eF-site ID 5ftu-ABCDEFGHIJKL PDB Code 5ftu Chain A, B, C, D, E, F, G, H, I, J, K, L click to enlarge Title Tetrameric complex of Latrophilin 3, Unc5D and FLRT2 Classification SIGNALING PROTEIN Compound NETRIN RECEPTOR UNC5D Source (AGRL3_MOUSE) Sequence A:  SAPGTLPHFIEEPEDAYIIKSNPIALRCKARPAMQIFFKC NGEWVHQNEHVSEESLDESSGLKVREVFINVTRQQVEDFH GPEDYWCQCVAWSHLGTSKSRKASVR B:  CPSVCRCDRNFVYCNERSLTSVPLGIPEGVTVLYLHNNQI NNAGFPAELHNVQSVHTVYLYGNQLDEFPMNLPKNVRVLH LQENNIQTISRAALAQLLKLEELHLDDNSISTVGVEDGAF REAISLKLLFLSKNHLSSVPVGLPVDLQELRVDENRIAVI SDMAFQNLTSLERLIVDGNLLTNKGIAEGTFSHLTKLKEF SIVRNSLSHPPPDLPGTHLIRLYLQDNQINHIPLTAFANL RKLERLDISNNQLRMLTQGVFDHLSNLKQLTARNNPWFCD CSIKWVTEWLKYIPSSLNVRGFMCQGPEQVRGMAVRELNM NLLSCP C:  RELSCESYPIELRCPGTDVIMIESANYGRTDDKICDSDPA QMENIRCYLPDAYKIMSQRCNNRTQCAVVAGPDVFPDPCP GTYKYLEVQYECVPYKVEQKVFLCPGLLKGVYQSEHLFES DHQSGAWCKDPLQASDKIYYMPWTPYRTDTLTEYSSKDDF IAGRPTTTYKLPHRVDGTGFVVYDGALFFNKERTRNIVKF DLRTRIKSGEAIIANANYHDTSPYRWGGKSDIDLAVDENG LWVIYATEQNNGKIVISQLNPYTLRIEGTWDTAYDKRSAS NAFMICGILYVVKSVYEDDDNEATGNKIDYIYNTDQSKDS LVDVPFPNSYQYIAAVDYNPRDNLLYVWNNYHVVKYSLDF GPLDG D:  LCPGLLKGVYQSEHLFESDHQSGAWCKDPLQASDKIYYMP WTPYRTDTLTEYSSKDDFIAGRPTTTYKLPHRVDGTGFVV YDGALFFNKERTRNIVKFDLRTRIKSGEAIIANANYHDTS PYRWGGKSDIDLAVDENGLWVIYATEQNNGKIVISQLNPY TLRIEGTWDTAYDKRSASNAFMICGILYVVKSVYEDDDNE ATGNKIDYIYNTDQSKDSLVDVPFPNSYQYIAAVDYNPRD NLLYVWNNYHVVKYSLDFGPLDG E:  SAPGTLPHFIEEPEDAYIIKSNPIALRCKARPAMQIFFKC NGEWVHQNEHVSEESLDESSGLKVREVFINVTRQQVEDFH GPEDYWCQCVAWSHLGTSKSRKASVR F:  CPSVCRCDRNFVYCNERSLTSVPLGIPEGVTVLYLHNNQI NNAGFPAELHNVQSVHTVYLYGNQLDEFPMNLPKNVRVLH LQENNIQTISRAALAQLLKLEELHLDDNSISTVGVEDGAF REAISLKLLFLSKNHLSSVPVGLPVDLQELRVDENRIAVI SDMAFQNLTSLERLIVDGNLLTNKGIAEGTFSHLTKLKEF SIVRNSLSHPPPDLPGTHLIRLYLQDNQINHIPLTAFANL RKLERLDISNNQLRMLTQGVFDHLSNLKQLTARNNPWFCD CSIKWVTEWLKYIPSSLNVRGFMCQGPEQVRGMAVRELNM NLLSCP G:  RELSCESYPIELRCPGTDVIMIESANYGRTDDKICDSDPA QMENIRCYLPDAYKIMSQRCNNRTQCAVVAGPDVFPDPCP GTYKYLEVQYECVPYKVEQKVFLCPGLLKGVYQSEHLFES DHQSGAWCKDPLQASDKIYYMPWTPYRTDTLTEYSSKDDF IAGRPTTTYKLPHRVDGTGFVVYDGALFFNKERTRNIVKF DLRTRIKSGEAIIANANYHDTSPYRWGGKSDIDLAVDENG LWVIYATEQNNGKIVISQLNPYTLRIEGTWDTAYDKRSAS NAFMICGILYVVKSVYEDDDNEATGNKIDYIYNTDQSKDS LVDVPFPNSYQYIAAVDYNPRDNLLYVWNNYHVVKYSLDF GPLDG H:  LCPGLLKGVYQSEHLFESDHQSGAWCKDPLQASDKIYYMP WTPYRTDTLTEYSSKDDFIAGRPTTTYKLPHRVDGTGFVV YDGALFFNKERTRNIVKFDLRTRIKSGEAIIANANYHDTS PYRWGGKSDIDLAVDENGLWVIYATEQNNGKIVISQLNPY TLRIEGTWDTAYDKRSASNAFMICGILYVVKSVYEDDDNE ATGNKIDYIYNTDQSKDSLVDVPFPNSYQYIAAVDYNPRD NLLYVWNNYHVVKYSLDFGPLDG I:  SAPGTLPHFIEEPEDAYIIKSNPIALRCKARPAMQIFFKC NGEWVHQNEHVSEESLDESSGLKVREVFINVTRQQVEDFH GPEDYWCQCVAWSHLGTSKSRKASVR J:  CPSVCRCDRNFVYCNERSLTSVPLGIPEGVTVLYLHNNQI NNAGFPAELHNVQSVHTVYLYGNQLDEFPMNLPKNVRVLH LQENNIQTISRAALAQLLKLEELHLDDNSISTVGVEDGAF REAISLKLLFLSKNHLSSVPVGLPVDLQELRVDENRIAVI SDMAFQNLTSLERLIVDGNLLTNKGIAEGTFSHLTKLKEF SIVRNSLSHPPPDLPGTHLIRLYLQDNQINHIPLTAFANL RKLERLDISNNQLRMLTQGVFDHLSNLKQLTARNNPWFCD CSIKWVTEWLKYIPSSLNVRGFMCQGPEQVRGMAVRELNM NLLSCP K:  RELSCESYPIELRCPGTDVIMIESANYGRTDDKICDSDPA QMENIRCYLPDAYKIMSQRCNNRTQCAVVAGPDVFPDPCP GTYKYLEVQYECVPYKVEQKVFLCPGLLKGVYQSEHLFES DHQSGAWCKDPLQASDKIYYMPWTPYRTDTLTEYSSKDDF IAGRPTTTYKLPHRVDGTGFVVYDGALFFNKERTRNIVKF DLRTRIKSGEAIIANANYHDTSPYRWGGKSDIDLAVDENG LWVIYATEQNNGKIVISQLNPYTLRIEGTWDTAYDKRSAS NAFMICGILYVVKSVYEDDDNEATGNKIDYIYNTDQSKDS LVDVPFPNSYQYIAAVDYNPRDNLLYVWNNYHVVKYSLDF GPLDG L:  LCPGLLKGVYQSEHLFESDHQSGAWCKDPLQASDKIYYMP WTPYRTDTLTEYSSKDDFIAGRPTTTYKLPHRVDGTGFVV YDGALFFNKERTRNIVKFDLRTRIKSGEAIIANANYHDTS PYRWGGKSDIDLAVDENGLWVIYATEQNNGKIVISQLNPY TLRIEGTWDTAYDKRSASNAFMICGILYVVKSVYEDDDNE ATGNKIDYIYNTDQSKDSLVDVPFPNSYQYIAAVDYNPRD NLLYVWNNYHVVKYSLDFGPLDG Description Functional site 1) chain C residue 332 type BINDING sequence D description BINDING => ECO:0000269|PubMed:25728924 source Swiss-Prot : SWS_FT_FI1 2) chain G residue 380 type BINDING sequence N description BINDING => ECO:0000269|PubMed:25728924 source Swiss-Prot : SWS_FT_FI1 3) chain G residue 381 type BINDING sequence A description BINDING => ECO:0000269|PubMed:25728924 source Swiss-Prot : SWS_FT_FI1 4) chain G residue 435 type BINDING sequence V description BINDING => ECO:0000269|PubMed:25728924 source Swiss-Prot : SWS_FT_FI1 5) chain H residue 332 type BINDING sequence D description BINDING => ECO:0000269|PubMed:25728924 source Swiss-Prot : SWS_FT_FI1 6) chain H residue 380 type BINDING sequence N description BINDING => ECO:0000269|PubMed:25728924 source Swiss-Prot : SWS_FT_FI1 7) chain H residue 381 type BINDING sequence A description BINDING => ECO:0000269|PubMed:25728924 source Swiss-Prot : SWS_FT_FI1 8) chain H residue 435 type BINDING sequence V description BINDING => ECO:0000269|PubMed:25728924 source Swiss-Prot : SWS_FT_FI1 9) chain K residue 332 type BINDING sequence D description BINDING => ECO:0000269|PubMed:25728924 source Swiss-Prot : SWS_FT_FI1 10) chain K residue 380 type BINDING sequence N description BINDING => ECO:0000269|PubMed:25728924 source Swiss-Prot : SWS_FT_FI1 11) chain K residue 381 type BINDING sequence A description BINDING => ECO:0000269|PubMed:25728924 source Swiss-Prot : SWS_FT_FI1 12) chain C residue 380 type BINDING sequence N description BINDING => ECO:0000269|PubMed:25728924 source Swiss-Prot : SWS_FT_FI1 13) chain K residue 435 type BINDING sequence V description BINDING => ECO:0000269|PubMed:25728924 source Swiss-Prot : SWS_FT_FI1 14) chain L residue 332 type BINDING sequence D description BINDING => ECO:0000269|PubMed:25728924 source Swiss-Prot : SWS_FT_FI1 15) chain L residue 380 type BINDING sequence N description BINDING => ECO:0000269|PubMed:25728924 source Swiss-Prot : SWS_FT_FI1 16) chain L residue 381 type BINDING sequence A description BINDING => ECO:0000269|PubMed:25728924 source Swiss-Prot : SWS_FT_FI1 17) chain L residue 435 type BINDING sequence V description BINDING => ECO:0000269|PubMed:25728924 source Swiss-Prot : SWS_FT_FI1 18) chain C residue 381 type BINDING sequence A description BINDING => ECO:0000269|PubMed:25728924 source Swiss-Prot : SWS_FT_FI1 19) chain C residue 435 type BINDING sequence V description BINDING => ECO:0000269|PubMed:25728924 source Swiss-Prot : SWS_FT_FI1 20) chain D residue 332 type BINDING sequence D description BINDING => ECO:0000269|PubMed:25728924 source Swiss-Prot : SWS_FT_FI1 21) chain D residue 380 type BINDING sequence N description BINDING => ECO:0000269|PubMed:25728924 source Swiss-Prot : SWS_FT_FI1 22) chain D residue 381 type BINDING sequence A description BINDING => ECO:0000269|PubMed:25728924 source Swiss-Prot : SWS_FT_FI1 23) chain D residue 435 type BINDING sequence V description BINDING => ECO:0000269|PubMed:25728924 source Swiss-Prot : SWS_FT_FI1 24) chain G residue 332 type BINDING sequence D description BINDING => ECO:0000269|PubMed:25728924 source Swiss-Prot : SWS_FT_FI1 25) chain C residue 161 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255, ECO:0000269|PubMed:25728924, ECO:0007744|PDB:5AFB source Swiss-Prot : SWS_FT_FI2 26) chain G residue 161 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255, ECO:0000269|PubMed:25728924, ECO:0007744|PDB:5AFB source Swiss-Prot : SWS_FT_FI2 27) chain K residue 161 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255, ECO:0000269|PubMed:25728924, ECO:0007744|PDB:5AFB source Swiss-Prot : SWS_FT_FI2 28) chain B residue 39-49 type prosite sequence VCRCDRNFVYC description PA2_ASP Phospholipase A2 aspartic acid active site. VCRCDRNFvYC source prosite : PS00119

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