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   24-JAN-2024, entry version 143.
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=a ganglioside GM3 + CMP-N-acetyl-beta-neuraminate = a
CC         ganglioside GD3 + CMP + H(+); Xref=Rhea:RHEA:48288,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57812, ChEBI:CHEBI:60377,
CC         ChEBI:CHEBI:79210, ChEBI:CHEBI:79214;
CC         Evidence={ECO:0000269|PubMed:11980897};
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:0000269|PubMed:11980897};
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:0000269|PubMed:11980897};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a ganglioside GD1a + CMP-N-acetyl-beta-neuraminate = a
CC         ganglioside GT1a + CMP + H(+); Xref=Rhea:RHEA:48912,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57812, ChEBI:CHEBI:60377,
CC         ChEBI:CHEBI:82637, ChEBI:CHEBI:90501;
CC         Evidence={ECO:0000269|PubMed:11980897};
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:0000269|PubMed:11980897};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a ganglioside GM1b + CMP-N-acetyl-beta-neuraminate = a
CC         ganglioside GD1c + CMP + H(+); Xref=Rhea:RHEA:48916,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57812, ChEBI:CHEBI:60377,
CC         ChEBI:CHEBI:90151, ChEBI:CHEBI:90856;
CC         Evidence={ECO:0000269|PubMed:11980897};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a ganglioside GM4 (d18:1(4E)) + CMP-N-acetyl-beta-neuraminate
CC         = an N-acetyl-alpha-neuraminosyl-(2->8)-N-acetyl-alpha-neuraminosyl-
CC         (2->3)-beta-D-galactosyl-(1<->1')-N-acylsphing-4-enine + CMP + H(+);
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=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:0000269|PubMed:11980897};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a ganglioside GT1b + CMP-N-acetyl-beta-neuraminate = a
CC         ganglioside GQ1b + CMP + H(+); Xref=Rhea:RHEA:48932,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57812, ChEBI:CHEBI:60377,
CC         ChEBI:CHEBI:82940, ChEBI:CHEBI:90862;
CC         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   GlyCosmos; Q8K4T1; 4 sites, No reported glycans.
DR   GlyGen; Q8K4T1; 4 sites.
DR   PhosphoSitePlus; Q8K4T1; -.
DR   PaxDb; 10090-ENSMUSP00000003509; -.
DR   ProteomicsDB; 257239; -.
DR   Antibodypedia; 2510; 87 antibodies from 17 providers.
DR   DNASU; 241230; -.
DR   Ensembl; ENSMUST00000003509.10; ENSMUSP00000003509.9; ENSMUSG00000003418.12.
DR   GeneID; 241230; -.
DR   KEGG; mmu:241230; -.
DR   UCSC; uc008ikc.2; mouse.
DR   AGR; MGI:2386797; -.
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; CDAVHNF; -.
DR   OrthoDB; 5348004at2759; -.
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 80 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 154 other cell types or tissues.
DR   ExpressionAtlas; Q8K4T1; baseline and differential.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
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; Glycosyl transferase family 29; 1.
DR   InterPro; IPR001675; Glyco_trans_29.
DR   InterPro; IPR038578; GT29-like_sf.
DR   InterPro; IPR012163; Sialyl_trans.
DR   PANTHER; PTHR11987; ALPHA-2,8-SIALYLTRANSFERASE; 1.
DR   PANTHER; PTHR11987:SF29; ALPHA-2,8-SIALYLTRANSFERASE 8F; 1.
DR   Pfam; PF00777; Glyco_transf_29; 1.
DR   PIRSF; PIRSF005557; Sialyl_trans; 1.
DR   Genevisible; Q8K4T1; MM.
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
//