UniProtKB - Q9JI60 (LRAT_MOUSE)
Protein
Lecithin retinol acyltransferase
Gene
Lrat
Organism
Mus musculus (Mouse)
Status
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 (PubMed:28758396). LRAT plays a critical role in vision (By similarity). 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). Required for the survival of cone photoreceptors and correct rod photoreceptor cell morphology (PubMed:25416279).By similarity2 Publications
Catalytic activityi
- a 1,2-diacyl-sn-glycero-3-phosphocholine + all-trans-retinol--[retinol-binding protein] = a 2-acyl-sn-glycero-3-phosphocholine + an all-trans-retinyl ester + apo--[retinol-binding protein]1 PublicationEC:2.3.1.1351 PublicationThis reaction proceeds in the forward1 Publication direction.
- 1,2-diheptanoyl-sn-glycero-3-phosphocholine + all-trans-retinol--[retinol-binding protein] = 2-heptanoyl-sn-glycero-3-phosphocholine + all-trans-retinyl heptanoate + apo--[retinol-binding protein]2 PublicationsThis reaction proceeds in the forward2 Publications direction.
- 1,2-dioctanoyl-sn-glycero-3-phosphocholine + all-trans-retinol--[retinol-binding protein] = 2-octanoyl-sn-glycero-3-phosphocholine + all-trans-retinyl octanoate + apo--[retinol-binding protein]1 PublicationThis reaction proceeds in the forward1 Publication direction.
- 1,2-dihexadecanoyl-sn-glycero-3-phosphocholine + all-trans-retinol--[retinol-binding protein] = 2-hexadecanoyl-sn-glycero-3-phosphocholine + all-trans-retinyl hexadecanoate + apo--[retinol-binding protein]1 PublicationThis reaction proceeds in the forward1 Publication direction.
- 1,2-didodecanoyl-sn-glycero-3-phosphocholine + all-trans-retinol--[retinol-binding protein] = 2-dodecanoyl-sn-glycero-3-phosphocholine + all-trans-retinyl dodecanoate + apo--[retinol-binding protein]1 PublicationThis reaction proceeds in the forward1 Publication direction.
- 1,2-dihexadecanoyl-sn-glycero-3-phosphocholine + all-trans-retinol = all-trans-retinyl hexadecanoate + hexadecanoyl-sn-glycero-3-phosphocholineBy similarityThis reaction proceeds in the forwardBy similarity direction.
Activity regulationi
Inhibited by all-trans-retinyl alpha-bromoacetate and N-boc-L-biocytinyl-11-aminoundecane chloro-methyl ketone (BACMK).By similarity
Kineticsi
- KM=4.9 µM for all-trans-retinol--[retinol-binding protein]1 Publication
: retinol metabolism Pathwayi
This protein is involved in the pathway retinol metabolism, which is part of Cofactor metabolism.View all proteins of this organism that are known to be involved in the pathway retinol metabolism and in Cofactor metabolism.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Active sitei | 60 | PROSITE-ProRule annotation | 1 | |
Active sitei | 72 | PROSITE-ProRule annotation | 1 | |
Active sitei | 161 | Acyl-thioester intermediatePROSITE-ProRule annotation1 Publication | 1 |
GO - Molecular functioni
- lecithin:11-cis retinol acyltransferase activity Source: UniProtKB-EC
- O-acyltransferase activity Source: MGI
- phosphatidylcholine-retinol O-acyltransferase activity Source: UniProtKB
- retinoic acid binding Source: MGI
- retinol binding Source: MGI
GO - Biological processi
- 1,2-diacyl-sn-glycero-3-phosphocholine metabolic process Source: MGI
- cellular response to leukemia inhibitory factor Source: MGI
- positive regulation of lipid transport Source: MGI
- response to bacterium Source: MGI
- response to retinoic acid Source: Ensembl
- response to vitamin A Source: Ensembl
- retinol metabolic process Source: UniProtKB
- visual perception Source: UniProtKB-KW
- vitamin A metabolic process Source: MGI
Keywordsi
Molecular function | Acyltransferase, Transferase |
Biological process | Sensory transduction, Vision |
Enzyme and pathway databases
BRENDAi | 2.3.1.135, 3474 |
Reactomei | R-MMU-2453902, The canonical retinoid cycle in rods (twilight vision) R-MMU-975634, Retinoid metabolism and transport |
UniPathwayi | UPA00912 |
Chemistry databases
SwissLipidsi | SLP:000001899 |
Names & Taxonomyi
Protein namesi | Recommended name: Lecithin retinol acyltransferase (EC:2.3.1.1351 Publication)Alternative name(s): Phosphatidylcholine--retinol O-acyltransferase Phosphatidylcholine-retinol-O-acyltransferase |
Gene namesi | Name:Lrat |
Organismi | Mus musculus (Mouse) |
Taxonomic identifieri | 10090 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus |
Proteomesi |
|
Organism-specific databases
MGIi | MGI:1891259, Lrat |
Subcellular locationi
Endosome
- multivesicular body By similarity
Endoplasmic reticulum
- Endoplasmic reticulum membrane 2 Publications; Single-pass membrane protein 1 Publication
- Rough endoplasmic reticulum By similarity
Other locations
- 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).By similarity
Endoplasmic reticulum
- endoplasmic reticulum Source: UniProtKB
- endoplasmic reticulum membrane Source: UniProtKB-SubCell
- rough endoplasmic reticulum Source: MGI
Endosome
- multivesicular body Source: MGI
Other locations
- integral component of membrane Source: UniProtKB-KW
- intracellular membrane-bounded organelle Source: MGI
- perinuclear region of cytoplasm Source: MGI
Topology
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Topological domaini | 1 – 194 | Cytoplasmic1 PublicationAdd BLAST | 194 | |
Transmembranei | 195 – 215 | HelicalSequence analysisAdd BLAST | 21 | |
Topological domaini | 216 – 231 | Lumenal1 PublicationAdd BLAST | 16 |
Keywords - Cellular componenti
Cytoplasm, Endoplasmic reticulum, Endosome, MembranePathology & Biotechi
Disruption phenotypei
Knockout mice are viable (PubMed:25416279). Knockout mice at one month of age show loss of nearly all cone photoreceptors in the central and ventral retina (PubMed:25416279). Surviving cone cells show severe degeneration, the dorsal retinal also exhibits a significant reduction in cone photoreceptors (PubMed:25416279). At one month of age rod photoreceptors show shorter outer segments (PubMed:25416279). Nearly all cone photoreceptors are lost by six months of age (PubMed:25416279). Remaining cone cells show disrupted structures with the majority showing abnormal cell bodies or lack of an outer segment (PubMed:25416279).1 Publication
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 14 | E → L: Increases degradation via the proteasomal pathway. No effect on endoplasmic reticulum location. Impairs vitamin A uptake. No effect on retinol acyltransferase activity. 1 Publication | 1 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000152479 | 1 – 231 | Lecithin retinol acyltransferaseAdd BLAST | 231 |
Proteomic databases
MaxQBi | Q9JI60 |
PaxDbi | Q9JI60 |
PRIDEi | Q9JI60 |
PTM databases
iPTMneti | Q9JI60 |
PhosphoSitePlusi | Q9JI60 |
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
Bgeei | ENSMUSG00000028003, Expressed in pigmented layer of retina and 95 other tissues |
Genevisiblei | Q9JI60, MM |
Interactioni
Protein-protein interaction databases
STRINGi | 10090.ENSMUSP00000029632 |
Miscellaneous databases
RNActi | Q9JI60, protein |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | Q9JI60 |
ModBasei | Search... |
PDBe-KBi | Search... |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 50 – 177 | LRATPROSITE-ProRule annotationAdd BLAST | 128 |
Sequence similaritiesi
Belongs to the H-rev107 family.Curated
Keywords - Domaini
Transmembrane, Transmembrane helixPhylogenomic databases
eggNOGi | ENOG502QWSA, Eukaryota |
GeneTreei | ENSGT00510000047351 |
HOGENOMi | CLU_105262_0_0_1 |
InParanoidi | Q9JI60 |
OMAi | FCLWMAG |
OrthoDBi | 1602481at2759 |
PhylomeDBi | Q9JI60 |
TreeFami | TF330836 |
Family and domain databases
InterProi | View protein in InterPro IPR042288, LRAT IPR007053, LRAT_dom |
PANTHERi | PTHR46678, PTHR46678, 1 hit |
Pfami | View protein in Pfam PF04970, LRAT, 1 hit |
PROSITEi | View protein in PROSITE PS51934, LRAT, 1 hit |
i Sequence
Sequence statusi: Complete.
Q9JI60-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MKNPMLEAAS LLLEKLLLIS NFKLFSVSVP GGGTGKNRPY EISSFVRGDV
60 70 80 90 100
LEVSRTHFIH YGIYLGENRV AHLMPDILLA LTNDKERTQK VVSNKRLLLG
110 120 130 140 150
VICKVASIRV DTVEDFAYGA DILVNHLDGT LKKKSLLNEE VARRAEQQLG
160 170 180 190 200
LTPYSLLWNN CEHFVTYCRY GSRISPQAEK FYDTVKIIIR DQRSSLASAV
210 220 230
LGLASIVYTG LASYMTLPAI CIPFCLWMMS G
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AF255061 mRNA Translation: AAF97787.1 AK004953 mRNA Translation: BAB23696.1 |
CCDSi | CCDS17430.1 |
RefSeqi | NP_076113.1, NM_023624.4 |
Genome annotation databases
Ensembli | ENSMUST00000029632; ENSMUSP00000029632; ENSMUSG00000028003 |
GeneIDi | 79235 |
KEGGi | mmu:79235 |
UCSCi | uc012cqv.1, mouse |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AF255061 mRNA Translation: AAF97787.1 AK004953 mRNA Translation: BAB23696.1 |
CCDSi | CCDS17430.1 |
RefSeqi | NP_076113.1, NM_023624.4 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
4Q95 | X-ray | 2.20 | A/B | 76-106 | [»] | |
SMRi | Q9JI60 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
STRINGi | 10090.ENSMUSP00000029632 |
Chemistry databases
SwissLipidsi | SLP:000001899 |
PTM databases
iPTMneti | Q9JI60 |
PhosphoSitePlusi | Q9JI60 |
Proteomic databases
MaxQBi | Q9JI60 |
PaxDbi | Q9JI60 |
PRIDEi | Q9JI60 |
Protocols and materials databases
Antibodypediai | 2389, 263 antibodies |
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 | ENOG502QWSA, Eukaryota |
GeneTreei | ENSGT00510000047351 |
HOGENOMi | CLU_105262_0_0_1 |
InParanoidi | Q9JI60 |
OMAi | FCLWMAG |
OrthoDBi | 1602481at2759 |
PhylomeDBi | Q9JI60 |
TreeFami | TF330836 |
Enzyme and pathway databases
UniPathwayi | UPA00912 |
BRENDAi | 2.3.1.135, 3474 |
Reactomei | R-MMU-2453902, The canonical retinoid cycle in rods (twilight vision) R-MMU-975634, Retinoid metabolism and transport |
Miscellaneous databases
BioGRID-ORCSi | 79235, 0 hits in 17 CRISPR screens |
PROi | PR:Q9JI60 |
RNActi | Q9JI60, protein |
SOURCEi | Search... |
Gene expression databases
Bgeei | ENSMUSG00000028003, Expressed in pigmented layer of retina and 95 other tissues |
Genevisiblei | Q9JI60, MM |
Family and domain databases
InterProi | View protein in InterPro IPR042288, LRAT IPR007053, LRAT_dom |
PANTHERi | PTHR46678, PTHR46678, 1 hit |
Pfami | View protein in Pfam PF04970, LRAT, 1 hit |
PROSITEi | View protein in PROSITE PS51934, LRAT, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | LRAT_MOUSE | |
Accessioni | Q9JI60Primary (citable) accession number: Q9JI60 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | April 26, 2004 |
Last sequence update: | October 1, 2000 | |
Last modified: | December 2, 2020 | |
This is version 144 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Reference proteomeDocuments
- MGD cross-references
Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot - PATHWAY comments
Index of metabolic and biosynthesis pathways - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families