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SIA8D_MOUSE
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   03-AUG-2022, entry version 148.
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, 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].
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 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   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000305}; Single-
CC       pass type II membrane protein {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Strongly expressed in lung, heart and spleen and
CC       weakly in brain.
CC   -!- DEVELOPMENTAL STAGE: Expressed throughout development at a low level.
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   GlyGen; Q64692; 5 sites.
DR   PhosphoSitePlus; Q64692; -.
DR   EPD; Q64692; -.
DR   MaxQB; Q64692; -.
DR   PaxDb; Q64692; -.
DR   PRIDE; Q64692; -.
DR   ProteomicsDB; 257176; -.
DR   Antibodypedia; 25167; 182 antibodies from 24 providers.
DR   DNASU; 20452; -.
DR   Ensembl; ENSMUST00000043336; ENSMUSP00000043477; ENSMUSG00000040710.
DR   GeneID; 20452; -.
DR   KEGG; mmu:20452; -.
DR   UCSC; uc007cfa.1; mouse.
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; 825014at2759; -.
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   UniPathway; UPA00378; -.
DR   BioGRID-ORCS; 20452; 0 hits in 72 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 244 other tissues.
DR   ExpressionAtlas; Q64692; baseline and differential.
DR   Genevisible; Q64692; 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; 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   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_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         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;  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
 
 
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