LOCUS       NP_036730                474 aa            linear   ROD 28-APR-2025
DEFINITION  lipoprotein lipase precursor [Rattus norvegicus].
ACCESSION   NP_036730
VERSION     NP_036730.1
DBSOURCE    REFSEQ: accession NM_012598.2
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 474)
  AUTHORS   Hernandez-Baixauli,J., Chomiciute,G., Alcaide-Hidalgo,J.M.,
            Crescenti,A., Baselga-Escudero,L., Palacios-Jordan,H.,
            Foguet-Romero,E., Pedret,A., Valls,R.M., Sola,R., Mulero,M. and Del
            Bas,J.M.
  TITLE     Developing a model to predict the early risk of
            hypertriglyceridemia based on inhibiting lipoprotein lipase (LPL):
            a translational study
  JOURNAL   Sci Rep 13 (1), 22646 (2023)
   PUBMED   38114521
  REMARK    GeneRIF: Developing a model to predict the early risk of
            hypertriglyceridemia based on inhibiting lipoprotein lipase (LPL):
            a translational study.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 474)
  AUTHORS   Gao,J., Ding,G., Li,Q., Gong,L., Huang,J. and Sang,Y.
  TITLE     Tibet kefir milk decreases fat deposition by regulating the gut
            microbiota and gene expression of Lpl and Angptl4 in high fat
            diet-fed rats
  JOURNAL   Food Res Int 121, 278-287 (2019)
   PUBMED   31108749
  REMARK    GeneRIF: Tibet kefir milk decreases fat deposition by regulating
            the gut microbiota and gene expression of Lpl and Angptl4 in high
            fat diet-fed rats.
REFERENCE   3  (residues 1 to 474)
  AUTHORS   Huo,W., Hou,Y., Li,Y. and Li,H.
  TITLE     Downregulated lncRNA-MIAT confers protection against erectile
            dysfunction by downregulating lipoprotein lipase via activation of
            miR-328a-5p in diabetic rats
  JOURNAL   Biochim Biophys Acta Mol Basis Dis 1865 (6), 1226-1240 (2019)
   PUBMED   30660685
  REMARK    GeneRIF: Data indicate that long noncoding RNA (lncRNA-MIAT)
            suppressed lipoprotein lipase (LPL) by increasing miR-328a-5p,
            thereby inhibiting vascular endothelial cells (VECs) injury to
            attenuate erectile dysfunction (ED) in diabetic rats.
REFERENCE   4  (residues 1 to 474)
  AUTHORS   Birrane,G., Beigneux,A.P., Dwyer,B., Strack-Logue,B.,
            Kristensen,K.K., Francone,O.L., Fong,L.G., Mertens,H.D.T.,
            Pan,C.Q., Ploug,M., Young,S.G. and Meiyappan,M.
  TITLE     Structure of the lipoprotein lipase-GPIHBP1 complex that mediates
            plasma triglyceride hydrolysis
  JOURNAL   Proc Natl Acad Sci U S A 116 (5), 1723-1732 (2019)
   PUBMED   30559189
REFERENCE   5  (residues 1 to 474)
  AUTHORS   Al-Muzafar,H.M. and Amin,K.A.
  TITLE     Thiazolidinedione induces a therapeutic effect on hepatosteatosis
            by regulating stearoyl-CoA desaturase-1, lipase activity, leptin
            and resistin
  JOURNAL   Exp Ther Med 16 (4), 2938-2948 (2018)
   PUBMED   30214514
REFERENCE   6  (residues 1 to 474)
  AUTHORS   Brault,D., Noe,L., Etienne,J., Hamelin,J., Raisonnier,A., Souli,A.,
            Chuat,J.C., Dugail,I., Quignard-Boulange,A., Lavau,M. et al.
  TITLE     Sequence of rat lipoprotein lipase-encoding cDNA
  JOURNAL   Gene 121 (2), 237-246 (1992)
   PUBMED   1339374
REFERENCE   7  (residues 1 to 474)
  AUTHORS   Etienne,J. and Brault,D.
  TITLE     [Lipoprotein lipase deficiencies]
  JOURNAL   Ann Biol Clin (Paris) 50 (5), 299-309 (1992)
   PUBMED   1485686
  REMARK    Review article
REFERENCE   8  (residues 1 to 474)
  AUTHORS   Faustinella,F., Chang,A., Van Biervliet,J.P., Rosseneu,M.,
            Vinaimont,N., Smith,L.C., Chen,S.H. and Chan,L.
  TITLE     Catalytic triad residue mutation (Asp156----Gly) causing familial
            lipoprotein lipase deficiency. Co-inheritance with a nonsense
            mutation (Ser447----Ter) in a Turkish family
  JOURNAL   J Biol Chem 266 (22), 14418-14424 (1991)
   PUBMED   1907278
  REMARK    Erratum:[J Biol Chem 1992 Apr 5;267(10):7194]
REFERENCE   9  (residues 1 to 474)
  AUTHORS   Beg,O.U., Meng,M.S., Skarlatos,S.I., Previato,L., Brunzell,J.D.,
            Brewer,H.B. Jr. and Fojo,S.S.
  TITLE     Lipoprotein lipaseBethesda: a single amino acid substitution
            (Ala-176----Thr) leads to abnormal heparin binding and loss of
            enzymic activity
  JOURNAL   Proc Natl Acad Sci U S A 87 (9), 3474-3478 (1990)
   PUBMED   2110364
REFERENCE   10 (residues 1 to 474)
  AUTHORS   Kinnunen,P.K. and Ehnolm,C.
  TITLE     Effect of serum and C-apoproteins from very low density
            lipoproteins on human postheparin plasma hepatic lipase
  JOURNAL   FEBS Lett 65 (3), 354-357 (1976)
   PUBMED   182536
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC081836.1.
            
            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 :: BC081836.1, L03294.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN11044071, SAMN16676785
                                           [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..474
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16p14"
     Protein         1..474
                     /product="lipoprotein lipase precursor"
                     /EC_number="3.1.1.34"
                     /EC_number="3.1.1.32"
                     /note="phospholipase A1"
                     /calculated_mol_wt=50298
     sig_peptide     1..27
                     /note="/evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (Q06000.1)"
                     /calculated_mol_wt=2802
     mat_peptide     28..474
                     /product="Lipoprotein lipase. /id=PRO_0000017779"
                     /note="propagated from UniProtKB/Swiss-Prot (Q06000.1)"
                     /calculated_mol_wt=50298
     Region          32..53
                     /region_name="Interaction with GPIHBP1.
                     /evidence=ECO:0000250|UniProtKB:P06858"
                     /note="propagated from UniProtKB/Swiss-Prot (Q06000.1)"
     Region          33..472
                     /region_name="lipo_lipase"
                     /note="lipoprotein lipase; TIGR03230"
                     /db_xref="CDD:132274"
     Site            70
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q06000.1)"
     Region          243..266
                     /region_name="Essential for determining substrate
                     specificity. /evidence=ECO:0000250|UniProtKB:P06858"
                     /note="propagated from UniProtKB/Swiss-Prot (Q06000.1)"
     Site            386
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q06000.1)"
     Region          417..421
                     /region_name="Important for interaction with lipoprotein
                     particles. /evidence=ECO:0000250|UniProtKB:P06858"
                     /note="propagated from UniProtKB/Swiss-Prot (Q06000.1)"
     Region          430..434
                     /region_name="Important for heparin binding.
                     /evidence=ECO:0000250|UniProtKB:P06858"
                     /note="propagated from UniProtKB/Swiss-Prot (Q06000.1)"
     Region          443..467
                     /region_name="Interaction with GPIHBP1.
                     /evidence=ECO:0000250|UniProtKB:P06858"
                     /note="propagated from UniProtKB/Swiss-Prot (Q06000.1)"
     CDS             1..474
                     /gene="Lpl"
                     /coded_by="NM_012598.2:190..1614"
                     /db_xref="GeneID:24539"
                     /db_xref="RGD:3017"
ORIGIN      
        1 meskalllva lgvwlqslta frggvaaadg grdfsdiesk falrtpedta edtchlipgl
       61 adsvsnchfn hssktfvvih gwtvtgmyes wvpklvaaly krepdsnviv vdwlyraqqh
      121 ypvsagytkl vgndvarfin wleeefnypl dnvhllgysl gahaagvags ltnkkvnrit
      181 gldpagpnfe yaeapsrlsp ddadfvdvlh tftrgspgrs igiqkpvghv diypnggtfq
      241 pgcnigeair viaekglgdv dqlvkcsher sihlfidsll neenpskayr cnskeafekg
      301 lclscrknrc nnvgyeinkv rakrsskmyl ktrsqmpykv fhyqvkihfs gtendkqnnq
      361 afeislygtv aesenipftl pevatnktys fliytevdig ellmmklkwk ndsyfrwsdw
      421 wsspsfviek irvkagetqk kvifcarekv shlqkgkdaa vfvkchdksl kksg
//
