ID   SIA8C_PANTR             Reviewed;         380 AA.
AC   P61644;
DT   07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2004, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=Sia-alpha-2,3-Gal-beta-1,4-GlcNAc-R:alpha 2,8-sialyltransferase;
DE            EC=2.4.99.-;
DE   AltName: Full=Alpha-2,8-sialyltransferase 8C;
DE   AltName: Full=Alpha-2,8-sialyltransferase III;
DE   AltName: Full=ST8 alpha-N-acetyl-neuraminide alpha-2,8-sialyltransferase 3;
DE   AltName: Full=Sialyltransferase 8C;
DE            Short=SIAT8-C;
DE   AltName: Full=Sialyltransferase St8Sia III;
DE            Short=ST8SiaIII;
GN   Name=ST8SIA3; Synonyms=SIAT8C;
OS   Pan troglodytes (Chimpanzee).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pan.
OX   NCBI_TaxID=9598;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Harduin-Lepers A., Martinez-Duncker I., Mollicone R., Delannoy P.,
RA   Oriol R.;
RT   "Phylogeny of sialyltransferases.";
RL   Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the transfer of sialic acid from a CMP-linked
CC       sialic acid donor onto the terminal sialic acid of an acceptor through
CC       alpha-2,8-linkages. Is active with alpha-2,3-linked, alpha-2,6-linked
CC       and alpha-2,8-linked sialic acid of N-linked oligosaccharides of
CC       glycoproteins and glycolipids. Displays preference for substrates with
CC       alpha-2,3-linked terminal sialic acid. It can form polysialic acid in
CC       vitro directly on alpha-2,3-, alpha-2,6-, or alpha-2,8-linked sialic
CC       acid. {ECO:0000250|UniProtKB:O43173}.
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC       {ECO:0000250|UniProtKB:O43173}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:O43173}.
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; AJ697660; CAG26898.1; -; mRNA.
DR   RefSeq; NP_001032374.1; NM_001037297.1.
DR   AlphaFoldDB; P61644; -.
DR   SMR; P61644; -.
DR   STRING; 9598.ENSPTRP00000017068; -.
DR   CAZy; GT29; Glycosyltransferase Family 29.
DR   PaxDb; P61644; -.
DR   GeneID; 455436; -.
DR   KEGG; ptr:455436; -.
DR   CTD; 51046; -.
DR   eggNOG; KOG2692; Eukaryota.
DR   InParanoid; P61644; -.
DR   OrthoDB; 825014at2759; -.
DR   UniPathway; UPA00378; -.
DR   Proteomes; UP000002277; 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:0008373; F:sialyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0006491; P:N-glycan processing; ISS:UniProtKB.
DR   GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR   GO; GO:1990743; P:protein sialylation; ISS:UniProtKB.
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..380
FT                   /note="Sia-alpha-2,3-Gal-beta-1,4-GlcNAc-R:alpha 2,8-
FT                   sialyltransferase"
FT                   /id="PRO_0000149291"
FT   TOPO_DOM        1..9
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        10..33
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        34..380
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        354
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:O43173"
FT   BINDING         190
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:O43173"
FT   BINDING         211..213
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:O43173"
FT   BINDING         300..302
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:O43173"
FT   BINDING         336..337
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:O43173"
FT   CARBOHYD        93
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        113
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        206
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        162..313
FT                   /evidence="ECO:0000250|UniProtKB:O43173"
FT   DISULFID        176..379
FT                   /evidence="ECO:0000250|UniProtKB:O43173"
SQ   SEQUENCE   380 AA;  43930 MW;  DFB471236A5F2012 CRC64;
     MRNCKMARVA SVLGLVMLSV ALLNLSLISY VSLKKENIFA TPKYASPGAP RMYMFHAGYR
     SQFALKFLDP SFVPITNSLT QELQEKPSKW TFNRTAFLHQ RQEILQHVDV IKNFSLTKNS
     VRIGQLMHYD YSSHKYVFSI SNNFRSLLPD VSPIMNKHYN ICAVVGNSGI LTGSQCGQEI
     DKSDFVFRCN FAPTEAFQRD VGRKTNLTTF NPSILEKYYN NLLTIQDRNN FFLSLKKLDG
     AILWIPAFFF HTSATVTRTL VDFFVEHRGQ LKVQLAWPGN IMQHVNRYWK NKHLSPKRLS
     TGILMYTLAS AICEEIHLYG FWPFGFDPNT REDLPYHYYD KKGTKFTTKW QESHQLPAEF
     QLLYRMHGEG LTKLTLSHCA