SIA8F_MOUSE
ID SIA8F_MOUSE Reviewed; 398 AA.
AC Q8K4T1;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Alpha-2,8-sialyltransferase 8F {ECO:0000305};
DE EC=2.4.99.-;
DE AltName: Full=Sialyltransferase 8F;
DE Short=SIAT8-F;
DE AltName: Full=Sialyltransferase St8Sia VI;
DE Short=ST8SiaVI;
GN Name=St8sia6 {ECO:0000312|MGI:MGI:2386797}; Synonyms=Siat8f;
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, CATALYTIC ACTIVITY, AND
RP TISSUE SPECIFICITY.
RX PubMed=11980897; DOI=10.1074/jbc.m112367200;
RA Takashima S., Ishida H.K., Inazu T., Ando T., Ishida H., Kiso M., Tsuji S.,
RA Tsujimoto M.;
RT "Molecular cloning and expression of a sixth type of alpha 2,8-
RT sialyltransferase (ST8Sia VI) that sialylates O-glycans.";
RL J. Biol. Chem. 277:24030-24038(2002).
CC -!- FUNCTION: Alpha-2,8-sialyltransferase that prefers O-glycans to N-
CC glycans or glycolipids as acceptor substrates. The minimal acceptor
CC substrate is the NeuAc-alpha-2,3(6)-Gal sequence at the non-reducing
CC end of their carbohydrate groups. {ECO:0000269|PubMed:11980897}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CMP-N-acetyl-beta-neuraminate + ganglioside GM3 = CMP +
CC ganglioside GD3 + H(+); Xref=Rhea:RHEA:48288, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57812, ChEBI:CHEBI:60377, ChEBI:CHEBI:79210,
CC ChEBI:CHEBI:79214; Evidence={ECO:0000269|PubMed:11980897};
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:11980897};
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:11980897};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CMP-N-acetyl-beta-neuraminate + ganglioside GD1a = CMP +
CC ganglioside GT1a + H(+); Xref=Rhea:RHEA:48912, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57812, ChEBI:CHEBI:60377, ChEBI:CHEBI:82637,
CC ChEBI:CHEBI:90501; Evidence={ECO:0000269|PubMed:11980897};
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:11980897};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CMP-N-acetyl-beta-neuraminate + ganglioside GM1b = CMP +
CC ganglioside GD1c + H(+); Xref=Rhea:RHEA:48916, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57812, ChEBI:CHEBI:60377, ChEBI:CHEBI:90151,
CC ChEBI:CHEBI:90856; Evidence={ECO:0000269|PubMed:11980897};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CMP-N-acetyl-beta-neuraminate + ganglioside GM4 (d18:1(4E)) =
CC CMP + H(+) + N-acetyl-alpha-neuraminosyl-(2->8)-N-acetyl-alpha-
CC neuraminosyl-(2->3)-beta-D-galactosyl-(1<->1')-N-acylsphing-4-enine;
CC Xref=Rhea:RHEA:48924, ChEBI:CHEBI:15378, ChEBI:CHEBI:57812,
CC ChEBI:CHEBI:60377, ChEBI:CHEBI:78482, ChEBI:CHEBI:90858;
CC Evidence={ECO:0000269|PubMed:11980897};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CMP-N-acetyl-beta-neuraminate + N-acetyl-alpha-neuraminosyl-
CC (2->3)-beta-D-galactosyl-(1<->1')-ceramide = CMP + H(+) + N-acetyl-
CC alpha-neuraminosyl-(2->8)-N-acetyl-alpha-neuraminosyl-(2->3)-beta-D-
CC galactosyl-(1<->1')-ceramide; Xref=Rhea:RHEA:48928,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57812, ChEBI:CHEBI:60377,
CC ChEBI:CHEBI:82643, ChEBI:CHEBI:90859;
CC Evidence={ECO:0000269|PubMed:11980897};
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:11980897};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CMP-N-acetyl-beta-neuraminate + ganglioside GT1b = CMP +
CC ganglioside GQ1b + H(+); Xref=Rhea:RHEA:48932, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57812, ChEBI:CHEBI:60377, ChEBI:CHEBI:82940,
CC ChEBI:CHEBI:90862; Evidence={ECO:0000269|PubMed:11980897};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000305}; Single-
CC pass type II membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Highly expressed in kidney and expressed and all
CC tissues tested. {ECO:0000269|PubMed:11980897}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 29 family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase; Note=ST8Sia
CC VI;
CC URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_mou_661";
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DR EMBL; AB059554; BAC01265.1; -; mRNA.
DR CCDS; CCDS15697.1; -.
DR RefSeq; NP_665837.1; NM_145838.1.
DR AlphaFoldDB; Q8K4T1; -.
DR SMR; Q8K4T1; -.
DR BioGRID; 232295; 1.
DR STRING; 10090.ENSMUSP00000003509; -.
DR SwissLipids; SLP:000001419; -.
DR CAZy; GT29; Glycosyltransferase Family 29.
DR GlyGen; Q8K4T1; 4 sites.
DR PhosphoSitePlus; Q8K4T1; -.
DR PaxDb; Q8K4T1; -.
DR PRIDE; Q8K4T1; -.
DR ProteomicsDB; 257239; -.
DR Antibodypedia; 2510; 83 antibodies from 17 providers.
DR DNASU; 241230; -.
DR Ensembl; ENSMUST00000003509; ENSMUSP00000003509; ENSMUSG00000003418.
DR GeneID; 241230; -.
DR KEGG; mmu:241230; -.
DR UCSC; uc008ikc.2; mouse.
DR CTD; 338596; -.
DR MGI; MGI:2386797; St8sia6.
DR VEuPathDB; HostDB:ENSMUSG00000003418; -.
DR eggNOG; KOG2692; Eukaryota.
DR GeneTree; ENSGT01030000234535; -.
DR HOGENOM; CLU_048583_1_1_1; -.
DR InParanoid; Q8K4T1; -.
DR OMA; EQASKCK; -.
DR OrthoDB; 825014at2759; -.
DR PhylomeDB; Q8K4T1; -.
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; 241230; 1 hit in 75 CRISPR screens.
DR ChiTaRS; St8sia6; mouse.
DR PRO; PR:Q8K4T1; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q8K4T1; protein.
DR Bgee; ENSMUSG00000003418; Expressed in conjunctival fornix and 153 other tissues.
DR ExpressionAtlas; Q8K4T1; baseline and differential.
DR Genevisible; Q8K4T1; 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; IBA:GO_Central.
DR GO; GO:0008373; F:sialyltransferase activity; IDA:MGI.
DR GO; GO:0001835; P:blastocyst hatching; IMP:MGI.
DR GO; GO:0016051; P:carbohydrate biosynthetic process; IDA:MGI.
DR GO; GO:0001574; P:ganglioside biosynthetic process; IDA:BHF-UCL.
DR GO; GO:0009247; P:glycolipid biosynthetic process; IDA:MGI.
DR GO; GO:0009100; P:glycoprotein metabolic process; IDA:BHF-UCL.
DR GO; GO:0006491; P:N-glycan processing; IBA:GO_Central.
DR GO; GO:0009311; P:oligosaccharide metabolic process; IDA:BHF-UCL.
DR GO; GO:0006486; P:protein glycosylation; IBA:GO_Central.
DR GO; GO:0006493; P:protein O-linked glycosylation; IDA:MGI.
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 Lipid metabolism; Membrane; Reference proteome; Signal-anchor; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..398
FT /note="Alpha-2,8-sialyltransferase 8F"
FT /id="PRO_0000149300"
FT TOPO_DOM 1..3
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 4..24
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 25..398
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT ACT_SITE 370
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:O43173"
FT BINDING 214
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O43173"
FT BINDING 236..238
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O43173"
FT BINDING 322..324
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O43173"
FT CARBOHYD 66
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 93
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 151
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 196
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 186..335
FT /evidence="ECO:0000250|UniProtKB:O43173"
FT DISULFID 200..395
FT /evidence="ECO:0000250|UniProtKB:O43173"
SQ SEQUENCE 398 AA; 45428 MW; A73A7A29640D4917 CRC64;
MRSGGTLFAL IGSLMLLLLL RMLWCPADAP ARSRLLMEGS REDTSGTSAA LKTLWSPTTP
VPRTRNSTYL DEKTTQITEK CKDLQYSLNS LSNKTRRYSE DDYLQTITNI QRCPWNRQAE
EYDNFRAKLA SCCDAIQDFV VSQNNTPVGT NMSYEVESKK HIPIRENIFH MFPVSQPFVD
YPYNQCAVVG NGGILNKSLC GAEIDKSDFV FRCNLPPITG SASKDVGSKT NLVTVNPSII
TLKYQNLKEK KAQFLEDIST YGDAFLLLPA FSYRANTGIS FKVYQTLKES KMRQKVLFFH
PRYLRHLALF WRTKGVTAYR LSTGLMIASV AVELCENVKL YGFWPFSKTI EDTPLSHHYY
DNMLPKHGFH QMPKEYSQML QLHMRGILKL QFSKCETA
