Sia-alpha-2,3-Gal-beta-1,4-GlcNAc-R:alpha 2,8-sialyltransferase (EC 2.4.99.-) (Alpha-2,8-sialyltransferase 8C) (Alpha-2,8-sialyltransferase III) (ST8 alpha-N-acetyl-neuraminide alpha-2,8-sialyltransferase 3) (Sialyltransferase 8C) (SIAT8-C) (Sialyltransferase St8Sia III) (ST8SiaIII)
1_MRNCK 6_ MARVA 11_ SVLGL 16_ VMLSV 21_ ALLIL 26_ SLISY 31_ VSLKK 36_ ENIFT 41_ TPKYA 46_ SPGAP 51_ RMYMF 56_ HAGFR 61_ SQFAL 66_ KFLDP 71_ SFVPI 76_ TNSLT 81_ QELQE 86_ KPSKW 91_ KFNRT 96_ AFLHQ 101_ RQEIL 106_ QHVDV 111_ IKNFS 116_ LTKNS 121_ VRIGQ 126_ LMHYD 131_ YSSHK 136_ YVFSI 141_ SNNFR 146_ SLLPD 151_ VSPIM 156_ NKHYN 161_ ICAVV 166_ GNSGI 171_ LTGSQ 176_ CGQEI 181_ DKSDF 186_ VFRCN 191_ FAPTE 196_ AFQRD 201_ VGRKT 206_ NLTTF 211_ NPSIL 216_ EKYYN 221_ NLLTI 226_ QDRNN 231_ FFLSL 236_ KKLDG 241_ AILWI 246_ PAFFF 251_ HTSAT 256_ VTRTL 261_ VDFFV 266_ EHRGQ 271_ LKVQL 276_ AWPGN 281_ IMQHV 286_ NRYWK 291_ NKHLS 296_ PKRLS 301_ TGILM 306_ YTLAS 311_ AICEE 316_ IHLYG 321_ FWPFG 326_ FDPNT 331_ REDLP 336_ YHYYD 341_ KKGTK 346_ FTTKW 351_ QESHQ 356_ LPAEF 361_ QLLYR 366_ MHGEG 371_LTKLT
1: Catalyzes the transfer of sialic acid from a CMP-linked sialic acid donor onto a terminal alpha-2,3-, alpha-2,6-, or alpha-2,8-linked sialic acid of an acceptor, such as N-linked oligosaccharides of glycoproteins and glycolipids through alpha-2,8-linkages (PubMed:10766765, PubMed:26192331, PubMed:9826427). Forms oligosialic and polysialic acid on various sialylated N-acetyllactosamine oligosaccharides of glycoproteins, including FETUB N-glycans, a2-HS-glycoprotein (AHSG) and alpha 2,3-sialylated glycosphingolipids, such as alpha 2,3-sialylparagloboside and ganglioside GM3 and to a lesser extent NCAM1 N-glycans (PubMed:10766765, PubMed:9826427). However, it is much more specific to N-linked oligosaccharides of glycoproteins than glycosphingolipids (By similarity). 2,3-sialylparagloboside serves as the best acceptor substrate among the glycolipids (By similarity). alpha-Neu5Ac-(2->8)-alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-6S-D-GlcNAc and monosialyl and disialyl N-acetyllactosamines are the best acceptor substrates among glycoproteins (PubMed:10766765, PubMed:26192331). May plays critical role in the striatum by mediating the formation of disialylated and trisialylated terminal glycotopes on N- and O-glycans of specific striatal proteins, regulating their distribution in lipid rafts, affecting their interaction with other binding partners, and subsequently modulating striatal functions (By similarity)