SIA8B_MOUSE
ID SIA8B_MOUSE Reviewed; 375 AA.
AC O35696; Q4VA47;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Alpha-2,8-sialyltransferase 8B;
DE EC=2.4.99.-;
DE AltName: Full=Polysialic acid synthase;
DE AltName: Full=Sialyltransferase 8B;
DE Short=SIAT8-B;
DE AltName: Full=Sialyltransferase St8Sia II;
DE Short=ST8SiaII;
DE AltName: Full=Sialyltransferase X;
DE Short=STX;
GN Name=St8sia2; Synonyms=Siat8b, Stx;
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 [GENOMIC DNA / MRNA].
RC TISSUE=Brain;
RX PubMed=8939967; DOI=10.1074/jbc.271.47.30167;
RA Yoshida Y., Kurosawa N., Kanematsu T., Kojima N., Tsuji S.;
RT "Genomic structure and promoter activity of the mouse polysialic acid
RT synthase gene (mST8Sia II). Brain-specific expression from a TATA-less GC-
RT rich sequence.";
RL J. Biol. Chem. 271:30167-30173(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=7875291; DOI=10.1016/0014-5793(95)00059-i;
RA Kojima N., Yoshida Y., Kurosawa N., Lee Y.C., Tsuji S.;
RT "Enzymatic activity of a developmentally regulated member of the
RT sialyltransferase family (STX): evidence for alpha 2,8-sialyltransferase
RT activity toward N-linked oligosaccharides.";
RL FEBS Lett. 360:1-4(1995).
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: May transfer sialic acid through alpha-2,8-linkages to the
CC alpha-2,3-linked and alpha-2,6-linked sialic acid of N-linked
CC oligosaccharides of glycoproteins and may be involved in PSA
CC (polysialic acid) expression. {ECO:0000250}.
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- INTERACTION:
CC O35696; Q9BY67: CADM1; Xeno; NbExp=2; IntAct=EBI-15854779, EBI-5652260;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000305}; Single-
CC pass type II membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 29 family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase; Note=ST8Sia
CC II;
CC URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_mou_657";
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DR EMBL; X99646; CAA67965.1; -; Genomic_DNA.
DR EMBL; X99647; CAA67965.1; JOINED; Genomic_DNA.
DR EMBL; X99648; CAA67965.1; JOINED; Genomic_DNA.
DR EMBL; X99651; CAA67965.1; JOINED; Genomic_DNA.
DR EMBL; X99649; CAA67965.1; JOINED; Genomic_DNA.
DR EMBL; X99650; CAA67965.1; JOINED; Genomic_DNA.
DR EMBL; X83562; CAA58548.1; -; mRNA.
DR EMBL; BC096546; AAH96546.1; -; mRNA.
DR EMBL; CH466543; EDL07123.1; -; Genomic_DNA.
DR CCDS; CCDS21365.1; -.
DR PIR; I48686; I48686.
DR RefSeq; NP_033207.2; NM_009181.2.
DR AlphaFoldDB; O35696; -.
DR SMR; O35696; -.
DR BioGRID; 203244; 1.
DR DIP; DIP-59528N; -.
DR IntAct; O35696; 2.
DR STRING; 10090.ENSMUSP00000026896; -.
DR CAZy; GT29; Glycosyltransferase Family 29.
DR GlyGen; O35696; 6 sites.
DR iPTMnet; O35696; -.
DR PhosphoSitePlus; O35696; -.
DR MaxQB; O35696; -.
DR PaxDb; O35696; -.
DR PRIDE; O35696; -.
DR ProteomicsDB; 261360; -.
DR Antibodypedia; 29022; 132 antibodies from 30 providers.
DR DNASU; 20450; -.
DR Ensembl; ENSMUST00000026896; ENSMUSP00000026896; ENSMUSG00000025789.
DR GeneID; 20450; -.
DR KEGG; mmu:20450; -.
DR UCSC; uc009hwe.2; mouse.
DR CTD; 8128; -.
DR MGI; MGI:106020; St8sia2.
DR VEuPathDB; HostDB:ENSMUSG00000025789; -.
DR eggNOG; KOG2692; Eukaryota.
DR GeneTree; ENSGT01030000234535; -.
DR HOGENOM; CLU_048583_3_0_1; -.
DR InParanoid; O35696; -.
DR OMA; TWRHNQT; -.
DR OrthoDB; 825014at2759; -.
DR PhylomeDB; O35696; -.
DR TreeFam; TF352820; -.
DR BRENDA; 2.4.99.8; 3474.
DR Reactome; R-MMU-4085001; Sialic acid metabolism.
DR Reactome; R-MMU-419037; NCAM1 interactions.
DR Reactome; R-MMU-975577; N-Glycan antennae elongation.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 20450; 2 hits in 77 CRISPR screens.
DR ChiTaRS; St8sia2; mouse.
DR PRO; PR:O35696; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; O35696; protein.
DR Bgee; ENSMUSG00000025789; Expressed in rostral migratory stream and 160 other tissues.
DR ExpressionAtlas; O35696; baseline and differential.
DR Genevisible; O35696; MM.
DR GO; GO:0005769; C:early endosome; IDA:MGI.
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:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0055037; C:recycling endosome; IDA:MGI.
DR GO; GO:0003828; F:alpha-N-acetylneuraminate alpha-2,8-sialyltransferase activity; IDA:MGI.
DR GO; GO:0008373; F:sialyltransferase activity; ISO:MGI.
DR GO; GO:0001574; P:ganglioside biosynthetic process; ISO:MGI.
DR GO; GO:0006491; P:N-glycan processing; ISO:MGI.
DR GO; GO:1990138; P:neuron projection extension; ISO:MGI.
DR GO; GO:0009311; P:oligosaccharide metabolic process; ISO:MGI.
DR GO; GO:1901216; P:positive regulation of neuron death; ISO:MGI.
DR GO; GO:0051965; P:positive regulation of synapse assembly; ISO:MGI.
DR GO; GO:0006486; P:protein glycosylation; ISO:MGI.
DR GO; GO:0042220; P:response to cocaine; IEA:Ensembl.
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..375
FT /note="Alpha-2,8-sialyltransferase 8B"
FT /id="PRO_0000149286"
FT TOPO_DOM 1..6
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 7..23
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 24..375
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT ACT_SITE 346
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:O43173"
FT BINDING 185
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O43173"
FT BINDING 206..208
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O43173"
FT BINDING 294..296
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O43173"
FT BINDING 329..330
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O43173"
FT CARBOHYD 60
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 72
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 89
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 134
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 219
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 234
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 157..307
FT /evidence="ECO:0000250|UniProtKB:O43173"
FT DISULFID 171..371
FT /evidence="ECO:0000250|UniProtKB:O43173"
FT CONFLICT 186
FT /note="L -> R (in Ref. 1; CAA67965/CAA58548)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 375 AA; 42411 MW; 34F43C519A0236CF CRC64;
MQLQFRSWML AALTLLVVFL IFADISEIEE EIGNSGGRGT IRSAVNSLHS KSNRAEVVIN
GSSPPAVADR SNESLKHNIQ PASSKWRHNQ TLSLRIRKQI LKFLDAEKDI SVLKGTLKPG
DIIHYIFDRD STMNVSQNLY ELLPRTSPLK NKHFQTCAIV GNSGVLLNSG CGQEIDTHSF
VIRCNLAPVQ EYARDVGLKT DLVTMNPSVI QRAFEDLVNA TWREKLLQRL HGLNGSILWI
PAFMARGGKE RVEWVNALIL KHHVNVRTAY PSLRLLHAVR GYWLTNKVHI KRPTTGLLMY
TLATRFCNQI YLYGFWPFPL DQNQNPVKYH YYDSLKYGYT SQASPHTMPL EFKALKSLHE
QGALKLTVGQ CDGAT
