Eukaryotic translation initiation factor 5 (eIF-5)
1_MSVNV 6_ NRSVS 11_ DQFYR 16_ YKMPR 21_ LIAKV 26_ EGKGN 31_ GIKTV 36_ IVNMV 41_ DVAKA 46_ LNRPP 51_ TYPTK 56_ YFGCE 61_ LGAQT 66_ QFDVK 71_ NDRYI 76_ VNGSH 81_ EANKL 86_ QDMLD 91_ GFIKK 96_ FVLCP 101_ ECENP 106_ ETDLH 111_ VNPKK 116_ QTIGN 121_ SCKAC 126_ GYRGM 131_ LDTHH 136_ KLCTF 141_ ILKNP 146_ PENSD 151_ SGTGK 156_ KEKEK 161_ KNRKG 166_ KDKEN 171_ GSVSS 176_ SETPP 181_ PPPPP 186_ NEINP 191_ PPHTM 196_ EEEED 201_ DDWGE 206_ DTTEE 211_ AQRRR 216_ MDEIS 221_ DHAKV 226_ LTLSD 231_ DLERT 236_ IEERV 241_ NILFD 246_ FVKKK 251_ KEEGV 256_ IDSSD 261_ KEIVA 266_ EAERL 271_ DVKAM 276_ GPLVL 281_ TEVLF 286_ NEKIR 291_ EQIKK 296_ YRRHF 301_ LRFCH 306_ NNKKA 311_ QRYLL 316_ HGLEC 321_ VVAMH 326_ QAQLI 331_ SKIPH 336_ ILKEM 341_ YDADL 346_ LEEEV 351_ IISWS 356_ EKASK 361_ KYVSK 366_ ELAKE 371_ IRVKA 376_ EPFIK 381_ WLKEA 386_ EEESS 391_ GGEEE 396_ DEDEN 401_ IEVVY 406_ SKAAS 411_ VPKVE 416_ TVKSD 421_ NKDDD 426_IDIDA
1: Component of the 43S pre-initiation complex (43S PIC), which binds to the mRNA cap-proximal region, scans mRNA 5'-untranslated region, and locates the initiation codon (PubMed:11166181, PubMed:22813744, PubMed:24319994). In this complex, acts as a GTPase-activating protein, by promoting GTP hydrolysis by eIF2G (EIF2S3) (PubMed:11166181). During scanning, interacts with both EIF1 (via its C-terminal domain (CTD)) and EIF1A (via its NTD) (PubMed:22813744). This interaction with EIF1A contributes to the maintenance of EIF1 within the open 43S PIC (PubMed:24319994). When start codon is recognized, EIF5, via its NTD, induces eIF2G (EIF2S3) to hydrolyze the GTP (PubMed:11166181). Start codon recognition also induces a conformational change of the PIC to a closed state (PubMed:22813744). This change increases the affinity of EIF5-CTD for EIF2-beta (EIF2S2), which allows the release, by an indirect mechanism, of EIF1 from the PIC (PubMed:22813744). Finally, EIF5 stabilizes the PIC in its closed conformation (PubMed:22813744)