bhf-ucl Sortilin/neurotensin receptor-3 binds and mediates degradation of lipoprotein lipase. Sortilin/neurotensin receptor-3 binds and mediates degradation of lipoprotein lipase. J. Biol. Chem. (0021-9258) 1999 imex curation Nielsen M.S., Jacobsen C., Olivecrona G., Gliemann J., Petersen C.M. Cardiac - Interactions involving cardiac related proteins I put the two domains D2 and D3 as sufficient to bind here because figure 1 B does not show that D1 does not bind. In contrast, I put D2 and D3 as required to bind in EBI-8794703 because experiment in figure 2 shows that domain 1 does not bind. Is this appropriate? LpL, s-sortilin and RAP were purified before cross-linking followed by SDS-PAGE and autoradiography. Determination of protein origin: LpL purified from bovine milk as the enzymatically active dimeric enzyme (author citation Bengtsson-Olivecrona and Olivecrona, 1991 PMID 2051931), the construct LpL-(347–389/394–448) is human expressed in E. coli (author citation of previous work Nielsen et al., 1997 PMID 9038197), s-sortilin is human (author citation of previous work Tauris et al., 1998 PMID 9657377), his-tagged RAP is human as stated by author. RAP protein was identified as alph2macroglobulin receptor associated protein in author reference Ellgaard et al., 1996 PMID 9119022 which correlated with an unambiguous entry in UniProt. The amino acid sequence was remapped to match UniProt and InterPro i.e. full length of 357 amino acids instead of 323 amino acids (a shift of 34 amino acids). Consequently, this was used to map domain1 to 52-146 instead of 18-112, and domains2 and 3 to 147-357 instead of 113-323. Consequently, the entry now correlates with InterPro domains. mn@biokemi.au.dk 22-Nov-2013: Contacted by IntAct-Help. Only protein-protein interactions mouse-3t3_l1 Mus musculus embryonic cells Fibroblast-like. Adipose like when confluent 3t3_l1 Mouse embryo cells Fibroblast-like. Adipose like when confluent bifunctional agent crosslink protein cross-linking with a bifunctional reagent Label transfer techniques Photoaffinity labelling Label transfer techniques Photoaffinity labelling bifunctional agent crosslink weight autoradiogra molecular weight estimation by autoradiography weight autoradiogra Nielsen M.S., Jacobsen C., Olivecrona G., Gliemann J., Petersen C.M. Cardiac - Interactions involving cardiac related proteins I put the two domains D2 and D3 as sufficient to bind here because figure 1 B does not show that D1 does not bind. In contrast, I put D2 and D3 as required to bind in EBI-8794703 because experiment in figure 2 shows that domain 1 does not bind. Is this appropriate? LpL, s-sortilin and RAP were purified before cross-linking followed by SDS-PAGE and autoradiography. Determination of protein origin: LpL purified from bovine milk as the enzymatically active dimeric enzyme (author citation Bengtsson-Olivecrona and Olivecrona, 1991 PMID 2051931), the construct LpL-(347–389/394–448) is human expressed in E. coli (author citation of previous work Nielsen et al., 1997 PMID 9038197), s-sortilin is human (author citation of previous work Tauris et al., 1998 PMID 9657377), his-tagged RAP is human as stated by author. mn@biokemi.au.dk Accepted 2013-NOV-07 by ORCHARD 22-Nov-2013: Contacted by IntAct-Help. J. Biol. Chem. (0021-9258) 1999 imex curation Sortilin/neurotensin receptor-3 binds and mediates degradation of lipoprotein lipase. Sortilin/neurotensin receptor-3 binds and mediates degradation of lipoprotein lipase. J. Biol. Chem. (0021-9258) 1999 imex curation Nielsen M.S., Jacobsen C., Olivecrona G., Gliemann J., Petersen C.M. Cardiac - Interactions involving cardiac related proteins I put the two domains D2 and D3 as sufficient to bind here because figure 1 B does not show that D1 does not bind. In contrast, I put D2 and D3 as required to bind in EBI-8794703 because experiment in figure 2 shows that domain 1 does not bind. Is this appropriate? LpL, s-sortilin and RAP were purified before cross-linking followed by SDS-PAGE and autoradiography. Determination of protein origin: LpL purified from bovine milk as the enzymatically active dimeric enzyme (author citation Bengtsson-Olivecrona and Olivecrona, 1991 PMID 2051931), the construct LpL-(347–389/394–448) is human expressed in E. coli (author citation of previous work Nielsen et al., 1997 PMID 9038197), s-sortilin is human (author citation of previous work Tauris et al., 1998 PMID 9657377), his-tagged RAP is human as stated by author. RAP protein was identified as alph2macroglobulin receptor associated protein in author reference Ellgaard et al., 1996 PMID 9119022 which correlated with an unambiguous entry in UniProt. The amino acid sequence was remapped to match UniProt and InterPro i.e. full length of 357 amino acids instead of 323 amino acids (a shift of 34 amino acids). Consequently, this was used to map domain1 to 52-146 instead of 18-112, and domains2 and 3 to 147-357 instead of 113-323. Consequently, the entry now correlates with InterPro domains. mn@biokemi.au.dk 22-Nov-2013: Contacted by IntAct-Help. Only protein-protein interactions in vitro In vitro bifunctional agent crosslink protein cross-linking with a bifunctional reagent Label transfer techniques Photoaffinity labelling Label transfer techniques Photoaffinity labelling bifunctional agent crosslink predetermined predetermined participant predetermined Nielsen M.S., Jacobsen C., Olivecrona G., Gliemann J., Petersen C.M. Cardiac - Interactions involving cardiac related proteins I put the two domains D2 and D3 as sufficient to bind here because figure 1 B does not show that D1 does not bind. In contrast, I put D2 and D3 as required to bind in EBI-8794703 because experiment in figure 2 shows that domain 1 does not bind. Is this appropriate? LpL, s-sortilin and RAP were purified before cross-linking followed by SDS-PAGE and autoradiography. Determination of protein origin: LpL purified from bovine milk as the enzymatically active dimeric enzyme (author citation Bengtsson-Olivecrona and Olivecrona, 1991 PMID 2051931), the construct LpL-(347–389/394–448) is human expressed in E. coli (author citation of previous work Nielsen et al., 1997 PMID 9038197), s-sortilin is human (author citation of previous work Tauris et al., 1998 PMID 9657377), his-tagged RAP is human as stated by author. mn@biokemi.au.dk Accepted 2013-NOV-07 by ORCHARD 22-Nov-2013: Contacted by IntAct-Help. J. Biol. Chem. (0021-9258) 1999 imex curation Sortilin/neurotensin receptor-3 binds and mediates degradation of lipoprotein lipase. Sortilin/neurotensin receptor-3 binds and mediates degradation of lipoprotein lipase. J. Biol. Chem. (0021-9258) 1999 imex curation Nielsen M.S., Jacobsen C., Olivecrona G., Gliemann J., Petersen C.M. Cardiac - Interactions involving cardiac related proteins I put the two domains D2 and D3 as sufficient to bind here because figure 1 B does not show that D1 does not bind. In contrast, I put D2 and D3 as required to bind in EBI-8794703 because experiment in figure 2 shows that domain 1 does not bind. Is this appropriate? LpL, s-sortilin and RAP were purified before cross-linking followed by SDS-PAGE and autoradiography. Determination of protein origin: LpL purified from bovine milk as the enzymatically active dimeric enzyme (author citation Bengtsson-Olivecrona and Olivecrona, 1991 PMID 2051931), the construct LpL-(347–389/394–448) is human expressed in E. coli (author citation of previous work Nielsen et al., 1997 PMID 9038197), s-sortilin is human (author citation of previous work Tauris et al., 1998 PMID 9657377), his-tagged RAP is human as stated by author. RAP protein was identified as alph2macroglobulin receptor associated protein in author reference Ellgaard et al., 1996 PMID 9119022 which correlated with an unambiguous entry in UniProt. The amino acid sequence was remapped to match UniProt and InterPro i.e. full length of 357 amino acids instead of 323 amino acids (a shift of 34 amino acids). Consequently, this was used to map domain1 to 52-146 instead of 18-112, and domains2 and 3 to 147-357 instead of 113-323. Consequently, the entry now correlates with InterPro domains. mn@biokemi.au.dk 22-Nov-2013: Contacted by IntAct-Help. Only protein-protein interactions in vitro In vitro solid phase assay solid phase assay predetermined predetermined participant predetermined Nielsen M.S., Jacobsen C., Olivecrona G., Gliemann J., Petersen C.M. Cardiac - Interactions involving cardiac related proteins I put the two domains D2 and D3 as sufficient to bind here because figure 1 B does not show that D1 does not bind. In contrast, I put D2 and D3 as required to bind in EBI-8794703 because experiment in figure 2 shows that domain 1 does not bind. Is this appropriate? LpL, s-sortilin and RAP were purified before cross-linking followed by SDS-PAGE and autoradiography. Determination of protein origin: LpL purified from bovine milk as the enzymatically active dimeric enzyme (author citation Bengtsson-Olivecrona and Olivecrona, 1991 PMID 2051931), the construct LpL-(347–389/394–448) is human expressed in E. coli (author citation of previous work Nielsen et al., 1997 PMID 9038197), s-sortilin is human (author citation of previous work Tauris et al., 1998 PMID 9657377), his-tagged RAP is human as stated by author. mn@biokemi.au.dk Accepted 2013-NOV-07 by ORCHARD 22-Nov-2013: Contacted by IntAct-Help. J. Biol. Chem. (0021-9258) 1999 imex curation Sortilin/neurotensin receptor-3 binds and mediates degradation of lipoprotein lipase. Sortilin/neurotensin receptor-3 binds and mediates degradation of lipoprotein lipase. J. Biol. Chem. (0021-9258) 1999 imex curation Nielsen M.S., Jacobsen C., Olivecrona G., Gliemann J., Petersen C.M. Cardiac - Interactions involving cardiac related proteins I put the two domains D2 and D3 as sufficient to bind here because figure 1 B does not show that D1 does not bind. In contrast, I put D2 and D3 as required to bind in EBI-8794703 because experiment in figure 2 shows that domain 1 does not bind. Is this appropriate? LpL, s-sortilin and RAP were purified before cross-linking followed by SDS-PAGE and autoradiography. Determination of protein origin: LpL purified from bovine milk as the enzymatically active dimeric enzyme (author citation Bengtsson-Olivecrona and Olivecrona, 1991 PMID 2051931), the construct LpL-(347–389/394–448) is human expressed in E. coli (author citation of previous work Nielsen et al., 1997 PMID 9038197), s-sortilin is human (author citation of previous work Tauris et al., 1998 PMID 9657377), his-tagged RAP is human as stated by author. RAP protein was identified as alph2macroglobulin receptor associated protein in author reference Ellgaard et al., 1996 PMID 9119022 which correlated with an unambiguous entry in UniProt. The amino acid sequence was remapped to match UniProt and InterPro i.e. full length of 357 amino acids instead of 323 amino acids (a shift of 34 amino acids). Consequently, this was used to map domain1 to 52-146 instead of 18-112, and domains2 and 3 to 147-357 instead of 113-323. Consequently, the entry now correlates with InterPro domains. mn@biokemi.au.dk 22-Nov-2013: Contacted by IntAct-Help. Only protein-protein interactions in vitro In vitro spr surface plasmon resonance Optical biosensor BIAcore(r) BIAcore(r) Optical biosensor spr predetermined predetermined participant predetermined Nielsen M.S., Jacobsen C., Olivecrona G., Gliemann J., Petersen C.M. Cardiac - Interactions involving cardiac related proteins I put the two domains D2 and D3 as sufficient to bind here because figure 1 B does not show that D1 does not bind. In contrast, I put D2 and D3 as required to bind in EBI-8794703 because experiment in figure 2 shows that domain 1 does not bind. Is this appropriate? LpL, s-sortilin and RAP were purified before cross-linking followed by SDS-PAGE and autoradiography. Determination of protein origin: LpL purified from bovine milk as the enzymatically active dimeric enzyme (author citation Bengtsson-Olivecrona and Olivecrona, 1991 PMID 2051931), the construct LpL-(347–389/394–448) is human expressed in E. coli (author citation of previous work Nielsen et al., 1997 PMID 9038197), s-sortilin is human (author citation of previous work Tauris et al., 1998 PMID 9657377), his-tagged RAP is human as stated by author. mn@biokemi.au.dk Accepted 2013-NOV-07 by ORCHARD 22-Nov-2013: Contacted by IntAct-Help. J. Biol. Chem. (0021-9258) 1999 imex curation lipl_bovin Lipoprotein lipase LPL Phospholipase A1 protein protein bovin Bos taurus (Bovine) Bovine MESKALLLLALSVCLQSLTVSRGGLVAADRITGGKDFRDIESKFALRTPEDTAEDTCHLIPGVTESVANCHFNHSSKTFVVIHGWTVTGMYESWVPKLVAALYKREPDSNVIVVDWLSRAQQHYPVSAGYTKLVGQDVAKFMNWMADEFNYPLGNVHLLGYSLGAHAAGIAGSLTNKKVNRITGLDPAGPNFEYAEAPSRLSPDDADFVDVLHTFTRGSPGRSIGIQKPVGHVDIYPNGGTFQPGCNIGEALRVIAERGLGDVDQLVKCSHERSVHLFIDSLLNEENPSKAYRCNSKEAFEKGLCLSCRKNRCNNMGYEINKVRAKRSSKMYLKTRSQMPYKVFHYQVKIHFSGTESNTYTNQAFEISLYGTVAESENIPFTLPEVSTNKTYSFLLYTEVDIGELLMLKLKWISDSYFSWSNWWSSPGFDIGKIRVKAGETQKKVIFCSREKMSYLQKGKSPVIFVKCHDKSLNRKSG DIP protein P11151 original sequence version: 125 06FDD429DD194A1F sort_human Sortilin SORT1 Neurotensin receptor 3 Glycoprotein 95 100 kDa NT receptor protein protein human Homo sapiens Human MERPWGAADGLSRWPHGLGLLLLLQLLPPSTLSQDRLDAPPPPAAPLPRWSGPIGVSWGLRAAAAGGAFPRGGRWRRSAPGEDEECGRVRDFVAKLANNTHQHVFDDLRGSVSLSWVGDSTGVILVLTTFHVPLVIMTFGQSKLYRSEDYGKNFKDITDLINNTFIRTEFGMAIGPENSGKVVLTAEVSGGSRGGRIFRSSDFAKNFVQTDLPFHPLTQMMYSPQNSDYLLALSTENGLWVSKNFGGKWEEIHKAVCLAKWGSDNTIFFTTYANGSCKADLGALELWRTSDLGKSFKTIGVKIYSFGLGGRFLFASVMADKDTTRRIHVSTDQGDTWSMAQLPSVGQEQFYSILAANDDMVFMHVDEPGDTGFGTIFTSDDRGIVYSKSLDRHLYTTTGGETDFTNVTSLRGVYITSVLSEDNSIQTMITFDQGGRWTHLRKPENSECDATAKNKNECSLHIHASYSISQKLNVPMAPLSEPNAVGIVIAHGSVGDAISVMVPDVYISDDGGYSWTKMLEGPHYYTILDSGGIIVAIEHSSRPINVIKFSTDEGQCWQTYTFTRDPIYFTGLASEPGARSMNISIWGFTESFLTSQWVSYTIDFKDILERNCEEKDYTIWLAHSTDPEDYEDGCILGYKEQFLRLRKSSVCQNGRDYVVTKQPSICLCSLEDFLCDFGYYRPENDSKCVEQPELKGHDLEFCLYGREEHLTTNGYRKIPGDKCQGGVNPVREVKDLKKKCTSNFLSPEKQNSKSNSVPIILAIVGLMLVTVVAGVLIVKKYVCGGRFLVHRYSVLQQHAEANGVDGVDALDTASHTNKSGYHDDSDEDLLE DIP protein Q99523 original sequence version: 97 DIP protein Q99523-1 original sequence version: 127 91F96A3035A4B43A lipl_human Lipoprotein lipase LPL LIPD Phospholipase A1 protein protein human Homo sapiens Human MESKALLVLTLAVWLQSLTASRGGVAAADQRRDFIDIESKFALRTPEDTAEDTCHLIPGVAESVATCHFNHSSKTFMVIHGWTVTGMYESWVPKLVAALYKREPDSNVIVVDWLSRAQEHYPVSAGYTKLVGQDVARFINWMEEEFNYPLDNVHLLGYSLGAHAAGIAGSLTNKKVNRITGLDPAGPNFEYAEAPSRLSPDDADFVDVLHTFTRGSPGRSIGIQKPVGHVDIYPNGGTFQPGCNIGEAIRVIAERGLGDVDQLVKCSHERSIHLFIDSLLNEENPSKAYRCSSKEAFEKGLCLSCRKNRCNNLGYEINKVRAKRSSKMYLKTRSQMPYKVFHYQVKIHFSGTESETHTNQAFEISLYGTVAESENIPFTLPEVSTNKTYSFLIYTEVDIGELLMLKLKWKSDSYFSWSDWWSSPGFAIQKIRVKAGETQKKVIFCSREKVSHLQKGKAPAVFVKCHDKSLNKKSG FBD00FCD334FB8AA amrp_human Alpha-2-macroglobulin receptor-associated protein Low density lipoprotein receptor-related protein-associated protein 1 LRPAP1 A2MRAP protein protein human Homo sapiens Human MAPRRVRSFLRGLPALLLLLLFLGPWPAASHGGKYSREKNQPKPSPKRESGEEFRMEKLNQLWEKAQRLHLPPVRLAELHADLKIQERDELAWKKLKLDGLDEDGEKEARLIRNLNVILAKYGLDGKKDARQVTSNSLSGTQEDGLDDPRLEKLWHKAKTSGKFSGEELDKLWREFLHHKEKVHEYNVLLETLSRTEEIHENVISPSDLSDIKGSVLHSRHTELKEKLRSINQGLDRLRRVSHQGYSTEAEFEEPRVIDLWDLAQSANLTDKELEAFREELKHFEAKIEKHNHYQKQLEIAHEKLRHAESVGDGERVSRSREKHALLEGRTKELGYTVKKHLQDLSGRISRARHNEL DIP protein P30533 original sequence version: 105 DIP protein P30533 original sequence version: 103 D56A7DA754125CFA sort_mouse Sortilin Sort1 Neurotensin receptor 3 protein protein mouse Mus musculus Mouse MERPRGAADGLLRWPLGLLLLLQLLPPAAVGQDRLDAPPPPAPPLLRWAGPVGVSWGLRAAAPGGPVPRAGRWRRGAPAEDQDCGRLPDFIAKLTNNTHQHVFDDLSGSVSLSWVGDSTGVILVLTTFQVPLVIVSFGQSKLYRSEDYGKNFKDITNLINNTFIRTEFGMAIGPENSGKVILTAEVSGGSRGGRVFRSSDFAKNFVQTDLPFHPLTQMMYSPQNSDYLLALSTENGLWVSKNFGEKWEEIHKAVCLAKWGPNNIIFFTTHVNGSCKADLGALELWRTSDLGKTFKTIGVKIYSFGLGGRFLFASVMADKDTTRRIHVSTDQGDTWSMAQLPSVGQEQFYSILAANEDMVFMHVDEPGDTGFGTIFTSDDRGIVYSKSLDRHLYTTTGGETDFTNVTSLRGVYITSTLSEDNSIQSMITFDQGGRWEHLRKPENSKCDATAKNKNECSLHIHASYSISQKLNVPMAPLSEPNAVGIVIAHGSVGDAISVMVPDVYISDDGGYSWAKMLEGPHYYTILDSGGIIVAIEHSNRPINVIKFSTDEGQCWQSYVFTQEPIYFTGLASEPGARSMNISIWGFTESFITRQWVSYTVDFKDILERNCEEDDYTTWLAHSTDPGDYKDGCILGYKEQFLRLRKSSVCQNGRDYVVAKQPSVCPCSLEDFLCDFGYFRPENASECVEQPELKGHELEFCLYGKEEHLTTNGYRKIPGDKCQGGMNPAREVKDLKKKCTSNFLNPTKQNSKSNSVPIILAIVGLMLVTVVAGVLIVKKYVCGGRFLVHRYSVLQQHAEADGVEALDSTSHAKSGYHDDSDEDLLE DIP protein Q6PHU5 original sequence version: 45 DIP protein Q6PHU5 original sequence version: 62 Functions as a sorting receptor in the Golgi compartment and as a clearance receptor on the cell surface. Required for protein transport from the Golgi apparatus to the lysosomes by a pathway that is independent of the mannose-6-phosphate receptor (M6PR). Also required for protein transport from the Golgi apparatus to the endosomes. Promotes neuronal apoptosis by mediating endocytosis of the proapoptotic precursor forms of BDNF (proBDNF) and NGFB (proNGFB). Also acts as a receptor for neurotensin. May promote mineralization of the extracellular matrix during osteogenic differentiation by scavenging extracellular LPL. Probably required in adipocytes for the formation of specialized storage vesicles containing the glucose transporter SLC2A4/GLUT4 (GLUT4 storage vesicles, or GSVs). These vesicles provide a stable pool of SLC2A4 and confer increased responsiveness to insulin. May also mediate transport from the endoplasmic reticulum to the Golgi mint 9A7A73C6FE1C8201 neurotensin neurotensin <Glu-Leu-Tyr-Glu-Asn-Lys-Pro-Arg-Arg-Pro-Tyr-Ile-Leu-OH Neurotensin 5-oxo-L-prolyl-L-leucyl-L-tyrosyl-L-alpha-glutamyl-L-asparaginyl-L-lysyl-L-prolyl-L-arginyl-L-arginyl-L-prolyl-L-tyrosyl-L-isoleucyl-L-leucine Glp-Leu-Tyr-Glu-Asn-Lys-Pro-Arg-Arg-Pro-Tyr-Ile-Leu-OH small molecule small molecule chemical synthesis Chemical synthesis (Chemical synthesis) PCJGZPGTCUMMOT-UHFFFAOYSA-N PCJGZPGTCUMMOT-UHFFFAOYSA-N lipl_mouse Lipoprotein lipase Lpl Phospholipase A1 protein protein mouse Mus musculus Mouse MESKALLLVVLGVWLQSLTAFRGGVAAADAGRDFSDIESKFALRTPEDTAEDTCHLIPGLADSVSNCHFNHSSKTFVVIHGWTVTGMYESWVPKLVAALYKREPDSNVIVVDWLYRAQQHYPVSAGYTKLVGNDVARFINWMEEEFNYPLDNVHLLGYSLGAHAAGVAGSLTNKKVNRITGLDPAGPNFEYAEAPSRLSPDDADFVDVLHTFTRGSPGRSIGIQKPVGHVDIYPNGGTFQPGCNIGEAIRVIAERGLGDVDQLVKCSHERSIHLFIDSLLNEENPSKAYRCNSKEAFEKGLCLSCRKNRCNNLGYEINKVRAKRSSKMYLKTRSQMPYKVFHYQVKIHFSGTEDGKQHNQAFEISLYGTVAESENIPFTLPEVSTNKTYSFLIYTEVDIGELLMMKLKWISDSYFSWPDWWSSPSFVIERIRVKAGETQKKVIFCAREKVSHLQKGKDSAVFVKCHDKSLKKSG E5895C98B7AE16CD heparin Heparin small molecule small molecule chemical synthesis Chemical synthesis (Chemical synthesis) lpl-sort1 2 5 unspecified role unspecified role neutral component neutral component purified purified bovin-milk Bos taurus milk milk 6 autoradiography autoradiography predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified 125 iodine radiolabel 125i radiolabel 125i radiolabel I125 125I 125I I125 undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined extra cellular domain sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain crigr-cho_k1 Cricetulus griseus ovary K1 cho_k1 Chinese Hamster Ovary K1 direct interaction direct interaction Figure 1 A lpl-sort1-2 2 6 autoradiography autoradiography predetermined predetermined participant predetermined predetermined predetermined participant predetermined stimulator stimulator neutral component neutral component purified purified extra cellular domain sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain crigr-cho_k1 Cricetulus griseus ovary K1 cho_k1 Chinese Hamster Ovary K1 6 autoradiography autoradiography predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified extra cellular domain sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain 125 iodine radiolabel 125i radiolabel 125i radiolabel I125 125I 125I I125 undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined crigr-cho_k1 Cricetulus griseus ovary K1 cho_k1 Chinese Hamster Ovary K1 5 unspecified role unspecified role neutral component neutral component purified purified bovin-milk Bos taurus milk milk association association Figures 1 A Author states that the labeled complex was increased by unlabeled soluble sortilin at low concentration (9 nm) (lane 3). lpl-sort1-3 2 6 autoradiography autoradiography predetermined predetermined participant predetermined predetermined predetermined participant predetermined inhibitor inhibitor neutral component neutral component purified purified extra cellular domain sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain crigr-cho_k1 Cricetulus griseus ovary K1 cho_k1 Chinese Hamster Ovary K1 5 unspecified role unspecified role neutral component neutral component purified purified bovin-milk Bos taurus milk milk 6 autoradiography autoradiography predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified extra cellular domain sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain 125 iodine radiolabel 125i radiolabel 125i radiolabel I125 125I 125I I125 undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined crigr-cho_k1 Cricetulus griseus ovary K1 cho_k1 Chinese Hamster Ovary K1 association association Figures 1 A Author states that the formation of complex was inhibited by 180–540 nm unlabeled soluble sortilin (lanes 4 and 5). heparin-lpl 2 12 competitor competitor competitor neutral component neutral component 5 unspecified role unspecified role neutral component neutral component purified purified bovin-milk Bos taurus milk milk 6 autoradiography autoradiography predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified extra cellular domain sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain 125 iodine radiolabel 125i radiolabel 125i radiolabel I125 125I 125I I125 undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined crigr-cho_k1 Cricetulus griseus ovary K1 cho_k1 Chinese Hamster Ovary K1 association association Figures 1 A lpl-lrpap1-1 2 6 autoradiography autoradiography predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified 125 iodine radiolabel 125i radiolabel 125i radiolabel I125 125I 125I I125 undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined extra cellular domain sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain crigr-cho_k1 Cricetulus griseus ovary K1 cho_k1 Chinese Hamster Ovary K1 RAP D23 8 competitor competitor competitor neutral component neutral component domains 2 and 3 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain hexa his tag his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined ecoli Escherichia coli (strain K12) 5 unspecified role unspecified role neutral component neutral component bovin-milk Bos taurus milk milk association association Figure 1 B Author states that at 5 μm, RAP D23 markedly inhibited sortilin-LpL complex and caused the formation of a smaller complex (lane 4), whereas 125 nm D23 caused partial inhibition (lane 5). lpl-lrpap1-4 3 8 competitor competitor competitor prey prey domains 2 and 3 required to bind necessary binding region required to bind certain certain sequence position certain certain certain sequence position certain hexa his tag his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined ecoli Escherichia coli (strain K12) 6 autoradiography autoradiography predetermined predetermined participant predetermined unspecified role unspecified role prey prey purified purified 125 iodine radiolabel 125i radiolabel 125i radiolabel I125 125I 125I I125 undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined extra cellular domain sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain crigr-cho_k1 Cricetulus griseus ovary K1 cho_k1 Chinese Hamster Ovary K1 5 unspecified role unspecified role bait bait bovin-milk Bos taurus milk milk 48 52 association association Figure 2 sort1-lpl 4 5 unspecified role unspecified role prey prey bovin-milk Bos taurus milk milk 6 autoradiography autoradiography predetermined predetermined participant predetermined unspecified role unspecified role bait bait purified purified extra cellular domain sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain crigr-cho_k1 Cricetulus griseus ovary K1 cho_k1 Chinese Hamster Ovary K1 direct interaction direct interaction Figure 3 A Author states that Fig.3A shows that LpL binds readily and demonstrates a marked decrease in binding when LpL was made monomeric by treatment with guanidinium hydrochloride. sort1-lpl-1 4 7 unspecified role unspecified role prey prey binding region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain certain certain sequence position certain certain certain sequence position certain hexa his tag his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined The author states that the tag consists of the hexahistidine-Factor X substrate sequence Met-Gly-Ser-(His)6-Ser-Ile-Glu-Gly-Arg. ecoli Escherichia coli (strain K12) 6 autoradiography autoradiography predetermined predetermined participant predetermined unspecified role unspecified role bait bait purified purified extra cellular domain sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain crigr-cho_k1 Cricetulus griseus ovary K1 cho_k1 Chinese Hamster Ovary K1 60 63 direct interaction direct interaction Figure 3 B Deletion of the sequence Trp390-Ser-Asp-Trp393 from the construct LpL-(347–448) increases the solubility of the peptide. Q99523 increases degradation of protein levels of P06858 sort1-lpl-3 4 5 unspecified role unspecified role prey prey bovin-milk Bos taurus milk milk 6 autoradiography autoradiography predetermined predetermined participant predetermined unspecified role unspecified role bait bait purified purified extra cellular domain sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain crigr-cho_k1 Cricetulus griseus ovary K1 cho_k1 Chinese Hamster Ovary K1 10 competitor competitor competitor prey prey physical association physical association Figure 3 B lpl-sort1-6 1 9 unspecified role unspecified role neutral component neutral component partially purified partially purified 35s radiolabel 35s radiolabel 35s radiolabel 35S s35 radiolabelled S35 s35 radiolabelled 35S S35 undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined 11 unspecified role unspecified role neutral component neutral component partially purified partially purified 35s radiolabel 35s radiolabel 35s radiolabel 35S s35 radiolabelled S35 s35 radiolabelled 35S S35 undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined physical association physical association Figure 4