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LIPL_BOVIN
ID   LIPL_BOVIN              Reviewed;         478 AA.
AC   P11151; Q17R03;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 2.
DT   03-AUG-2022, entry version 173.
DE   RecName: Full=Lipoprotein lipase;
DE            Short=LPL;
DE            EC=3.1.1.34 {ECO:0000269|PubMed:10727238, ECO:0000269|PubMed:16179346, ECO:0000269|PubMed:27929370, ECO:0000269|PubMed:2885834, ECO:0000269|PubMed:9188470};
DE   AltName: Full=Phospholipase A1;
DE            EC=3.1.1.32 {ECO:0000250|UniProtKB:P06858};
DE   Flags: Precursor;
GN   Name=LPL;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Uterus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 29-478, PARTIAL PROTEIN SEQUENCE, CATALYTIC
RP   ACTIVITY, TISSUE SPECIFICITY, AND HEPARIN BINDING.
RX   PubMed=2885834; DOI=10.1073/pnas.84.13.4369;
RA   Senda M., Oka K., Brown W.V., Qasba P.K., Furuichi Y.;
RT   "Molecular cloning and sequence of a cDNA coding for bovine lipoprotein
RT   lipase.";
RL   Proc. Natl. Acad. Sci. U.S.A. 84:4369-4373(1987).
RN   [3]
RP   PROTEIN SEQUENCE OF 29-478, GLYCOSYLATION AT ASN-73 AND ASN-389, DISULFIDE
RP   BONDS, SUBCELLULAR LOCATION, HEPARIN-BINDING, AND TISSUE SPECIFICITY.
RC   TISSUE=Mammary gland;
RX   PubMed=2674142; DOI=10.1016/s0021-9258(19)84780-4;
RA   Yang C.-Y., Gu Z.-W., Yang H.-X., Rohde M.F., Gotto A.M. Jr., Pownall H.J.;
RT   "Structure of bovine milk lipoprotein lipase.";
RL   J. Biol. Chem. 264:16822-16827(1989).
RN   [4]
RP   PROTEIN SEQUENCE OF 29-55.
RX   PubMed=3536511; DOI=10.1111/j.1432-1033.1986.tb10444.x;
RA   Bengtsson-Olivecrona G., Olivecrona T., Joernvall H.;
RT   "Lipoprotein lipases from cow, guinea-pig and man. Structural
RT   characterization and identification of protease-sensitive internal
RT   regions.";
RL   Eur. J. Biochem. 161:281-288(1986).
RN   [5]
RP   HEPARIN BINDING, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=2142941; DOI=10.1016/s0021-9258(19)38242-0;
RA   Saxena U., Klein M.G., Goldberg I.J.;
RT   "Metabolism of endothelial cell-bound lipoprotein lipase. Evidence for
RT   heparan sulfate proteoglycan-mediated internalization and recycling.";
RL   J. Biol. Chem. 265:12880-12886(1990).
RN   [6]
RP   FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, HEPARIN-BINDING, AND
RP   SUBUNIT.
RX   PubMed=9188470; DOI=10.1074/jbc.272.25.15753;
RA   Pillarisetti S., Paka L., Sasaki A., Vanni-Reyes T., Yin B.,
RA   Parthasarathy N., Wagner W.D., Goldberg I.J.;
RT   "Endothelial cell heparanase modulation of lipoprotein lipase activity.
RT   Evidence that heparan sulfate oligosaccharide is an extracellular
RT   chaperone.";
RL   J. Biol. Chem. 272:15753-15759(1997).
RN   [7]
RP   SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=9555944;
RA   Casaroli-Marano R.P., Garcia R., Vilella E., Olivecrona G., Reina M.,
RA   Vilaro S.;
RT   "Binding and intracellular trafficking of lipoprotein lipase and
RT   triacylglycerol-rich lipoproteins by liver cells.";
RL   J. Lipid Res. 39:789-806(1998).
RN   [8]
RP   FUNCTION, INTERACTION WITH APOC2, CATALYTIC ACTIVITY, AND ACTIVITY
RP   REGULATION.
RX   PubMed=10727238; DOI=10.1021/bi992523t;
RA   MacPhee C.E., Hatters D.M., Sawyer W.H., Howlett G.J.;
RT   "Apolipoprotein C-II39-62 activates lipoprotein lipase by direct lipid-
RT   independent binding.";
RL   Biochemistry 39:3433-3440(2000).
RN   [9]
RP   FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, SUBUNIT, CALCIUM
RP   BINDING, ACTIVITY REGULATION, AND TISSUE SPECIFICITY.
RX   PubMed=16179346; DOI=10.1074/jbc.m507252200;
RA   Zhang L., Lookene A., Wu G., Olivecrona G.;
RT   "Calcium triggers folding of lipoprotein lipase into active dimers.";
RL   J. Biol. Chem. 280:42580-42591(2005).
RN   [10]
RP   CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND INTERACTION WITH GPIHBP1.
RX   PubMed=27929370; DOI=10.7554/elife.20958;
RA   Mysling S., Kristensen K.K., Larsson M., Kovrov O., Bensadouen A.,
RA   Joergensen T.J., Olivecrona G., Young S.G., Ploug M.;
RT   "The angiopoietin-like protein ANGPTL4 catalyzes unfolding of the hydrolase
RT   domain in lipoprotein lipase and the endothelial membrane protein GPIHBP1
RT   counteracts this unfolding.";
RL   Elife 5:0-0(2016).
RN   [11]
RP   INTERACTION WITH GPIHBP1, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX   PubMed=29899144; DOI=10.1073/pnas.1806774115;
RA   Kristensen K.K., Midtgaard S.R., Mysling S., Kovrov O., Hansen L.B.,
RA   Skar-Gislinge N., Beigneux A.P., Kragelund B.B., Olivecrona G., Young S.G.,
RA   Joergensen T.J.D., Fong L.G., Ploug M.;
RT   "A disordered acidic domain in GPIHBP1 harboring a sulfated tyrosine
RT   regulates lipoprotein lipase.";
RL   Proc. Natl. Acad. Sci. U.S.A. 115:E6020-E6029(2018).
CC   -!- FUNCTION: Key enzyme in triglyceride metabolism (PubMed:9188470,
CC       PubMed:16179346, PubMed:10727238). Catalyzes the hydrolysis of
CC       triglycerides from circulating chylomicrons and very low density
CC       lipoproteins (VLDL), and thereby plays an important role in lipid
CC       clearance from the blood stream, lipid utilization and storage
CC       (PubMed:9188470, PubMed:16179346, PubMed:10727238). Although it has
CC       both phospholipase and triglyceride lipase activities it is primarily a
CC       triglyceride lipase with low but detectable phospholipase activity (By
CC       similarity). Mediates margination of triglyceride-rich lipoprotein
CC       particles in capillaries (By similarity). Recruited to its site of
CC       action on the luminal surface of vascular endothelium by binding to
CC       GPIHBP1 and cell surface heparan sulfate proteoglycans
CC       (PubMed:9188470). {ECO:0000250|UniProtKB:P06858,
CC       ECO:0000269|PubMed:10727238, ECO:0000269|PubMed:16179346,
CC       ECO:0000269|PubMed:9188470}.
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=3.1.1.34;
CC         Evidence={ECO:0000269|PubMed:10727238, ECO:0000269|PubMed:16179346,
CC         ECO:0000269|PubMed:27929370, ECO:0000269|PubMed:2885834,
CC         ECO:0000269|PubMed:9188470};
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:0000250|UniProtKB:P06858};
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:0000250|UniProtKB:P06858};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38576;
CC         Evidence={ECO:0000250|UniProtKB:P06858};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + H2O =
CC         (9Z)-octadecenoate + (9Z-octadecenoyl)-sn-glycero-3-phosphocholine +
CC         H(+); Xref=Rhea:RHEA:38699, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30823, ChEBI:CHEBI:74669, ChEBI:CHEBI:76083;
CC         Evidence={ECO:0000250|UniProtKB:P06858};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38700;
CC         Evidence={ECO:0000250|UniProtKB:P06858};
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:0000250|UniProtKB:P06858};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40476;
CC         Evidence={ECO:0000250|UniProtKB:P06858};
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:0000250|UniProtKB:P06858};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41385;
CC         Evidence={ECO:0000250|UniProtKB:P06858};
CC   -!- ACTIVITY REGULATION: The apolipoprotein APOC2 acts as a coactivator of
CC       LPL activity (PubMed:10727238). Ca(2+) binding promotes protein
CC       stability and formation of the active homodimer (PubMed:16179346).
CC       Interaction with GPIHBP1 protects LPL against inactivation by ANGPTL4
CC       (PubMed:27929370). {ECO:0000269|PubMed:10727238,
CC       ECO:0000269|PubMed:16179346, ECO:0000269|PubMed:27929370}.
CC   -!- SUBUNIT: Homodimer (PubMed:16179346). Interacts with GPIHBP1 with 1:1
CC       stoichiometry (PubMed:27929370, PubMed:29899144). Interacts with APOC2;
CC       the interaction activates LPL activity in the presence of lipids
CC       (PubMed:10727238). Interaction with heparan sulfate proteoglycans is
CC       required to protect LPL against loss of activity (PubMed:9188470).
CC       Associates with lipoprotein particles in blood plasma. Interacts with
CC       LMF1 and SEL1L; interaction with SEL1L is required to prevent
CC       aggregation of newly synthesized LPL in the endoplasmic reticulum (ER),
CC       and for normal export of LPL from the ER to the extracellular space (By
CC       similarity). Interacts with SORL1; SORL1 acts as a sorting receptor,
CC       promoting LPL localization to endosomes and later to lysosomes, leading
CC       to degradation of newly synthesized LPL (By similarity).
CC       {ECO:0000250|UniProtKB:P06858, ECO:0000269|PubMed:10727238,
CC       ECO:0000269|PubMed:16179346, ECO:0000269|PubMed:27929370,
CC       ECO:0000269|PubMed:29899144, ECO:0000269|PubMed:9188470}.
CC   -!- INTERACTION:
CC       P11151; Q99523: SORT1; Xeno; NbExp=6; IntAct=EBI-8794090, EBI-1057058;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:2142941};
CC       Peripheral membrane protein {ECO:0000269|PubMed:2142941}; Extracellular
CC       side {ECO:0000269|PubMed:2142941}. Secreted
CC       {ECO:0000269|PubMed:16179346, ECO:0000269|PubMed:2142941,
CC       ECO:0000269|PubMed:2674142, ECO:0000269|PubMed:2885834,
CC       ECO:0000269|PubMed:29899144, ECO:0000269|PubMed:9188470,
CC       ECO:0000269|PubMed:9555944}. Secreted, extracellular space,
CC       extracellular matrix {ECO:0000269|PubMed:9188470}. Note=Newly
CC       synthesized LPL binds to cell surface heparan proteoglycans and is then
CC       released by heparanase. Subsequently, it becomes attached to heparan
CC       proteoglycan on endothelial cells (PubMed:9188470). Locates to the
CC       plasma membrane of microvilli of hepatocytes with triglyceride-rich
CC       lipoproteins (TRL). Some of the bound LPL is then internalized and
CC       located inside non-coated endocytic vesicles (PubMed:9555944).
CC       {ECO:0000269|PubMed:9188470, ECO:0000269|PubMed:9555944}.
CC   -!- TISSUE SPECIFICITY: Detected in milk (at protein level).
CC       {ECO:0000269|PubMed:16179346, ECO:0000269|PubMed:2142941,
CC       ECO:0000269|PubMed:2674142, ECO:0000269|PubMed:2885834,
CC       ECO:0000269|PubMed:29899144, ECO:0000269|PubMed:9555944}.
CC   -!- PTM: Tyrosine nitration after lipopolysaccharide (LPS) challenge down-
CC       regulates the lipase activity. {ECO:0000250|UniProtKB:Q06000}.
CC   -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC       {ECO:0000305}.
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DR   EMBL; BC118091; AAI18092.1; -; mRNA.
DR   EMBL; M16966; AAA30624.1; -; mRNA.
DR   PIR; A27053; A27053.
DR   RefSeq; NP_001068588.1; NM_001075120.1.
DR   PDB; 6U7M; EM; 3.80 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/a/b/c/d/e/f/g/h/i=1-478.
DR   PDBsum; 6U7M; -.
DR   AlphaFoldDB; P11151; -.
DR   SMR; P11151; -.
DR   BioGRID; 158237; 1.
DR   DIP; DIP-61310N; -.
DR   IntAct; P11151; 4.
DR   STRING; 9913.ENSBTAP00000017086; -.
DR   BindingDB; P11151; -.
DR   ChEMBL; CHEMBL3064; -.
DR   ESTHER; bovin-lipli; Lipoprotein_Lipase.
DR   iPTMnet; P11151; -.
DR   PaxDb; P11151; -.
DR   PeptideAtlas; P11151; -.
DR   PRIDE; P11151; -.
DR   ABCD; P11151; 1 sequenced antibody.
DR   Ensembl; ENSBTAT00000017086; ENSBTAP00000017086; ENSBTAG00000012855.
DR   GeneID; 280843; -.
DR   KEGG; bta:280843; -.
DR   CTD; 4023; -.
DR   VEuPathDB; HostDB:ENSBTAG00000012855; -.
DR   VGNC; VGNC:30969; LPL.
DR   eggNOG; ENOG502QQ7P; Eukaryota.
DR   GeneTree; ENSGT00940000157178; -.
DR   HOGENOM; CLU_027171_1_0_1; -.
DR   InParanoid; P11151; -.
DR   OMA; TIWITLG; -.
DR   OrthoDB; 534956at2759; -.
DR   TreeFam; TF324997; -.
DR   BRENDA; 3.1.1.34; 908.
DR   Reactome; R-BTA-8963889; Assembly of active LPL and LIPC lipase complexes.
DR   PRO; PR:P11151; -.
DR   Proteomes; UP000009136; Chromosome 8.
DR   Bgee; ENSBTAG00000012855; Expressed in omental fat pad and 105 other tissues.
DR   GO; GO:1902494; C:catalytic complex; IEA:Ensembl.
DR   GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR   GO; GO:0042627; C:chylomicron; IEA:UniProtKB-KW.
DR   GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0034361; C:very-low-density lipoprotein particle; IEA:UniProtKB-KW.
DR   GO; GO:0052740; F:1-acyl-2-lysophosphatidylserine acylhydrolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0034185; F:apolipoprotein binding; IPI:BHF-UCL.
DR   GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR   GO; GO:0043395; F:heparan sulfate proteoglycan binding; IDA:UniProtKB.
DR   GO; GO:0008201; F:heparin binding; ISS:UniProtKB.
DR   GO; GO:0016298; F:lipase activity; IBA:GO_Central.
DR   GO; GO:0004465; F:lipoprotein lipase activity; IDA:UniProtKB.
DR   GO; GO:0071813; F:lipoprotein particle binding; ISS:UniProtKB.
DR   GO; GO:0052739; F:phosphatidylserine 1-acylhydrolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008970; F:phospholipase A1 activity; ISS:UniProtKB.
DR   GO; GO:0004620; F:phospholipase activity; IDA:BHF-UCL.
DR   GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR   GO; GO:0005102; F:signaling receptor binding; IEA:Ensembl.
DR   GO; GO:0004806; F:triglyceride lipase activity; IDA:BHF-UCL.
DR   GO; GO:0071398; P:cellular response to fatty acid; IEA:Ensembl.
DR   GO; GO:0031670; P:cellular response to nutrient; IEA:Ensembl.
DR   GO; GO:0042632; P:cholesterol homeostasis; IEA:Ensembl.
DR   GO; GO:0034371; P:chylomicron remodeling; ISS:UniProtKB.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IDA:BHF-UCL.
DR   GO; GO:0016042; P:lipid catabolic process; IBA:GO_Central.
DR   GO; GO:0055096; P:low-density lipoprotein particle mediated signaling; IEA:Ensembl.
DR   GO; GO:0006644; P:phospholipid metabolic process; IDA:BHF-UCL.
DR   GO; GO:2000343; P:positive regulation of chemokine (C-X-C motif) ligand 2 production; IEA:Ensembl.
DR   GO; GO:0010886; P:positive regulation of cholesterol storage; IEA:Ensembl.
DR   GO; GO:0045600; P:positive regulation of fat cell differentiation; IEA:Ensembl.
DR   GO; GO:0050729; P:positive regulation of inflammatory response; IEA:Ensembl.
DR   GO; GO:0032731; P:positive regulation of interleukin-1 beta production; IEA:Ensembl.
DR   GO; GO:0032755; P:positive regulation of interleukin-6 production; IEA:Ensembl.
DR   GO; GO:0010744; P:positive regulation of macrophage derived foam cell differentiation; IEA:Ensembl.
DR   GO; GO:0010890; P:positive regulation of sequestering of triglyceride; IEA:Ensembl.
DR   GO; GO:0032760; P:positive regulation of tumor necrosis factor production; IEA:Ensembl.
DR   GO; GO:0009617; P:response to bacterium; IEA:Ensembl.
DR   GO; GO:0009749; P:response to glucose; IDA:AgBase.
DR   GO; GO:0019433; P:triglyceride catabolic process; IDA:UniProtKB.
DR   GO; GO:0070328; P:triglyceride homeostasis; IEA:Ensembl.
DR   GO; GO:0006641; P:triglyceride metabolic process; IDA:BHF-UCL.
DR   GO; GO:0034372; P:very-low-density lipoprotein particle remodeling; IDA:BHF-UCL.
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   PANTHER; PTHR11610:SF3; PTHR11610:SF3; 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   TIGRFAMs; TIGR03230; lipo_lipase; 1.
DR   PROSITE; PS00120; LIPASE_SER; 1.
DR   PROSITE; PS50095; PLAT; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Calcium; Cell membrane; Chylomicron;
KW   Direct protein sequencing; Disulfide bond; Extracellular matrix;
KW   Glycoprotein; Heparin-binding; Hydrolase; Lipid degradation;
KW   Lipid metabolism; Membrane; Metal-binding; Nitration; Reference proteome;
KW   Secreted; Signal; VLDL.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000269|PubMed:2674142,
FT                   ECO:0000269|PubMed:2885834, ECO:0000269|PubMed:3536511"
FT   CHAIN           29..478
FT                   /note="Lipoprotein lipase"
FT                   /id="PRO_0000017772"
FT   DOMAIN          344..467
FT                   /note="PLAT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00152"
FT   REGION          35..56
FT                   /note="Interaction with GPIHBP1"
FT                   /evidence="ECO:0000250|UniProtKB:P06858"
FT   REGION          246..269
FT                   /note="Essential for determining substrate specificity"
FT                   /evidence="ECO:0000250|UniProtKB:P06858"
FT   REGION          420..424
FT                   /note="Important for interaction with lipoprotein
FT                   particles"
FT                   /evidence="ECO:0000250|UniProtKB:P06858"
FT   REGION          433..437
FT                   /note="Important for heparin binding"
FT                   /evidence="ECO:0000250|UniProtKB:P06858"
FT   REGION          446..470
FT                   /note="Interaction with GPIHBP1"
FT                   /evidence="ECO:0000250|UniProtKB:P06858"
FT   ACT_SITE        162
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:P06858"
FT   ACT_SITE        186
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10037"
FT   ACT_SITE        271
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10037"
FT   BINDING         197
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P06858"
FT   BINDING         200
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P06858"
FT   BINDING         202
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P06858"
FT   BINDING         205
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P06858"
FT   MOD_RES         124
FT                   /note="3'-nitrotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q06000"
FT   MOD_RES         194
FT                   /note="3'-nitrotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q06000"
FT   MOD_RES         346
FT                   /note="3'-nitrotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q06000"
FT   CARBOHYD        73
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:2674142"
FT   CARBOHYD        287
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        389
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:2674142"
FT   DISULFID        57..70
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00152,
FT                   ECO:0000269|PubMed:2674142"
FT   DISULFID        246..269
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00152,
FT                   ECO:0000269|PubMed:2674142"
FT   DISULFID        294..313
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00152,
FT                   ECO:0000269|PubMed:2674142"
FT   DISULFID        305..308
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00152,
FT                   ECO:0000269|PubMed:2674142"
FT   DISULFID        448..468
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00152,
FT                   ECO:0000269|PubMed:2674142"
SQ   SEQUENCE   478 AA;  53378 MW;  06FDD429DD194A1F CRC64;
     MESKALLLLA LSVCLQSLTV SRGGLVAADR ITGGKDFRDI ESKFALRTPE DTAEDTCHLI
     PGVTESVANC HFNHSSKTFV VIHGWTVTGM YESWVPKLVA ALYKREPDSN VIVVDWLSRA
     QQHYPVSAGY TKLVGQDVAK FMNWMADEFN YPLGNVHLLG YSLGAHAAGI AGSLTNKKVN
     RITGLDPAGP NFEYAEAPSR LSPDDADFVD VLHTFTRGSP GRSIGIQKPV GHVDIYPNGG
     TFQPGCNIGE ALRVIAERGL GDVDQLVKCS HERSVHLFID SLLNEENPSK AYRCNSKEAF
     EKGLCLSCRK NRCNNMGYEI NKVRAKRSSK MYLKTRSQMP YKVFHYQVKI HFSGTESNTY
     TNQAFEISLY GTVAESENIP FTLPEVSTNK TYSFLLYTEV DIGELLMLKL KWISDSYFSW
     SNWWSSPGFD IGKIRVKAGE TQKKVIFCSR EKMSYLQKGK SPVIFVKCHD KSLNRKSG
 
 
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