ID   SIA8D_CRIGR             Reviewed;         359 AA.
AC   Q64690;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=CMP-N-acetylneuraminate-poly-alpha-2,8-sialyltransferase;
DE            EC=2.4.99.-;
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; Synonyms=PST-1, PST1, SIAT8D;
OS   Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Cricetidae; Cricetinae; Cricetulus.
OX   NCBI_TaxID=10029;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=7854457; DOI=10.1038/373715a0;
RA   Eckhardt M., Muehlenhoff M., Bethe A., Koopman J., Frosch M.,
RA   Gerardy-Schahn R.;
RT   "Molecular characterization of eukaryotic polysialyltransferase-1.";
RL   Nature 373:715-718(1995).
CC   -!- FUNCTION: Catalyzes the polycondensation of alpha-2,8-linked sialic
CC       acid required for the synthesis of polysialic acid (PSA), which is
CC       present on the embryonic neural cell adhesion molecule (N-CAM),
CC       necessary for plasticity of neural cells.
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC   -!- INTERACTION:
CC       Q64690; Q9BY67: CADM1; Xeno; NbExp=2; IntAct=EBI-15854853, 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}.
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DR   EMBL; Z46801; CAA86822.1; -; mRNA.
DR   PIR; S52425; S52425.
DR   RefSeq; NP_001231179.1; NM_001244250.1.
DR   AlphaFoldDB; Q64690; -.
DR   SMR; Q64690; -.
DR   DIP; DIP-59529N; -.
DR   IntAct; Q64690; 2.
DR   STRING; 10029.NP_001231179.1; -.
DR   CAZy; GT29; Glycosyltransferase Family 29.
DR   GeneID; 100689217; -.
DR   KEGG; cge:100689217; -.
DR   CTD; 7903; -.
DR   eggNOG; KOG2692; Eukaryota.
DR   OMA; HAAEGWK; -.
DR   OrthoDB; 825014at2759; -.
DR   UniPathway; UPA00378; -.
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; IEA:Ensembl.
DR   GO; GO:0001574; P:ganglioside biosynthetic process; IEA:Ensembl.
DR   GO; GO:0006491; P:N-glycan processing; IEA:Ensembl.
DR   GO; GO:0009311; P:oligosaccharide metabolic process; IEA:Ensembl.
DR   GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
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; Signal-anchor; Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..359
FT                   /note="CMP-N-acetylneuraminate-poly-alpha-2,8-
FT                   sialyltransferase"
FT                   /id="PRO_0000149292"
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         170
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:O43173"
FT   BINDING         191..193
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:O43173"
FT   BINDING         279..281
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:O43173"
FT   BINDING         314..315
FT                   /ligand="substrate"
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;  41227 MW;  C31AF4C27F8A336F CRC64;
     MRSIRKRWTI CTISLLLIFY KTKEIARTEE HQETQLIGDG ELCLSRSLVN SSDKIIRKAG
     STIFQHSVQG WRINSSLVLE IRKNILRFLD AERDVSVVKS SFKPGDVIHY VLDRRRTLNI
     SHDLHSLLPE VSPMKNRRFK TCAVVGNSGI LLDSGCGKEI DSHNFVIRCN LAPVVEFAAD
     VGTKSDFITM NPSVVQRAFG GFRNESDRAK FVHRLSMLND SVLWIPAFMV KGGEKHVEWV
     NALILKNKLK VRTAYPSLRL IHAVRGYWLT NKVPIKRPST GLLMYTLATR FCDEIHLYGF
     WPFPKDLNGK AVKYHYYDDL KYRYFSNASP HRMPLEFKTL NVLHNRGALK LTTGKCMKQ