lpl

Lysophospholipase

653 amino acids

Catalyzes the release of fatty acids from lysophospholipids.

Belongs to the lysophospholipase family.

70.111 kDa

MHLPSSLLIAAPLLANVSAEPIRIPQRDVSVVSTSQQLAVRALPDSPSGGYAPAVVDCPKTKPTLRKAVDLSNEEKNWLSIRRKNTIQPMRDLLKRANITGFDSETFMNEAANNISQLPNVAIAISGGGYRALMNGAGFVAAADNRIQNTTGAGGIGGLLQSSTYLAGLSGGGWLVGSLFSNNFSSIETLLSENKVWDFENSIFKGPKEAGLSTVNRIQYWSEVAKEVAKKKDAGFETSITDYWGRALSYQLIGADMGGPAYTFSSIAQTDNFQKAETPFPILVADGRAPGDTIISLNATNYEFNPFETGSWDPTVYGFAPTKYLGANFSNGVIPSGGKCVEGLDQAGFVMGTSSTLFNQFLLANISSYDGVPDVLIEAVTSVLKEIGAKRDDVSQIIPNPFLDWNNRTNPNADTLELDLVDGGEDLQNIPLNPLTQPVRAVDVIFAVDSSADVTNWPNGTALRATYERTFGSISNGTLFPSIPDDWTFINLGLNNRPSFFGCDVKNFTLNANQKVPPLIVYVPNAPYTALSNVSTFDPSYTMSQRNDIIGNGWNSATQGNGTLDSEWPTCVACAVISRSLDRLGRQTPAACKTCFERYCWNGTVNSKDTGVYMPEFKIADAHALDSGAVAIGKMVNVWSSVVVGVVAATLLL

LPL

Lipoprotein lipase

490 amino acids

Key enzyme in triglyceride metabolism. Catalyzes the hydrolysis of triglycerides from circulating chylomicrons and very low density lipoproteins (VLDL), and thereby plays an important role in lipid clearance from the blood stream, lipid utilization and storage. Mediates margination of triglyceride-rich lipoprotein particles in capillaries. Recruited to its site of action on the luminal surface of vascular endothelium by binding to GPIHBP1 and cell surface heparan sulfate proteoglycans.

Belongs to the AB hydrolase superfamily. Lipase family.

55.132 kDa

MERGRGMGKTALLAVLCLCLRGAAGSDPEAEMNFEGIESKFSLRTPAEPDEDVCYLVPGQMDSLAQCNFNHTSKTFVVIHGWTVTGMYESWVPKLVDALYKREPDSNVIVVDWLVRAQQHYPVSAAYTKLVGKDVAMFIDWMEEKFNYPLNNVHLLGYSLGAHAAGIAGSLTKKKVNRITGLDPAGPTFEYADAPIRLSPDDADFVDVLHTYTRGSPDRSIGIQKPVGHIDIYPNGGGFQPGCNLGEALRLIAEKGFSDVDQLVKCSHERSIHLFIDSLLYEEKPSMAYRCNTKEAFEKGLCLSCRKNRCNNLGYKVNRVRTKRNTKMYLKTRAQMPYKVFHYQVKIHFFGKTNVTKVDQPFLISLYGTLDESENIPFTLPEVSSNKTFSFLIYTEVDIGDLLMLKLQWEKDTFFSWSDWWTPFAFTIQRVRVKSGETQKKVVFCSRDGSSRLGKGEEAAIFVKCLEQPVSRKRGGAKKASKENSAHESA

LPL

Lipoprotein lipase

478 amino acids

Key enzyme in triglyceride metabolism. Catalyzes the hydrolysis of triglycerides from circulating chylomicrons and very low density lipoproteins (VLDL), and thereby plays an important role in lipid clearance from the blood stream, lipid utilization and storage. Mediates margination of triglyceride-rich lipoprotein particles in capillaries (By similarity). Recruited to its site of action on the luminal surface of vascular endothelium by binding to GPIHBP1 and cell surface heparan sulfate proteoglycans (PubMed:9188470).

Belongs to the AB hydrolase superfamily. Lipase family.

53.378 kDa

MESKALLLLALSVCLQSLTVSRGGLVAADRITGGKDFRDIESKFALRTPEDTAEDTCHLIPGVTESVANCHFNHSSKTFVVIHGWTVTGMYESWVPKLVAALYKREPDSNVIVVDWLSRAQQHYPVSAGYTKLVGQDVAKFMNWMADEFNYPLGNVHLLGYSLGAHAAGIAGSLTNKKVNRITGLDPAGPNFEYAEAPSRLSPDDADFVDVLHTFTRGSPGRSIGIQKPVGHVDIYPNGGTFQPGCNIGEALRVIAERGLGDVDQLVKCSHERSVHLFIDSLLNEENPSKAYRCNSKEAFEKGLCLSCRKNRCNNMGYEINKVRAKRSSKMYLKTRSQMPYKVFHYQVKIHFSGTESNTYTNQAFEISLYGTVAESENIPFTLPEVSTNKTYSFLLYTEVDIGELLMLKLKWISDSYFSWSNWWSSPGFDIGKIRVKAGETQKKVIFCSREKMSYLQKGKSPVIFVKCHDKSLNRKSG

LPL

Lipoprotein lipase

478 amino acids

Key enzyme in triglyceride metabolism. Catalyzes the hydrolysis of triglycerides from circulating chylomicrons and very low density lipoproteins (VLDL), and thereby plays an important role in lipid clearance from the blood stream, lipid utilization and storage (PubMed:8636438). Mediates margination of triglyceride-rich lipoprotein particles in capillaries. Recruited to its site of action on the luminal surface of vascular endothelium by binding to GPIHBP1 and cell surface heparan sulfate proteoglycans (By similarity).

Belongs to the AB hydrolase superfamily. Lipase family.

53.668 kDa

MESKTLFLMALGIWLQSLTTTRGWVAADDRITGGRDFIDIESKFALRTPEDIAEDTCHLIPGVTESVANCHFNHTSKTFVVIHGWTVTGMYESWVPKLVAAPYKREPDSNVIVVDWLSRAQQHYPVSAGYTKLVGKDVAKFINWMAEEFHYPLDNVHLLGYSLGAHAAGIAGSLTNKKVNRITGLDPAGPNFEYAEAPSRLSPDDADFVDVLHTFTRGSPGRSIGIQKPVGHVDIYPNGGTFQPGCNIGEAIRVIAERGLGDVDQLVKCSHERSIHLFIDSLLNEENPSKAYRCNSKEAFEKGLCLSCRKNRCNNLGYEINKVRAKRSSKMYLKTRSQMPYKVFHYQVKIHFSGTESDTQTNQVFEISLYGTVAESENIPFTLPEISANKTYSFLIYTEVDIGELLMLKLKWKSDSYFSWSDWWSSPGFTIEKIRVKAGETQKKVIFCSREKVSHLQKGKASVVFVKCHDKSLNKKSG

LPL

Lipoprotein lipase

478 amino acids

Key enzyme in triglyceride metabolism. Catalyzes the hydrolysis of triglycerides from circulating chylomicrons and very low density lipoproteins (VLDL), and thereby plays an important role in lipid clearance from the blood stream, lipid utilization and storage. Mediates margination of triglyceride-rich lipoprotein particles in capillaries. Recruited to its site of action on the luminal surface of vascular endothelium by binding to GPIHBP1 and cell surface heparan sulfate proteoglycans.

Belongs to the AB hydrolase superfamily. Lipase family.

53.455 kDa

MESKALLLVALSVWLQSLIVSREGLATADRISGGRDFTDIESKFALRTPEDTVEDTCHLIPGVTESVANCHFNHSSKTFVVIHGWTVTGMYESWVPKLVAALYKREPDSNVIVVDWLSRAQQHYPISAGYTKLVGQDVATFIDWMAVEFSYPPNNVHLLGYSLGAHAAGIAGSLTKKKVNRITGLDPAGPNFEYAEAPSRLSPDDADFVDVLHTFTRGSPGRSIGIQKPVGHVDIYPNGGTFQPGCNIGEAIRVIAERGLGDVDQLVKCSHERSIHLFIDSLLNEENPSKAYRCNSKEAFEKGLCLSCRKNRCNNLGYEINKVRAKRSSKMYLKTRAQMPYKVFHYQVKMRFSGTESDTHTNQAFEISLYGTVAESENIPFTLPEVSTNKTYSFLIYTEVDIGELLMLKLKWVSDSYFSWSNWWSSPGFAIEKIRVKAGETQKKVIFCSREKKSHLQKGKSSVVFVKCHDKSLNRKSG

LPL

Lipoprotein lipase

478 amino acids

Key enzyme in triglyceride metabolism. Catalyzes the hydrolysis of triglycerides from circulating chylomicrons and very low density lipoproteins (VLDL), and thereby plays an important role in lipid clearance from the blood stream, lipid utilization and storage. Mediates margination of triglyceride-rich lipoprotein particles in capillaries. Recruited to its site of action on the luminal surface of vascular endothelium by binding to GPIHBP1 and cell surface heparan sulfate proteoglycans.

Belongs to the AB hydrolase superfamily. Lipase family.

53.588 kDa

MESKVLLLLALSVWLQSLTVSRGGLVAADRITRGKDFRDIESKFALRTPEDTAEDTCHLIPGVTESVANCHFNHSSKTFVVIHGWTVTGMYESWVPKLVAALYKREPDSNVIVVDWLSRAQQHYPVSAGYTKLVGQDVAKFMNWMADEFNYPLGNVHLLGYSLGAHAAGIAGSLTNKKVNRITGLDPAGPNFEYAEAPSRLSPDDADFVDVLHTFTRGSPGRSIGIQKPVGHVDIYPNGGTFQPGCNIGEALRVIAERGLGDVDQLVKCSHERSVHLFIDSLLNEENPSKAYRCNSKEAFEKGLCLSCRKNRCNNMGYEINKVRAKRSSKMYLKTRSQMPYKVFHYQVKIHFSGTESNTYTNQAFEISLYGTVAESENIPFTLPEVSTNKTYSFLLYTEVDIGELLMLKLKWISDSYFSWSNWWSSPGFDIGKIRVKAGETQKKVIFCSREKMSYLQKGKSPVIFVKCHDKSLNRKSG

LPL

Lipoprotein lipase

475 amino acids

Key enzyme in triglyceride metabolism. Catalyzes the hydrolysis of triglycerides from circulating chylomicrons and very low density lipoproteins (VLDL), and thereby plays an important role in lipid clearance from the blood stream, lipid utilization and storage (PubMed:8675619, PubMed:11342582, PubMed:27578112). Mediates margination of triglyceride-rich lipoprotein particles in capillaries (PubMed:24726386). Recruited to its site of action on the luminal surface of vascular endothelium by binding to GPIHBP1 and cell surface heparan sulfate proteoglycans (PubMed:11342582, PubMed:27811232).

Belongs to the AB hydrolase superfamily. Lipase family.

53.162 kDa

MESKALLVLTLAVWLQSLTASRGGVAAADQRRDFIDIESKFALRTPEDTAEDTCHLIPGVAESVATCHFNHSSKTFMVIHGWTVTGMYESWVPKLVAALYKREPDSNVIVVDWLSRAQEHYPVSAGYTKLVGQDVARFINWMEEEFNYPLDNVHLLGYSLGAHAAGIAGSLTNKKVNRITGLDPAGPNFEYAEAPSRLSPDDADFVDVLHTFTRGSPGRSIGIQKPVGHVDIYPNGGTFQPGCNIGEAIRVIAERGLGDVDQLVKCSHERSIHLFIDSLLNEENPSKAYRCSSKEAFEKGLCLSCRKNRCNNLGYEINKVRAKRSSKMYLKTRSQMPYKVFHYQVKIHFSGTESETHTNQAFEISLYGTVAESENIPFTLPEVSTNKTYSFLIYTEVDIGELLMLKLKWKSDSYFSWSDWWSSPGFAIQKIRVKAGETQKKVIFCSREKVSHLQKGKAPAVFVKCHDKSLNKKSG

LPL

Lipoprotein lipase

475 amino acids

Key enzyme in triglyceride metabolism. Catalyzes the hydrolysis of triglycerides from circulating chylomicrons and very low density lipoproteins (VLDL), and thereby plays an important role in lipid clearance from the blood stream, lipid utilization and storage (PubMed:9852258). Mediates margination of triglyceride-rich lipoprotein particles in capillaries. Recruited to its site of action on the luminal surface of vascular endothelium by binding to GPIHBP1 and cell surface heparan sulfate proteoglycans (By similarity).

Belongs to the AB hydrolase superfamily. Lipase family.

52.968 kDa

MESKALLLVALGMWFQSLTATRGGVAAADRGGDFIDIESKFALRTPEDTAEDTCHLIPGVTESVANCHFNHSSKTFVVIHGWTVTGMYESWVPKLVAALYKREPDSNVIVVDWLSRAQQHYPVSAGYTKLVGKDVAKFINWMAEEFHYPLDNVHLLGYSLGAHAAGIAGSLTNKKVNRITGLDPAGPNFEYAEAPSRLSPDDADFVDVLHTFTRGSPGRSIGIQKPVGHVDIYPNGGTFQPGCNIGEAIRVIAERGLGDVDQLVKCSHERSIHLFIDSLLNEENPSKAYRCNSKEAFEKGLCLSCRKNRCNNLGYEINKVRAKRSSKMYLKTRSQMPYKVFHYQVKIHFSGTESDTQTNQAFEISLYGTVAESENIPFTLPEVSANKTYSFLIYTEVDIGELLMLKLKWKSDSYFSWSDWWSSPGFAIEKIRVKAGETQKKVIFCSREKVSHLQKGKASVVFVKCHDKSLNKKSG

LPL

Lipoprotein lipase

475 amino acids

Key enzyme in triglyceride metabolism. Catalyzes the hydrolysis of triglycerides from circulating chylomicrons and very low density lipoproteins (VLDL), and thereby plays an important role in lipid clearance from the blood stream, lipid utilization and storage. Mediates margination of triglyceride-rich lipoprotein particles in capillaries. Recruited to its site of action on the luminal surface of vascular endothelium by binding to GPIHBP1 and cell surface heparan sulfate proteoglycans.

Belongs to the AB hydrolase superfamily. Lipase family.

53.146 kDa

MESKALLLLALAVWLQSLTASRGGVAAADQRRDFIDIESKFALRTPEDTAEDTCHLIPGVAESVATCHFNHSSKTFMVIHGWTVTGMYESWVPKLVAALYKREPDSNVIVVDWLSRAQQHYPVSAGYTKLVGQDVARFINWMEEEFNYPLDNVHLLGYSLGAHAAGIAGSLTNKKVNRITGLDPAGPNFEYAEAPSRLSPDDADFVDVLHTFTRGSPGRSIGIQKPVGHVDIYPNGGTFQPGCNIGEAIRVIAERGLGDVDQLVKCSHERSIHLFIDSLLNEENPSKAYRCSSKEAFEKGLCLSCRKNRCNNLGYEINKVRAKRSSKMYLKTRSQMPYKVFHYQVKIHFSGTESETHTNQAFEISLYGTVAESENIPFTLPEVSTNKTYSFLIYTEVDIGELLMLKLKWKSDSYFSWSDWWSSPGFAIQKIRVKAGETQKKVIFCSREKVSHLQKGKAPAVFVKCHDKSLNKKSG

Lpl

Lipoprotein lipase

474 amino acids

Key enzyme in triglyceride metabolism. Catalyzes the hydrolysis of triglycerides from circulating chylomicrons and very low density lipoproteins (VLDL), and thereby plays an important role in lipid clearance from the blood stream, lipid utilization and storage (PubMed:8675619). Mediates margination of triglyceride-rich lipoprotein particles in capillaries (PubMed:24726386). Recruited to its site of action on vascular endothelium by binding to GPIHBP1 and cell surface heparan sulfate proteoglycans (PubMed:20620994, PubMed:24726386, PubMed:27811232).

Belongs to the AB hydrolase superfamily. Lipase family.

53.109 kDa

MESKALLLVVLGVWLQSLTAFRGGVAAADAGRDFSDIESKFALRTPEDTAEDTCHLIPGLADSVSNCHFNHSSKTFVVIHGWTVTGMYESWVPKLVAALYKREPDSNVIVVDWLYRAQQHYPVSAGYTKLVGNDVARFINWMEEEFNYPLDNVHLLGYSLGAHAAGVAGSLTNKKVNRITGLDPAGPNFEYAEAPSRLSPDDADFVDVLHTFTRGSPGRSIGIQKPVGHVDIYPNGGTFQPGCNIGEAIRVIAERGLGDVDQLVKCSHERSIHLFIDSLLNEENPSKAYRCNSKEAFEKGLCLSCRKNRCNNLGYEINKVRAKRSSKMYLKTRSQMPYKVFHYQVKIHFSGTEDGKQHNQAFEISLYGTVAESENIPFTLPEVSTNKTYSFLIYTEVDIGELLMMKLKWISDSYFSWPDWWSSPSFVIERIRVKAGETQKKVIFCAREKVSHLQKGKDSAVFVKCHDKSLKKSG

Lpl

Lipoprotein lipase

474 amino acids

Key enzyme in triglyceride metabolism. Catalyzes the hydrolysis of triglycerides from circulating chylomicrons and very low density lipoproteins (VLDL), and thereby plays an important role in lipid clearance from the blood stream, lipid utilization and storage. Mediates margination of triglyceride-rich lipoprotein particles in capillaries. Recruited to its site of action on the luminal surface of vascular endothelium by binding to GPIHBP1 and cell surface heparan sulfate proteoglycans.

Belongs to the AB hydrolase superfamily. Lipase family.

53.082 kDa

MESKALLLVALGVWLQSLTAFRGGVAAADGGRDFSDIESKFALRTPEDTAEDTCHLIPGLADSVSNCHFNHSSKTFVVIHGWTVTGMYESWVPKLVAALYKREPDSNVIVVDWLYRAQQHYPVSAGYTKLVGNDVARFINWLEEEFNYPLDNVHLLGYSLGAHAAGVAGSLTNKKVNRITGLDPAGPNFEYAEAPSRLSPDDADFVDVLHTFTRGSPGRSIGIQKPVGHVDIYPNGGTFQPGCNIGEAIRVIAEKGLGDVDQLVKCSHERSIHLFIDSLLNEENPSKAYRCNSKEAFEKGLCLSCRKNRCNNVGYEINKVRAKRSSKMYLKTRSQMPYKVFHYQVKIHFSGTENDKQNNQAFEISLYGTVAESENIPFTLPEVATNKTYSFLIYTEVDIGELLMMKLKWKNDSYFRWSDWWSSPSFVIEKIRVKAGETQKKVIFCAREKVSHLQKGKDAAVFVKCHDKSLKKSG

LPL

Lipoprotein lipase

465 amino acids

Key enzyme in triglyceride metabolism. Catalyzes the hydrolysis of triglycerides from circulating chylomicrons and very low density lipoproteins (VLDL), and thereby plays an important role in lipid clearance from the blood stream, lipid utilization and storage. Mediates margination of triglyceride-rich lipoprotein particles in capillaries. Recruited to its site of action on the luminal surface of vascular endothelium by binding to GPIHBP1 and cell surface heparan sulfate proteoglycans.

Belongs to the AB hydrolase superfamily. Lipase family.

52.781 kDa

MNIDRKILNKALAKEKVANCQKDYTDIESKFARRTPENTVEDTCHLIPGVTESVANCHFNHSSKTFMVIHGWTVTGMYESWVPKLVAALYKREPDSNVIVVDWLRRAQHHYPESADYTKLVGEDVARFINWMEDEFKYSVDNVHLLGYSLGAHAAGVAGSRTNTKVSRITGLDPAGPNFEYAEATSRLSPDDAQFVDVLHTFTRGSPGRSIGIQKPVGHVDIYPNGGSFQPGCNIQDALRVISQKGFGDMDQLVKCSHERSIHLFIDSLLNEENPSKAYRCNSKEAFEKGLCLSCRKNRCNNVGYEINKVRAKRSSKMYLKTRSQMPYKVFHYQVKIYFSGTETTTYTNQAFEISLYGTVAESENIPFTLPEVSANNTYSFLIYTEVDIGELLMLKLKWITESYFSWSSWWGRPTFTIEKIRVKAGETQKKIVFCSREKVSKLQKGKEAPVFVKCHDKSLNKKSG