SIA8A_HUMAN
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 03-AUG-2022, entry version 177.
DE RecName: Full=Alpha-N-acetylneuraminide alpha-2,8-sialyltransferase;
DE EC=2.4.99.8 {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; 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 glycosphinglolipds 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=2.4.99.8;
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=CMP-N-acetyl-beta-neuraminate + ganglioside GM3 (d18:1(4E)) =
CC CMP + ganglioside GD3 (d18:1(4E)) + 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=CMP-N-acetyl-beta-neuraminate + ganglioside GD3 (d18:1(4E)) =
CC CMP + ganglioside GT3 (d18:1(4E)) + 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=CMP-N-acetyl-beta-neuraminate + ganglioside GD1a (d18:1(4E)) =
CC CMP + ganglioside GT1a (d18:1(4E)) + 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=CMP-N-acetyl-beta-neuraminate + ganglioside GT1b (d18:1(4E)) =
CC CMP + ganglioside GQ1b (d18:1(4E)) + 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=CMP-N-acetyl-beta-neuraminate + ganglioside GM1b (d18:1(4E)) =
CC CMP + ganglioside GD1c (d18:1(4E)) + 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 -!- 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; Evidence={ECO:0000305};
CC Sequence=CAA54891.1; Type=Erroneous initiation; 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";
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DR EMBL; X77922; CAA54891.1; ALT_INIT; 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 GlyGen; Q92185; 4 sites.
DR iPTMnet; Q92185; -.
DR PhosphoSitePlus; Q92185; -.
DR SwissPalm; Q92185; -.
DR BioMuta; ST8SIA1; -.
DR MassIVE; Q92185; -.
DR PaxDb; Q92185; -.
DR PeptideAtlas; Q92185; -.
DR PRIDE; Q92185; -.
DR ProteomicsDB; 75252; -. [Q92185-1]
DR Antibodypedia; 12441; 70 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 CTD; 6489; -.
DR DisGeNET; 6489; -.
DR GeneCards; ST8SIA1; -.
DR HGNC; HGNC:10869; ST8SIA1.
DR HPA; ENSG00000111728; Tissue enhanced (brain).
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; NSPMGKN; -.
DR OrthoDB; 825014at2759; -.
DR PhylomeDB; Q92185; -.
DR TreeFam; TF323961; -.
DR BioCyc; MetaCyc:HS03456-MON; -.
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; 9 hits in 1054 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 144 other tissues.
DR ExpressionAtlas; Q92185; baseline and differential.
DR Genevisible; Q92185; HS.
DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR GO; GO:0016021; C:integral component of 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; -; 1.
DR InterPro; IPR001675; Glyco_trans_29.
DR InterPro; IPR038578; GT29-like_sf.
DR InterPro; IPR012163; Sialyl_trans.
DR Pfam; PF00777; Glyco_transf_29; 1.
DR PIRSF; PIRSF005557; Sialyl_trans; 1.
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 166
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O43173"
FT BINDING 188..190
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O43173"
FT BINDING 274..276
FT /ligand="substrate"
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 CMP-N-acetyl-beta-
FT neuraminate. A 2.3-fold decrease in Vmax for both CMP-N-
FT acetyl-beta-neuraminate and ganglioside 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 2-
FT fold increase in Km value for ganglioside GM3 and 1.25 fold
FT increase in Km value for CMP-N-acetyl-beta-neuraminate. A
FT 3-fold decrease in Vmax for both CMP-N-acetyl-beta-
FT neuraminate and ganglioside GM3."
FT MUTAGEN 272
FT /note="R->A: Enzyme activity is 20% of the wild-type. A 10-
FT 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
