##gff-version 3 Q14849 UniProtKB Chain 1 445 . . . ID=PRO_0000220653;Note=StAR-related lipid transfer protein 3 Q14849 UniProtKB Topological domain 1 51 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:11053434;Dbxref=PMID:11053434 Q14849 UniProtKB Transmembrane 52 72 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00770 Q14849 UniProtKB Topological domain 73 94 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q14849 UniProtKB Transmembrane 95 115 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00770 Q14849 UniProtKB Topological domain 116 120 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q14849 UniProtKB Transmembrane 121 141 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00770 Q14849 UniProtKB Topological domain 142 148 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q14849 UniProtKB Transmembrane 149 169 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00770 Q14849 UniProtKB Topological domain 170 445 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:11053434;Dbxref=PMID:11053434 Q14849 UniProtKB Domain 46 217 . . . Note=MENTAL;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00770 Q14849 UniProtKB Domain 230 443 . . . Note=START;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00197 Q14849 UniProtKB Motif 206 212 . . . Note=FFAT;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:24105263,ECO:0000269|PubMed:33124732;Dbxref=PMID:24105263,PMID:33124732 Q14849 UniProtKB Modified residue 209 209 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:33124732;Dbxref=PMID:33124732 Q14849 UniProtKB Alternative sequence 122 183 . . . ID=VSP_045361;Note=In isoform 3. WVIAVTTLVSSAFLIVKVILSELLSKGAFGYLLPIVSFVLAWLETWFLDFKVLPQEAEEERW->SRRWCPVHSSLSRSSSLSCSAKGHLATCSPSSLLSSPGWRPGSLTSKSYPRKLKRSDSAPPG;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:14702039;Dbxref=PMID:14702039 Q14849 UniProtKB Alternative sequence 126 143 . . . ID=VSP_042710;Note=In isoform 2. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:14702039;Dbxref=PMID:14702039 Q14849 UniProtKB Natural variant 117 117 . . . ID=VAR_027877;Note=R->Q;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:14702039,ECO:0000269|PubMed:15489334,ECO:0000269|PubMed:7490069,ECO:0000269|PubMed:9270027,ECO:0000269|Ref.3;Dbxref=dbSNP:rs1877031,PMID:14702039,PMID:15489334,PMID:7490069,PMID:9270027 Q14849 UniProtKB Natural variant 216 216 . . . ID=VAR_027878;Note=G->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15489334;Dbxref=dbSNP:rs11556624,PMID:15489334 Q14849 UniProtKB Mutagenesis 66 67 . . . Note=Abolishes localization to late endosomes and leads to mislocalization to the endoplasmic reticulum. LL->AS;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11053434;Dbxref=PMID:11053434 Q14849 UniProtKB Mutagenesis 89 89 . . . Note=Abolishes localization to late endosomes and leads to mislocalization to the endoplasmic reticulum. Y->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11053434;Dbxref=PMID:11053434 Q14849 UniProtKB Mutagenesis 113 113 . . . Note=Does not affect localization to late endosomes. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11053434;Dbxref=PMID:11053434 Q14849 UniProtKB Mutagenesis 206 212 . . . Note=Abolishes interaction with VAPA and VAPB%2C thereby preventing contact with the endoplasmic reticulum membrane. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24105263;Dbxref=PMID:24105263 Q14849 UniProtKB Mutagenesis 207 208 . . . Note=Abolishes interaction with VAPA%2C VAPB and MOSPD2%2C thereby preventing contact with the endoplasmic reticulum membrane. Abolishes cholesterol accumulation in endosomes. FY->AA;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:28377464,ECO:0000269|PubMed:29858488;Dbxref=PMID:28377464,PMID:29858488 Q14849 UniProtKB Mutagenesis 209 209 . . . Note=Impairs VAPA and VAPB interaction. Does not affect endoplasmic reticulum membrane location of VAPA%2C VAPB and MOSPD2. Is unable to make ER-endosome contacts. Does not accumulate cholesterol in late endosomes (LEs). Does not interact with MOSPD2. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:33124732;Dbxref=PMID:33124732 Q14849 UniProtKB Mutagenesis 209 209 . . . Note=Does not affect VAPA and VAPB interactions%3B when associated with A-210. Does not interact with VAPA and VAPB. Recruits VAPA and VAPB around the endosome%3B when associated with A-210. Restores cholesterol accumulation in late endosomes%3B when associated with A-210. Moderately interacts with MOSPD2. Almost impairs interaction with MOSPD2%3B when associated with A-210. S->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:33124732;Dbxref=PMID:33124732 Q14849 UniProtKB Mutagenesis 210 210 . . . Note=Does not affect VAPA and VAPB interactions%3B when associated with D-209. Improve VAPA interaction. Does not interact with VAPA and VAPB. Recruits VAPA and VAPB around the endosome%3B when associated with D-209.Restores cholesterol accumulation in late endosomes%3B when associated with A-209. Almost impairs interaction with MOSPD2%3B when associated with A-209. P->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:33124732;Dbxref=PMID:33124732 Q14849 UniProtKB Mutagenesis 219 219 . . . Note=Does not affect localization to late endosomes. N->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11053434;Dbxref=PMID:11053434 Q14849 UniProtKB Mutagenesis 307 311 . . . Note=Abolishes ability to transfer cholesterol between membranes. MVLWN->NVLWD;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28377464;Dbxref=PMID:28377464 Q14849 UniProtKB Mutagenesis 311 311 . . . Note=Does not affect localization to late endosomes. N->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11053434;Dbxref=PMID:11053434 Q14849 UniProtKB Helix 233 254 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5I9J Q14849 UniProtKB Helix 255 258 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5I9J Q14849 UniProtKB Beta strand 260 264 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5I9J Q14849 UniProtKB Beta strand 270 276 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5I9J Q14849 UniProtKB Turn 277 279 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5I9J Q14849 UniProtKB Beta strand 280 291 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5I9J Q14849 UniProtKB Helix 293 300 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5I9J Q14849 UniProtKB Helix 304 310 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5I9J Q14849 UniProtKB Beta strand 314 323 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5I9J Q14849 UniProtKB Turn 324 326 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5I9J Q14849 UniProtKB Beta strand 327 334 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5I9J Q14849 UniProtKB Beta strand 340 342 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5I9J Q14849 UniProtKB Beta strand 345 355 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5I9J Q14849 UniProtKB Beta strand 357 366 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5I9J Q14849 UniProtKB Beta strand 378 380 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5I9J Q14849 UniProtKB Beta strand 385 392 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5I9J Q14849 UniProtKB Beta strand 400 406 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5I9J Q14849 UniProtKB Beta strand 412 414 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5I9J Q14849 UniProtKB Helix 416 443 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5I9J