SIA8E_MOUSE
ID SIA8E_MOUSE Reviewed; 412 AA.
AC P70126; E9QKY5; P70127; P70128;
DT 11-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Alpha-2,8-sialyltransferase 8E {ECO:0000305};
DE EC=2.4.99.- {ECO:0000269|PubMed:8910600};
DE AltName: Full=Sialyltransferase 8E;
DE Short=SIAT8-E;
DE AltName: Full=Sialyltransferase St8Sia V;
DE Short=ST8SiaV;
GN Name=St8sia5 {ECO:0000312|EMBL:CAA66642.1}; Synonyms=Siat8e, St8siav;
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], CHARACTERIZATION, ALTERNATIVE SPLICING,
RP FUNCTION, CATALYTIC ACTIVITY, DEVELOPMENTAL STAGE, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RC TISSUE=Brain;
RX PubMed=8910600; DOI=10.1074/jbc.271.46.29366;
RA Kono M., Yoshida Y., Kojima N., Tsuji S.;
RT "Molecular cloning and expression of a fifth type of alpha2,8-
RT sialyltransferase (ST8Sia V). Its substrate specificity is similar to that
RT of SAT-V/III, which synthesize GD1c, GT1a, GQ1b and GT3.";
RL J. Biol. Chem. 271:29366-29371(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
CC -!- FUNCTION: Involved in the synthesis of gangliosides GD1c, GT1a, GQ1b,
CC GP1c and GT3 from GD1a, GT1b, GM1b and GD3 respectively.
CC {ECO:0000269|PubMed:8910600}.
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:8910600};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41773;
CC Evidence={ECO:0000269|PubMed:8910600};
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:8910600};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41765;
CC Evidence={ECO:0000269|PubMed:8910600};
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:8910600};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41769;
CC Evidence={ECO:0000269|PubMed:8910600};
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:0000250|UniProtKB:O15466};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47577;
CC Evidence={ECO:0000250|UniProtKB:O15466};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CMP-N-acetyl-beta-neuraminate + ganglioside GQ1c (d18:1(4E)) =
CC CMP + ganglioside GP1c (d18:1(4E)) + H(+); Xref=Rhea:RHEA:47592,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57812, ChEBI:CHEBI:60377,
CC ChEBI:CHEBI:87791, ChEBI:CHEBI:87792;
CC Evidence={ECO:0000250|UniProtKB:Q6ZXC8};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47593;
CC Evidence={ECO:0000250|UniProtKB:Q6ZXC8};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES: [Isoform V-L]:
CC Kinetic parameters:
CC KM=1 mM for GM1b {ECO:0000269|PubMed:8910600};
CC KM=0.068 mM for GT1b {ECO:0000269|PubMed:8910600};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES: [Isoform V-M]:
CC Kinetic parameters:
CC KM=1.1 mM for GM1b {ECO:0000269|PubMed:8910600};
CC KM=0.070 mM for GT1b {ECO:0000269|PubMed:8910600};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES: [Isoform V-S]:
CC Kinetic parameters:
CC KM=1 mM for GM1b {ECO:0000269|PubMed:8910600};
CC KM=0.072 mM for GT1b {ECO:0000269|PubMed:8910600};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000269|PubMed:8910600}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:Q6ZXC8}; Single-pass type II membrane protein
CC {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=V-L; Synonyms=Long;
CC IsoId=P70126-1; Sequence=Displayed;
CC Name=V-M; Synonyms=Middle;
CC IsoId=P70126-2; Sequence=VSP_001789;
CC Name=V-S; Synonyms=Short;
CC IsoId=P70126-3; Sequence=VSP_001790;
CC -!- TISSUE SPECIFICITY: Highly expressed in brain. Expressed at low levels
CC in other tissues, including liver, testis, lung, placenta and spleen.
CC {ECO:0000269|PubMed:8910600}.
CC -!- DEVELOPMENTAL STAGE: First detected at 14 dpc, expression increases
CC until at least 7 weeks after birth. {ECO:0000269|PubMed:8910600}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 29 family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase; Note=ST8Sia V;
CC URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_mou_660";
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DR EMBL; X98014; CAA66642.1; -; mRNA.
DR EMBL; X98014; CAA66643.1; -; mRNA.
DR EMBL; X98014; CAA66644.1; -; mRNA.
DR EMBL; AC157991; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS29353.1; -. [P70126-2]
DR CCDS; CCDS50325.1; -. [P70126-1]
DR RefSeq; NP_038694.2; NM_013666.2. [P70126-1]
DR AlphaFoldDB; P70126; -.
DR SMR; P70126; -.
DR STRING; 10090.ENSMUSP00000074764; -.
DR SwissLipids; SLP:000000750; -. [P70126-2]
DR CAZy; GT29; Glycosyltransferase Family 29.
DR GlyGen; P70126; 5 sites.
DR iPTMnet; P70126; -.
DR PhosphoSitePlus; P70126; -.
DR PaxDb; P70126; -.
DR PRIDE; P70126; -.
DR ProteomicsDB; 257236; -. [P70126-1]
DR ProteomicsDB; 257237; -. [P70126-2]
DR ProteomicsDB; 257238; -. [P70126-3]
DR Antibodypedia; 54885; 39 antibodies from 10 providers.
DR DNASU; 225742; -.
DR Ensembl; ENSMUST00000075290; ENSMUSP00000074764; ENSMUSG00000025425. [P70126-1]
DR Ensembl; ENSMUST00000079618; ENSMUSP00000078566; ENSMUSG00000025425. [P70126-2]
DR GeneID; 225742; -.
DR KEGG; mmu:225742; -.
DR UCSC; uc008frh.2; mouse. [P70126-1]
DR CTD; 29906; -.
DR MGI; MGI:109243; St8sia5.
DR VEuPathDB; HostDB:ENSMUSG00000025425; -.
DR eggNOG; KOG2692; Eukaryota.
DR GeneTree; ENSGT01030000234535; -.
DR HOGENOM; CLU_048583_1_1_1; -.
DR InParanoid; P70126; -.
DR OMA; FEFNSTA; -.
DR OrthoDB; 825014at2759; -.
DR PhylomeDB; P70126; -.
DR TreeFam; TF323961; -.
DR Reactome; R-MMU-4085001; Sialic acid metabolism.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 225742; 6 hits in 74 CRISPR screens.
DR PRO; PR:P70126; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; P70126; protein.
DR Bgee; ENSMUSG00000025425; Expressed in cerebellar cortex and 77 other tissues.
DR ExpressionAtlas; P70126; baseline and differential.
DR Genevisible; P70126; MM.
DR GO; GO:0000139; C:Golgi membrane; ISS:UniProtKB.
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:0008373; F:sialyltransferase activity; ISO:MGI.
DR GO; GO:0006688; P:glycosphingolipid biosynthetic process; ISS:UniProtKB.
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: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; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..412
FT /note="Alpha-2,8-sialyltransferase 8E"
FT /id="PRO_0000149297"
FT TOPO_DOM 1..16
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 17..37
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 38..412
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT ACT_SITE 384
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:O43173"
FT BINDING 228
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O43173"
FT BINDING 250..252
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O43173"
FT BINDING 336..338
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O43173"
FT CARBOHYD 58
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 64
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 73
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 92
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 277
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 200..349
FT /evidence="ECO:0000250|UniProtKB:O43173"
FT DISULFID 214..409
FT /evidence="ECO:0000250|UniProtKB:O43173"
FT VAR_SEQ 44..110
FT /note="Missing (in isoform V-S)"
FT /evidence="ECO:0000305"
FT /id="VSP_001790"
FT VAR_SEQ 44..79
FT /note="Missing (in isoform V-M)"
FT /evidence="ECO:0000305"
FT /id="VSP_001789"
FT CONFLICT 132..134
FT /note="DTA -> GAS (in Ref. 1; CAA66642/CAA66643/CAA66644)"
FT /evidence="ECO:0000305"
FT CONFLICT 151
FT /note="S -> N (in Ref. 1; CAA66642/CAA66643/CAA66644)"
FT /evidence="ECO:0000305"
FT CONFLICT 340
FT /note="I -> S (in Ref. 1; CAA66642/CAA66643/CAA66644)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 412 AA; 47829 MW; 1BBF9256017F7305 CRC64;
MRYADPSANR DLLGNRTLLF IFICAFALVT LLQQILYSKS YIKRGFQFGW QRGDQQANWT
GLFNDSDSPT EQNITGSSSR YFEFYKEPLE FNSTRCLELR QEILEVKVLS MVKQSELFER
WKSLQICKWA MDTAEASLFK STLSRCCNAP SFLFTTQKNT PVETNLRYEV ESSGLYHIDQ
EIFKMFPKEM PYYRSQFKKC AVVGNGGILK NSGCGKEINS ADFVFRCNLP PISGIYTTDV
GEKTDVVTVN PSIIIDRFHK LEKWRRPFFS VLQRYENASV LLPAFYNVRN TLVSFRVKYM
LDDFQSRQPV YFFHPQYLSS VSRYWLSLGV RARRISTGLI LVTAALELCE EVHLFGFWAF
PMNPSGFFIT HHYYDNVKPK PGFHAMPSEI FTFLRMHSRG ILRVHTGTCN CC
