LOCUS       NP_001012759             493 aa            linear   ROD 30-APR-2025
DEFINITION  endothelial lipase precursor [Rattus norvegicus].
ACCESSION   NP_001012759 XP_225720
VERSION     NP_001012759.1
DBSOURCE    REFSEQ: accession NM_001012741.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 493)
  AUTHORS   Essalmani,R., Susan-Resiga,D., Chamberland,A., Asselin,M.C.,
            Canuel,M., Constam,D., Creemers,J.W., Day,R., Gauthier,D., Prat,A.
            and Seidah,N.G.
  TITLE     Furin is the primary in vivo convertase of angiopoietin-like 3 and
            endothelial lipase in hepatocytes
  JOURNAL   J Biol Chem 288 (37), 26410-26418 (2013)
   PUBMED   23918928
REFERENCE   2  (residues 1 to 493)
  AUTHORS   Wu,X., Huang,H., Tang,F., Le,K., Xu,S. and Liu,P.
  TITLE     Regulated expression of endothelial lipase in atherosclerosis
  JOURNAL   Mol Cell Endocrinol 315 (1-2), 233-238 (2010)
   PUBMED   19931348
  REMARK    GeneRIF: Data show that endothelial lipase (EL) was upregulated in
            rat atherosclerosis and taht lipopolysaccharide stimulates EL
            expression in vitro through NFkappaB activation.
REFERENCE   3  (residues 1 to 493)
  AUTHORS   Griffon,N., Jin,W., Petty,T.J., Millar,J., Badellino,K.O.,
            Saven,J.G., Marchadier,D.H., Kempner,E.S., Billheimer,J.,
            Glick,J.M. and Rader,D.J.
  TITLE     Identification of the active form of endothelial lipase, a
            homodimer in a head-to-tail conformation
  JOURNAL   J Biol Chem 284 (35), 23322-23330 (2009)
   PUBMED   19567873
REFERENCE   4  (residues 1 to 493)
  AUTHORS   Nijstad,N., Wiersma,H., Gautier,T., van der Giet,M., Maugeais,C.
            and Tietge,U.J.
  TITLE     Scavenger receptor BI-mediated selective uptake is required for the
            remodeling of high density lipoprotein by endothelial lipase
  JOURNAL   J Biol Chem 284 (10), 6093-6100 (2009)
   PUBMED   19136670
REFERENCE   5  (residues 1 to 493)
  AUTHORS   Jin,W., Wang,X., Millar,J.S., Quertermous,T., Rothblat,G.H.,
            Glick,J.M. and Rader,D.J.
  TITLE     Hepatic proprotein convertases modulate HDL metabolism
  JOURNAL   Cell Metab 6 (2), 129-136 (2007)
   PUBMED   17681148
REFERENCE   6  (residues 1 to 493)
  AUTHORS   Bonne,A.C., Den Bieman,M.G., Van Lith,H.A. and Van Zutphen,B.F.
  TITLE     Sequencing and chromosomal assignment of the rat
            endothelial-derived lipase gene (Lipg)
  JOURNAL   DNA Seq 12 (4), 285-287 (2001)
   PUBMED   11924532
REFERENCE   7  (residues 1 to 493)
  AUTHORS   Stevenson,F.T., Shearer,G.C. and Atkinson,D.N.
  TITLE     Lipoprotein-stimulated mesangial cell proliferation and gene
            expression are regulated by lipoprotein lipase
  JOURNAL   Kidney Int 59 (6), 2062-2068 (2001)
   PUBMED   11380807
REFERENCE   8  (residues 1 to 493)
  AUTHORS   Hirata,K., Dichek,H.L., Cioffi,J.A., Choi,S.Y., Leeper,N.J.,
            Quintana,L., Kronmal,G.S., Cooper,A.D. and Quertermous,T.
  TITLE     Cloning of a unique lipase from endothelial cells extends the
            lipase gene family
  JOURNAL   J Biol Chem 274 (20), 14170-14175 (1999)
   PUBMED   10318835
REFERENCE   9  (residues 1 to 493)
  AUTHORS   Jaye,M., Lynch,K.J., Krawiec,J., Marchadier,D., Maugeais,C.,
            Doan,K., South,V., Amin,D., Perrone,M. and Rader,D.J.
  TITLE     A novel endothelial-derived lipase that modulates HDL metabolism
  JOURNAL   Nat Genet 21 (4), 424-428 (1999)
   PUBMED   10192396
REFERENCE   10 (residues 1 to 493)
  AUTHORS   Peinado-Onsurbe,J., Soler,C., Galan,X., Poveda,B., Soley,M.,
            Llobera,M. and Ramirez,I.
  TITLE     Involvement of catecholamines in the effect of fasting on hepatic
            endothelial lipase activity in the rat
  JOURNAL   Endocrinology 129 (5), 2599-2606 (1991)
   PUBMED   1935790
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000018.1.
            
            On Apr 20, 2005 this sequence version replaced XP_225720.3.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY916123.1, SRR26643297.50654.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN16676785 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..493
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18q12.2"
     Protein         1..493
                     /product="endothelial lipase precursor"
                     /EC_number="3.1.1.3"
                     /EC_number="3.1.1.32"
                     /note="endothelial lipase; endothelial-derived lipase;
                     EDL; lipase, endothelial; phospholipase A1"
                     /calculated_mol_wt=53318
     sig_peptide     1..23
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8VBX1.2)"
                     /calculated_mol_wt=2624
     mat_peptide     24..493
                     /product="Endothelial lipase. /id=PRO_0000043409"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8VBX1.2)"
                     /calculated_mol_wt=53318
     Region          53..488
                     /region_name="lipo_lipase"
                     /note="lipoprotein lipase; TIGR03230"
                     /db_xref="CDD:132274"
     Site            67
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8VBX1.2)"
     Site            82
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8VBX1.2)"
     Site            395
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8VBX1.2)"
     CDS             1..493
                     /gene="Lipg"
                     /gene_synonym="lipase"
                     /coded_by="NM_001012741.2:277..1758"
                     /db_xref="GeneID:291437"
                     /db_xref="RGD:1310740"
ORIGIN      
        1 mrdpvfllgf wslyccfpag slttlrpqgs lrdehhkptg vpvtittkps vtfnirtskd
       61 pehegcnlsl gdskllencg fnmtaktffi ihgwtmsgmf eswlhklvsa lqtrekeanv
      121 vvvdwlplah qlyidavsnt rvvgrrvagm lnwlqekgef slgdvhligy slgahvagya
      181 gnfvkgtvgr itgldpagpm fegvdinrrl spddadfvdv lhtytlsfgl sigirmpvgh
      241 idiypnggdf qpgcgfndvm gsfaygtise mvkceherav hlfvdslvnq dkpsfafqct
      301 dpnrfkrgic lscrknrcnn igynakkmrk krnskmylkt ragmpfrvyh yqlkvhmfsy
      361 knsgdiqpdl yitlygsnad sqnlpleive kielnatntf lvyteeylgd lfkirltweg
      421 vssswynlwn efrsylsqps spsrelhirr irvksgetqr kvafcvqdpm knsispgqel
      481 wfykcqndcr vkn
//
