##gff-version 3 P55157 UniProtKB Signal peptide 1 18 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 P55157 UniProtKB Chain 19 894 . . . ID=PRO_0000041593;Note=Microsomal triglyceride transfer protein large subunit P55157 UniProtKB Domain 28 659 . . . Note=Vitellogenin;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00557 P55157 UniProtKB Disulfide bond 174 194 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00557 P55157 UniProtKB Alternative sequence 134 151 . . . ID=VSP_056325;Note=In isoform 2. EFYSYQNEAVAIENIKRG->GRLDSTTFSPTSYFSSLQ;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:15489334;Dbxref=PMID:15489334 P55157 UniProtKB Alternative sequence 152 894 . . . ID=VSP_056326;Note=In isoform 2. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:15489334;Dbxref=PMID:15489334 P55157 UniProtKB Natural variant 95 95 . . . ID=VAR_014016;Note=Q->H;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11792722;Dbxref=dbSNP:rs61733139,PMID:11792722 P55157 UniProtKB Natural variant 98 98 . . . ID=VAR_052961;Note=E->D;Dbxref=dbSNP:rs2306986 P55157 UniProtKB Natural variant 128 128 . . . ID=VAR_014017;Note=I->T;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11792722,ECO:0000269|PubMed:14732481;Dbxref=dbSNP:rs3816873,PMID:11792722,PMID:14732481 P55157 UniProtKB Natural variant 166 166 . . . ID=VAR_052962;Note=N->S;Dbxref=dbSNP:rs3792683 P55157 UniProtKB Natural variant 168 168 . . . ID=VAR_022658;Note=V->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14732481;Dbxref=dbSNP:rs61750974,PMID:14732481 P55157 UniProtKB Natural variant 169 169 . . . ID=VAR_074553;Note=In ABL%3B no loss on localization to the endoplasmic reticulum%3B does not reduce interaction with APOB%3B inhibits interaction with P4HB/PDI%3B inhibits phospholipid or triglyceride transfer activity%3B inhibits apolipoprotein B secretion. D->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26224785;Dbxref=PMID:26224785 P55157 UniProtKB Natural variant 244 244 . . . ID=VAR_014018;Note=Q->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11792722;Dbxref=dbSNP:rs17599091,PMID:11792722 P55157 UniProtKB Natural variant 264 264 . . . ID=VAR_074554;Note=In ABL%3B uncertain significance%3B does not reduce interaction with P4HB/PDI and APOB%3B does not reduce triglyceride transfer activity. G->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25108285;Dbxref=dbSNP:rs1367079155,PMID:25108285 P55157 UniProtKB Natural variant 297 297 . . . ID=VAR_010640;Note=Does not inhibit apolipoprotein B secretion. H->Q;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11792722,ECO:0000269|PubMed:14732481,ECO:0000269|PubMed:8939939;Dbxref=dbSNP:rs2306985,PMID:11792722,PMID:14732481,PMID:8939939 P55157 UniProtKB Natural variant 384 384 . . . ID=VAR_010641;Note=No loss on localization to the endoplasmic reticulum%3B does not reduce interaction with P4HB/PDI%3B reduces phospholipid or triglyceride transfer activity%3B does not inhibit apolipoprotein B secretion. D->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:23475612,ECO:0000269|PubMed:8939939;Dbxref=dbSNP:rs17029215,PMID:23475612,PMID:8939939 P55157 UniProtKB Natural variant 435 435 . . . ID=VAR_074555;Note=In ABL%3B no loss on localization to the endoplasmic reticulum%3B inhibits triglyceride transfer activity. L->H;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22236406;Dbxref=PMID:22236406 P55157 UniProtKB Natural variant 528 528 . . . ID=VAR_074556;Note=In ABL%3B does not reduce interaction with P4HB/PDI and APOB%3B inhibits triglyceride transfer activity. Y->H;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25108285;Dbxref=dbSNP:rs1485375137,PMID:25108285 P55157 UniProtKB Natural variant 540 540 . . . ID=VAR_074557;Note=In ABL%3B does not reduce interaction with P4HB/PDI and APOB%3B inhibits triglyceride transfer activity. R->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25108285;Dbxref=dbSNP:rs372321643,PMID:25108285 P55157 UniProtKB Natural variant 540 540 . . . ID=VAR_010642;Note=In ABL%3B no loss on localization to the endoplasmic reticulum%3B reduces interaction with P4HB/PDI%3B inhibits phospholipid or triglyceride transfer activity%3B inhibits apolipoprotein B secretion. R->H;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10679949,ECO:0000269|PubMed:23475612,ECO:0000269|PubMed:25108285,ECO:0000269|PubMed:8939939;Dbxref=dbSNP:rs199422220,PMID:10679949,PMID:23475612,PMID:25108285,PMID:8939939 P55157 UniProtKB Natural variant 590 590 . . . ID=VAR_010643;Note=In ABL%3B no loss on localization to the endoplasmic reticulum%3B does not reduce interaction with P4HB/PDI%3B inhibits phospholipid or triglyceride transfer activity%3B inhibits apolipoprotein B secretion. S->I;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10679949,ECO:0000269|PubMed:23475612;Dbxref=dbSNP:rs199422222,PMID:10679949,PMID:23475612 P55157 UniProtKB Natural variant 649 649 . . . ID=VAR_074558;Note=In ABL%3B uncertain significance%3B does not reduce interaction with P4HB/PDI and APOB%3B reduces triglyceride transfer activity. N->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25108285;Dbxref=PMID:25108285 P55157 UniProtKB Natural variant 746 746 . . . ID=VAR_010644;Note=In ABL%3B no loss on localization to the endoplasmic reticulum%3B does not reduce interaction with P4HB/PDI%3B inhibits phospholipid or triglyceride transfer activity%3B inhibits apolipoprotein B secretion. G->E;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10679949,ECO:0000269|PubMed:23475612;Dbxref=dbSNP:rs767833468,PMID:10679949,PMID:23475612 P55157 UniProtKB Natural variant 780 780 . . . ID=VAR_014019;Note=In ABL%3B no loss on localization to the endoplasmic reticulum%3B does not reduce interaction with P4HB/PDI%3B inhibits phospholipid or triglyceride transfer activity%3B inhibits apolipoprotein B secretion. N->Y;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10946006,ECO:0000269|PubMed:23475612;Dbxref=dbSNP:rs199422221,PMID:10946006,PMID:23475612 P55157 UniProtKB Mutagenesis 169 169 . . . Note=No loss on localization to the endoplasmic reticulum and does not reduce interaction with APOB or P4HB/PDI%2C does partially reduce phospholipid or triglyceride transfer activity and apolipoprotein B secretion. D->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26224785;Dbxref=PMID:26224785 P55157 UniProtKB Mutagenesis 187 187 . . . Note=No loss on localization to the endoplasmic reticulum and does not reduce interaction with APOB%2C but inhibits interaction with P4HB/PDI%2C phospholipid or triglyceride transfer activity and apolipoprotein B secretion. K->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26224785;Dbxref=PMID:26224785 P55157 UniProtKB Mutagenesis 187 187 . . . Note=No loss on localization to the endoplasmic reticulum%2C does not reduce interaction with APOB or P4HB/PDI%2C partially inhibits triglyceride transfer activity%2C does not inhibit phospholipid transfer activity and apolipoprotein B secretion. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26224785;Dbxref=PMID:26224785 P55157 UniProtKB Mutagenesis 189 189 . . . Note=No loss on localization to the endoplasmic reticulum and does not reduce interaction with APOB%2C but inhibits interaction with P4HB/PDI%2C phospholipid or triglyceride transfer activity and apolipoprotein B secretion. K->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26224785;Dbxref=PMID:26224785 P55157 UniProtKB Mutagenesis 189 189 . . . Note=No loss on localization to the endoplasmic reticulum%2C does not reduce interaction with APOB or P4HB/PDI%2C partially inhibits triglyceride transfer activity%2C does not inhibit phospholipid transfer activity and apolipoprotein B secretion. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26224785;Dbxref=PMID:26224785 P55157 UniProtKB Mutagenesis 435 435 . . . Note=No loss on localization to the endoplasmic reticulum. Inhibits triglyceride transfer activity. L->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22236406;Dbxref=PMID:22236406 P55157 UniProtKB Mutagenesis 435 435 . . . Note=No loss on localization to the endoplasmic reticulum. Does not inhibit triglyceride transfer activity. L->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22236406;Dbxref=PMID:22236406 P55157 UniProtKB Mutagenesis 528 528 . . . Note=Does not inhibit triglyceride transfer activity. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25108285;Dbxref=PMID:25108285 P55157 UniProtKB Mutagenesis 528 528 . . . Note=Inhibits triglyceride transfer activity. Y->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25108285;Dbxref=PMID:25108285 P55157 UniProtKB Mutagenesis 540 540 . . . Note=Strongly reduces triglyceride transfer activity. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25108285;Dbxref=PMID:25108285 P55157 UniProtKB Mutagenesis 540 540 . . . Note=Does not inhibit triglyceride transfer activity and apolipoprotein B secretion. R->K;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:25108285,ECO:0000269|PubMed:8939939;Dbxref=PMID:25108285,PMID:8939939 P55157 UniProtKB Mutagenesis 878 878 . . . Note=Inhibits triglyceride transfer activity. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8533758;Dbxref=PMID:8533758 P55157 UniProtKB Sequence conflict 585 585 . . . Note=F->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 P55157 UniProtKB Beta strand 34 45 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8EOJ P55157 UniProtKB Beta strand 47 50 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8EOJ P55157 UniProtKB Beta strand 57 67 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8EOJ P55157 UniProtKB Beta strand 77 92 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8EOJ P55157 UniProtKB Beta strand 100 102 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8EOJ P55157 UniProtKB Helix 107 111 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8EOJ P55157 UniProtKB Helix 113 120 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8EOJ P55157 UniProtKB Beta strand 123 128 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8EOJ P55157 UniProtKB Beta strand 131 137 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8EOJ P55157 UniProtKB Helix 143 153 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8EOJ P55157 UniProtKB Helix 154 156 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8EOJ P55157 UniProtKB Beta strand 163 166 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8EOJ P55157 UniProtKB Beta strand 169 171 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8EOJ P55157 UniProtKB Beta strand 173 180 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8EOJ P55157 UniProtKB Beta strand 182 195 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8EOJ P55157 UniProtKB Beta strand 218 232 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8EOJ P55157 UniProtKB Beta strand 236 238 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8EOJ P55157 UniProtKB Beta strand 248 261 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8EOJ P55157 UniProtKB Helix 274 280 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8EOJ P55157 UniProtKB Beta strand 285 287 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8EOJ P55157 UniProtKB Beta strand 297 300 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8EOJ P55157 UniProtKB Turn 304 306 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8EOJ P55157 UniProtKB Helix 307 312 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8EOJ P55157 UniProtKB Helix 317 319 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8EOJ P55157 UniProtKB Helix 323 337 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8EOJ P55157 UniProtKB Helix 341 347 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8EOJ P55157 UniProtKB Beta strand 353 355 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8EOJ P55157 UniProtKB Helix 356 364 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8EOJ P55157 UniProtKB Helix 369 378 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8EOJ P55157 UniProtKB Helix 387 398 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8EOJ P55157 UniProtKB Helix 405 416 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8EOJ P55157 UniProtKB Helix 422 440 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8EOJ P55157 UniProtKB Turn 441 443 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8EOJ P55157 UniProtKB Helix 448 462 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8EOJ P55157 UniProtKB Helix 467 480 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8EOJ P55157 UniProtKB Helix 483 485 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8EOJ P55157 UniProtKB Helix 486 493 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8EOJ P55157 UniProtKB Helix 498 510 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8EOJ P55157 UniProtKB Helix 518 528 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8EOJ P55157 UniProtKB Beta strand 531 533 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8EOJ P55157 UniProtKB Helix 537 549 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8EOJ P55157 UniProtKB Helix 554 563 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8EOJ P55157 UniProtKB Turn 564 566 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8EOJ P55157 UniProtKB Helix 569 584 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8EOJ P55157 UniProtKB Helix 590 597 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8EOJ P55157 UniProtKB Turn 600 602 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8EOJ P55157 UniProtKB Helix 605 608 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8EOJ P55157 UniProtKB Beta strand 617 623 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8EOJ P55157 UniProtKB Beta strand 625 637 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8EOJ P55157 UniProtKB Beta strand 643 654 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8EOJ P55157 UniProtKB Beta strand 657 668 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8EOJ P55157 UniProtKB Beta strand 690 698 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8EOJ P55157 UniProtKB Beta strand 704 707 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8EOJ P55157 UniProtKB Beta strand 728 737 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8EOJ P55157 UniProtKB Beta strand 740 742 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8EOJ P55157 UniProtKB Beta strand 748 761 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8EOJ P55157 UniProtKB Beta strand 781 793 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8EOJ P55157 UniProtKB Beta strand 795 810 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8EOJ P55157 UniProtKB Beta strand 812 818 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8EOJ P55157 UniProtKB Beta strand 820 823 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8EOJ P55157 UniProtKB Beta strand 825 831 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8EOJ P55157 UniProtKB Beta strand 835 846 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8EOJ P55157 UniProtKB Beta strand 855 863 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8EOJ P55157 UniProtKB Helix 872 878 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8EOJ P55157 UniProtKB Turn 879 881 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8EOJ