Primary Information |
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| BoMiProt ID | Bomi302 |
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| Protein Name | Lipoprotein lipase |
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| Organism | Bos taurus |
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| Uniprot ID | P11151 |
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| Milk Fraction | Whey, MFGM, Exosome |
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| Ref Sequence ID | NP_001068588.1 |
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| Aminoacid Length | 478 |
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| Molecular Weight | 53378 |
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| FASTA Sequence |
Download |
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| Gene Name | LPL |
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| Gene ID | 280843 |
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| Protein Existence Status | Reviewed: Experimental evidence at protein level |
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Secondary Information |
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| Protein Function | lipase is highly specific for the primary esters of acylglycerols and exhibits a slight stereospecificity for the sn-1 ester in preference to the sn-3-ester; LPL activity has been detected histochemically in the capillaries of lactating rat mammary tissue associated with chylomicrons attached to the luminal surface of the endothelium; transfer of chylomicron TG fatty acids into rat mammary alveolar cells. Lipoprotein lipase (LPL) is a glycoprotein enzyme that is produced in several cells and tissues. LPL belongs to a large lipase gene family that includes, among others, hepatic lipase and pancreatic lipase.It plays a pivotal role both in energy and in lipoprotein metabolism. |
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| Biochemical Properties | inhibited by protamine sulfate, 1.0 M
sodium chloride, apolipoprotein C-I (apolipoprotein-
serine), and apolipoprotein
C-Ill (apolipoprotein-alanine); activated by apolipoprotein C-II
(apolipoprotein-glutamic acid), serum,
and by heparin to which it also binds; milk lipoprotein lipase is bound to an endogenous
heparin-like glycosaminoglycan; The LPL in both cow's and human's milk is
most active at pH 8 to 9 |
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| Significance in milk | associated with milk
microsomes;assist in the transfer of
blood lipoprotein triacylglycerol fatty
acids into milk triacylglycerols; skim milk is one of the richest sources of
lipoprotein lipase; Human milk
contains a serum stimulated lipoprotein
lipase with many of the characteristics of
the enzyme in bovine milk, as well as an
enzyme stimulated by bile salts which
resembles the sterol ester hydrolase of rat
pancreatic juice |
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| PTMs | Glycosylated: As found in bovine milk - 10 cysteine
residues which are in disulfide bridges. Disulfide bonds are
formed between Cys29 and Cys42, CYS 218 and Cys241,C266 and
Cys285, C,YS277and Cys280",a nd Cys420 and CYS 440; residues Asn44 and 361
and were identified as potential N-glycosylation
sites in bLPL |
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Site(s) of PTM(s)
N-glycosylation,
O-glycosylation,
Phosphorylation
| >sp|P11151|LIPL_BOVIN Lipoprotein lipase OS=Bos taurus OX=9913 GN=LPL PE=1 SV=2
MESKALLLLALSVCLQSLTVSRGGLVAADRITGGKDFRDIESKFALRTPE
DTAEDTCHLIPGVTESVANCHFN*73HSSKTFVVIHGWTVTGMYESWVPKLVA
ALYKREPDSNVIVVDWLSRAQQHYPVSAGYTKLVGQDVAKFMNWMADEFN
YPLGNVHLLGYSLGAHAAGIAGSLTNKKVNRITGLDPAGPNFEYAEAPSR
LSPDDADFVDVLHTFTRGSPGRSIGIQKPVGHVDIYPNGGTFQPGCNIGE
ALRVIAERGLGDVDQLVKCSHERSVHLFIDSLLNEENPSKAYRCNSKEAF
EKGLCLSCRKNRCNNMGYEINKVRAKRSSKMYLKTRSQMPYKVFHYQVKI
HFSGTESNTYTNQAFEISLYGTVAESENIPFTLPEVSTN*389KTYSFLLYTEV
DIGELLMLKLKWISDSYFSWSNWWSSPGFDIGKIRVKAGETQKKVIFCSR
EKMSYLQKGKSPVIFVKCHDKSLNRKSG
|
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| Predicted Disorder Regions | NA |
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| DisProt Annotation | |
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| TM Helix Prediction | No TM helices |
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| Significance of PTMs | disulfide links
restrict the number of conformations available to the protein; glycosylated regions are regions of low hydrophobicity
and are probably located on the surface of the enzyme |
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| Bibliography | 1. Yang, C. Y. et al. (1989) ‘Structure of bovine milk lipoprotein lipase.’, The Journal of biological chemistry, 264(28), pp. 16822–7. Available at: http://www.ncbi.nlm.nih.gov/pubmed/2674142 (Accessed: 4 October 2019).
2. Morton, R. K. (1954) ‘The lipoprotein particles in cow’s milk’, Biochemical Journal, 57(2), pp. 231–237. doi: 10.1042/bj0570231. |
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