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 27-MAR-2024, entry version 182. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 PDB; 8ERL; EM; 3.90 A; A/B=1-478. DR PDBsum; 6U7M; -. DR PDBsum; 8ERL; -. DR AlphaFoldDB; P11151; -. DR EMDB; EMD-20673; -. DR EMDB; EMD-28554; -. 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 GlyCosmos; P11151; 3 sites, No reported glycans. DR iPTMnet; P11151; -. DR PaxDb; 9913-ENSBTAP00000017086; -. DR PeptideAtlas; P11151; -. DR ABCD; P11151; 1 sequenced antibody. DR Ensembl; ENSBTAT00000017086.6; ENSBTAP00000017086.5; ENSBTAG00000012855.6. 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; IRAQQHY; -. DR OrthoDB; 3428256at2759; -. DR TreeFam; TF324997; -. DR BRENDA; 3.1.1.34; 908. DR Reactome; R-BTA-8963889; Assembly of active LPL and LIPC lipase complexes. DR Reactome; R-BTA-8963901; Chylomicron remodeling. DR Reactome; R-BTA-975634; Retinoid metabolism and transport. DR PRO; PR:P11151; -. DR Proteomes; UP000009136; Chromosome 8. DR Bgee; ENSBTAG00000012855; Expressed in omental fat pad and 105 other cell types or 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: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:0055096; P:low-density lipoprotein particle mediated signaling; IEA:Ensembl. DR GO; GO:0006644; P:phospholipid metabolic process; IDA:BHF-UCL. DR GO; GO:1904179; P:positive regulation of adipose tissue development; IEA:Ensembl. 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 CDD; cd01758; PLAT_LPL; 1. DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1. DR Gene3D; 2.60.60.20; PLAT/LH2 domain; 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 NCBIfam; TIGR03230; lipo_lipase; 1. DR PANTHER; PTHR11610; LIPASE; 1. DR PANTHER; PTHR11610:SF3; LIPOPROTEIN LIPASE; 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; SSF53474; alpha/beta-Hydrolases; 1. DR SUPFAM; SSF49723; Lipase/lipooxygenase domain (PLAT/LH2 domain); 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 //