ID Q8BWI0_MOUSE Unreviewed; 355 AA. AC Q8BWI0; DT 01-MAR-2003, integrated into UniProtKB/TrEMBL. DT 01-MAR-2003, sequence version 1. DT 24-JUL-2024, entry version 102. DE RecName: Full=Alpha-N-acetylneuraminide alpha-2,8-sialyltransferase {ECO:0000256|ARBA:ARBA00041024}; DE EC=2.4.3.8 {ECO:0000256|ARBA:ARBA00039110}; DE AltName: Full=Alpha-2,8-sialyltransferase 8A {ECO:0000256|ARBA:ARBA00041984}; DE AltName: Full=Ganglioside GD3 synthase {ECO:0000256|ARBA:ARBA00041950}; DE AltName: Full=Sialyltransferase 8A {ECO:0000256|ARBA:ARBA00042694}; DE AltName: Full=Sialyltransferase St8Sia I {ECO:0000256|ARBA:ARBA00042820}; GN Name=St8sia1 {ECO:0000313|MGI:MGI:106011}; GN Synonyms=Siat8a {ECO:0000313|MGI:MGI:106011}; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090 {ECO:0000313|EMBL:BAC34994.1}; RN [1] {ECO:0000313|EMBL:BAC34994.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAC34994.1}; RC TISSUE=Lung {ECO:0000313|EMBL:BAC34994.1}; RX PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9; RA Carninci P., Hayashizaki Y.; RT "High-efficiency full-length cDNA cloning."; RL Methods Enzymol. 303:19-44(1999). RN [2] {ECO:0000313|EMBL:BAC34994.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAC34994.1}; RC TISSUE=Lung {ECO:0000313|EMBL:BAC34994.1}; RX PubMed=11042159; DOI=10.1101/gr.145100; RA Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M., RA Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.; RT "Normalization and subtraction of cap-trapper-selected cDNAs to prepare RT full-length cDNA libraries for rapid discovery of new genes."; RL Genome Res. 10:1617-1630(2000). RN [3] {ECO:0000313|EMBL:BAC34994.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAC34994.1}; RC TISSUE=Lung {ECO:0000313|EMBL:BAC34994.1}; RX PubMed=11076861; DOI=10.1101/gr.152600; RA Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P., RA Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M., Sumi N., RA Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A., Yamamoto R., RA Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K., Fujiwake S., RA Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M., Yoneda Y., RA Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J., Okazaki Y., RA Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.; RT "RIKEN integrated sequence analysis (RISA) system--384-format sequencing RT pipeline with 384 multicapillary sequencer."; RL Genome Res. 10:1757-1771(2000). RN [4] {ECO:0000313|EMBL:BAC34994.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAC34994.1}; RC TISSUE=Lung {ECO:0000313|EMBL:BAC34994.1}; RX PubMed=11217851; DOI=10.1038/35055500; RG The RIKEN Genome Exploration Research Group Phase II Team and the FANTOM Consortium; RT "Functional annotation of a full-length mouse cDNA collection."; RL Nature 409:685-690(2001). RN [5] {ECO:0000313|EMBL:BAC34994.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAC34994.1}; RC TISSUE=Lung {ECO:0000313|EMBL:BAC34994.1}; RA Adachi J., Aizawa K., Akimura T., Arakawa T., Bono H., Carninci P., RA Fukuda S., Furuno M., Hanagaki T., Hara A., Hashizume W., Hayashida K., RA Hayatsu N., Hiramoto K., Hiraoka T., Hirozane T., Hori F., Imotani K., RA Ishii Y., Itoh M., Kagawa I., Kasukawa T., Katoh H., Kawai J., Kojima Y., RA Kondo S., Konno H., Kouda M., Koya S., Kurihara C., Matsuyama T., RA Miyazaki A., Murata M., Nakamura M., Nishi K., Nomura K., Numazaki R., RA Ohno M., Ohsato N., Okazaki Y., Saito R., Saitoh H., Sakai C., Sakai K., RA Sakazume N., Sano H., Sasaki D., Shibata K., Shinagawa A., Shiraki T., RA Sogabe Y., Tagami M., Tagawa A., Takahashi F., Takaku-Akahira S., RA Takeda Y., Tanaka T., Tomaru A., Toya T., Yasunishi A., Muramatsu M., RA Hayashizaki Y.; RL Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases. RN [6] {ECO:0000313|EMBL:BAC34994.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAC34994.1}; RC TISSUE=Lung {ECO:0000313|EMBL:BAC34994.1}; RX PubMed=12466851; DOI=10.1038/nature01266; RG The FANTOM Consortium and the RIKEN Genome Exploration Research Group Phase I and II Team; RT "Analysis of the mouse transcriptome based on functional annotation of RT 60,770 full-length cDNAs."; RL Nature 420:563-573(2002). RN [7] {ECO:0000313|EMBL:BAC34994.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAC34994.1}; RC TISSUE=Lung {ECO:0000313|EMBL:BAC34994.1}; RG The FANTOM Consortium; RG Riken Genome Exploration Research Group and Genome Science Group (Genome Network Project Core Group); RT "The Transcriptional Landscape of the Mammalian Genome."; RL Science 309:1559-1563(2005). RN [8] {ECO:0000313|EMBL:BAC34994.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAC34994.1}; RC TISSUE=Lung {ECO:0000313|EMBL:BAC34994.1}; RX PubMed=16141073; DOI=10.1126/science.1112009; RG RIKEN Genome Exploration Research Group and Genome Science Group (Genome Network Project Core Group) and the FANTOM Consortium; RT "Antisense Transcription in the Mammalian Transcriptome."; RL Science 309:1564-1566(2005). 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:0000256|ARBA:ARBA00044457}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77372; CC Evidence={ECO:0000256|ARBA:ARBA00044457}; 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:0000256|ARBA:ARBA00043743}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41769; CC Evidence={ECO:0000256|ARBA:ARBA00043743}; 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:0000256|ARBA:ARBA00043833}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41765; CC Evidence={ECO:0000256|ARBA:ARBA00043833}; 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:0000256|ARBA:ARBA00044471}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77296; CC Evidence={ECO:0000256|ARBA:ARBA00044471}; 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:0000256|ARBA:ARBA00043723}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47577; CC Evidence={ECO:0000256|ARBA:ARBA00043723}; 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:0000256|ARBA:ARBA00043813}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41761; CC Evidence={ECO:0000256|ARBA:ARBA00043813}; 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:0000256|ARBA:ARBA00043792}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41773; CC Evidence={ECO:0000256|ARBA:ARBA00043792}; 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:0000256|ARBA:ARBA00036589}; CC -!- PATHWAY: Lipid metabolism; sphingolipid metabolism. CC {ECO:0000256|ARBA:ARBA00004760}. CC -!- PATHWAY: Protein modification; protein glycosylation. CC {ECO:0000256|ARBA:ARBA00004922}. CC -!- PATHWAY: Sphingolipid metabolism. {ECO:0000256|ARBA:ARBA00004991}. CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane CC {ECO:0000256|ARBA:ARBA00004323}; Single-pass type II membrane protein CC {ECO:0000256|ARBA:ARBA00004323}. Membrane CC {ECO:0000256|ARBA:ARBA00004606}; Single-pass type II membrane protein CC {ECO:0000256|ARBA:ARBA00004606}. CC -!- SIMILARITY: Belongs to the glycosyltransferase 29 family. CC {ECO:0000256|ARBA:ARBA00006003}. 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; AK052444; BAC34994.1; -; mRNA. DR AlphaFoldDB; Q8BWI0; -. DR CAZy; GT29; Glycosyltransferase Family 29. DR AGR; MGI:106011; -. DR MGI; MGI:106011; St8sia1. DR ChiTaRS; St8sia1; mouse. DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell. DR GO; GO:0003828; F:alpha-N-acetylneuraminate alpha-2,8-sialyltransferase activity; IEA:TreeGrafter. DR GO; GO:0006491; P:N-glycan processing; IEA:TreeGrafter. DR GO; GO:0009311; P:oligosaccharide metabolic process; IEA:TreeGrafter. DR GO; GO:0006486; P:protein glycosylation; IEA:InterPro. DR GO; GO:0006665; P:sphingolipid metabolic process; IEA:UniProtKB-KW. DR Gene3D; 3.90.1480.20; Glycosyl transferase family 29; 1. DR InterPro; IPR001675; Glyco_trans_29. DR InterPro; IPR050943; Glycosyltr_29_Sialyltrsf. 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. PE 2: Evidence at transcript level; KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157}; KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180}; KW Golgi apparatus {ECO:0000256|ARBA:ARBA00023034}; KW Lipid metabolism {ECO:0000256|ARBA:ARBA00022919}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius}; KW Signal-anchor {ECO:0000256|ARBA:ARBA00022968}; KW Sphingolipid metabolism {ECO:0000256|ARBA:ARBA00022919}; KW Transferase {ECO:0000256|ARBA:ARBA00022679}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, KW ECO:0000256|SAM:Phobius}. FT TRANSMEM 27..48 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DISULFID 137..286 FT /evidence="ECO:0000256|PIRSR:PIRSR005557-2" SQ SEQUENCE 355 AA; 40338 MW; 143DA51BB9E194E1 CRC64; MSPCGRALHT SRGAMAMLAR KFPRTRLPVG ASALCVVVLC WLYIFPVYRL PNEKEIVQGV LAQRTAWRTN QTSASLFRRQ MEDCCDPAHL FAMTKMNSPM GKSLWYDGEL LYSFTIDNST YSLFPQATPF QLPLKKCAVV GNGGILKMSG CGRQIDEANF VMRCNLPPLS SEYTRDVGSK TQLVTANPSI IRQRFEKLLW SRKKFVDNMK IYNHSYIYMP AFSMKTGTEP SLRVYYTLKD VGANQTVLFA NPNFLRNIGK FWKSRGIHAK RLSTGLFLVS AALGLCEEVS IYGFWPFSVN MQGDPISHHY YDNVLPFSGY HAMPEEFLQL WYLHKIGALR MQLDPCEEPS PQPTS //