ID SIA8A_HUMAN Reviewed; 356 AA. AC Q92185; A8K4H6; Q17RL0; Q6PZN5; Q93064; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 27-MAR-2024, entry version 186. DE RecName: Full=Alpha-N-acetylneuraminide alpha-2,8-sialyltransferase {ECO:0000305}; DE EC=2.4.3.8 {ECO:0000269|PubMed:18348864, ECO:0000269|PubMed:22885356, ECO:0000269|PubMed:7937974, ECO:0000269|PubMed:8058740, ECO:0000269|PubMed:8195250, ECO:0000269|PubMed:8631981, ECO:0000269|PubMed:8706663}; DE AltName: Full=Alpha-2,8-sialyltransferase 8A; DE AltName: Full=Ganglioside GD3 synthase; DE AltName: Full=Ganglioside GT3 synthase; DE AltName: Full=Sialyltransferase 8A; DE Short=SIAT8-A; DE AltName: Full=Sialyltransferase St8Sia I; DE Short=ST8SiaI; GN Name=ST8SIA1 {ECO:0000312|HGNC:HGNC:10869}; Synonyms=SIAT8, SIAT8A; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND CATALYTIC ACTIVITY. RC TISSUE=Melanoma; RX PubMed=8195250; DOI=10.1016/s0021-9258(17)40773-3; RA Sasaki K., Kurata K., Kojima N., Kurosawa N., Ohta S., Hanai N., Tsuji S., RA Nishi T.; RT "Expression cloning of a GM3-specific alpha-2,8-sialyltransferase (GD3 RT synthase)."; RL J. Biol. Chem. 269:15950-15956(1994). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND CATALYTIC ACTIVITY. RC TISSUE=Melanoma; RX PubMed=8058740; DOI=10.1073/pnas.91.17.7952; RA Nara K., Watanabe Y., Maruyama K., Kasahara K., Nagai Y., Sanai Y.; RT "Expression cloning of a CMP-NeuAc:NeuAc alpha 2-3Gal beta 1-4Glc beta 1- RT 1'Cer alpha 2,8-sialyltransferase (GD3 synthase) from human melanoma RT cells."; RL Proc. Natl. Acad. Sci. U.S.A. 91:7952-7956(1994). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY, AND RP TISSUE SPECIFICITY. RX PubMed=7937974; DOI=10.1073/pnas.91.22.10455; RA Haraguchi M., Yamashiro S., Yamamoto A., Furukawa K., Takamiya K., RA Lloyd K.O., Shiku H., Furukawa K.; RT "Isolation of GD3 synthase gene by expression cloning of GM3 alpha-2,8- RT sialyltransferase cDNA using anti-GD2 monoclonal antibody."; RL Proc. Natl. Acad. Sci. U.S.A. 91:10455-10459(1994). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY, AND RP TISSUE SPECIFICITY. RX PubMed=8631981; RA Nakayama J., Fukuda M.N., Hirabayashi Y., Kanamori A., Sasaki K., Nishi T., RA Fukuda M.; RT "Expression cloning of a human GT3 synthase. GD3 and GT3 are synthesized by RT a single enzyme."; RL J. Biol. Chem. 271:3684-3691(1996). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND ALTERNATIVE SPLICING. RA Rimoldi S., Papis E., Bernardini G., Gornati R.; RT "Cloning of alternative human SAT-2 mRNA."; RL Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND ALTERNATIVE SPLICING. RA Konta L., Laws S.M., Riemenschneider M., Adamski J.; RT "Alternative splice variant of the ST8SIA1 gene."; RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Stomach, and Teratocarcinoma; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16541075; DOI=10.1038/nature04569; RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., RA Gibbs R.A.; RT "The finished DNA sequence of human chromosome 12."; RL Nature 440:346-351(2006). RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [10] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Colon; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [11] RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=8706663; DOI=10.1111/j.1432-1033.1996.0647w.x; RA Nara K., Watanabe Y., Kawashima I., Tai T., Nagai Y., Sanai Y.; RT "Acceptor substrate specificity of a cloned GD3 synthase that catalyzes the RT biosynthesis of both GD3 and GD1c/GT1a/GQ1b."; RL Eur. J. Biochem. 238:647-652(1996). RN [12] RP IDENTIFICATION. RX PubMed=15843597; DOI=10.1093/glycob/cwi063; RA Harduin-Lepers A., Mollicone R., Delannoy P., Oriol R.; RT "The animal sialyltransferases and sialyltransferase-related genes: a RT phylogenetic approach."; RL Glycobiology 15:805-817(2005). RN [13] RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND RP MUTAGENESIS OF ASN-188; PRO-189; SER-190 AND ARG-272. RX PubMed=18348864; DOI=10.1016/j.bbrc.2008.03.029; RA Gu Y., Yu R.K.; RT "Identification and analysis of novel functional sites in human GD3- RT synthase."; RL Biochem. Biophys. Res. Commun. 370:67-71(2008). RN [14] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=22885356; DOI=10.3390/molecules17089559; RA Steenackers A., Vanbeselaere J., Cazet A., Bobowski M., Rombouts Y., RA Colomb F., Le Bourhis X., Guerardel Y., Delannoy P.; RT "Accumulation of unusual gangliosides G(Q3) and G(P3) in breast cancer RT cells expressing the G(D3) synthase."; RL Molecules 17:9559-9572(2012). CC -!- FUNCTION: Catalyzes the addition of sialic acid in alpha 2,8-linkage to CC the sialic acid moiety of the ganglioside GM3 to form ganglioside GD3; CC gangliosides are a subfamily of complex glycosphingolipds that contain CC one or more residues of sialic acid (PubMed:7937974, PubMed:8058740, CC PubMed:8195250, PubMed:8631981, PubMed:8706663, PubMed:18348864, CC PubMed:22885356). Can catalyze the addition of a second alpha-2,8- CC sialic acid to GD3 to form GT3 (PubMed:8631981). Can use GM1b, GD1a and CC GT1b as acceptor substrates to synthesize GD1c, GT1a and GQ1b CC respectively (PubMed:8706663). Can synthesize unusual tetra- and CC pentasialylated lactosylceramide derivatives identified as GQ3 CC (II3Neu5Ac4-Gg2Cer) and GP3 (II3Neu5Ac5-Gg2Cer) in breast cancer cells CC (PubMed:22885356). {ECO:0000269|PubMed:18348864, CC ECO:0000269|PubMed:22885356, ECO:0000269|PubMed:7937974, CC ECO:0000269|PubMed:8058740, ECO:0000269|PubMed:8195250, CC ECO:0000269|PubMed:8631981, ECO:0000269|PubMed:8706663}. CC -!- CATALYTIC ACTIVITY: CC Reaction=an N-acetyl-alpha-neuraminyl-(2->3)-beta-D-galactosyl CC derivative + CMP-N-acetyl-beta-neuraminate = an N-acetyl-alpha- CC neuraminyl-(2->8)-N-acetyl-alpha-neuraminyl-(2->3)-beta-D-galactosyl CC derivative + CMP + H(+); Xref=Rhea:RHEA:19313, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:57812, ChEBI:CHEBI:60377, ChEBI:CHEBI:140308, CC ChEBI:CHEBI:140309; EC=2.4.3.8; CC Evidence={ECO:0000269|PubMed:18348864, ECO:0000269|PubMed:22885356, CC ECO:0000269|PubMed:7937974, ECO:0000269|PubMed:8058740, CC ECO:0000269|PubMed:8195250, ECO:0000269|PubMed:8631981, CC ECO:0000269|PubMed:8706663}; CC -!- CATALYTIC ACTIVITY: CC Reaction=a ganglioside GM3 (d18:1(4E)) + CMP-N-acetyl-beta-neuraminate CC = a ganglioside GD3 (d18:1(4E)) + CMP + H(+); Xref=Rhea:RHEA:41760, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57812, ChEBI:CHEBI:60065, CC ChEBI:CHEBI:60377, ChEBI:CHEBI:78436; CC Evidence={ECO:0000269|PubMed:18348864, ECO:0000269|PubMed:22885356, CC ECO:0000269|PubMed:7937974, ECO:0000269|PubMed:8058740, CC ECO:0000269|PubMed:8195250, ECO:0000269|PubMed:8631981, CC ECO:0000269|PubMed:8706663}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41761; CC Evidence={ECO:0000305|PubMed:8195250}; CC -!- CATALYTIC ACTIVITY: CC Reaction=a ganglioside GD3 (d18:1(4E)) + CMP-N-acetyl-beta-neuraminate CC = a ganglioside GT3 (d18:1(4E)) + CMP + H(+); Xref=Rhea:RHEA:41764, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57812, ChEBI:CHEBI:60377, CC ChEBI:CHEBI:78436, ChEBI:CHEBI:78438; CC Evidence={ECO:0000269|PubMed:22885356, ECO:0000269|PubMed:8631981}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41765; CC Evidence={ECO:0000305|PubMed:8631981}; CC -!- CATALYTIC ACTIVITY: CC Reaction=a ganglioside GD1a (d18:1(4E)) + CMP-N-acetyl-beta-neuraminate CC = a ganglioside GT1a (d18:1(4E)) + CMP + H(+); Xref=Rhea:RHEA:41768, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57812, ChEBI:CHEBI:60377, CC ChEBI:CHEBI:78445, ChEBI:CHEBI:78447; CC Evidence={ECO:0000269|PubMed:8706663}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41769; CC Evidence={ECO:0000305|PubMed:8706663}; CC -!- CATALYTIC ACTIVITY: CC Reaction=a ganglioside GT1b (d18:1(4E)) + CMP-N-acetyl-beta-neuraminate CC = a ganglioside GQ1b (d18:1(4E)) + CMP + H(+); Xref=Rhea:RHEA:41772, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57812, ChEBI:CHEBI:60377, CC ChEBI:CHEBI:78452, ChEBI:CHEBI:78455; CC Evidence={ECO:0000269|PubMed:8706663}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41773; CC Evidence={ECO:0000305|PubMed:8706663}; CC -!- CATALYTIC ACTIVITY: CC Reaction=a ganglioside GM1b (d18:1(4E)) + CMP-N-acetyl-beta-neuraminate CC = a ganglioside GD1c (d18:1(4E)) + CMP + H(+); Xref=Rhea:RHEA:47576, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57812, ChEBI:CHEBI:60377, CC ChEBI:CHEBI:78568, ChEBI:CHEBI:87787; CC Evidence={ECO:0000269|PubMed:8706663}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47577; CC Evidence={ECO:0000305|PubMed:8706663}; CC -!- CATALYTIC ACTIVITY: CC Reaction=a ganglioside GD3 + CMP-N-acetyl-beta-neuraminate = a CC ganglioside GT3 + CMP + H(+); Xref=Rhea:RHEA:77295, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57812, ChEBI:CHEBI:60377, CC ChEBI:CHEBI:79214, ChEBI:CHEBI:79216; CC Evidence={ECO:0000269|PubMed:8631981}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77296; CC Evidence={ECO:0000269|PubMed:8631981}; CC -!- CATALYTIC ACTIVITY: CC Reaction=[alpha-N-acetylneuraminyl-(2->8)](n)-alpha-N-acetylneuraminyl- CC (2->8)-alpha-N-acetylneuraminyl-(2->3)-beta-D-galactosyl-(1->4)-beta- CC D-glucosyl-(1<->1)-ceramide + CMP-N-acetyl-beta-neuraminate = [alpha- CC N-acetylneuraminyl-(2->8)](n+1)-alpha-N-acetylneuraminyl-(2->8)- CC alpha-N-acetylneuraminyl-(2->3)-beta-D-galactosyl-(1->4)-beta-D- CC glucosyl-(1<->1)-ceramide + CMP + H(+); Xref=Rhea:RHEA:77371, CC Rhea:RHEA-COMP:18881, Rhea:RHEA-COMP:18935, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:57812, ChEBI:CHEBI:60377, ChEBI:CHEBI:197322; CC Evidence={ECO:0000269|PubMed:8631981}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77372; CC Evidence={ECO:0000269|PubMed:8631981}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=190 uM for ganglioside GM3 {ECO:0000269|PubMed:8706663}; CC KM=83 uM for ganglioside GM3 {ECO:0000269|PubMed:18348864}; CC KM=62.5 uM for ganglioside GD1a {ECO:0000269|PubMed:8706663}; CC KM=100 uM for ganglioside GT1b {ECO:0000269|PubMed:8706663}; CC KM=88 uM for CMP-N-acetyl-beta-neuraminate CC {ECO:0000269|PubMed:18348864}; CC Vmax=121 pmol/h/mg enzyme for ganglioside GM3 CC {ECO:0000269|PubMed:8706663}; CC Vmax=165 pmol/h/mg enzyme for ganglioside GM3 CC {ECO:0000269|PubMed:18348864}; CC Vmax=14.2 pmol/h/mg enzyme for ganglioside GD1a CC {ECO:0000269|PubMed:8706663}; CC Vmax=20.9 pmol/h/mg enzyme for ganglioside GT1b CC {ECO:0000269|PubMed:8706663}; CC Vmax=167 pmol/h/mg enzyme for CMP-N-acetyl-beta-neuraminate CC {ECO:0000269|PubMed:18348864}; CC -!- PATHWAY: Protein modification; protein glycosylation. CC -!- PATHWAY: Lipid metabolism; sphingolipid metabolism. CC -!- INTERACTION: CC Q92185; Q96CV9: OPTN; NbExp=3; IntAct=EBI-21541735, EBI-748974; CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000305}; Single- CC pass type II membrane protein {ECO:0000305}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q92185-1; Sequence=Displayed; CC Name=2; Synonyms=Sat-2; CC IsoId=Q92185-2; Sequence=VSP_047583, VSP_047584; CC -!- TISSUE SPECIFICITY: Strongly expressed in melanoma cell lines, adult CC and fetal brain and to a lesser extent in adult and fetal lung. CC {ECO:0000269|PubMed:7937974, ECO:0000269|PubMed:8631981}. CC -!- SIMILARITY: Belongs to the glycosyltransferase 29 family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC37586.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase; Note=ST8Sia I; CC URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_hum_636"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X77922; CAA54891.1; -; mRNA. DR EMBL; D26360; BAA05391.1; -; mRNA. DR EMBL; L32867; AAA62366.1; -; mRNA. DR EMBL; L43494; AAC37586.1; ALT_INIT; mRNA. DR EMBL; AY569975; AAS75783.1; -; mRNA. DR EMBL; EU041716; ABU62753.1; -; mRNA. DR EMBL; AK290941; BAF83630.1; -; mRNA. DR EMBL; AK315340; BAG37739.1; -; mRNA. DR EMBL; AC007544; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC007671; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC053513; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC087318; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC138468; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471094; EAW96468.1; -; Genomic_DNA. DR EMBL; BC117285; AAI17286.1; -; mRNA. DR EMBL; BC126162; AAI26163.1; -; mRNA. DR CCDS; CCDS8697.1; -. [Q92185-1] DR PIR; A54032; A54032. DR RefSeq; NP_001291379.1; NM_001304450.1. DR RefSeq; NP_003025.1; NM_003034.3. [Q92185-1] DR AlphaFoldDB; Q92185; -. DR SMR; Q92185; -. DR BioGRID; 112380; 26. DR IntAct; Q92185; 9. DR STRING; 9606.ENSP00000379353; -. DR SwissLipids; SLP:000000749; -. DR SwissLipids; SLP:000000871; -. DR CAZy; GT29; Glycosyltransferase Family 29. DR GlyCosmos; Q92185; 4 sites, No reported glycans. DR GlyGen; Q92185; 4 sites. DR iPTMnet; Q92185; -. DR PhosphoSitePlus; Q92185; -. DR SwissPalm; Q92185; -. DR BioMuta; ST8SIA1; -. DR MassIVE; Q92185; -. DR PaxDb; 9606-ENSP00000379353; -. DR PeptideAtlas; Q92185; -. DR ProteomicsDB; 75252; -. [Q92185-1] DR Antibodypedia; 12441; 83 antibodies from 20 providers. DR DNASU; 6489; -. DR Ensembl; ENST00000261197.7; ENSP00000261197.3; ENSG00000111728.11. [Q92185-2] DR Ensembl; ENST00000396037.9; ENSP00000379353.3; ENSG00000111728.11. [Q92185-1] DR GeneID; 6489; -. DR KEGG; hsa:6489; -. DR MANE-Select; ENST00000396037.9; ENSP00000379353.3; NM_003034.4; NP_003025.1. DR UCSC; uc001rfo.4; human. [Q92185-1] DR AGR; HGNC:10869; -. DR CTD; 6489; -. DR DisGeNET; 6489; -. DR GeneCards; ST8SIA1; -. DR HGNC; HGNC:10869; ST8SIA1. DR HPA; ENSG00000111728; Low tissue specificity. DR MIM; 601123; gene. DR neXtProt; NX_Q92185; -. DR OpenTargets; ENSG00000111728; -. DR PharmGKB; PA35770; -. DR VEuPathDB; HostDB:ENSG00000111728; -. DR eggNOG; KOG2692; Eukaryota. DR GeneTree; ENSGT01030000234535; -. DR HOGENOM; CLU_048583_1_0_1; -. DR InParanoid; Q92185; -. DR OMA; MAGLAWK; -. DR OrthoDB; 5348004at2759; -. DR PhylomeDB; Q92185; -. DR TreeFam; TF323961; -. DR BioCyc; MetaCyc:HS03456-MONOMER; -. DR BRENDA; 2.4.99.8; 2681. DR PathwayCommons; Q92185; -. DR Reactome; R-HSA-4085001; Sialic acid metabolism. DR SABIO-RK; Q92185; -. DR SignaLink; Q92185; -. DR UniPathway; UPA00222; -. DR UniPathway; UPA00378; -. DR BioGRID-ORCS; 6489; 10 hits in 1132 CRISPR screens. DR ChiTaRS; ST8SIA1; human. DR GeneWiki; ST8SIA1; -. DR GenomeRNAi; 6489; -. DR Pharos; Q92185; Tbio. DR PRO; PR:Q92185; -. DR Proteomes; UP000005640; Chromosome 12. DR RNAct; Q92185; Protein. DR Bgee; ENSG00000111728; Expressed in ventricular zone and 146 other cell types or tissues. DR ExpressionAtlas; Q92185; baseline and differential. DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome. DR GO; GO:0016020; C:membrane; TAS:ProtInc. DR GO; GO:0003828; F:alpha-N-acetylneuraminate alpha-2,8-sialyltransferase activity; IDA:UniProtKB. DR GO; GO:0008373; F:sialyltransferase activity; TAS:ProtInc. DR GO; GO:0005975; P:carbohydrate metabolic process; TAS:ProtInc. DR GO; GO:0034605; P:cellular response to heat; IEA:Ensembl. DR GO; GO:0050673; P:epithelial cell proliferation; IEA:Ensembl. DR GO; GO:0006688; P:glycosphingolipid biosynthetic process; TAS:ProtInc. DR GO; GO:0006491; P:N-glycan processing; IBA:GO_Central. DR GO; GO:0009311; P:oligosaccharide metabolic process; IBA:GO_Central. DR GO; GO:0050679; P:positive regulation of epithelial cell proliferation; IEA:Ensembl. DR GO; GO:0006486; P:protein glycosylation; IBA:GO_Central. DR Gene3D; 3.90.1480.20; Glycosyl transferase family 29; 1. DR InterPro; IPR001675; Glyco_trans_29. DR InterPro; IPR038578; GT29-like_sf. DR InterPro; IPR012163; Sialyl_trans. DR PANTHER; PTHR11987; ALPHA-2,8-SIALYLTRANSFERASE; 1. DR PANTHER; PTHR11987:SF3; ALPHA-N-ACETYLNEURAMINIDE ALPHA-2,8-SIALYLTRANSFERASE; 1. DR Pfam; PF00777; Glyco_transf_29; 1. DR PIRSF; PIRSF005557; Sialyl_trans; 1. DR Genevisible; Q92185; HS. PE 1: Evidence at protein level; KW Alternative splicing; Disulfide bond; Glycoprotein; Glycosyltransferase; KW Golgi apparatus; Lipid metabolism; Membrane; Reference proteome; KW Signal-anchor; Sphingolipid metabolism; Transferase; Transmembrane; KW Transmembrane helix. FT CHAIN 1..356 FT /note="Alpha-N-acetylneuraminide alpha-2,8- FT sialyltransferase" FT /id="PRO_0000149282" FT TOPO_DOM 1..29 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 30..48 FT /note="Helical; Signal-anchor for type II membrane protein" FT /evidence="ECO:0000255" FT TOPO_DOM 49..356 FT /note="Lumenal" FT /evidence="ECO:0000255" FT ACT_SITE 322 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000250|UniProtKB:O43173" FT BINDING 143 FT /ligand="CMP-N-acetyl-beta-neuraminate" FT /ligand_id="ChEBI:CHEBI:57812" FT /evidence="ECO:0000250|UniProtKB:O43173" FT BINDING 166 FT /ligand="CMP-N-acetyl-beta-neuraminate" FT /ligand_id="ChEBI:CHEBI:57812" FT /evidence="ECO:0000250|UniProtKB:O43173" FT BINDING 274 FT /ligand="CMP-N-acetyl-beta-neuraminate" FT /ligand_id="ChEBI:CHEBI:57812" FT /evidence="ECO:0000250|UniProtKB:O43173" FT BINDING 275 FT /ligand="CMP-N-acetyl-beta-neuraminate" FT /ligand_id="ChEBI:CHEBI:57812" FT /evidence="ECO:0000250|UniProtKB:O43173" FT BINDING 276 FT /ligand="CMP-N-acetyl-beta-neuraminate" FT /ligand_id="ChEBI:CHEBI:57812" FT /evidence="ECO:0000250|UniProtKB:O43173" FT BINDING 296 FT /ligand="CMP-N-acetyl-beta-neuraminate" FT /ligand_id="ChEBI:CHEBI:57812" FT /evidence="ECO:0000250|UniProtKB:O43173" FT BINDING 310 FT /ligand="CMP-N-acetyl-beta-neuraminate" FT /ligand_id="ChEBI:CHEBI:57812" FT /evidence="ECO:0000250|UniProtKB:O43173" FT CARBOHYD 71 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 119 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 214 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 245 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 138..287 FT /evidence="ECO:0000250|UniProtKB:O43173" FT DISULFID 152..347 FT /evidence="ECO:0000250|UniProtKB:O43173" FT VAR_SEQ 128..135 FT /note="ATPFQLPL -> MQSPSFVK (in isoform 2)" FT /evidence="ECO:0000303|Ref.5, ECO:0000303|Ref.6" FT /id="VSP_047583" FT VAR_SEQ 136..356 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|Ref.5, ECO:0000303|Ref.6" FT /id="VSP_047584" FT MUTAGEN 188 FT /note="N->D: Enzyme activity is 42% of the wild-type. A FT 2.5-fold increase in Km value for FT CMP-N-acetyl-beta-neuraminate. A 2.3-fold decrease in Vmax FT for both CMP-N-acetyl-beta-neuraminate and ganglioside FT GM3." FT /evidence="ECO:0000269|PubMed:18348864" FT MUTAGEN 189 FT /note="P->A: Enzyme activity is 91% of the wild-type." FT /evidence="ECO:0000269|PubMed:18348864" FT MUTAGEN 190 FT /note="S->A: Enzyme activity is 33% of the wild-type. A FT 2-fold increase in Km value for ganglioside GM3 and 1.25 FT fold increase in Km value for FT CMP-N-acetyl-beta-neuraminate. A 3-fold decrease in Vmax FT for both CMP-N-acetyl-beta-neuraminate and ganglioside FT GM3." FT MUTAGEN 272 FT /note="R->A: Enzyme activity is 20% of the wild-type. A FT 10-fold increase in Km value for ganglioside GM3. A 5-fold FT decrease in Vmax for both CMP-N-acetyl-beta-neuraminate and FT ganglioside GM3." FT /evidence="ECO:0000269|PubMed:18348864" FT MUTAGEN 272 FT /note="R->I: Enzyme activity is 19% of the wild-type." FT /evidence="ECO:0000269|PubMed:18348864" FT MUTAGEN 272 FT /note="R->K: Enzyme activity is 98% of the wild-type." FT /evidence="ECO:0000269|PubMed:18348864" SQ SEQUENCE 356 AA; 40519 MW; 452FE04856964395 CRC64; MSPCGRARRQ TSRGAMAVLA WKFPRTRLPM GASALCVVVL CWLYIFPVYR LPNEKEIVQG VLQQGTAWRR NQTAARAFRK QMEDCCDPAH LFAMTKMNSP MGKSMWYDGE FLYSFTIDNS TYSLFPQATP FQLPLKKCAV VGNGGILKKS GCGRQIDEAN FVMRCNLPPL SSEYTKDVGS KSQLVTANPS IIRQRFQNLL WSRKTFVDNM KIYNHSYIYM PAFSMKTGTE PSLRVYYTLS DVGANQTVLF ANPNFLRSIG KFWKSRGIHA KRLSTGLFLV SAALGLCEEV AIYGFWPFSV NMHEQPISHH YYDNVLPFSG FHAMPEEFLQ LWYLHKIGAL RMQLDPCEDT SLQPTS //