SIA8C_MOUSE
ID SIA8C_MOUSE Reviewed; 380 AA.
AC Q64689; Q6DIB7;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Sia-alpha-2,3-Gal-beta-1,4-GlcNAc-R:alpha 2,8-sialyltransferase;
DE EC=2.4.99.- {ECO:0000269|PubMed:7782326};
DE AltName: Full=Alpha-2,8-sialyltransferase 8C;
DE AltName: Full=Alpha-2,8-sialyltransferase III;
DE AltName: Full=ST8 alpha-N-acetyl-neuraminide alpha-2,8-sialyltransferase 3;
DE AltName: Full=Sialyltransferase 8C;
DE Short=SIAT8-C;
DE AltName: Full=Sialyltransferase St8Sia III;
DE Short=ST8SiaIII;
GN Name=St8sia3; Synonyms=Siat8c;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, PATHWAY, CATALYTIC ACTIVITY, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC TISSUE=Brain;
RX PubMed=7782326; DOI=10.1074/jbc.270.24.14628;
RA Yoshida Y., Kojima N., Kurosawa N., Hamamoto T., Tsuji S.;
RT "Molecular cloning of Sia alpha 2,3Gal beta 1,4GlcNAc alpha 2,8-
RT sialyltransferase from mouse brain.";
RL J. Biol. Chem. 270:14628-14633(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Medulla oblongata;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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).
CC -!- FUNCTION: Catalyzes the transfer of sialic acid from a CMP-linked
CC sialic acid donor onto the terminal sialic acid of an acceptor through
CC alpha-2,8-linkages. Is active with alpha-2,3-linked, alpha-2,6-linked
CC and alpha-2,8-linked sialic acid of N-linked oligosaccharides of
CC glycoproteins and glycolipids. Displays preference for substrates with
CC alpha-2,3-linked terminal sialic acid. It can form polysialic acid in
CC vitro directly on alpha-2,3-, alpha-2,6-, or alpha-2,8-linked sialic
CC acid. {ECO:0000269|PubMed:7782326}.
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000269|PubMed:7782326}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:O43173}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000305}; Single-
CC pass type II membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in brain and testes.
CC {ECO:0000269|PubMed:7782326}.
CC -!- DEVELOPMENTAL STAGE: Expressed first in 20 dpc fetal brain and
CC decreases thereafter during development. {ECO:0000269|PubMed:7782326}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 29 family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase; Note=ST8Sia
CC III;
CC URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_mou_658";
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DR EMBL; X80502; CAA56665.1; -; mRNA.
DR EMBL; AK133780; BAE21835.1; -; mRNA.
DR EMBL; AK134678; BAE22237.1; -; mRNA.
DR EMBL; CH466528; EDL09712.1; -; Genomic_DNA.
DR EMBL; BC075645; AAH75645.1; -; mRNA.
DR CCDS; CCDS29301.1; -.
DR PIR; A56950; A56950.
DR RefSeq; NP_033208.2; NM_009182.3.
DR AlphaFoldDB; Q64689; -.
DR SMR; Q64689; -.
DR STRING; 10090.ENSMUSP00000025477; -.
DR CAZy; GT29; Glycosyltransferase Family 29.
DR GlyConnect; 2707; 5 N-Linked glycans (2 sites).
DR GlyGen; Q64689; 3 sites, 5 N-linked glycans (2 sites).
DR PhosphoSitePlus; Q64689; -.
DR MaxQB; Q64689; -.
DR PaxDb; Q64689; -.
DR PRIDE; Q64689; -.
DR ProteomicsDB; 261361; -.
DR Antibodypedia; 22809; 73 antibodies from 19 providers.
DR DNASU; 20451; -.
DR Ensembl; ENSMUST00000025477; ENSMUSP00000025477; ENSMUSG00000056812.
DR Ensembl; ENSMUST00000237770; ENSMUSP00000158392; ENSMUSG00000056812.
DR GeneID; 20451; -.
DR KEGG; mmu:20451; -.
DR UCSC; uc008fed.1; mouse.
DR CTD; 51046; -.
DR MGI; MGI:106019; St8sia3.
DR VEuPathDB; HostDB:ENSMUSG00000056812; -.
DR eggNOG; KOG2692; Eukaryota.
DR GeneTree; ENSGT01030000234535; -.
DR HOGENOM; CLU_048583_0_0_1; -.
DR InParanoid; Q64689; -.
DR OMA; VPRMYMF; -.
DR OrthoDB; 825014at2759; -.
DR PhylomeDB; Q64689; -.
DR TreeFam; TF323961; -.
DR BRENDA; 2.4.99.8; 3474.
DR Reactome; R-MMU-4085001; Sialic acid metabolism.
DR Reactome; R-MMU-975577; N-Glycan antennae elongation.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 20451; 0 hits in 73 CRISPR screens.
DR ChiTaRS; St8sia3; mouse.
DR PRO; PR:Q64689; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; Q64689; protein.
DR Bgee; ENSMUSG00000056812; Expressed in caudate-putamen and 116 other tissues.
DR Genevisible; Q64689; MM.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0003828; F:alpha-N-acetylneuraminate alpha-2,8-sialyltransferase activity; IDA:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0008373; F:sialyltransferase activity; ISO:MGI.
DR GO; GO:0001574; P:ganglioside biosynthetic process; ISO:MGI.
DR GO; GO:0009100; P:glycoprotein metabolic process; ISO:MGI.
DR GO; GO:0006491; P:N-glycan processing; ISS:UniProtKB.
DR GO; GO:0009311; P:oligosaccharide metabolic process; ISO:MGI.
DR GO; GO:0006486; P:protein glycosylation; ISO:MGI.
DR GO; GO:1990743; P:protein sialylation; ISS:UniProtKB.
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 Disulfide bond; Glycoprotein; Glycosyltransferase; Golgi apparatus;
KW Membrane; Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..380
FT /note="Sia-alpha-2,3-Gal-beta-1,4-GlcNAc-R:alpha 2,8-
FT sialyltransferase"
FT /id="PRO_0000149290"
FT TOPO_DOM 1..17
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 18..33
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 34..380
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT ACT_SITE 354
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:O43173"
FT BINDING 190
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O43173"
FT BINDING 211..213
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O43173"
FT BINDING 300..302
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O43173"
FT BINDING 336..337
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O43173"
FT CARBOHYD 93
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 113
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 206
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 162..313
FT /evidence="ECO:0000250|UniProtKB:O43173"
FT DISULFID 176..379
FT /evidence="ECO:0000250|UniProtKB:O43173"
FT CONFLICT 187
FT /note="F -> S (in Ref. 1; CAA56665)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 380 AA; 43942 MW; A4F607853DF67A1E CRC64;
MRNCKMARVA SVLGLVMLSV ALLILSLISY VSLKKENIFT TPKYASPGAP RMYMFHAGFR
SQFALKFLDQ SFVPITNSLT HELQEKPSKW TFNRTAFLHQ RQEILQHVDV IKNFSLTKSS
VRIGQLMHYD YSSHKYVFSI SNNFRSLLPD VSPIMNKRYN VCAVVGNSGI LTGSQCGQEI
DKSDFVFRCN FAPTEAFHKD VGRKTNLTTF NPSILEKYYN NLLTIQDRNN FFLSLKKLDG
AILWIPAFFF HTSATVTRTL VDFFVEHRGQ LKVQLAWPGN IMQHVNRYWK NKHLSPKRLS
TGILMYTLAS AICEEIHLYG FWPFGFDPNT REDLPYHYYD KKGTKFTTKW QESHQLPAEF
QLLYRMHGEG LTKLTLSHCA
