:rough endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0102279; F:lecithin:11-cis retinol acyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0008374; F:O-acyltransferase activity; ISO:RGD.
DR GO; GO:0047173; F:phosphatidylcholine-retinol O-acyltransferase activity; IDA:RGD.
DR GO; GO:0001972; F:retinoic acid binding; IDA:RGD.
DR GO; GO:0019841; F:retinol binding; IDA:RGD.
DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; ISO:RGD.
DR GO; GO:0032370; P:positive regulation of lipid transport; ISO:RGD.
DR GO; GO:0009617; P:response to bacterium; ISO:RGD.
DR GO; GO:0032526; P:response to retinoic acid; IEP:RGD.
DR GO; GO:0033189; P:response to vitamin A; IEP:RGD.
DR GO; GO:0042572; P:retinol metabolic process; IDA:RGD.
DR GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
DR GO; GO:0006776; P:vitamin A metabolic process; IDA:RGD.
DR InterPro; IPR042288; LRAT.
DR InterPro; IPR007053; LRAT_dom.
DR PANTHER; PTHR46678; PTHR46678; 1.
DR Pfam; PF04970; LRAT; 1.
DR PROSITE; PS51934; LRAT; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Cytoplasm; Endoplasmic reticulum; Endosome;
KW Lipid metabolism; Membrane; Reference proteome; Sensory transduction;
KW Transferase; Transmembrane; Transmembrane helix; Vision.
FT CHAIN 1..231
FT /note="Lecithin retinol acyltransferase"
FT /id="PRO_0000152480"
FT TOPO_DOM 1..194
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 195..215
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 216..231
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT DOMAIN 50..177
FT /note="LRAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01283"
FT ACT_SITE 60
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01283"
FT ACT_SITE 72
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01283"
FT ACT_SITE 161
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01283"
SQ SEQUENCE 231 AA; 25810 MW; 61583C82D76A28A6 CRC64;
MKNSMLEAAS LLLEKLLLIS NFKIFSVCAP GGGTGKKHPY EINSFLRGDV LEVSRTHFTH
YGIYLGDNRV AHLMPDILLA LTSDKERTQK VVSNKRLLPG VICKVASIRV DTVEDFAYGA
DILVNHLDET LKKKSLLNEE VARRAEQQLG LTPYSLLWNN CEHFVTYCRY GSPISPQAEK
FHETVKILIR DQRSCLASAV LGLVSIIYTG LASYMTLPAV CIPFCLWMMS G
