Search by BoMiProt ID - Bomi302


Primary Information

BoMiProt ID Bomi302
Protein Name Lipoprotein lipase
Organism Bos taurus
Uniprot IdP11151
Milk FractionWhey, MFGM, Exosome
Ref Sequence Id NP_001068588.1
Amino Acid Lenth 478
Molecular Weight 53378
Fasta Sequence https://www.uniprot.org/uniprot/P11151.fasta
Gene Name LPL
Gene Id 280843
Protein Existence Status Reviewed: Experimental evidence at protein level

Secondry Information

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
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
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
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
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
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
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.