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O95237

- LRAT_HUMAN

UniProt

O95237 - LRAT_HUMAN

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Protein

Lecithin retinol acyltransferase

Gene
LRAT
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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.1 Publication

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).1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei161 – 1611Acyl-thioester intermediate By similarity

GO - Molecular functioni

  1. phosphatidylcholine-retinol O-acyltransferase activity Source: UniProtKB-EC
  2. retinoic acid binding Source: Ensembl
  3. retinol binding Source: Ensembl
  4. transferase activity, transferring acyl groups Source: ProtInc

GO - Biological processi

  1. embryo development Source: Ensembl
  2. phototransduction, visible light Source: Reactome
  3. retinoic acid metabolic process Source: Ensembl
  4. retinoid metabolic process Source: Reactome
  5. retinol metabolic process Source: UniProtKB-UniPathway
  6. visual perception Source: UniProtKB-KW
  7. vitamin A metabolic process Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Sensory transduction, Vision

Enzyme and pathway databases

BioCyciMetaCyc:HS04474-MONOMER.
BRENDAi2.3.1.135. 2681.
ReactomeiREACT_160156. The canonical retinoid cycle in rods (twilight vision).
REACT_24968. 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
Gene namesi
Name:LRAT
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 4

Organism-specific databases

HGNCiHGNC:6685. LRAT.

Subcellular locationi

Endoplasmic reticulum membrane; Single-pass membrane protein By similarity. 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.

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 194194Cytoplasmic By similarityAdd
BLAST
Transmembranei195 – 21521Helical; Reviewed predictionAdd
BLAST
Topological domaini216 – 23015Lumenal By similarityAdd
BLAST

GO - Cellular componenti

  1. endoplasmic reticulum membrane Source: Reactome
  2. integral component of membrane Source: UniProtKB-KW
  3. multivesicular body Source: UniProtKB
  4. perinuclear region of cytoplasm Source: UniProtKB
  5. rough endoplasmic reticulum Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum, Endosome, Membrane

Pathology & Biotechi

Involvement in diseasei

Leber congenital amaurosis 14 (LCA14) [MIM:613341]: A severe dystrophy of the retina, typically becoming evident in the first years of life. Visual function is usually poor and often accompanied by nystagmus, sluggish or near-absent pupillary responses, photophobia, high hyperopia and keratoconus.
Note: The disease is caused by mutations affecting the gene represented in this entry.3 Publications
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti175 – 1751S → R in LCA14; loss of function. 1 Publication
VAR_018386

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi161 – 1611C → A or S: Loss of activity. 1 Publication
Mutagenesisi168 – 1681C → A: Loss of activity. 1 Publication
Mutagenesisi168 – 1681C → S: Does not affect activity. 1 Publication
Mutagenesisi182 – 1821C → A: Does not affect activity. 1 Publication
Mutagenesisi208 – 2081C → A: Does not affect activity. 1 Publication

Keywords - Diseasei

Disease mutation, Leber congenital amaurosis

Organism-specific databases

MIMi613341. phenotype.
Orphaneti65. Leber congenital amaurosis.
791. Retinitis pigmentosa.
364055. Severe early-childhood-onset retinal dystrophy.
PharmGKBiPA30443.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 230230Lecithin retinol acyltransferasePRO_0000152478Add
BLAST

Proteomic databases

MaxQBiO95237.
PaxDbiO95237.
PRIDEiO95237.

PTM databases

PhosphoSiteiO95237.

Expressioni

Tissue specificityi

Hepatic stellate cells and endothelial cells (at protein level). Found at high levels in testis and liver, followed by retinal pigment epithelium, small intestine, prostate, pancreas and colon. Low expression observed in brain. In fetal tissues, expressed in retinal pigment epithelium and liver, and barely in the brain.2 Publications

Inductioni

LRAT activity is up-regulated by dietary vitamin A. Under conditions of vitamin A depletion, LRAT expression in the liver is induced by retinoic acid By similarity.1 Publication

Gene expression databases

ArrayExpressiO95237.
BgeeiO95237.
CleanExiHS_LRAT.
GenevestigatoriO95237.

Organism-specific databases

HPAiHPA008397.

Interactioni

Protein-protein interaction databases

BioGridi114658. 1 interaction.
STRINGi9606.ENSP00000337224.

Structurei

3D structure databases

ProteinModelPortaliO95237.
SMRiO95237. Positions 48-171.

Family & Domainsi

Sequence similaritiesi

Belongs to the H-rev107 family.

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG40588.
HOGENOMiHOG000013187.
HOVERGENiHBG047861.
InParanoidiO95237.
KOiK00678.
OMAiAIFIPFC.
PhylomeDBiO95237.
TreeFamiTF330836.

Family and domain databases

InterProiIPR007053. LRAT-like_dom.
[Graphical view]
PfamiPF04970. LRAT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O95237-1 [UniParc]FASTAAdd to Basket

« Hide

MKNPMLEVVS LLLEKLLLIS NFTLFSSGAA GEDKGRNSFY ETSSFHRGDV    50
LEVPRTHLTH YGIYLGDNRV AHMMPDILLA LTDDMGRTQK VVSNKRLILG 100
VIVKVASIRV DTVEDFAYGA NILVNHLDES LQKKALLNEE VARRAEKLLG 150
FTPYSLLWNN CEHFVTYCRY GTPISPQSDK FCETVKIIIR DQRSVLASAV 200
LGLASIVCTG LVSYTTLPAI FIPFFLWMAG 230
Length:230
Mass (Da):25,703
Last modified:April 26, 2004 - v2
Checksum:iDCB7F5A1C3FF7689
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti173 – 1731P → L.1 Publication
VAR_063559
Natural varianti175 – 1751S → R in LCA14; loss of function. 1 Publication
VAR_018386

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti32 – 321E → K in AAD13529. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF071510 mRNA. Translation: AAD13529.1.
AY546085 mRNA. Translation: AAS49412.1.
AY546086 mRNA. Translation: AAS49413.1.
AK292598 mRNA. Translation: BAF85287.1.
CH471056 Genomic DNA. Translation: EAX04904.1.
BC031053 mRNA. Translation: AAH31053.1.
CCDSiCCDS3789.1.
RefSeqiNP_004735.2. NM_004744.3.
XP_006714475.1. XM_006714412.1.
UniGeneiHs.658427.

Genome annotation databases

EnsembliENST00000336356; ENSP00000337224; ENSG00000121207.
ENST00000507827; ENSP00000426761; ENSG00000121207.
GeneIDi9227.
KEGGihsa:9227.
UCSCiuc003iom.1. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF071510 mRNA. Translation: AAD13529.1 .
AY546085 mRNA. Translation: AAS49412.1 .
AY546086 mRNA. Translation: AAS49413.1 .
AK292598 mRNA. Translation: BAF85287.1 .
CH471056 Genomic DNA. Translation: EAX04904.1 .
BC031053 mRNA. Translation: AAH31053.1 .
CCDSi CCDS3789.1.
RefSeqi NP_004735.2. NM_004744.3.
XP_006714475.1. XM_006714412.1.
UniGenei Hs.658427.

3D structure databases

ProteinModelPortali O95237.
SMRi O95237. Positions 48-171.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 114658. 1 interaction.
STRINGi 9606.ENSP00000337224.

Chemistry

BindingDBi O95237.
ChEMBLi CHEMBL2202.
DrugBanki DB00162. Vitamin A.

PTM databases

PhosphoSitei O95237.

Proteomic databases

MaxQBi O95237.
PaxDbi O95237.
PRIDEi O95237.

Protocols and materials databases

DNASUi 9227.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000336356 ; ENSP00000337224 ; ENSG00000121207 .
ENST00000507827 ; ENSP00000426761 ; ENSG00000121207 .
GeneIDi 9227.
KEGGi hsa:9227.
UCSCi uc003iom.1. human.

Organism-specific databases

CTDi 9227.
GeneCardsi GC04P155549.
GeneReviewsi LRAT.
HGNCi HGNC:6685. LRAT.
HPAi HPA008397.
MIMi 604863. gene.
613341. phenotype.
neXtProti NX_O95237.
Orphaneti 65. Leber congenital amaurosis.
791. Retinitis pigmentosa.
364055. Severe early-childhood-onset retinal dystrophy.
PharmGKBi PA30443.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG40588.
HOGENOMi HOG000013187.
HOVERGENi HBG047861.
InParanoidi O95237.
KOi K00678.
OMAi AIFIPFC.
PhylomeDBi O95237.
TreeFami TF330836.

Enzyme and pathway databases

UniPathwayi UPA00912 .
BioCyci MetaCyc:HS04474-MONOMER.
BRENDAi 2.3.1.135. 2681.
Reactomei REACT_160156. The canonical retinoid cycle in rods (twilight vision).
REACT_24968. Retinoid metabolism and transport.

Miscellaneous databases

ChiTaRSi LRAT. human.
GeneWikii Lecithin_retinol_acyltransferase.
GenomeRNAii 9227.
NextBioi 34583.
PROi O95237.
SOURCEi Search...

Gene expression databases

ArrayExpressi O95237.
Bgeei O95237.
CleanExi HS_LRAT.
Genevestigatori O95237.

Family and domain databases

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

Publicationsi

« Hide 'large scale' publications
  1. "Molecular and biochemical characterization of lecithin retinol acyltransferase."
    Ruiz A., Winston A., Lim Y.-H., Gilbert B.A., Rando R.R., Bok D.
    J. Biol. Chem. 274:3834-3841(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, ENZYME REGULATION, TISSUE SPECIFICITY.
  2. "Cloning, gene organization and identification of an alternative splicing process in lecithin:retinol acyltransferase (LRAT) cDNA from human liver."
    Zolfaghari R., Ross A.C.
    Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Liver.
  3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Testis.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Testis.
  6. "Lecithin retinol acyltransferase contains cysteine residues essential for catalysis."
    Mondal M.S., Ruiz A., Bok D., Rando R.R.
    Biochemistry 39:5215-5220(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF CYS-161; CYS-168; CYS-182 AND CYS-208.
  7. "Identification of novel mutations in patients with Leber congenital amaurosis and juvenile RP by genome-wide homozygosity mapping with SNP microarrays."
    den Hollander A.I., Lopez I., Yzer S., Zonneveld M.N., Janssen I.M., Strom T.M., Hehir-Kwa J.Y., Veltman J.A., Arends M.L., Meitinger T., Musarella M.A., van den Born L.I., Fishman G.A., Maumenee I.H., Rohrschneider K., Cremers F.P., Koenekoop R.K.
    Invest. Ophthalmol. Vis. Sci. 48:5690-5698(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN LCA14.
  8. "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.
  9. "Mutations in the gene encoding lecithin retinol acyltransferase are associated with early-onset severe retinal dystrophy."
    Thompson D.A., Li Y., McHenry C.L., Carlson T.J., Ding X., Sieving P.A., Apfelstedt-Sylla E., Gal A.
    Nat. Genet. 28:123-124(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT LCA14 ARG-175.
  10. "Screening genes of the retinoid metabolism: novel LRAT mutation in Leber congenital amaurosis."
    Senechal A., Humbert G., Surget M.O., Bazalgette C., Bazalgette C., Arnaud B., Arndt C., Laurent E., Brabet P., Hamel C.P.
    Am. J. Ophthalmol. 142:702-704(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT LEU-173, INVOLVEMENT IN LCA14.

Entry informationi

Entry nameiLRAT_HUMAN
AccessioniPrimary (citable) accession number: O95237
Secondary accession number(s): A8K983, Q8N716
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 26, 2004
Last sequence update: April 26, 2004
Last modified: September 3, 2014
This is version 114 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 4
    Human chromosome 4: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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