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
