ID   LIPG_HUMAN              Reviewed;         500 AA.
AC   Q9Y5X9; B0LPG6; Q6P9C8; Q6UW82;
DT   26-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   24-JAN-2024, entry version 197.
DE   RecName: Full=Endothelial lipase;
DE            EC=3.1.1.3 {ECO:0000269|PubMed:10192396, ECO:0000269|PubMed:10318835, ECO:0000269|PubMed:12032167};
DE   AltName: Full=Endothelial cell-derived lipase;
DE            Short=EDL;
DE            Short=EL;
DE   AltName: Full=Phospholipase A1;
DE            EC=3.1.1.32 {ECO:0000269|PubMed:12032167};
DE   Flags: Precursor;
GN   Name=LIPG; ORFNames=UNQ387/PRO719;
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] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY,
RP   SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC   TISSUE=Endothelial cell;
RX   PubMed=10318835; DOI=10.1074/jbc.274.20.14170;
RA   Hirata K., Dichek H.L., Cioffi J.A., Choi S.Y., Leeper N.J., Quintana L.,
RA   Kronmal G.S., Cooper A.D., Quertermous T.;
RT   "Cloning of a unique lipase from endothelial cells extends the lipase gene
RT   family.";
RL   J. Biol. Chem. 274:14170-14175(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY, AND
RP   TISSUE SPECIFICITY.
RC   TISSUE=Placenta;
RX   PubMed=10192396; DOI=10.1038/7766;
RA   Jaye M., Lynch K.J., Krawiec J., Marchadier D., Maugeais C., Doan K.,
RA   South V., Amin D., Perrone M., Rader D.J.;
RT   "A novel endothelial-derived lipase that modulates HDL metabolism.";
RL   Nat. Genet. 21:424-428(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX   PubMed=12975309; DOI=10.1101/gr.1293003;
RA   Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA   Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA   Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA   Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA   Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA   Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA   Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA   Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT   "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT   identify novel human secreted and transmembrane proteins: a bioinformatics
RT   assessment.";
RL   Genome Res. 13:2265-2270(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG   NHLBI resequencing and genotyping service (RS&G);
RL   Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases.
RN   [5]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Placenta;
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   [7]
RP   FUNCTION, CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
RX   PubMed=12032167;
RA   McCoy M.G., Sun G.-S., Marchadier D., Maugeais C., Glick J.M., Rader D.J.;
RT   "Characterization of the lipolytic activity of endothelial lipase.";
RL   J. Lipid Res. 43:921-929(2002).
RN   [8]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-393.
RC   TISSUE=Plasma;
RX   PubMed=16335952; DOI=10.1021/pr0502065;
RA   Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J.,
RA   Smith R.D.;
RT   "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT   hydrazide chemistry, and mass spectrometry.";
RL   J. Proteome Res. 4:2070-2080(2005).
RN   [9]
RP   SUBUNIT.
RX   PubMed=19567873; DOI=10.1074/jbc.m109.037002;
RA   Griffon N., Jin W., Petty T.J., Millar J., Badellino K.O., Saven J.G.,
RA   Marchadier D.H., Kempner E.S., Billheimer J., Glick J.M., Rader D.J.;
RT   "Identification of the active form of endothelial lipase, a homodimer in a
RT   head-to-tail conformation.";
RL   J. Biol. Chem. 284:23322-23330(2009).
RN   [10]
RP   VARIANTS SER-96; ILE-111 AND HIS-312.
RX   PubMed=12966036; DOI=10.1093/hmg/ddg314;
RA   Morabia A., Cayanis E., Costanza M.C., Ross B.M., Flaherty M.S.,
RA   Alvin G.B., Das K., Gilliam T.C.;
RT   "Association of extreme blood lipid profile phenotypic variation with 11
RT   reverse cholesterol transport genes and 10 non-genetic cardiovascular
RT   disease risk factors.";
RL   Hum. Mol. Genet. 12:2733-2743(2003).
CC   -!- FUNCTION: Exerts both phospholipase and triglyceride lipase activities
CC       (PubMed:12032167, PubMed:10318835, PubMed:10192396). More active as a
CC       phospholipase than a triglyceride lipase (PubMed:12032167). Hydrolyzes
CC       triglycerides, both with short-chain fatty acyl groups (tributyrin) and
CC       long-chain fatty acyl groups (triolein) with similar levels of activity
CC       toward both types of substrates (PubMed:12032167). Hydrolyzes high
CC       density lipoproteins (HDL) more efficiently than other lipoproteins
CC       (PubMed:12032167, PubMed:10192396). {ECO:0000269|PubMed:10192396,
CC       ECO:0000269|PubMed:10318835, ECO:0000269|PubMed:12032167}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a triacylglycerol + H2O = a diacylglycerol + a fatty acid +
CC         H(+); Xref=Rhea:RHEA:12044, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17855, ChEBI:CHEBI:18035, ChEBI:CHEBI:28868; EC=3.1.1.3;
CC         Evidence={ECO:0000269|PubMed:10192396, ECO:0000269|PubMed:10318835,
CC         ECO:0000269|PubMed:12032167};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 2-acyl-sn-
CC         glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:18689,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868,
CC         ChEBI:CHEBI:57643, ChEBI:CHEBI:57875; EC=3.1.1.32;
CC         Evidence={ECO:0000269|PubMed:12032167};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1,2,3-tri-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-
CC         octadecenoate + di-(9Z)-octadecenoylglycerol + H(+);
CC         Xref=Rhea:RHEA:38575, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30823, ChEBI:CHEBI:53753, ChEBI:CHEBI:75945;
CC         Evidence={ECO:0000269|PubMed:12032167};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38576;
CC         Evidence={ECO:0000305|PubMed:12032167};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1,2,3-tributanoylglycerol + H2O = butanoate +
CC         dibutanoylglycerol + H(+); Xref=Rhea:RHEA:40475, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17968, ChEBI:CHEBI:35020,
CC         ChEBI:CHEBI:76478; Evidence={ECO:0000269|PubMed:12032167};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40476;
CC         Evidence={ECO:0000305|PubMed:12032167};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1,2-dihexadecanoyl-sn-glycero-3-phosphocholine + H2O = H(+) +
CC         hexadecanoate + hexadecanoyl-sn-glycero-3-phosphocholine;
CC         Xref=Rhea:RHEA:41384, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:64563, ChEBI:CHEBI:72999;
CC         Evidence={ECO:0000269|PubMed:12032167};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41385;
CC         Evidence={ECO:0000305|PubMed:12032167};
CC   -!- ACTIVITY REGULATION: Inhibited by serum and NaCl.
CC       {ECO:0000269|PubMed:12032167}.
CC   -!- SUBUNIT: Head to tail homodimer. {ECO:0000269|PubMed:19567873}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10318835}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9Y5X9-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9Y5X9-2; Sequence=VSP_013302, VSP_013303;
CC   -!- TISSUE SPECIFICITY: High level of expression in the liver, placenta,
CC       lung, thyroid, kidney, testis and in the corpus luteum of the ovary.
CC       Expressed also in coronary artery endothelial cells, umbilical vein
CC       endothelial cells and in hepatocytes and osteosarcoma cell lines. Not
CC       detected in heart, brain and muscle. {ECO:0000269|PubMed:10192396,
CC       ECO:0000269|PubMed:10318835}.
CC   -!- MISCELLANEOUS: It is termed endothelial lipase due to the fact that it
CC       is synthesized in endothelial cells, a characteristic that
CC       distinguishes it from other members of the family. However, this
CC       protein is also expressed in other cell types.
CC   -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC       {ECO:0000305}.
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DR   EMBL; AF118767; AAD30434.1; -; mRNA.
DR   EMBL; AY358928; AAQ89287.1; -; mRNA.
DR   EMBL; EU332856; ABY87545.1; -; Genomic_DNA.
DR   EMBL; CH471096; EAW62947.1; -; Genomic_DNA.
DR   EMBL; BC060825; AAH60825.1; -; mRNA.
DR   CCDS; CCDS11938.1; -. [Q9Y5X9-1]
DR   RefSeq; NP_001294935.1; NM_001308006.1.
DR   RefSeq; NP_006024.1; NM_006033.3. [Q9Y5X9-1]
DR   AlphaFoldDB; Q9Y5X9; -.
DR   SMR; Q9Y5X9; -.
DR   BioGRID; 114788; 81.
DR   IntAct; Q9Y5X9; 22.
DR   MINT; Q9Y5X9; -.
DR   STRING; 9606.ENSP00000261292; -.
DR   BindingDB; Q9Y5X9; -.
DR   ChEMBL; CHEMBL5080; -.
DR   GuidetoPHARMACOLOGY; 2591; -.
DR   SwissLipids; SLP:000000567; -.
DR   ESTHER; human-LIPG; Lipoprotein_Lipase.
DR   GlyCosmos; Q9Y5X9; 5 sites, No reported glycans.
DR   GlyGen; Q9Y5X9; 9 sites, 1 O-linked glycan (4 sites).
DR   iPTMnet; Q9Y5X9; -.
DR   PhosphoSitePlus; Q9Y5X9; -.
DR   BioMuta; LIPG; -.
DR   DMDM; 22001808; -.
DR   EPD; Q9Y5X9; -.
DR   jPOST; Q9Y5X9; -.
DR   MassIVE; Q9Y5X9; -.
DR   MaxQB; Q9Y5X9; -.
DR   PaxDb; 9606-ENSP00000261292; -.
DR   PeptideAtlas; Q9Y5X9; -.
DR   ProteomicsDB; 86535; -. [Q9Y5X9-1]
DR   ProteomicsDB; 86536; -. [Q9Y5X9-2]
DR   Antibodypedia; 1561; 1192 antibodies from 32 providers.
DR   DNASU; 9388; -.
DR   Ensembl; ENST00000261292.9; ENSP00000261292.4; ENSG00000101670.12. [Q9Y5X9-1]
DR   Ensembl; ENST00000580036.5; ENSP00000462420.1; ENSG00000101670.12. [Q9Y5X9-2]
DR   GeneID; 9388; -.
DR   KEGG; hsa:9388; -.
DR   MANE-Select; ENST00000261292.9; ENSP00000261292.4; NM_006033.4; NP_006024.1.
DR   UCSC; uc002ldu.2; human. [Q9Y5X9-1]
DR   AGR; HGNC:6623; -.
DR   CTD; 9388; -.
DR   DisGeNET; 9388; -.
DR   GeneCards; LIPG; -.
DR   HGNC; HGNC:6623; LIPG.
DR   HPA; ENSG00000101670; Group enriched (placenta, thyroid gland).
DR   MIM; 603684; gene.
DR   neXtProt; NX_Q9Y5X9; -.
DR   OpenTargets; ENSG00000101670; -.
DR   PharmGKB; PA30395; -.
DR   VEuPathDB; HostDB:ENSG00000101670; -.
DR   eggNOG; ENOG502QU8P; Eukaryota.
DR   GeneTree; ENSGT00940000159394; -.
DR   HOGENOM; CLU_027171_1_2_1; -.
DR   InParanoid; Q9Y5X9; -.
DR   OMA; QMPVGHV; -.
DR   OrthoDB; 3428256at2759; -.
DR   PhylomeDB; Q9Y5X9; -.
DR   TreeFam; TF324997; -.
DR   PathwayCommons; Q9Y5X9; -.
DR   Reactome; R-HSA-8964058; HDL remodeling.
DR   SignaLink; Q9Y5X9; -.
DR   BioGRID-ORCS; 9388; 9 hits in 1154 CRISPR screens.
DR   ChiTaRS; LIPG; human.
DR   GenomeRNAi; 9388; -.
DR   Pharos; Q9Y5X9; Tchem.
DR   PRO; PR:Q9Y5X9; -.
DR   Proteomes; UP000005640; Chromosome 18.
DR   RNAct; Q9Y5X9; Protein.
DR   Bgee; ENSG00000101670; Expressed in ventricular zone and 124 other cell types or tissues.
DR   ExpressionAtlas; Q9Y5X9; baseline and differential.
DR   GO; GO:0009986; C:cell surface; IDA:MGI.
DR   GO; GO:0005769; C:early endosome; IDA:MGI.
DR   GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR   GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
DR   GO; GO:0005794; C:Golgi apparatus; IDA:MGI.
DR   GO; GO:0052740; F:1-acyl-2-lysophosphatidylserine acylhydrolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
DR   GO; GO:0004465; F:lipoprotein lipase activity; IBA:GO_Central.
DR   GO; GO:0052739; F:phosphatidylserine 1-acylhydrolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008970; F:phospholipase A1 activity; IDA:UniProtKB.
DR   GO; GO:0004620; F:phospholipase activity; IDA:BHF-UCL.
DR   GO; GO:0004806; F:triglyceride lipase activity; IDA:UniProtKB.
DR   GO; GO:0042632; P:cholesterol homeostasis; IMP:BHF-UCL.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IBA:GO_Central.
DR   GO; GO:0034375; P:high-density lipoprotein particle remodeling; IMP:BHF-UCL.
DR   GO; GO:0006629; P:lipid metabolic process; TAS:ProtInc.
DR   GO; GO:0009395; P:phospholipid catabolic process; NAS:BHF-UCL.
DR   GO; GO:0055091; P:phospholipid homeostasis; IMP:BHF-UCL.
DR   GO; GO:0032376; P:positive regulation of cholesterol transport; IDA:BHF-UCL.
DR   GO; GO:0010983; P:positive regulation of high-density lipoprotein particle clearance; IMP:BHF-UCL.
DR   GO; GO:0050746; P:regulation of lipoprotein metabolic process; IEA:Ensembl.
DR   GO; GO:0007584; P:response to nutrient; IEA:Ensembl.
DR   GO; GO:0043691; P:reverse cholesterol transport; IMP:BHF-UCL.
DR   GO; GO:0019433; P:triglyceride catabolic process; IBA:GO_Central.
DR   CDD; cd00707; Pancreat_lipase_like; 1.
DR   CDD; cd01758; PLAT_LPL; 1.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   Gene3D; 2.60.60.20; PLAT/LH2 domain; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR013818; Lipase.
DR   InterPro; IPR016272; Lipase_LIPH.
DR   InterPro; IPR033906; Lipase_N.
DR   InterPro; IPR002330; Lipo_Lipase.
DR   InterPro; IPR001024; PLAT/LH2_dom.
DR   InterPro; IPR036392; PLAT/LH2_dom_sf.
DR   InterPro; IPR000734; TAG_lipase.
DR   PANTHER; PTHR11610:SF13; ENDOTHELIAL LIPASE; 1.
DR   PANTHER; PTHR11610; LIPASE; 1.
DR   Pfam; PF00151; Lipase; 1.
DR   Pfam; PF01477; PLAT; 1.
DR   PIRSF; PIRSF000865; Lipoprotein_lipase_LIPH; 1.
DR   PRINTS; PR00822; LIPOLIPASE.
DR   PRINTS; PR00821; TAGLIPASE.
DR   SMART; SM00308; LH2; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR   SUPFAM; SSF49723; Lipase/lipooxygenase domain (PLAT/LH2 domain); 1.
DR   PROSITE; PS00120; LIPASE_SER; 1.
DR   PROSITE; PS50095; PLAT; 1.
DR   Genevisible; Q9Y5X9; HS.
PE   1: Evidence at protein level;
KW   Alternative splicing; Disulfide bond; Glycoprotein; Heparin-binding;
KW   Hydrolase; Lipid degradation; Lipid metabolism; Reference proteome;
KW   Secreted; Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..500
FT                   /note="Endothelial lipase"
FT                   /id="PRO_0000017797"
FT   DOMAIN          347..482
FT                   /note="PLAT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00152"
FT   ACT_SITE        169
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        193
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10037"
FT   ACT_SITE        274
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10037"
FT   BINDING         325..337
FT                   /ligand="heparin"
FT                   /ligand_id="ChEBI:CHEBI:28304"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        80
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        136
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        393
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:16335952"
FT   CARBOHYD        469
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        491
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        64..77
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00152"
FT   DISULFID        252..272
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00152"
FT   DISULFID        297..316
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00152"
FT   DISULFID        308..311
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00152"
FT   DISULFID        463..483
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00152"
FT   VAR_SEQ         346..354
FT                   /note="VYHYQMKIH -> GNLQSLECP (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:12975309"
FT                   /id="VSP_013302"
FT   VAR_SEQ         355..500
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:12975309"
FT                   /id="VSP_013303"
FT   VARIANT         26
FT                   /note="G -> S (in dbSNP:rs9963243)"
FT                   /id="VAR_034082"
FT   VARIANT         96
FT                   /note="G -> S (in dbSNP:rs150879681)"
FT                   /evidence="ECO:0000269|PubMed:12966036"
FT                   /id="VAR_017027"
FT   VARIANT         111
FT                   /note="T -> I (in dbSNP:rs2000813)"
FT                   /evidence="ECO:0000269|PubMed:12966036"
FT                   /id="VAR_017028"
FT   VARIANT         312
FT                   /note="R -> H"
FT                   /evidence="ECO:0000269|PubMed:12966036"
FT                   /id="VAR_017029"
FT   CONFLICT        476
FT                   /note="R -> Q (in Ref. 6; AAH60825)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   500 AA;  56795 MW;  96EC95125CD2A3FD CRC64;
     MSNSVPLLCF WSLCYCFAAG SPVPFGPEGR LEDKLHKPKA TQTEVKPSVR FNLRTSKDPE
     HEGCYLSVGH SQPLEDCSFN MTAKTFFIIH GWTMSGIFEN WLHKLVSALH TREKDANVVV
     VDWLPLAHQL YTDAVNNTRV VGHSIARMLD WLQEKDDFSL GNVHLIGYSL GAHVAGYAGN
     FVKGTVGRIT GLDPAGPMFE GADIHKRLSP DDADFVDVLH TYTRSFGLSI GIQMPVGHID
     IYPNGGDFQP GCGLNDVLGS IAYGTITEVV KCEHERAVHL FVDSLVNQDK PSFAFQCTDS
     NRFKKGICLS CRKNRCNSIG YNAKKMRNKR NSKMYLKTRA GMPFRVYHYQ MKIHVFSYKN
     MGEIEPTFYV TLYGTNADSQ TLPLEIVERI EQNATNTFLV YTEEDLGDLL KIQLTWEGAS
     QSWYNLWKEF RSYLSQPRNP GRELNIRRIR VKSGETQRKL TFCTEDPENT SISPGRELWF
     RKCRDGWRMK NETSPTVELP
//