Protein Aster-C (GRAM domain-containing protein 1C)
1_MEGAP 6_ TVRQV 11_ MNEGD 16_ SSLAT 21_ DLQED 26_ VEENP 31_ SPTVE 36_ ENNVV 41_ VKKQG 46_ PNLHN 51_ WSGDW 56_ SFWIS 61_ SSTYK 66_ DRNEE 71_ YRRQF 76_ THLPD 81_ TERLI 86_ ADYAC 91_ ALQRD 96_ ILLQG 101_ RLYLS 106_ ENWLC 111_ FYSNI 116_ FRWET 121_ TISIA 126_ LKNIT 131_ FMTKE 136_ KTARL 141_ IPNAI 146_ QIVTE 151_ SEKFF 156_ FTSFG 161_ ARDRS 166_ YLSIF 171_ RLWQN 176_ VLLDK 181_ SLTRQ 186_ EFWQL 191_ LQQNY 196_ GTELG 201_ LNAEE 206_ MENLS 211_ LSIED 216_ VQPRS 221_ PGRSS 226_ LDDSG 231_ ERDEK 236_ LSKSI 241_ SFTSE 246_ SISRV 251_ SETES 256_ FDGNS 261_ SKGGL 266_ GKEES 271_ QNEKQ 276_ TKKSL 281_ LPTLE 286_ KKLTR 291_ VPSKS 296_ LDLNK 301_ NEYLS 306_ LDKSS 311_ TSDSV 316_ DEENV 321_ PEKDL 326_ HGRLF 331_ INRIF 336_ HISAD 341_ RMFEL 346_ LFTSS 351_ RFMQK 356_ FASSR 361_ NIIDV 366_ VSTPW 371_ TAELG 376_ GDQLR 381_ TMTYT 386_ IVLNS 391_ PLTGK 396_ CTAAT 401_ EKQTL 406_ YKESR 411_ EARFY 416_ LVDSE 421_ VLTHD 426_ VPYHD 431_ YFYTV 436_ NRYCI 441_ IRSSK 446_ QKCRL 451_ RVSTD 456_ LKYRK 461_ QPWGL 466_ VKSLI 471_ EKNSW 476_ SSLED 481_ YFKQL 486_ ESDLL 491_ IEESV 496_ LNQAI 501_ EDPGK 506_ LTGLR 511_ RRRRT 516_ FNRTA 521_ ETVPK 526_ LSSQH 531_ SSGDV 536_ GLGAK 541_ GDITG 546_ KKKEM 551_ ENYNV 556_ TLIVV 561_ MSIFV 566_ LLLVL 571_ LNVTL 576_ FLKLS 581_ KIEHA 586_ AQSFY 591_ RLRLQ 596_ EEKSL 601_ NLASD 606_ MVSRA 611_ ETIQK 616_ NKDQA 621_ HRLKG 626_ VLRDS 631_ IVMLE 636_ QLKSS 641_ LIMLQ 646_ KTFDL 651_ LNKNK 656_TGMAV
1: Cholesterol transporter that mediates non-vesicular transport of cholesterol from the plasma membrane (PM) to the endoplasmic reticulum (ER) (By similarity). Contains unique domains for binding cholesterol and the PM, thereby serving as a molecular bridge for the transfer of cholesterol from the PM to the ER (By similarity). Plays a crucial role in cholesterol homeostasis and has the unique ability to localize to the PM based on the level of membrane cholesterol (By similarity). In lipid-poor conditions localizes to the ER membrane and in response to excess cholesterol in the PM is recruited to the endoplasmic reticulum-plasma membrane contact sites (EPCS) which is mediated by the GRAM domain (By similarity). At the EPCS, the sterol-binding VASt/ASTER domain binds to the cholesterol in the PM and facilitates its transfer from the PM to ER (By similarity)