LOCUS       NP_034850                500 aa            linear   ROD 28-APR-2025
DEFINITION  endothelial lipase precursor [Mus musculus].
ACCESSION   NP_034850
VERSION     NP_034850.3
DBSOURCE    REFSEQ: accession NM_010720.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 500)
  AUTHORS   Shirasaki,T., Murai,K., Ishida,A., Kuroki,K., Kawaguchi,K.,
            Wang,Y., Yamanaka,S., Yasukawa,R., Kawasaki,N., Li,Y.Y.,
            Shimakami,T., Sumiyadorj,A., Nio,K., Sugimoto,S., Orita,N.,
            Takayama,H., Okada,H., Thi Bich,P.D., Iwabuchi,S., Hashimoto,S.,
            Ide,M., Tabata,N., Ito,S., Matsushima,K., Yanagawa,H.,
            Yamashita,T., Kaneko,S. and Honda,M.
  TITLE     Functional involvement of endothelial lipase in hepatitis B virus
            infection
  JOURNAL   Hepatol Commun 7 (9), e0206 (2023)
   PUBMED   37655967
  REMARK    GeneRIF: Functional involvement of endothelial lipase in hepatitis
            B virus infection.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 500)
  AUTHORS   Sugasini,D., Yang,P., Ng,D., Khetarpal,S.A., Vitali,C., Rader,D.J.
            and Subbaiah,P.V.
  TITLE     Potential role of hepatic lipase in the accretion of
            docosahexaenoic acid (DHA) by the brain
  JOURNAL   Biochim Biophys Acta Mol Cell Biol Lipids 1866 (10), 159002 (2021)
   PUBMED   34197964
  REMARK    GeneRIF: Potential role of hepatic lipase in the accretion of
            docosahexaenoic acid (DHA) by the brain.
REFERENCE   3  (residues 1 to 500)
  AUTHORS   Khetarpal,S.A., Vitali,C., Levin,M.G., Klarin,D., Park,J.,
            Pampana,A., Millar,J.S., Kuwano,T., Sugasini,D., Subbaiah,P.V.,
            Billheimer,J.T., Natarajan,P. and Rader,D.J.
  TITLE     Endothelial lipase mediates efficient lipolysis of
            triglyceride-rich lipoproteins
  JOURNAL   PLoS Genet 17 (9), e1009802 (2021)
   PUBMED   34543263
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 500)
  AUTHORS   Bedogni,F. and Hevner,R.F.
  TITLE     Cell-Type-Specific Gene Expression in Developing Mouse Neocortex:
            Intermediate Progenitors Implicated in Axon Development
  JOURNAL   Front Mol Neurosci 14, 686034 (2021)
   PUBMED   34321999
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 500)
  AUTHORS   Burke,T.P., Engstrom,P., Chavez,R.A., Fonbuena,J.A., Vance,R.E. and
            Welch,M.D.
  TITLE     Inflammasome-mediated antagonism of type I interferon enhances
            Rickettsia pathogenesis
  JOURNAL   Nat Microbiol 5 (5), 688-696 (2020)
   PUBMED   32123346
REFERENCE   6  (residues 1 to 500)
  AUTHORS   Jin,W., Millar,J.S., Broedl,U., Glick,J.M. and Rader,D.J.
  TITLE     Inhibition of endothelial lipase causes increased HDL cholesterol
            levels in vivo
  JOURNAL   J Clin Invest 111 (3), 357-362 (2003)
   PUBMED   12569161
  REMARK    GeneRIF: endothelial lipase has a role in regulating HDL
            cholesterol levels
REFERENCE   7  (residues 1 to 500)
  AUTHORS   Ishida,T., Choi,S., Kundu,R.K., Hirata,K., Rubin,E.M., Cooper,A.D.
            and Quertermous,T.
  TITLE     Endothelial lipase is a major determinant of HDL level
  JOURNAL   J Clin Invest 111 (3), 347-355 (2003)
   PUBMED   12569160
  REMARK    GeneRIF: endothelial lipase has a role in regulating HDL levels
REFERENCE   8  (residues 1 to 500)
  AUTHORS   Cohen,J.C.
  TITLE     Endothelial lipase: direct evidence for a role in HDL metabolism
  JOURNAL   J Clin Invest 111 (3), 318-321 (2003)
   PUBMED   12569156
  REMARK    GeneRIF: Endothelial lipase has a role in HDL metabolism [review]
            Review article
REFERENCE   9  (residues 1 to 500)
  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   10 (residues 1 to 500)
  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
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK152872.1, AK152430.1, AK152161.1, AK014047.1 and AK150054.1.
            
            On May 15, 2008 this sequence version replaced NP_034850.2.
            
            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 :: AK172101.1, AK090224.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849381 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..500
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="18"
                     /map="18 50.94 cM"
     Protein         1..500
                     /product="endothelial lipase precursor"
                     /EC_number="3.1.1.3"
                     /EC_number="3.1.1.32"
                     /note="lipose, endothelial; EDL; endothelial cell-derived
                     lipase; endothelial lipase; phospholipase A1"
                     /calculated_mol_wt=54275
     sig_peptide     1..20
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9WVG5.3)"
                     /calculated_mol_wt=2372
     mat_peptide     21..500
                     /product="Endothelial lipase. /id=PRO_0000017798"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9WVG5.3)"
                     /calculated_mol_wt=54275
     Region          51..485
                     /region_name="lipo_lipase"
                     /note="lipoprotein lipase; TIGR03230"
                     /db_xref="CDD:132274"
     Site            65
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9WVG5.3)"
     Site            80
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9WVG5.3)"
     Site            136
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9WVG5.3)"
     Site            359
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9WVG5.3)"
     Site            393
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9WVG5.3)"
     Site            491
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9WVG5.3)"
     CDS             1..500
                     /gene="Lipg"
                     /gene_synonym="3110013K01Rik; EL; lipase; mEDL"
                     /coded_by="NM_010720.3:290..1792"
                     /db_xref="CCDS:CCDS29343.1"
                     /db_xref="GeneID:16891"
                     /db_xref="MGI:MGI:1341803"
ORIGIN      
        1 mrntvfllgf wsvycyfpag sittlrpqgs lrdehhkptg vpatarpsva fnirtskdpe
       61 qegcnlslgd skllencgfn mtaktffiih gwtmsgmfes wlhklvsalq mrekdanvvv
      121 vdwlplahql ytdavnntrv vgqrvagmld wlqekeefsl gnvhligysl gahvagyagn
      181 fvkgtvgrit gldpagpmfe gvdinrrlsp ddadfvdvlh tytlsfglsi girmpvghid
      241 iypnggdfqp gcgfndvigs faygtisemv kceheravhl fvdslvnqdk psfafqctds
      301 srfkrgicls crknrcnnig ynakkmrkkr nskmylktra gmpfkvyhyq lkvhmfsynn
      361 sgdtqptlyi tlygsnadsq nlpleiveki elnatntflv yteedlgdll kmrltwegva
      421 hswynlwnef rnylsqpsnp srelyirrir vksgetqrkv tfctqdptks sispgqelwf
      481 hkcqdgwkmk nktspfvnla
//
