ID   SIA8D_MOUSE             Reviewed;         359 AA.
AC   Q64692;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   27-MAR-2024, entry version 156.
DE   RecName: Full=CMP-N-acetylneuraminate-poly-alpha-2,8-sialyltransferase {ECO:0000305};
DE            EC=2.4.3.- {ECO:0000305|PubMed:8690732};
DE   AltName: Full=Alpha-2,8-sialyltransferase 8D;
DE   AltName: Full=Polysialyltransferase-1;
DE   AltName: Full=Sialyltransferase 8D;
DE            Short=SIAT8-D;
DE   AltName: Full=Sialyltransferase St8Sia IV;
DE            Short=ST8SiaIV;
GN   Name=St8sia4 {ECO:0000312|MGI:MGI:106018}; Synonyms=Pst, Siat8d;
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], CATALYTIC ACTIVITY, TISSUE SPECIFICITY, AND
RP   DEVELOPMENTAL STAGE.
RC   TISSUE=Lung;
RX   PubMed=8690732; DOI=10.1093/oxfordjournals.jbchem.a124960;
RA   Yoshida Y., Kojima N., Tsuji S.;
RT   "Molecular cloning and characterization of a third type of N-glycan alpha
RT   2,8-sialyltransferase from mouse lung.";
RL   J. Biochem. 118:658-664(1995).
CC   -!- FUNCTION: Catalyzes the transfer of a sialic acid from a CMP-linked
CC       sialic acid donor onto a terminal alpha-2,3-, alpha-2,6-, or alpha-2,8-
CC       linked sialic acid of an N-linked glycan protein acceptor through
CC       alpha-2,8-linkages (PubMed:8690732). Therefore, participates in
CC       polysialic acid synthesis on various sialylated N-acetyllactosaminyl
CC       oligosaccharides, including NCAM1 N-glycans, FETUB N-glycans and AHSG
CC       (By similarity). It is noteworthy that alpha-2,3-linked sialic acid is
CC       apparently a better acceptor than alpha-2,6-linked sialic acid (By
CC       similarity). {ECO:0000250|UniProtKB:Q92187,
CC       ECO:0000269|PubMed:8690732}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[N-acetyl-alpha-D-neuraminosyl-(2->8)](n) + CMP-N-acetyl-beta-
CC         neuraminate = [N-acetyl-alpha-D-neuraminosyl-(2->8)](n+1) + CMP +
CC         H(+); Xref=Rhea:RHEA:77367, Rhea:RHEA-COMP:14315, Rhea:RHEA-
CC         COMP:18878, ChEBI:CHEBI:15378, ChEBI:CHEBI:57812, ChEBI:CHEBI:60377,
CC         ChEBI:CHEBI:139252; Evidence={ECO:0000305|PubMed:8690732};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77368;
CC         Evidence={ECO:0000305|PubMed:8690732};
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC       {ECO:0000250|UniProtKB:Q92187}; Single-pass type II membrane protein
CC       {ECO:0000250|UniProtKB:Q92187}. Secreted
CC       {ECO:0000250|UniProtKB:Q92187}.
CC   -!- TISSUE SPECIFICITY: Strongly expressed in lung, heart and spleen and
CC       weakly in brain. {ECO:0000269|PubMed:8690732}.
CC   -!- DEVELOPMENTAL STAGE: Expressed throughout development at a low level.
CC       {ECO:0000269|PubMed:8690732}.
CC   -!- PTM: Autopolysialylated. {ECO:0000250|UniProtKB:Q92187}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 29 family.
CC       {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase; Note=ST8Sia
CC       IV;
CC       URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_mou_659";
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DR   EMBL; X86000; CAA59992.1; -; mRNA.
DR   CCDS; CCDS15201.1; -.
DR   PIR; JC4224; JC4224.
DR   RefSeq; NP_001153217.1; NM_001159745.1.
DR   RefSeq; NP_033209.1; NM_009183.2.
DR   AlphaFoldDB; Q64692; -.
DR   SMR; Q64692; -.
DR   STRING; 10090.ENSMUSP00000043477; -.
DR   CAZy; GT29; Glycosyltransferase Family 29.
DR   GlyCosmos; Q64692; 5 sites, No reported glycans.
DR   GlyGen; Q64692; 5 sites.
DR   PhosphoSitePlus; Q64692; -.
DR   EPD; Q64692; -.
DR   MaxQB; Q64692; -.
DR   PaxDb; 10090-ENSMUSP00000043477; -.
DR   ProteomicsDB; 257176; -.
DR   Antibodypedia; 25167; 204 antibodies from 24 providers.
DR   DNASU; 20452; -.
DR   Ensembl; ENSMUST00000043336.11; ENSMUSP00000043477.5; ENSMUSG00000040710.11.
DR   GeneID; 20452; -.
DR   KEGG; mmu:20452; -.
DR   UCSC; uc007cfa.1; mouse.
DR   AGR; MGI:106018; -.
DR   CTD; 7903; -.
DR   MGI; MGI:106018; St8sia4.
DR   VEuPathDB; HostDB:ENSMUSG00000040710; -.
DR   eggNOG; KOG2692; Eukaryota.
DR   GeneTree; ENSGT01030000234535; -.
DR   HOGENOM; CLU_048583_3_0_1; -.
DR   InParanoid; Q64692; -.
DR   OMA; HAAEGWK; -.
DR   OrthoDB; 5348004at2759; -.
DR   PhylomeDB; Q64692; -.
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   BioGRID-ORCS; 20452; 0 hits in 77 CRISPR screens.
DR   ChiTaRS; St8sia4; mouse.
DR   PRO; PR:Q64692; -.
DR   Proteomes; UP000000589; Chromosome 1.
DR   RNAct; Q64692; Protein.
DR   Bgee; ENSMUSG00000040710; Expressed in brain blood vessel and 245 other cell types or tissues.
DR   ExpressionAtlas; Q64692; baseline and differential.
DR   GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0003828; F:alpha-N-acetylneuraminate alpha-2,8-sialyltransferase activity; IDA:MGI.
DR   GO; GO:0001574; P:ganglioside biosynthetic process; ISO:MGI.
DR   GO; GO:0006491; P:N-glycan processing; ISO:MGI.
DR   GO; GO:0009311; P:oligosaccharide metabolic process; ISO:MGI.
DR   GO; GO:0006486; P:protein glycosylation; ISO:MGI.
DR   GO; GO:0097503; P:sialylation; IDA:UniProtKB.
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:SF48; CMP-N-ACETYLNEURAMINATE-POLY-ALPHA-2,8-SIALYLTRANSFERASE; 1.
DR   Pfam; PF00777; Glyco_transf_29; 1.
DR   PIRSF; PIRSF005557; Sialyl_trans; 1.
DR   Genevisible; Q64692; MM.
PE   1: Evidence at protein level;
KW   Disulfide bond; Glycoprotein; Glycosyltransferase; Golgi apparatus;
KW   Membrane; Reference proteome; Secreted; Signal-anchor; Transferase;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..359
FT                   /note="CMP-N-acetylneuraminate-poly-alpha-2,8-
FT                   sialyltransferase"
FT                   /id="PRO_0000149294"
FT   TOPO_DOM        1..7
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        8..20
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        21..359
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        331
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:O43173"
FT   BINDING         147
FT                   /ligand="CMP-N-acetyl-beta-neuraminate"
FT                   /ligand_id="ChEBI:CHEBI:57812"
FT                   /evidence="ECO:0000250|UniProtKB:O43173"
FT   BINDING         170
FT                   /ligand="CMP-N-acetyl-beta-neuraminate"
FT                   /ligand_id="ChEBI:CHEBI:57812"
FT                   /evidence="ECO:0000250|UniProtKB:O43173"
FT   BINDING         279
FT                   /ligand="CMP-N-acetyl-beta-neuraminate"
FT                   /ligand_id="ChEBI:CHEBI:57812"
FT                   /evidence="ECO:0000250|UniProtKB:O43173"
FT   BINDING         280
FT                   /ligand="CMP-N-acetyl-beta-neuraminate"
FT                   /ligand_id="ChEBI:CHEBI:57812"
FT                   /evidence="ECO:0000250|UniProtKB:O43173"
FT   BINDING         281
FT                   /ligand="CMP-N-acetyl-beta-neuraminate"
FT                   /ligand_id="ChEBI:CHEBI:57812"
FT                   /evidence="ECO:0000250|UniProtKB:O43173"
FT   BINDING         301
FT                   /ligand="CMP-N-acetyl-beta-neuraminate"
FT                   /ligand_id="ChEBI:CHEBI:57812"
FT                   /evidence="ECO:0000250|UniProtKB:O43173"
FT   CARBOHYD        50
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        74
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        119
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        204
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        219
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        142..292
FT                   /evidence="ECO:0000250|UniProtKB:O43173"
FT   DISULFID        156..356
FT                   /evidence="ECO:0000250|UniProtKB:O43173"
SQ   SEQUENCE   359 AA;  41256 MW;  81FE93468579D1EE CRC64;
     MRSIRKRWTI CTISLLLIFY KTKEIARTEE HQETQLIGDG ELCLSRSLVN SSDKIIRKAG
     STIFQHSVQG WKINSSLVLE IRKNILRFLD AERDVSVVKS SFKPGDVIHY VLDRRRTLNI
     SHNLHSLLPE VSPMKNRRFK TCAVVGNSGI LLDSGCGKEI DSHNFVIRCN LAPVVEFAAD
     VGTKSDFITM NPSVVQRAFG GFRNESDREK FVHRLSMLND SVLWIPAFMV KGGEKHVEWV
     NALILKNKLQ VRTAYPSLRL IHAVRGYWLT NKVPIKRPST GLLMYTLATR FCDEIHLYGF
     WPFPKDLNGK AVKYHYYDDL KYRYFSNASP HRMPLEFKTL NVLHNRGALK LTTGKCMKQ
//