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 27-MAR-2024, entry version 177. 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- CC retinol--[retinol-binding protein] = a 2-acyl-sn-glycero-3- CC phosphocholine + an all-trans-retinyl ester + apo--[retinol-binding CC protein]; Xref=Rhea:RHEA:17469, Rhea:RHEA-COMP:14426, Rhea:RHEA- CC COMP:14428, 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 = 2-hexadecanoyl-sn-glycero-3-phosphocholine + all-trans- CC retinyl hexadecanoate; Xref=Rhea:RHEA:43904, ChEBI:CHEBI:17336, CC ChEBI:CHEBI:17616, ChEBI:CHEBI:72999, ChEBI:CHEBI:76078; 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 9606-ENSP00000337224; -. DR PeptideAtlas; O95237; -. DR ProteomicsDB; 50736; -. DR Antibodypedia; 2389; 308 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 AGR; HGNC:6685; -. DR CTD; 9227; -. DR DisGeNET; 9227; -. DR GeneCards; LRAT; -. DR GeneReviews; LRAT; -. DR HGNC; HGNC:6685; LRAT. DR HPA; ENSG00000121207; Tissue enhanced (liver). 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; PFCLWMV; -. DR OrthoDB; 3059772at2759; -. DR PhylomeDB; O95237; -. DR TreeFam; TF330836; -. DR BioCyc; MetaCyc:HS04474-MONOMER; -. 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; 13 hits in 1149 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 90 other cell types or tissues. DR ExpressionAtlas; O95237; baseline and differential. DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB. DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome. 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 Gene3D; 3.90.1720.10; endopeptidase domain like (from Nostoc punctiforme); 1. DR InterPro; IPR042288; LRAT. DR InterPro; IPR007053; LRAT_dom. DR PANTHER; PTHR46678; LECITHIN RETINOL ACYLTRANSFERASE; 1. DR PANTHER; PTHR46678:SF1; LECITHIN RETINOL ACYLTRANSFERASE; 1. DR Pfam; PF04970; LRAT; 1. DR PROSITE; PS51934; LRAT; 1. DR Genevisible; O95237; HS. 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 //