LRAT_HUMAN
ID LRAT_HUMAN Reviewed; 230 AA.
AC O95237; A8K983; Q8N716;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2004, sequence version 2.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Lecithin retinol acyltransferase {ECO:0000305};
DE EC=2.3.1.135 {ECO:0000305|PubMed:10819989};
DE AltName: Full=Phosphatidylcholine--retinol O-acyltransferase;
GN Name=LRAT {ECO:0000312|HGNC:HGNC:6685};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, ACTIVITY REGULATION, AND TISSUE
RP SPECIFICITY.
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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=15474300; DOI=10.1016/j.gene.2004.06.043;
RA Zolfaghari R., Ross A.C.;
RT "Cloning, gene organization and identification of an alternative splicing
RT process in lecithin:retinol acyltransferase cDNA from human liver.";
RL Gene 341:181-188(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP MUTAGENESIS OF CYS-161; CYS-168; CYS-182 AND CYS-208, AND CATALYTIC
RP ACTIVITY.
RX PubMed=10819989; DOI=10.1021/bi9929554;
RA Mondal M.S., Ruiz A., Bok D., Rando R.R.;
RT "Lecithin retinol acyltransferase contains cysteine residues essential for
RT catalysis.";
RL Biochemistry 39:5215-5220(2000).
RN [7]
RP INVOLVEMENT IN LCA14.
RX PubMed=18055821; DOI=10.1167/iovs.07-0610;
RA den Hollander A.I., Lopez I., Yzer S., Zonneveld M.N., Janssen I.M.,
RA Strom T.M., Hehir-Kwa J.Y., Veltman J.A., Arends M.L., Meitinger T.,
RA Musarella M.A., van den Born L.I., Fishman G.A., Maumenee I.H.,
RA Rohrschneider K., Cremers F.P., Koenekoop R.K.;
RT "Identification of novel mutations in patients with Leber congenital
RT amaurosis and juvenile RP by genome-wide homozygosity mapping with SNP
RT microarrays.";
RL Invest. Ophthalmol. Vis. Sci. 48:5690-5698(2007).
RN [8]
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., 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).
RN [9]
RP VARIANT LCA14 ARG-175.
RX PubMed=11381255; DOI=10.1038/88828;
RA Thompson D.A., Li Y., McHenry C.L., Carlson T.J., Ding X., Sieving P.A.,
RA Apfelstedt-Sylla E., Gal A.;
RT "Mutations in the gene encoding lecithin retinol acyltransferase are
RT associated with early-onset severe retinal dystrophy.";
RL Nat. Genet. 28:123-124(2001).
RN [10]
RP VARIANT LEU-173, AND INVOLVEMENT IN LCA14.
RX PubMed=17011878; DOI=10.1016/j.ajo.2006.04.057;
RA Senechal A., Humbert G., Surget M.O., Bazalgette C., Bazalgette C.,
RA Arnaud B., Arndt C., Laurent E., Brabet P., Hamel C.P.;
RT "Screening genes of the retinoid metabolism: novel LRAT mutation in Leber
RT congenital amaurosis.";
RL Am. J. Ophthalmol. 142:702-704(2006).
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). Retinyl esters are storage forms of vitamin A
CC (Probable). LRAT plays a critical role in vision (Probable). It
CC 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:9920938,
CC 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:0000305|PubMed:10819989};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17470;
CC Evidence={ECO:0000305|PubMed:10819989};
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:10819989};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43905;
CC Evidence={ECO:0000305|PubMed:10819989};
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 -!- INTERACTION:
CC O95237; P62952: BLCAP; NbExp=3; IntAct=EBI-13291307, EBI-3895726;
CC O95237; Q7Z5P4: HSD17B13; NbExp=3; IntAct=EBI-13291307, EBI-18053395;
CC O95237; Q9Y320: TMX2; NbExp=3; IntAct=EBI-13291307, EBI-6447886;
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 -!- TISSUE SPECIFICITY: Hepatic stellate cells and endothelial cells (at
CC protein level). Found at high levels in testis and liver, followed by
CC retinal pigment epithelium, small intestine, prostate, pancreas and
CC colon. Low expression observed in brain. In fetal tissues, expressed in
CC retinal pigment epithelium and liver, and barely in the brain.
CC {ECO:0000269|PubMed:18544127, ECO:0000269|PubMed:9920938}.
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 -!- DISEASE: Leber congenital amaurosis 14 (LCA14) [MIM:613341]: A severe
CC dystrophy of the retina, typically becoming evident in the first years
CC of life. Visual function is usually poor and often accompanied by
CC nystagmus, sluggish or near-absent pupillary responses, photophobia,
CC high hyperopia and keratoconus. {ECO:0000269|PubMed:11381255,
CC ECO:0000269|PubMed:17011878, ECO:0000269|PubMed:18055821}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the H-rev107 family. {ECO:0000305}.
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DR EMBL; AF071510; AAD13529.1; -; mRNA.
DR EMBL; AY546085; AAS49412.1; -; mRNA.
DR EMBL; AY546086; AAS49413.1; -; mRNA.
DR EMBL; AK292598; BAF85287.1; -; mRNA.
DR EMBL; CH471056; EAX04904.1; -; Genomic_DNA.
DR EMBL; BC031053; AAH31053.1; -; mRNA.
DR CCDS; CCDS3789.1; -.
DR RefSeq; NP_001288574.1; NM_001301645.1.
DR RefSeq; NP_004735.2; NM_004744.4.
DR AlphaFoldDB; O95237; -.
DR SMR; O95237; -.
DR BioGRID; 114658; 6.
DR IntAct; O95237; 4.
DR STRING; 9606.ENSP00000337224; -.
DR BindingDB; O95237; -.
DR ChEMBL; CHEMBL2202; -.
DR DrugBank; DB00162; Vitamin A.
DR DrugCentral; O95237; -.
DR SwissLipids; SLP:000000686; -.
DR iPTMnet; O95237; -.
DR PhosphoSitePlus; O95237; -.
DR BioMuta; LRAT; -.
DR EPD; O95237; -.
DR MassIVE; O95237; -.
DR MaxQB; O95237; -.
DR PaxDb; O95237; -.
DR PeptideAtlas; O95237; -.
DR PRIDE; O95237; -.
DR ProteomicsDB; 50736; -.
DR Antibodypedia; 2389; 279 antibodies from 30 providers.
DR DNASU; 9227; -.
DR Ensembl; ENST00000336356.4; ENSP00000337224.3; ENSG00000121207.12.
DR Ensembl; ENST00000507827.5; ENSP00000426761.1; ENSG00000121207.12.
DR GeneID; 9227; -.
DR KEGG; hsa:9227; -.
DR MANE-Select; ENST00000336356.4; ENSP00000337224.3; NM_004744.5; NP_004735.2.
DR UCSC; uc003ion.2; human.
DR CTD; 9227; -.
DR DisGeNET; 9227; -.
DR GeneCards; LRAT; -.
DR GeneReviews; LRAT; -.
DR HGNC; HGNC:6685; LRAT.
DR HPA; ENSG00000121207; Tissue enhanced (brain).
DR MalaCards; LRAT; -.
DR MIM; 604863; gene.
DR MIM; 613341; phenotype.
DR neXtProt; NX_O95237; -.
DR OpenTargets; ENSG00000121207; -.
DR Orphanet; 65; Leber congenital amaurosis.
DR Orphanet; 791; Retinitis pigmentosa.
DR Orphanet; 364055; Severe early-childhood-onset retinal dystrophy.
DR PharmGKB; PA30443; -.
DR VEuPathDB; HostDB:ENSG00000121207; -.
DR eggNOG; ENOG502QWSA; Eukaryota.
DR GeneTree; ENSGT00510000047351; -.
DR HOGENOM; CLU_105262_0_0_1; -.
DR InParanoid; O95237; -.
DR OMA; ADKFCEY; -.
DR OrthoDB; 1602481at2759; -.
DR PhylomeDB; O95237; -.
DR TreeFam; TF330836; -.
DR BioCyc; MetaCyc:HS04474-MON; -.
DR BRENDA; 2.3.1.135; 2681.
DR PathwayCommons; O95237; -.
DR Reactome; R-HSA-2453864; Retinoid cycle disease events.
DR Reactome; R-HSA-2453902; The canonical retinoid cycle in rods (twilight vision).
DR Reactome; R-HSA-975634; Retinoid metabolism and transport.
DR SignaLink; O95237; -.
DR SIGNOR; O95237; -.
DR UniPathway; UPA00912; -.
DR BioGRID-ORCS; 9227; 11 hits in 1068 CRISPR screens.
DR ChiTaRS; LRAT; human.
DR GeneWiki; Lecithin_retinol_acyltransferase; -.
DR GenomeRNAi; 9227; -.
DR Pharos; O95237; Tbio.
DR PRO; PR:O95237; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; O95237; protein.
DR Bgee; ENSG00000121207; Expressed in pigmented layer of retina and 88 other tissues.
DR ExpressionAtlas; O95237; baseline and differential.
DR Genevisible; O95237; HS.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005771; C:multivesicular body; ISS:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR GO; GO:0005791; C:rough endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0016746; F:acyltransferase activity; TAS:ProtInc.
DR GO; GO:0102279; F:lecithin:11-cis retinol acyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0016416; F:O-palmitoyltransferase activity; TAS:Reactome.
DR GO; GO:0047173; F:phosphatidylcholine-retinol O-acyltransferase activity; IDA:UniProtKB.
DR GO; GO:0001972; F:retinoic acid binding; IEA:Ensembl.
DR GO; GO:0019841; F:retinol binding; IEA:Ensembl.
DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEA:Ensembl.
DR GO; GO:0032370; P:positive regulation of lipid transport; IEA:Ensembl.
DR GO; GO:0009617; P:response to bacterium; IEA:Ensembl.
DR GO; GO:0032526; P:response to retinoic acid; IEA:Ensembl.
DR GO; GO:0033189; P:response to vitamin A; IEA:Ensembl.
DR GO; GO:0001523; P:retinoid metabolic process; TAS:Reactome.
DR GO; GO:0042572; P:retinol metabolic process; IDA: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; Disease variant; Endoplasmic reticulum;
KW Endosome; Leber congenital amaurosis; 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_0000152478"
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"
FT VARIANT 173
FT /note="P -> L (in dbSNP:rs1448665709)"
FT /evidence="ECO:0000269|PubMed:17011878"
FT /id="VAR_063559"
FT VARIANT 175
FT /note="S -> R (in LCA14; loss of function;
FT dbSNP:rs104893848)"
FT /evidence="ECO:0000269|PubMed:11381255"
FT /id="VAR_018386"
FT MUTAGEN 161
FT /note="C->A,S: Loss of activity."
FT /evidence="ECO:0000269|PubMed:10819989"
FT MUTAGEN 168
FT /note="C->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:10819989"
FT MUTAGEN 168
FT /note="C->S: Does not affect activity."
FT /evidence="ECO:0000269|PubMed:10819989"
FT MUTAGEN 182
FT /note="C->A: Does not affect activity."
FT /evidence="ECO:0000269|PubMed:10819989"
FT MUTAGEN 208
FT /note="C->A: Does not affect activity."
FT /evidence="ECO:0000269|PubMed:10819989"
FT CONFLICT 32
FT /note="E -> K (in Ref. 1; AAD13529)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 230 AA; 25703 MW; DCB7F5A1C3FF7689 CRC64;
MKNPMLEVVS LLLEKLLLIS NFTLFSSGAA GEDKGRNSFY ETSSFHRGDV LEVPRTHLTH
YGIYLGDNRV AHMMPDILLA LTDDMGRTQK VVSNKRLILG VIVKVASIRV DTVEDFAYGA
NILVNHLDES LQKKALLNEE VARRAEKLLG FTPYSLLWNN CEHFVTYCRY GTPISPQSDK
FCETVKIIIR DQRSVLASAV LGLASIVCTG LVSYTTLPAI FIPFFLWMAG
