ID   SIA8D_BOVIN             Reviewed;         359 AA.
AC   Q6ZXC9;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 78.
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=SIAT8D;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=15843597; DOI=10.1093/glycob/cwi063;
RA   Harduin-Lepers A., Mollicone R., Delannoy P., Oriol R.;
RT   "The animal sialyltransferases and sialyltransferase-related genes: a
RT   phylogenetic approach.";
RL   Glycobiology 15:805-817(2005).
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. {ECO:0000250}.
CC   -!- PATHWAY: Protein modification; protein glycosylation.
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AJ699421; CAG27883.1; -; mRNA.
DR   RefSeq; NP_001001163.1; NM_001001163.1.
DR   AlphaFoldDB; Q6ZXC9; -.
DR   SMR; Q6ZXC9; -.
DR   STRING; 9913.ENSBTAP00000028590; -.
DR   CAZy; GT29; Glycosyltransferase Family 29.
DR   PaxDb; Q6ZXC9; -.
DR   PRIDE; Q6ZXC9; -.
DR   GeneID; 407768; -.
DR   KEGG; bta:407768; -.
DR   CTD; 7903; -.
DR   eggNOG; KOG2692; Eukaryota.
DR   InParanoid; Q6ZXC9; -.
DR   OrthoDB; 825014at2759; -.
DR   UniPathway; UPA00378; -.
DR   Proteomes; UP000009136; Unplaced.
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; ISS:AgBase.
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   2: Evidence at transcript level;
KW   Disulfide bond; Glycoprotein; Glycosyltransferase; Golgi apparatus;
KW   Membrane; Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..359
FT                   /note="CMP-N-acetylneuraminate-poly-alpha-2,8-
FT                   sialyltransferase"
FT                   /id="PRO_0000247931"
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;  41162 MW;  C7C0B4FFCDA967C4 CRC64;
     MRSIRKRWTI CTISLLLIFY KTKEMARTEE HQETQLIGDG ELSLSRSLVN SSDKIIRKAG
     SSIFQHSVEG GKINSSLVLE IRKNILRFLD AERDVSVVKS SFKPGDVIHY VLDRRRTLNI
     SQDLHSLLPE VSPMKNRRFK TCAVVGNSGI LLDSECGKEI DSHNFVIRCN LAPVVEFAAD
     VGTKSDFITM NPSVVQRAFG GFRNESDREK FVHRLSMLND SVLWIPAFMV KGGEKHVEWV
     NALILKNKLK VRTAYPSLRL IHAVRGYWLT NKVPIKRPST GLLMYTLATR FCDEIHLYGF
     WPFPKDLNGK AVKYHYYDDL KYRYFSNASP HRMPLEFKTL NVLHNRGALK LTTGKCIKQ