N-acetylneuraminate 9-O-acetyltransferase (EC 2.3.1.45) (CAS1 domain-containing protein 1) (Sialate O-acetyltransferase) (SOAT)
1_MAALA 6_ YNLGK 11_ REINH 16_ YFSVR 21_ SAKVL 26_ ALVAV 31_ LLLAA 36_ CHLAS 41_ RRYRG 46_ NDSCE 51_ YLLSS 56_ GRFLG 61_ EKVWQ 66_ PHSCM 71_ MHKYK 76_ ISEAK 81_ NCLVD 86_ KHIAF 91_ IGDSR 96_ IRQLF 101_ YSFVK 106_ IINPQ 111_ FKEEG 116_ NKHEN 121_ IPFED 126_ KTASV 131_ KVDFL 136_ WHPEV 141_ NGSMK 146_ QCIKV 151_ WTEDS 156_ IAKPH 161_ VIVAG 166_ AATWS 171_ IKIHN 176_ GSSEA 181_ LSQYK 186_ MNITS 191_ IAPLL 196_ EKLAK 201_ TSDVY 206_ WVLQD 211_ PVYED 216_ LLSEN 221_ RKMIT 226_ NEKID 231_ AYNEA 236_ AVSIL 241_ NSSTR 246_ NSKSN 251_ VKMFS 256_ VSKLI 261_ AQETI 266_ MESLD 271_ GLHLP 276_ ESSRE 281_ TTAMI 286_ LMNVY 291_ CNKIL 296_ KPVDG 301_ SCCQP 306_ RPPVT 311_ LIQKL 316_ AACFF 321_ TLSII 326_ GYLIF 331_ YIIHR 336_ NAHRK 341_ NKPCT 346_ DLESG 351_ EEKKN 356_ IINTP 361_ VSSLE 366_ ILLQS 371_ FCKLG 376_ LIMAY 381_ FYMCD 386_ RANLF 391_ MKENK 396_ FYTHS 401_ SFFIP 406_ IIYIL 411_ VLGVF 416_ YNENT 421_ KETKV 426_ LNREQ 431_ TDEWK 436_ GWMQL 441_ VILIY 446_ HISGA 451_ STFLP 456_ VYMHI 461_ RVLVA 466_ AYLFQ 471_ TGYGH 476_ FSYFW 481_ IKGDF 486_ GIYRV 491_ CQVLF 496_ RLNFL 501_ VVVLC 506_ IVMDR 511_ PYQFY 516_ YFVPL 521_ VTVWF 526_ MVIYV 531_ TLALW 536_ PQIIQ 541_ KKANG 546_ NCFWH 551_ FGLLL 556_ KLGFL 561_ LLFIC 566_ FLAYS 571_ QGAFE 576_ KIFSL 581_ WPLSK 586_ CFELK 591_ GNVYE 596_ WWFRW 601_ RLDRY 606_ VVFHG 611_ MLFAF 616_ IYLAL 621_ QKRQI 626_ LSEGK 631_ GEPLF 636_ SNKIS 641_ NFLLF 646_ ISVVS 651_ FLTYS 656_ IWASS 661_ CKNKA 666_ ECNEL 671_ HPSVS 676_ VVQIL 681_ AFILI 686_ RNIPG 691_ YARSV 696_ YSSFF 701_ AWFGK 706_ ISLEL 711_ FICQY 716_ HIWLA 721_ ADTRG 726_ ILVLI 731_ PGNPM 736_ LNIIV 741_ STFIF 746_ VCVAH 751_ EISQI 756_ TNDLA 761_ QIIIP 766_ KDNSS 771_ LLKRL 776_ ACIAA 781_ FFCGL 786_ LILSS 791_IQDKS
1: Key enzyme in the biosynthesis of O-acetylated (O-Ac) sialoglycans such as gangliosides O-AcGD3 and O-AcGD2, which affect various processes such as cell-cell interactions, host-pathogen recognition (PubMed:20947662, PubMed:26169044, PubMed:34208013). Catalyzes the transfer of an acetyl group from a donor, the acetyl-coenzyme-A molecule (acetyl-CoA), to the C7/8/9 OH-position of a sialic acid residue (PubMed:20947662, PubMed:26169044). The primary site of O-acetyl group transfer on sialic acid seems to depend on cell type and can be C7, from which the O-acetyl group could subsequently migrate to the C8 and then to the C9 position, or at C9 with possibility of migrating to the C8 and then to the C7 position (PubMed:20947662, PubMed:26169044). Together with ST8SIA1 (GD3 synthase) it increases the levels of ganglioside Ac-O-7-GD3 (PubMed:20947662). Can transfer the acetyl group from acetyl-CoA to free sialate (N-acetylneuraminate, Neu5Ac) in vitro, but has preferred substrate specificity for CMP-activated sialate (CMP-Neu5Ac), resulting in the formation of 9-O-acetylated CMP-Neu5Ac (CMP-Neu5,9Ac2) (PubMed:26169044). CMP-Neu5,9Ac2 may be used by sialyltransferases as a sialate donor for glycoconjugate acceptors such as ganglioside GD3 (PubMed:26169044). O-acetylation at position C9 of ganglioside GD3 can counteract the pro-apoptotic effects of the ganglioside GD3 in tumor cells (PubMed:12486096)