LIPE_HUMAN
ID LIPE_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 03-AUG-2022, entry version 189.
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 GlyGen; Q9Y5X9; 5 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; Q9Y5X9; -.
DR PeptideAtlas; Q9Y5X9; -.
DR PRIDE; Q9Y5X9; -.
DR ProteomicsDB; 86535; -. [Q9Y5X9-1]
DR ProteomicsDB; 86536; -. [Q9Y5X9-2]
DR Antibodypedia; 1561; 1074 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 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; 534956at2759; -.
DR PhylomeDB; Q9Y5X9; -.
DR TreeFam; TF324997; -.
DR PathwayCommons; Q9Y5X9; -.
DR Reactome; R-HSA-8964058; HDL remodeling.
DR SignaLink; Q9Y5X9; -.
DR BioGRID-ORCS; 9388; 8 hits in 1073 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 122 other tissues.
DR ExpressionAtlas; Q9Y5X9; baseline and differential.
DR Genevisible; Q9Y5X9; HS.
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:0016298; F:lipase activity; IBA:GO_Central.
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:0008283; P:cell population proliferation; IEA:Ensembl.
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:0016042; P:lipid catabolic process; IBA:GO_Central.
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 Gene3D; 3.40.50.1820; -; 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; PTHR11610; 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; SSF49723; SSF49723; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
DR PROSITE; PS00120; LIPASE_SER; 1.
DR PROSITE; PS50095; PLAT; 1.
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
