eF-site ID 6u2j-ABCDEFGHIJKLMNOP PDB Code 6u2j Chain A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P Title EM structure of MPEG-1 (L425K, alpha conformation) soluble pre-pore complex Classification IMMUNE SYSTEM Compound Macrophage-expressed gene 1 protein Source (MPEG1_HUMAN) Sequence A:  EVGVQKCKNALKLPVLEVLPGGGWDNLRNVDMGRVMELTY SNCRTTEDGQYIIPDEIFTIPQKQSNLEMNSEILESWANY QSSTSYSINTELSLFSKVNGKFSTEFQRMKTLQVKDQAIT TRVQVRNLVYTVKINPTLELSSGFRKELLDISDRLENNQT RMATYLAELLVLNYGTHVTTSVDAGAALIQEDHLRASFLQ DSSRSAVTASAGLAFQNTVNFKFEENYTSQNVLTKSYLSN RTNSRVQSIGGVPFYPGITLQAWQQGITNHLVAIDRSGLP LHFFINPNMLPDLPGPLVKKVSKTVETAVKRYYTFNTYPG CTDLNSPNFNFQANTDDGSCEGKMTNFSFGGVYQECTQLS GNRDVLLCQKLEQKNPLTGDFSHLLSQIHEEGYNHLECHR KTVCEDVFQVAKAEFRAFWCLLFGGLFSSKSINPMTNAQS CPAGYFPLRLFENLKVCVSLGSRFAVPFGGFFSCTVGNPL VSLKKCPGGFSQHPALISDGCQVSYCVKSGLFTGGSLPPA RLPPFTRPPLMSQAATNTVIVTNSENARSWIKDSQTHQWR LGEPIELRRAMNVIH B:  EVGVQKCKNALKLPVLEVLPGGGWDNLRNVDMGRVMELTY SNCRTTEDGQYIIPDEIFTIPQKQSNLEMNSEILESWANY QSSTSYSINTELSLFSKVNGKFSTEFQRMKTLQVKDQAIT TRVQVRNLVYTVKINPTLELSSGFRKELLDISDRLENNQT RMATYLAELLVLNYGTHVTTSVDAGAALIQEDHLRASFLQ DSSRSAVTASAGLAFQNTVNFKFEENYTSQNVLTKSYLSN RTNSRVQSIGGVPFYPGITLQAWQQGITNHLVAIDRSGLP LHFFINPNMLPDLPGPLVKKVSKTVETAVKRYYTFNTYPG CTDLNSPNFNFQANTDDGSCEGKMTNFSFGGVYQECTQLS GNRDVLLCQKLEQKNPLTGDFSHLLSQIHEEGYNHLECHR KTVCEDVFQVAKAEFRAFWCLLFGGLFSSKSINPMTNAQS CPAGYFPLRLFENLKVCVSLGSRFAVPFGGFFSCTVGNPL VSLKKCPGGFSQHPALISDGCQVSYCVKSGLFTGGSLPPA RLPPFTRPPLMSQAATNTVIVTNSENARSWIKDSQTHQWR LGEPIELRRAMNVIH C:  EVGVQKCKNALKLPVLEVLPGGGWDNLRNVDMGRVMELTY SNCRTTEDGQYIIPDEIFTIPQKQSNLEMNSEILESWANY QSSTSYSINTELSLFSKVNGKFSTEFQRMKTLQVKDQAIT TRVQVRNLVYTVKINPTLELSSGFRKELLDISDRLENNQT RMATYLAELLVLNYGTHVTTSVDAGAALIQEDHLRASFLQ DSSRSAVTASAGLAFQNTVNFKFEENYTSQNVLTKSYLSN RTNSRVQSIGGVPFYPGITLQAWQQGITNHLVAIDRSGLP LHFFINPNMLPDLPGPLVKKVSKTVETAVKRYYTFNTYPG CTDLNSPNFNFQANTDDGSCEGKMTNFSFGGVYQECTQLS GNRDVLLCQKLEQKNPLTGDFSHLLSQIHEEGYNHLECHR KTVCEDVFQVAKAEFRAFWCLLFGGLFSSKSINPMTNAQS CPAGYFPLRLFENLKVCVSLGSRFAVPFGGFFSCTVGNPL VSLKKCPGGFSQHPALISDGCQVSYCVKSGLFTGGSLPPA RLPPFTRPPLMSQAATNTVIVTNSENARSWIKDSQTHQWR LGEPIELRRAMNVIH D:  EVGVQKCKNALKLPVLEVLPGGGWDNLRNVDMGRVMELTY SNCRTTEDGQYIIPDEIFTIPQKQSNLEMNSEILESWANY QSSTSYSINTELSLFSKVNGKFSTEFQRMKTLQVKDQAIT TRVQVRNLVYTVKINPTLELSSGFRKELLDISDRLENNQT RMATYLAELLVLNYGTHVTTSVDAGAALIQEDHLRASFLQ DSSRSAVTASAGLAFQNTVNFKFEENYTSQNVLTKSYLSN RTNSRVQSIGGVPFYPGITLQAWQQGITNHLVAIDRSGLP LHFFINPNMLPDLPGPLVKKVSKTVETAVKRYYTFNTYPG CTDLNSPNFNFQANTDDGSCEGKMTNFSFGGVYQECTQLS GNRDVLLCQKLEQKNPLTGDFSHLLSQIHEEGYNHLECHR KTVCEDVFQVAKAEFRAFWCLLFGGLFSSKSINPMTNAQS CPAGYFPLRLFENLKVCVSLGSRFAVPFGGFFSCTVGNPL VSLKKCPGGFSQHPALISDGCQVSYCVKSGLFTGGSLPPA RLPPFTRPPLMSQAATNTVIVTNSENARSWIKDSQTHQWR LGEPIELRRAMNVIH E:  EVGVQKCKNALKLPVLEVLPGGGWDNLRNVDMGRVMELTY SNCRTTEDGQYIIPDEIFTIPQKQSNLEMNSEILESWANY QSSTSYSINTELSLFSKVNGKFSTEFQRMKTLQVKDQAIT TRVQVRNLVYTVKINPTLELSSGFRKELLDISDRLENNQT RMATYLAELLVLNYGTHVTTSVDAGAALIQEDHLRASFLQ DSSRSAVTASAGLAFQNTVNFKFEENYTSQNVLTKSYLSN RTNSRVQSIGGVPFYPGITLQAWQQGITNHLVAIDRSGLP LHFFINPNMLPDLPGPLVKKVSKTVETAVKRYYTFNTYPG CTDLNSPNFNFQANTDDGSCEGKMTNFSFGGVYQECTQLS GNRDVLLCQKLEQKNPLTGDFSHLLSQIHEEGYNHLECHR KTVCEDVFQVAKAEFRAFWCLLFGGLFSSKSINPMTNAQS CPAGYFPLRLFENLKVCVSLGSRFAVPFGGFFSCTVGNPL VSLKKCPGGFSQHPALISDGCQVSYCVKSGLFTGGSLPPA RLPPFTRPPLMSQAATNTVIVTNSENARSWIKDSQTHQWR LGEPIELRRAMNVIH F:  EVGVQKCKNALKLPVLEVLPGGGWDNLRNVDMGRVMELTY SNCRTTEDGQYIIPDEIFTIPQKQSNLEMNSEILESWANY QSSTSYSINTELSLFSKVNGKFSTEFQRMKTLQVKDQAIT TRVQVRNLVYTVKINPTLELSSGFRKELLDISDRLENNQT RMATYLAELLVLNYGTHVTTSVDAGAALIQEDHLRASFLQ DSSRSAVTASAGLAFQNTVNFKFEENYTSQNVLTKSYLSN RTNSRVQSIGGVPFYPGITLQAWQQGITNHLVAIDRSGLP LHFFINPNMLPDLPGPLVKKVSKTVETAVKRYYTFNTYPG CTDLNSPNFNFQANTDDGSCEGKMTNFSFGGVYQECTQLS GNRDVLLCQKLEQKNPLTGDFSHLLSQIHEEGYNHLECHR KTVCEDVFQVAKAEFRAFWCLLFGGLFSSKSINPMTNAQS CPAGYFPLRLFENLKVCVSLGSRFAVPFGGFFSCTVGNPL VSLKKCPGGFSQHPALISDGCQVSYCVKSGLFTGGSLPPA RLPPFTRPPLMSQAATNTVIVTNSENARSWIKDSQTHQWR LGEPIELRRAMNVIH G:  EVGVQKCKNALKLPVLEVLPGGGWDNLRNVDMGRVMELTY SNCRTTEDGQYIIPDEIFTIPQKQSNLEMNSEILESWANY QSSTSYSINTELSLFSKVNGKFSTEFQRMKTLQVKDQAIT TRVQVRNLVYTVKINPTLELSSGFRKELLDISDRLENNQT RMATYLAELLVLNYGTHVTTSVDAGAALIQEDHLRASFLQ DSSRSAVTASAGLAFQNTVNFKFEENYTSQNVLTKSYLSN RTNSRVQSIGGVPFYPGITLQAWQQGITNHLVAIDRSGLP LHFFINPNMLPDLPGPLVKKVSKTVETAVKRYYTFNTYPG CTDLNSPNFNFQANTDDGSCEGKMTNFSFGGVYQECTQLS GNRDVLLCQKLEQKNPLTGDFSHLLSQIHEEGYNHLECHR KTVCEDVFQVAKAEFRAFWCLLFGGLFSSKSINPMTNAQS CPAGYFPLRLFENLKVCVSLGSRFAVPFGGFFSCTVGNPL VSLKKCPGGFSQHPALISDGCQVSYCVKSGLFTGGSLPPA RLPPFTRPPLMSQAATNTVIVTNSENARSWIKDSQTHQWR LGEPIELRRAMNVIH H:  EVGVQKCKNALKLPVLEVLPGGGWDNLRNVDMGRVMELTY SNCRTTEDGQYIIPDEIFTIPQKQSNLEMNSEILESWANY QSSTSYSINTELSLFSKVNGKFSTEFQRMKTLQVKDQAIT TRVQVRNLVYTVKINPTLELSSGFRKELLDISDRLENNQT RMATYLAELLVLNYGTHVTTSVDAGAALIQEDHLRASFLQ DSSRSAVTASAGLAFQNTVNFKFEENYTSQNVLTKSYLSN RTNSRVQSIGGVPFYPGITLQAWQQGITNHLVAIDRSGLP LHFFINPNMLPDLPGPLVKKVSKTVETAVKRYYTFNTYPG CTDLNSPNFNFQANTDDGSCEGKMTNFSFGGVYQECTQLS GNRDVLLCQKLEQKNPLTGDFSHLLSQIHEEGYNHLECHR KTVCEDVFQVAKAEFRAFWCLLFGGLFSSKSINPMTNAQS CPAGYFPLRLFENLKVCVSLGSRFAVPFGGFFSCTVGNPL VSLKKCPGGFSQHPALISDGCQVSYCVKSGLFTGGSLPPA RLPPFTRPPLMSQAATNTVIVTNSENARSWIKDSQTHQWR LGEPIELRRAMNVIH I:  EVGVQKCKNALKLPVLEVLPGGGWDNLRNVDMGRVMELTY SNCRTTEDGQYIIPDEIFTIPQKQSNLEMNSEILESWANY QSSTSYSINTELSLFSKVNGKFSTEFQRMKTLQVKDQAIT TRVQVRNLVYTVKINPTLELSSGFRKELLDISDRLENNQT RMATYLAELLVLNYGTHVTTSVDAGAALIQEDHLRASFLQ DSSRSAVTASAGLAFQNTVNFKFEENYTSQNVLTKSYLSN RTNSRVQSIGGVPFYPGITLQAWQQGITNHLVAIDRSGLP LHFFINPNMLPDLPGPLVKKVSKTVETAVKRYYTFNTYPG CTDLNSPNFNFQANTDDGSCEGKMTNFSFGGVYQECTQLS GNRDVLLCQKLEQKNPLTGDFSHLLSQIHEEGYNHLECHR KTVCEDVFQVAKAEFRAFWCLLFGGLFSSKSINPMTNAQS CPAGYFPLRLFENLKVCVSLGSRFAVPFGGFFSCTVGNPL VSLKKCPGGFSQHPALISDGCQVSYCVKSGLFTGGSLPPA RLPPFTRPPLMSQAATNTVIVTNSENARSWIKDSQTHQWR LGEPIELRRAMNVIH J:  EVGVQKCKNALKLPVLEVLPGGGWDNLRNVDMGRVMELTY SNCRTTEDGQYIIPDEIFTIPQKQSNLEMNSEILESWANY QSSTSYSINTELSLFSKVNGKFSTEFQRMKTLQVKDQAIT TRVQVRNLVYTVKINPTLELSSGFRKELLDISDRLENNQT RMATYLAELLVLNYGTHVTTSVDAGAALIQEDHLRASFLQ DSSRSAVTASAGLAFQNTVNFKFEENYTSQNVLTKSYLSN RTNSRVQSIGGVPFYPGITLQAWQQGITNHLVAIDRSGLP LHFFINPNMLPDLPGPLVKKVSKTVETAVKRYYTFNTYPG CTDLNSPNFNFQANTDDGSCEGKMTNFSFGGVYQECTQLS GNRDVLLCQKLEQKNPLTGDFSHLLSQIHEEGYNHLECHR KTVCEDVFQVAKAEFRAFWCLLFGGLFSSKSINPMTNAQS CPAGYFPLRLFENLKVCVSLGSRFAVPFGGFFSCTVGNPL VSLKKCPGGFSQHPALISDGCQVSYCVKSGLFTGGSLPPA RLPPFTRPPLMSQAATNTVIVTNSENARSWIKDSQTHQWR LGEPIELRRAMNVIH K:  EVGVQKCKNALKLPVLEVLPGGGWDNLRNVDMGRVMELTY SNCRTTEDGQYIIPDEIFTIPQKQSNLEMNSEILESWANY QSSTSYSINTELSLFSKVNGKFSTEFQRMKTLQVKDQAIT TRVQVRNLVYTVKINPTLELSSGFRKELLDISDRLENNQT RMATYLAELLVLNYGTHVTTSVDAGAALIQEDHLRASFLQ DSSRSAVTASAGLAFQNTVNFKFEENYTSQNVLTKSYLSN RTNSRVQSIGGVPFYPGITLQAWQQGITNHLVAIDRSGLP LHFFINPNMLPDLPGPLVKKVSKTVETAVKRYYTFNTYPG CTDLNSPNFNFQANTDDGSCEGKMTNFSFGGVYQECTQLS GNRDVLLCQKLEQKNPLTGDFSHLLSQIHEEGYNHLECHR KTVCEDVFQVAKAEFRAFWCLLFGGLFSSKSINPMTNAQS CPAGYFPLRLFENLKVCVSLGSRFAVPFGGFFSCTVGNPL VSLKKCPGGFSQHPALISDGCQVSYCVKSGLFTGGSLPPA RLPPFTRPPLMSQAATNTVIVTNSENARSWIKDSQTHQWR LGEPIELRRAMNVIH L:  EVGVQKCKNALKLPVLEVLPGGGWDNLRNVDMGRVMELTY SNCRTTEDGQYIIPDEIFTIPQKQSNLEMNSEILESWANY QSSTSYSINTELSLFSKVNGKFSTEFQRMKTLQVKDQAIT TRVQVRNLVYTVKINPTLELSSGFRKELLDISDRLENNQT RMATYLAELLVLNYGTHVTTSVDAGAALIQEDHLRASFLQ DSSRSAVTASAGLAFQNTVNFKFEENYTSQNVLTKSYLSN RTNSRVQSIGGVPFYPGITLQAWQQGITNHLVAIDRSGLP LHFFINPNMLPDLPGPLVKKVSKTVETAVKRYYTFNTYPG CTDLNSPNFNFQANTDDGSCEGKMTNFSFGGVYQECTQLS GNRDVLLCQKLEQKNPLTGDFSHLLSQIHEEGYNHLECHR KTVCEDVFQVAKAEFRAFWCLLFGGLFSSKSINPMTNAQS CPAGYFPLRLFENLKVCVSLGSRFAVPFGGFFSCTVGNPL VSLKKCPGGFSQHPALISDGCQVSYCVKSGLFTGGSLPPA RLPPFTRPPLMSQAATNTVIVTNSENARSWIKDSQTHQWR LGEPIELRRAMNVIH M:  EVGVQKCKNALKLPVLEVLPGGGWDNLRNVDMGRVMELTY SNCRTTEDGQYIIPDEIFTIPQKQSNLEMNSEILESWANY QSSTSYSINTELSLFSKVNGKFSTEFQRMKTLQVKDQAIT TRVQVRNLVYTVKINPTLELSSGFRKELLDISDRLENNQT RMATYLAELLVLNYGTHVTTSVDAGAALIQEDHLRASFLQ DSSRSAVTASAGLAFQNTVNFKFEENYTSQNVLTKSYLSN RTNSRVQSIGGVPFYPGITLQAWQQGITNHLVAIDRSGLP LHFFINPNMLPDLPGPLVKKVSKTVETAVKRYYTFNTYPG CTDLNSPNFNFQANTDDGSCEGKMTNFSFGGVYQECTQLS GNRDVLLCQKLEQKNPLTGDFSHLLSQIHEEGYNHLECHR KTVCEDVFQVAKAEFRAFWCLLFGGLFSSKSINPMTNAQS CPAGYFPLRLFENLKVCVSLGSRFAVPFGGFFSCTVGNPL VSLKKCPGGFSQHPALISDGCQVSYCVKSGLFTGGSLPPA RLPPFTRPPLMSQAATNTVIVTNSENARSWIKDSQTHQWR LGEPIELRRAMNVIH N:  EVGVQKCKNALKLPVLEVLPGGGWDNLRNVDMGRVMELTY SNCRTTEDGQYIIPDEIFTIPQKQSNLEMNSEILESWANY QSSTSYSINTELSLFSKVNGKFSTEFQRMKTLQVKDQAIT TRVQVRNLVYTVKINPTLELSSGFRKELLDISDRLENNQT RMATYLAELLVLNYGTHVTTSVDAGAALIQEDHLRASFLQ DSSRSAVTASAGLAFQNTVNFKFEENYTSQNVLTKSYLSN RTNSRVQSIGGVPFYPGITLQAWQQGITNHLVAIDRSGLP LHFFINPNMLPDLPGPLVKKVSKTVETAVKRYYTFNTYPG CTDLNSPNFNFQANTDDGSCEGKMTNFSFGGVYQECTQLS GNRDVLLCQKLEQKNPLTGDFSHLLSQIHEEGYNHLECHR KTVCEDVFQVAKAEFRAFWCLLFGGLFSSKSINPMTNAQS CPAGYFPLRLFENLKVCVSLGSRFAVPFGGFFSCTVGNPL VSLKKCPGGFSQHPALISDGCQVSYCVKSGLFTGGSLPPA RLPPFTRPPLMSQAATNTVIVTNSENARSWIKDSQTHQWR LGEPIELRRAMNVIH O:  EVGVQKCKNALKLPVLEVLPGGGWDNLRNVDMGRVMELTY SNCRTTEDGQYIIPDEIFTIPQKQSNLEMNSEILESWANY QSSTSYSINTELSLFSKVNGKFSTEFQRMKTLQVKDQAIT TRVQVRNLVYTVKINPTLELSSGFRKELLDISDRLENNQT RMATYLAELLVLNYGTHVTTSVDAGAALIQEDHLRASFLQ DSSRSAVTASAGLAFQNTVNFKFEENYTSQNVLTKSYLSN RTNSRVQSIGGVPFYPGITLQAWQQGITNHLVAIDRSGLP LHFFINPNMLPDLPGPLVKKVSKTVETAVKRYYTFNTYPG CTDLNSPNFNFQANTDDGSCEGKMTNFSFGGVYQECTQLS GNRDVLLCQKLEQKNPLTGDFSHLLSQIHEEGYNHLECHR KTVCEDVFQVAKAEFRAFWCLLFGGLFSSKSINPMTNAQS CPAGYFPLRLFENLKVCVSLGSRFAVPFGGFFSCTVGNPL VSLKKCPGGFSQHPALISDGCQVSYCVKSGLFTGGSLPPA RLPPFTRPPLMSQAATNTVIVTNSENARSWIKDSQTHQWR LGEPIELRRAMNVIH P:  EVGVQKCKNALKLPVLEVLPGGGWDNLRNVDMGRVMELTY SNCRTTEDGQYIIPDEIFTIPQKQSNLEMNSEILESWANY QSSTSYSINTELSLFSKVNGKFSTEFQRMKTLQVKDQAIT TRVQVRNLVYTVKINPTLELSSGFRKELLDISDRLENNQT RMATYLAELLVLNYGTHVTTSVDAGAALIQEDHLRASFLQ DSSRSAVTASAGLAFQNTVNFKFEENYTSQNVLTKSYLSN RTNSRVQSIGGVPFYPGITLQAWQQGITNHLVAIDRSGLP LHFFINPNMLPDLPGPLVKKVSKTVETAVKRYYTFNTYPG CTDLNSPNFNFQANTDDGSCEGKMTNFSFGGVYQECTQLS GNRDVLLCQKLEQKNPLTGDFSHLLSQIHEEGYNHLECHR KTVCEDVFQVAKAEFRAFWCLLFGGLFSSKSINPMTNAQS CPAGYFPLRLFENLKVCVSLGSRFAVPFGGFFSCTVGNPL VSLKKCPGGFSQHPALISDGCQVSYCVKSGLFTGGSLPPA RLPPFTRPPLMSQAATNTVIVTNSENARSWIKDSQTHQWR LGEPIELRRAMNVIH Description (1)  Macrophage-expressed gene 1 protein Functional site 1) chain A residue 335 type SITE sequence D description Cleavage; by LGMN => ECO:0000250|UniProtKB:A1L314 source Swiss-Prot : SWS_FT_FI2 2) chain D residue 335 type SITE sequence D description Cleavage; by LGMN => ECO:0000250|UniProtKB:A1L314 source Swiss-Prot : SWS_FT_FI2 3) chain D residue 340 type SITE sequence N description Cleavage; by LGMN => ECO:0000250|UniProtKB:A1L314 source Swiss-Prot : SWS_FT_FI2 4) chain D residue 342 type SITE sequence N description Cleavage; by LGMN => ECO:0000250|UniProtKB:A1L314 source Swiss-Prot : SWS_FT_FI2 5) chain E residue 335 type SITE sequence D description Cleavage; by LGMN => ECO:0000250|UniProtKB:A1L314 source Swiss-Prot : SWS_FT_FI2 6) chain E residue 340 type SITE sequence N description Cleavage; by LGMN => ECO:0000250|UniProtKB:A1L314 source Swiss-Prot : SWS_FT_FI2 7) chain E residue 342 type SITE sequence N description Cleavage; by LGMN => ECO:0000250|UniProtKB:A1L314 source Swiss-Prot : SWS_FT_FI2 8) chain F residue 335 type SITE sequence D description Cleavage; by LGMN => ECO:0000250|UniProtKB:A1L314 source Swiss-Prot : SWS_FT_FI2 9) chain F residue 340 type SITE sequence N description Cleavage; by LGMN => ECO:0000250|UniProtKB:A1L314 source Swiss-Prot : SWS_FT_FI2 10) chain F residue 342 type SITE sequence N description Cleavage; by LGMN => ECO:0000250|UniProtKB:A1L314 source Swiss-Prot : SWS_FT_FI2 11) chain G residue 335 type SITE sequence D description Cleavage; by LGMN => ECO:0000250|UniProtKB:A1L314 source Swiss-Prot : SWS_FT_FI2 12) chain A residue 340 type SITE sequence N description Cleavage; by LGMN => ECO:0000250|UniProtKB:A1L314 source Swiss-Prot : SWS_FT_FI2 13) chain G residue 340 type SITE sequence N description Cleavage; by LGMN => ECO:0000250|UniProtKB:A1L314 source Swiss-Prot : SWS_FT_FI2 14) chain G residue 342 type SITE sequence N description Cleavage; by LGMN => ECO:0000250|UniProtKB:A1L314 source Swiss-Prot : SWS_FT_FI2 15) chain H residue 335 type SITE sequence D description Cleavage; by LGMN => ECO:0000250|UniProtKB:A1L314 source Swiss-Prot : SWS_FT_FI2 16) chain H residue 340 type SITE sequence N description Cleavage; by LGMN => ECO:0000250|UniProtKB:A1L314 source Swiss-Prot : SWS_FT_FI2 17) chain H residue 342 type SITE sequence N description Cleavage; by LGMN => ECO:0000250|UniProtKB:A1L314 source Swiss-Prot : SWS_FT_FI2 18) chain I residue 335 type SITE sequence D description Cleavage; by LGMN => ECO:0000250|UniProtKB:A1L314 source Swiss-Prot : SWS_FT_FI2 19) chain I residue 340 type SITE sequence N description Cleavage; by LGMN => ECO:0000250|UniProtKB:A1L314 source Swiss-Prot : SWS_FT_FI2 20) chain I residue 342 type SITE sequence N description Cleavage; by LGMN => ECO:0000250|UniProtKB:A1L314 source Swiss-Prot : SWS_FT_FI2 21) chain J residue 335 type SITE sequence D description Cleavage; by LGMN => ECO:0000250|UniProtKB:A1L314 source Swiss-Prot : SWS_FT_FI2 22) chain J residue 340 type SITE sequence N description Cleavage; by LGMN => ECO:0000250|UniProtKB:A1L314 source Swiss-Prot : SWS_FT_FI2 23) chain A residue 342 type SITE sequence N description Cleavage; by LGMN => ECO:0000250|UniProtKB:A1L314 source Swiss-Prot : SWS_FT_FI2 24) chain J residue 342 type SITE sequence N description Cleavage; by LGMN => ECO:0000250|UniProtKB:A1L314 source Swiss-Prot : SWS_FT_FI2 25) chain K residue 335 type SITE sequence D description Cleavage; by LGMN => ECO:0000250|UniProtKB:A1L314 source Swiss-Prot : SWS_FT_FI2 26) chain K residue 340 type SITE sequence N description Cleavage; by LGMN => ECO:0000250|UniProtKB:A1L314 source Swiss-Prot : SWS_FT_FI2 27) chain K residue 342 type SITE sequence N description Cleavage; by LGMN => ECO:0000250|UniProtKB:A1L314 source Swiss-Prot : SWS_FT_FI2 28) chain L residue 335 type SITE sequence D description Cleavage; by LGMN => ECO:0000250|UniProtKB:A1L314 source Swiss-Prot : SWS_FT_FI2 29) chain L residue 340 type SITE sequence N description Cleavage; by LGMN => ECO:0000250|UniProtKB:A1L314 source Swiss-Prot : SWS_FT_FI2 30) chain L residue 342 type SITE sequence N description Cleavage; by LGMN => ECO:0000250|UniProtKB:A1L314 source Swiss-Prot : SWS_FT_FI2 31) chain M residue 335 type SITE sequence D description Cleavage; by LGMN => ECO:0000250|UniProtKB:A1L314 source Swiss-Prot : SWS_FT_FI2 32) chain M residue 340 type SITE sequence N description Cleavage; by LGMN => ECO:0000250|UniProtKB:A1L314 source Swiss-Prot : SWS_FT_FI2 33) chain M residue 342 type SITE sequence N description Cleavage; by LGMN => ECO:0000250|UniProtKB:A1L314 source Swiss-Prot : SWS_FT_FI2 34) chain B residue 335 type SITE sequence D description Cleavage; by LGMN => ECO:0000250|UniProtKB:A1L314 source Swiss-Prot : SWS_FT_FI2 35) chain N residue 335 type SITE sequence D description Cleavage; by LGMN => ECO:0000250|UniProtKB:A1L314 source Swiss-Prot : SWS_FT_FI2 36) chain N residue 340 type SITE sequence N description Cleavage; by LGMN => ECO:0000250|UniProtKB:A1L314 source Swiss-Prot : SWS_FT_FI2 37) chain N residue 342 type SITE sequence N description Cleavage; by LGMN => ECO:0000250|UniProtKB:A1L314 source Swiss-Prot : SWS_FT_FI2 38) chain O residue 335 type SITE sequence D description Cleavage; by LGMN => ECO:0000250|UniProtKB:A1L314 source Swiss-Prot : SWS_FT_FI2 39) chain O residue 340 type SITE sequence N description Cleavage; by LGMN => ECO:0000250|UniProtKB:A1L314 source Swiss-Prot : SWS_FT_FI2 40) chain O residue 342 type SITE sequence N description Cleavage; by LGMN => ECO:0000250|UniProtKB:A1L314 source Swiss-Prot : SWS_FT_FI2 41) chain P residue 335 type SITE sequence D description Cleavage; by LGMN => ECO:0000250|UniProtKB:A1L314 source Swiss-Prot : SWS_FT_FI2 42) chain P residue 340 type SITE sequence N description Cleavage; by LGMN => ECO:0000250|UniProtKB:A1L314 source Swiss-Prot : SWS_FT_FI2 43) chain P residue 342 type SITE sequence N description Cleavage; by LGMN => ECO:0000250|UniProtKB:A1L314 source Swiss-Prot : SWS_FT_FI2 44) chain B residue 340 type SITE sequence N description Cleavage; by LGMN => ECO:0000250|UniProtKB:A1L314 source Swiss-Prot : SWS_FT_FI2 45) chain B residue 342 type SITE sequence N description Cleavage; by LGMN => ECO:0000250|UniProtKB:A1L314 source Swiss-Prot : SWS_FT_FI2 46) chain C residue 335 type SITE sequence D description Cleavage; by LGMN => ECO:0000250|UniProtKB:A1L314 source Swiss-Prot : SWS_FT_FI2 47) chain C residue 340 type SITE sequence N description Cleavage; by LGMN => ECO:0000250|UniProtKB:A1L314 source Swiss-Prot : SWS_FT_FI2 48) chain C residue 342 type SITE sequence N description Cleavage; by LGMN => ECO:0000250|UniProtKB:A1L314 source Swiss-Prot : SWS_FT_FI2 49) chain A residue 614 type SITE sequence R description Cleavage; by trypsin => ECO:0000250|UniProtKB:A1L314 source Swiss-Prot : SWS_FT_FI3 50) chain J residue 614 type SITE sequence R description Cleavage; by trypsin => ECO:0000250|UniProtKB:A1L314 source Swiss-Prot : SWS_FT_FI3 51) chain K residue 614 type SITE sequence R description Cleavage; by trypsin => ECO:0000250|UniProtKB:A1L314 source Swiss-Prot : SWS_FT_FI3 52) chain L residue 614 type SITE sequence R description Cleavage; by trypsin => ECO:0000250|UniProtKB:A1L314 source Swiss-Prot : SWS_FT_FI3 53) chain M residue 614 type SITE sequence R description Cleavage; by trypsin => ECO:0000250|UniProtKB:A1L314 source Swiss-Prot : SWS_FT_FI3 54) chain N residue 614 type SITE sequence R description Cleavage; by trypsin => ECO:0000250|UniProtKB:A1L314 source Swiss-Prot : SWS_FT_FI3 55) chain O residue 614 type SITE sequence R description Cleavage; by trypsin => ECO:0000250|UniProtKB:A1L314 source Swiss-Prot : SWS_FT_FI3 56) chain P residue 614 type SITE sequence R description Cleavage; by trypsin => ECO:0000250|UniProtKB:A1L314 source Swiss-Prot : SWS_FT_FI3 57) chain B residue 614 type SITE sequence R description Cleavage; by trypsin => ECO:0000250|UniProtKB:A1L314 source Swiss-Prot : SWS_FT_FI3 58) chain C residue 614 type SITE sequence R description Cleavage; by trypsin => ECO:0000250|UniProtKB:A1L314 source Swiss-Prot : SWS_FT_FI3 59) chain D residue 614 type SITE sequence R description Cleavage; by trypsin => ECO:0000250|UniProtKB:A1L314 source Swiss-Prot : SWS_FT_FI3 60) chain E residue 614 type SITE sequence R description Cleavage; by trypsin => ECO:0000250|UniProtKB:A1L314 source Swiss-Prot : SWS_FT_FI3 61) chain F residue 614 type SITE sequence R description Cleavage; by trypsin => ECO:0000250|UniProtKB:A1L314 source Swiss-Prot : SWS_FT_FI3 62) chain G residue 614 type SITE sequence R description Cleavage; by trypsin => ECO:0000250|UniProtKB:A1L314 source Swiss-Prot : SWS_FT_FI3 63) chain H residue 614 type SITE sequence R description Cleavage; by trypsin => ECO:0000250|UniProtKB:A1L314 source Swiss-Prot : SWS_FT_FI3 64) chain I residue 614 type SITE sequence R description Cleavage; by trypsin => ECO:0000250|UniProtKB:A1L314 source Swiss-Prot : SWS_FT_FI3 65) chain A residue 168 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:31537793, ECO:0007744|PDB:6U23, ECO:0007744|PDB:6U2J, ECO:0007744|PDB:6U2K, ECO:0007744|PDB:6U2L, ECO:0007744|PDB:6U2W source Swiss-Prot : SWS_FT_FI4 66) chain E residue 252 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:31537793, ECO:0007744|PDB:6U23, ECO:0007744|PDB:6U2J, ECO:0007744|PDB:6U2K, ECO:0007744|PDB:6U2L, ECO:0007744|PDB:6U2W source Swiss-Prot : SWS_FT_FI4 67) chain F residue 168 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:31537793, ECO:0007744|PDB:6U23, ECO:0007744|PDB:6U2J, ECO:0007744|PDB:6U2K, ECO:0007744|PDB:6U2L, ECO:0007744|PDB:6U2W source Swiss-Prot : SWS_FT_FI4 68) chain F residue 252 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:31537793, ECO:0007744|PDB:6U23, ECO:0007744|PDB:6U2J, ECO:0007744|PDB:6U2K, ECO:0007744|PDB:6U2L, ECO:0007744|PDB:6U2W source Swiss-Prot : SWS_FT_FI4 69) chain G residue 168 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:31537793, ECO:0007744|PDB:6U23, ECO:0007744|PDB:6U2J, ECO:0007744|PDB:6U2K, ECO:0007744|PDB:6U2L, ECO:0007744|PDB:6U2W source Swiss-Prot : SWS_FT_FI4 70) chain G residue 252 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:31537793, ECO:0007744|PDB:6U23, ECO:0007744|PDB:6U2J, ECO:0007744|PDB:6U2K, ECO:0007744|PDB:6U2L, ECO:0007744|PDB:6U2W source Swiss-Prot : SWS_FT_FI4 71) chain H residue 168 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:31537793, ECO:0007744|PDB:6U23, ECO:0007744|PDB:6U2J, ECO:0007744|PDB:6U2K, ECO:0007744|PDB:6U2L, ECO:0007744|PDB:6U2W source Swiss-Prot : SWS_FT_FI4 72) chain H residue 252 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:31537793, ECO:0007744|PDB:6U23, ECO:0007744|PDB:6U2J, ECO:0007744|PDB:6U2K, ECO:0007744|PDB:6U2L, ECO:0007744|PDB:6U2W source Swiss-Prot : SWS_FT_FI4 73) chain I residue 168 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:31537793, ECO:0007744|PDB:6U23, ECO:0007744|PDB:6U2J, ECO:0007744|PDB:6U2K, ECO:0007744|PDB:6U2L, ECO:0007744|PDB:6U2W source Swiss-Prot : SWS_FT_FI4 74) chain I residue 252 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:31537793, ECO:0007744|PDB:6U23, ECO:0007744|PDB:6U2J, ECO:0007744|PDB:6U2K, ECO:0007744|PDB:6U2L, ECO:0007744|PDB:6U2W source Swiss-Prot : SWS_FT_FI4 75) chain J residue 168 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:31537793, ECO:0007744|PDB:6U23, ECO:0007744|PDB:6U2J, ECO:0007744|PDB:6U2K, ECO:0007744|PDB:6U2L, ECO:0007744|PDB:6U2W source Swiss-Prot : SWS_FT_FI4 76) chain A residue 252 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:31537793, ECO:0007744|PDB:6U23, ECO:0007744|PDB:6U2J, ECO:0007744|PDB:6U2K, ECO:0007744|PDB:6U2L, ECO:0007744|PDB:6U2W source Swiss-Prot : SWS_FT_FI4 77) chain J residue 252 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:31537793, ECO:0007744|PDB:6U23, ECO:0007744|PDB:6U2J, ECO:0007744|PDB:6U2K, ECO:0007744|PDB:6U2L, ECO:0007744|PDB:6U2W source Swiss-Prot : SWS_FT_FI4 78) chain K residue 168 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:31537793, ECO:0007744|PDB:6U23, ECO:0007744|PDB:6U2J, ECO:0007744|PDB:6U2K, ECO:0007744|PDB:6U2L, ECO:0007744|PDB:6U2W source Swiss-Prot : SWS_FT_FI4 79) chain K residue 252 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:31537793, ECO:0007744|PDB:6U23, ECO:0007744|PDB:6U2J, ECO:0007744|PDB:6U2K, ECO:0007744|PDB:6U2L, ECO:0007744|PDB:6U2W source Swiss-Prot : SWS_FT_FI4 80) chain L residue 168 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:31537793, ECO:0007744|PDB:6U23, ECO:0007744|PDB:6U2J, ECO:0007744|PDB:6U2K, ECO:0007744|PDB:6U2L, ECO:0007744|PDB:6U2W source Swiss-Prot : SWS_FT_FI4 81) chain L residue 252 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:31537793, ECO:0007744|PDB:6U23, ECO:0007744|PDB:6U2J, ECO:0007744|PDB:6U2K, ECO:0007744|PDB:6U2L, ECO:0007744|PDB:6U2W source Swiss-Prot : SWS_FT_FI4 82) chain M residue 168 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:31537793, ECO:0007744|PDB:6U23, ECO:0007744|PDB:6U2J, ECO:0007744|PDB:6U2K, ECO:0007744|PDB:6U2L, ECO:0007744|PDB:6U2W source Swiss-Prot : SWS_FT_FI4 83) chain M residue 252 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:31537793, ECO:0007744|PDB:6U23, ECO:0007744|PDB:6U2J, ECO:0007744|PDB:6U2K, ECO:0007744|PDB:6U2L, ECO:0007744|PDB:6U2W source Swiss-Prot : SWS_FT_FI4 84) chain N residue 168 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:31537793, ECO:0007744|PDB:6U23, ECO:0007744|PDB:6U2J, ECO:0007744|PDB:6U2K, ECO:0007744|PDB:6U2L, ECO:0007744|PDB:6U2W source Swiss-Prot : SWS_FT_FI4 85) chain N residue 252 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:31537793, ECO:0007744|PDB:6U23, ECO:0007744|PDB:6U2J, ECO:0007744|PDB:6U2K, ECO:0007744|PDB:6U2L, ECO:0007744|PDB:6U2W source Swiss-Prot : SWS_FT_FI4 86) chain O residue 168 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:31537793, ECO:0007744|PDB:6U23, ECO:0007744|PDB:6U2J, ECO:0007744|PDB:6U2K, ECO:0007744|PDB:6U2L, ECO:0007744|PDB:6U2W source Swiss-Prot : SWS_FT_FI4 87) chain B residue 168 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:31537793, ECO:0007744|PDB:6U23, ECO:0007744|PDB:6U2J, ECO:0007744|PDB:6U2K, ECO:0007744|PDB:6U2L, ECO:0007744|PDB:6U2W source Swiss-Prot : SWS_FT_FI4 88) chain O residue 252 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:31537793, ECO:0007744|PDB:6U23, ECO:0007744|PDB:6U2J, ECO:0007744|PDB:6U2K, ECO:0007744|PDB:6U2L, ECO:0007744|PDB:6U2W source Swiss-Prot : SWS_FT_FI4 89) chain P residue 168 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:31537793, ECO:0007744|PDB:6U23, ECO:0007744|PDB:6U2J, ECO:0007744|PDB:6U2K, ECO:0007744|PDB:6U2L, ECO:0007744|PDB:6U2W source Swiss-Prot : SWS_FT_FI4 90) chain P residue 252 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:31537793, ECO:0007744|PDB:6U23, ECO:0007744|PDB:6U2J, ECO:0007744|PDB:6U2K, ECO:0007744|PDB:6U2L, ECO:0007744|PDB:6U2W source Swiss-Prot : SWS_FT_FI4 91) chain B residue 252 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:31537793, ECO:0007744|PDB:6U23, ECO:0007744|PDB:6U2J, ECO:0007744|PDB:6U2K, ECO:0007744|PDB:6U2L, ECO:0007744|PDB:6U2W source Swiss-Prot : SWS_FT_FI4 92) chain C residue 168 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:31537793, ECO:0007744|PDB:6U23, ECO:0007744|PDB:6U2J, ECO:0007744|PDB:6U2K, ECO:0007744|PDB:6U2L, ECO:0007744|PDB:6U2W source Swiss-Prot : SWS_FT_FI4 93) chain C residue 252 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:31537793, ECO:0007744|PDB:6U23, ECO:0007744|PDB:6U2J, ECO:0007744|PDB:6U2K, ECO:0007744|PDB:6U2L, ECO:0007744|PDB:6U2W source Swiss-Prot : SWS_FT_FI4 94) chain D residue 168 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:31537793, ECO:0007744|PDB:6U23, ECO:0007744|PDB:6U2J, ECO:0007744|PDB:6U2K, ECO:0007744|PDB:6U2L, ECO:0007744|PDB:6U2W source Swiss-Prot : SWS_FT_FI4 95) chain D residue 252 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:31537793, ECO:0007744|PDB:6U23, ECO:0007744|PDB:6U2J, ECO:0007744|PDB:6U2K, ECO:0007744|PDB:6U2L, ECO:0007744|PDB:6U2W source Swiss-Prot : SWS_FT_FI4 96) chain E residue 168 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:31537793, ECO:0007744|PDB:6U23, ECO:0007744|PDB:6U2J, ECO:0007744|PDB:6U2K, ECO:0007744|PDB:6U2L, ECO:0007744|PDB:6U2W source Swiss-Prot : SWS_FT_FI4 97) chain A residue 358 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI5 98) chain J residue 358 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI5 99) chain K residue 358 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI5 100) chain L residue 358 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI5 101) chain M residue 358 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI5 102) chain N residue 358 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI5 103) chain O residue 358 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI5 104) chain P residue 358 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI5 105) chain B residue 358 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI5 106) chain C residue 358 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI5 107) chain D residue 358 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI5 108) chain E residue 358 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI5 109) chain F residue 358 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI5 110) chain G residue 358 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI5 111) chain H residue 358 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI5 112) chain I residue 358 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI5 113) chain A residue 96-103 type TRANSMEM sequence YSINTELS description Beta stranded => ECO:0000250|UniProtKB:A1L314 source Swiss-Prot : SWS_FT_FI1 114) chain C residue 110-115 type TRANSMEM sequence GKFSTE description Beta stranded => ECO:0000250|UniProtKB:A1L314 source Swiss-Prot : SWS_FT_FI1 115) chain C residue 218-227 type TRANSMEM sequence AVTASAGLAF description Beta stranded => ECO:0000250|UniProtKB:A1L314 source Swiss-Prot : SWS_FT_FI1 116) chain C residue 231-239 type TRANSMEM sequence VNFKFEENY description Beta stranded => ECO:0000250|UniProtKB:A1L314 source Swiss-Prot : SWS_FT_FI1 117) chain D residue 96-103 type TRANSMEM sequence YSINTELS description Beta stranded => ECO:0000250|UniProtKB:A1L314 source Swiss-Prot : SWS_FT_FI1 118) chain D residue 110-115 type TRANSMEM sequence GKFSTE description Beta stranded => ECO:0000250|UniProtKB:A1L314 source Swiss-Prot : SWS_FT_FI1 119) chain D residue 218-227 type TRANSMEM sequence AVTASAGLAF description Beta stranded => ECO:0000250|UniProtKB:A1L314 source Swiss-Prot : SWS_FT_FI1 120) chain D residue 231-239 type TRANSMEM sequence VNFKFEENY description Beta stranded => ECO:0000250|UniProtKB:A1L314 source Swiss-Prot : SWS_FT_FI1 121) chain E residue 96-103 type TRANSMEM sequence YSINTELS description Beta stranded => ECO:0000250|UniProtKB:A1L314 source Swiss-Prot : SWS_FT_FI1 122) chain E residue 110-115 type TRANSMEM sequence GKFSTE description Beta stranded => ECO:0000250|UniProtKB:A1L314 source Swiss-Prot : SWS_FT_FI1 123) chain E residue 218-227 type TRANSMEM sequence AVTASAGLAF description Beta stranded => ECO:0000250|UniProtKB:A1L314 source Swiss-Prot : SWS_FT_FI1 124) chain A residue 110-115 type TRANSMEM sequence GKFSTE description Beta stranded => ECO:0000250|UniProtKB:A1L314 source Swiss-Prot : SWS_FT_FI1 125) chain E residue 231-239 type TRANSMEM sequence VNFKFEENY description Beta stranded => ECO:0000250|UniProtKB:A1L314 source Swiss-Prot : SWS_FT_FI1 126) chain F residue 96-103 type TRANSMEM sequence YSINTELS description Beta stranded => ECO:0000250|UniProtKB:A1L314 source Swiss-Prot : SWS_FT_FI1 127) chain F residue 110-115 type TRANSMEM sequence GKFSTE description Beta stranded => ECO:0000250|UniProtKB:A1L314 source Swiss-Prot : SWS_FT_FI1 128) chain F residue 218-227 type TRANSMEM sequence AVTASAGLAF description Beta stranded => ECO:0000250|UniProtKB:A1L314 source Swiss-Prot : SWS_FT_FI1 129) chain F residue 231-239 type TRANSMEM sequence VNFKFEENY description Beta stranded => ECO:0000250|UniProtKB:A1L314 source Swiss-Prot : SWS_FT_FI1 130) chain G residue 96-103 type TRANSMEM sequence YSINTELS description Beta stranded => ECO:0000250|UniProtKB:A1L314 source Swiss-Prot : SWS_FT_FI1 131) chain G residue 110-115 type TRANSMEM sequence GKFSTE description Beta stranded => ECO:0000250|UniProtKB:A1L314 source Swiss-Prot : SWS_FT_FI1 132) chain G residue 218-227 type TRANSMEM sequence AVTASAGLAF description Beta stranded => ECO:0000250|UniProtKB:A1L314 source Swiss-Prot : SWS_FT_FI1 133) chain G residue 231-239 type TRANSMEM sequence VNFKFEENY description Beta stranded => ECO:0000250|UniProtKB:A1L314 source Swiss-Prot : SWS_FT_FI1 134) chain H residue 96-103 type TRANSMEM sequence YSINTELS description Beta stranded => ECO:0000250|UniProtKB:A1L314 source Swiss-Prot : SWS_FT_FI1 135) chain A residue 218-227 type TRANSMEM sequence AVTASAGLAF description Beta stranded => ECO:0000250|UniProtKB:A1L314 source Swiss-Prot : SWS_FT_FI1 136) chain H residue 110-115 type TRANSMEM sequence GKFSTE description Beta stranded => ECO:0000250|UniProtKB:A1L314 source Swiss-Prot : SWS_FT_FI1 137) chain H residue 218-227 type TRANSMEM sequence AVTASAGLAF description Beta stranded => ECO:0000250|UniProtKB:A1L314 source Swiss-Prot : SWS_FT_FI1 138) chain H residue 231-239 type TRANSMEM sequence VNFKFEENY description Beta stranded => ECO:0000250|UniProtKB:A1L314 source Swiss-Prot : SWS_FT_FI1 139) chain I residue 96-103 type TRANSMEM sequence YSINTELS description Beta stranded => ECO:0000250|UniProtKB:A1L314 source Swiss-Prot : SWS_FT_FI1 140) chain I residue 110-115 type TRANSMEM sequence GKFSTE description Beta stranded => ECO:0000250|UniProtKB:A1L314 source Swiss-Prot : SWS_FT_FI1 141) chain I residue 218-227 type TRANSMEM sequence AVTASAGLAF description Beta stranded => ECO:0000250|UniProtKB:A1L314 source Swiss-Prot : SWS_FT_FI1 142) chain I residue 231-239 type TRANSMEM sequence VNFKFEENY description Beta stranded => ECO:0000250|UniProtKB:A1L314 source Swiss-Prot : SWS_FT_FI1 143) chain J residue 96-103 type TRANSMEM sequence YSINTELS description Beta stranded => ECO:0000250|UniProtKB:A1L314 source Swiss-Prot : SWS_FT_FI1 144) chain J residue 110-115 type TRANSMEM sequence GKFSTE description Beta stranded => ECO:0000250|UniProtKB:A1L314 source Swiss-Prot : SWS_FT_FI1 145) chain J residue 218-227 type TRANSMEM sequence AVTASAGLAF description Beta stranded => ECO:0000250|UniProtKB:A1L314 source Swiss-Prot : SWS_FT_FI1 146) chain A residue 231-239 type TRANSMEM sequence VNFKFEENY description Beta stranded => ECO:0000250|UniProtKB:A1L314 source Swiss-Prot : SWS_FT_FI1 147) chain J residue 231-239 type TRANSMEM sequence VNFKFEENY description Beta stranded => ECO:0000250|UniProtKB:A1L314 source Swiss-Prot : SWS_FT_FI1 148) chain K residue 96-103 type TRANSMEM sequence YSINTELS description Beta stranded => ECO:0000250|UniProtKB:A1L314 source Swiss-Prot : SWS_FT_FI1 149) chain K residue 110-115 type TRANSMEM sequence GKFSTE description Beta stranded => ECO:0000250|UniProtKB:A1L314 source Swiss-Prot : SWS_FT_FI1 150) chain K residue 218-227 type TRANSMEM sequence AVTASAGLAF description Beta stranded => ECO:0000250|UniProtKB:A1L314 source Swiss-Prot : SWS_FT_FI1 151) chain K residue 231-239 type TRANSMEM sequence VNFKFEENY description Beta stranded => ECO:0000250|UniProtKB:A1L314 source Swiss-Prot : SWS_FT_FI1 152) chain L residue 96-103 type TRANSMEM sequence YSINTELS description Beta stranded => ECO:0000250|UniProtKB:A1L314 source Swiss-Prot : SWS_FT_FI1 153) chain L residue 110-115 type TRANSMEM sequence GKFSTE description Beta stranded => ECO:0000250|UniProtKB:A1L314 source Swiss-Prot : SWS_FT_FI1 154) chain L residue 218-227 type TRANSMEM sequence AVTASAGLAF description Beta stranded => ECO:0000250|UniProtKB:A1L314 source Swiss-Prot : SWS_FT_FI1 155) chain L residue 231-239 type TRANSMEM sequence VNFKFEENY description Beta stranded => ECO:0000250|UniProtKB:A1L314 source Swiss-Prot : SWS_FT_FI1 156) chain M residue 96-103 type TRANSMEM sequence YSINTELS description Beta stranded => ECO:0000250|UniProtKB:A1L314 source Swiss-Prot : SWS_FT_FI1 157) chain B residue 96-103 type TRANSMEM sequence YSINTELS description Beta stranded => ECO:0000250|UniProtKB:A1L314 source Swiss-Prot : SWS_FT_FI1 158) chain M residue 110-115 type TRANSMEM sequence GKFSTE description Beta stranded => ECO:0000250|UniProtKB:A1L314 source Swiss-Prot : SWS_FT_FI1 159) chain M residue 218-227 type TRANSMEM sequence AVTASAGLAF description Beta stranded => ECO:0000250|UniProtKB:A1L314 source Swiss-Prot : SWS_FT_FI1 160) chain M residue 231-239 type TRANSMEM sequence VNFKFEENY description Beta stranded => ECO:0000250|UniProtKB:A1L314 source Swiss-Prot : SWS_FT_FI1 161) chain N residue 96-103 type TRANSMEM sequence YSINTELS description Beta stranded => ECO:0000250|UniProtKB:A1L314 source Swiss-Prot : SWS_FT_FI1 162) chain N residue 110-115 type TRANSMEM sequence GKFSTE description Beta stranded => ECO:0000250|UniProtKB:A1L314 source Swiss-Prot : SWS_FT_FI1 163) chain N residue 218-227 type TRANSMEM sequence AVTASAGLAF description Beta stranded => ECO:0000250|UniProtKB:A1L314 source Swiss-Prot : SWS_FT_FI1 164) chain N residue 231-239 type TRANSMEM sequence VNFKFEENY description Beta stranded => ECO:0000250|UniProtKB:A1L314 source Swiss-Prot : SWS_FT_FI1 165) chain O residue 96-103 type TRANSMEM sequence YSINTELS description Beta stranded => ECO:0000250|UniProtKB:A1L314 source Swiss-Prot : SWS_FT_FI1 166) chain O residue 110-115 type TRANSMEM sequence GKFSTE description Beta stranded => ECO:0000250|UniProtKB:A1L314 source Swiss-Prot : SWS_FT_FI1 167) chain O residue 218-227 type TRANSMEM sequence AVTASAGLAF description Beta stranded => ECO:0000250|UniProtKB:A1L314 source Swiss-Prot : SWS_FT_FI1 168) chain B residue 110-115 type TRANSMEM sequence GKFSTE description Beta stranded => ECO:0000250|UniProtKB:A1L314 source Swiss-Prot : SWS_FT_FI1 169) chain O residue 231-239 type TRANSMEM sequence VNFKFEENY description Beta stranded => ECO:0000250|UniProtKB:A1L314 source Swiss-Prot : SWS_FT_FI1 170) chain P residue 96-103 type TRANSMEM sequence YSINTELS description Beta stranded => ECO:0000250|UniProtKB:A1L314 source Swiss-Prot : SWS_FT_FI1 171) chain P residue 110-115 type TRANSMEM sequence GKFSTE description Beta stranded => ECO:0000250|UniProtKB:A1L314 source Swiss-Prot : SWS_FT_FI1 172) chain P residue 218-227 type TRANSMEM sequence AVTASAGLAF description Beta stranded => ECO:0000250|UniProtKB:A1L314 source Swiss-Prot : SWS_FT_FI1 173) chain P residue 231-239 type TRANSMEM sequence VNFKFEENY description Beta stranded => ECO:0000250|UniProtKB:A1L314 source Swiss-Prot : SWS_FT_FI1 174) chain B residue 218-227 type TRANSMEM sequence AVTASAGLAF description Beta stranded => ECO:0000250|UniProtKB:A1L314 source Swiss-Prot : SWS_FT_FI1 175) chain B residue 231-239 type TRANSMEM sequence VNFKFEENY description Beta stranded => ECO:0000250|UniProtKB:A1L314 source Swiss-Prot : SWS_FT_FI1 176) chain C residue 96-103 type TRANSMEM sequence YSINTELS description Beta stranded => ECO:0000250|UniProtKB:A1L314 source Swiss-Prot : SWS_FT_FI1

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