LRAT_BOVIN
ID LRAT_BOVIN Reviewed; 230 AA.
AC Q9BGL2;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 25-MAY-2022, entry version 98.
DE RecName: Full=Lecithin retinol acyltransferase {ECO:0000305};
DE EC=2.3.1.135 {ECO:0000269|PubMed:2722792};
DE AltName: Full=Phosphatidylcholine--retinol O-acyltransferase;
GN Name=LRAT;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=11133845;
RA Ruiz A., Kuehn M.H., Andorf J.L., Stone E., Hageman G.S., Bok D.;
RT "Genomic organization and mutation analysis of the gene encoding lecithin
RT retinol acyltransferase in human retinal pigment epithelium.";
RL Invest. Ophthalmol. Vis. Sci. 42:31-37(2001).
RN [2]
RP PROTEIN SEQUENCE OF 1-24 AND 57-69, FUNCTION, ACTIVITY REGULATION, AND
RP CATALYTIC ACTIVITY.
RX PubMed=9920938; DOI=10.1074/jbc.274.6.3834;
RA Ruiz A., Winston A., Lim Y.-H., Gilbert B.A., Rando R.R., Bok D.;
RT "Molecular and biochemical characterization of lecithin retinol
RT acyltransferase.";
RL J. Biol. Chem. 274:3834-3841(1999).
RN [3]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=2722792; DOI=10.1016/s0021-9258(18)81839-7;
RA Saari J.C., Bredberg D.L.;
RT "Lecithin:retinol acyltransferase in retinal pigment epithelial
RT microsomes.";
RL J. Biol. Chem. 264:8636-8640(1989).
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:9920938, PubMed:2722792). Retinyl esters are storage
CC forms of vitamin A (Probable). LRAT plays a critical role in vision
CC (Probable). 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 (Probable). Required for the survival of cone
CC photoreceptors and correct rod photoreceptor cell morphology (By
CC similarity). {ECO:0000250|UniProtKB:Q9JI60, ECO:0000269|PubMed:2722792,
CC ECO:0000269|PubMed:9920938, ECO:0000305|PubMed:9920938}.
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:0000269|PubMed:2722792};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17470;
CC Evidence={ECO:0000305|PubMed:2722792};
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:9920938};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43905;
CC Evidence={ECO:0000305|PubMed:9920938};
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:0000269|PubMed:9920938}.
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:0000250}. Endosome, multivesicular body {ECO:0000250}. Cytoplasm,
CC perinuclear region {ECO:0000250}. 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 (By similarity). {ECO:0000250}.
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 (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the H-rev107 family. {ECO:0000305}.
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DR EMBL; AF275344; AAK08701.1; -; mRNA.
DR RefSeq; NP_803469.1; NM_177503.2.
DR AlphaFoldDB; Q9BGL2; -.
DR SMR; Q9BGL2; -.
DR STRING; 9913.ENSBTAP00000046443; -.
DR ChEMBL; CHEMBL4523439; -.
DR SwissLipids; SLP:000001895; -.
DR PaxDb; Q9BGL2; -.
DR GeneID; 281285; -.
DR KEGG; bta:281285; -.
DR CTD; 9227; -.
DR eggNOG; ENOG502QWSA; Eukaryota.
DR InParanoid; Q9BGL2; -.
DR OrthoDB; 1602481at2759; -.
DR BRENDA; 2.3.1.135; 908.
DR SABIO-RK; Q9BGL2; -.
DR UniPathway; UPA00912; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
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:0102279; F:lecithin:11-cis retinol acyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0047173; F:phosphatidylcholine-retinol O-acyltransferase activity; ISS:UniProtKB.
DR GO; GO:0050896; P:response to stimulus; IEA:UniProtKB-KW.
DR GO; GO:0042572; P:retinol metabolic process; ISS:UniProtKB.
DR GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
DR GO; GO:0006776; P:vitamin A metabolic process; ISS:UniProtKB.
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; Direct protein sequencing;
KW Endoplasmic reticulum; Endosome; Lipid metabolism; Membrane;
KW Reference proteome; Sensory transduction; Transferase; Transmembrane;
KW Transmembrane helix; Vision.
FT CHAIN 1..230
FT /note="Lecithin retinol acyltransferase"
FT /id="PRO_0000152477"
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..230
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 230 AA; 25701 MW; A5BE4A79690C993F CRC64;
MKNPMLEAVS LVLEKLLFIS YFKFFSSGAP GQDKAGNTLY EISSFLRGDV LEVPRTHLTH
YGIYLGDNRV AHMMPDILLA LTDDKGRTQK VVSNKRLILG VIGRVASIRV DTVEDFAYGA
EILVNHLDRS LKKKALLNEE VAQRAEKLLG ITPYSLLWNN CEHFVTYCRY GTPISPQADK
FCENVKIIIR DQRSVLASAV LGLASIFCLG LTSYTTLPAI FIPFLLWMAG
