ID   SIA8B_PANTR             Reviewed;         375 AA.
AC   P61643;
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=Alpha-2,8-sialyltransferase 8B;
DE            EC=2.4.99.-;
DE   AltName: Full=Sialyltransferase 8B;
DE            Short=SIAT8-B;
DE   AltName: Full=Sialyltransferase St8Sia II;
DE            Short=ST8SiaII;
GN   Name=ST8SIA2; Synonyms=SIAT8B;
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: May transfer sialic acid through alpha-2,8-linkages to the
CC       alpha-2,3-linked and alpha-2,6-linked sialic acid of N-linked
CC       oligosaccharides of glycoproteins and may be involved in PSA
CC       (polysialic acid) expression. {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}.
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DR   EMBL; AJ697659; CAG26897.1; -; mRNA.
DR   RefSeq; NP_001032377.1; NM_001037300.1.
DR   AlphaFoldDB; P61643; -.
DR   SMR; P61643; -.
DR   STRING; 9598.ENSPTRP00000012772; -.
DR   CAZy; GT29; Glycosyltransferase Family 29.
DR   PaxDb; P61643; -.
DR   GeneID; 453661; -.
DR   KEGG; ptr:453661; -.
DR   CTD; 8128; -.
DR   eggNOG; KOG2692; Eukaryota.
DR   InParanoid; P61643; -.
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:0003828; F:alpha-N-acetylneuraminate alpha-2,8-sialyltransferase activity; IBA:GO_Central.
DR   GO; GO:0006491; P:N-glycan processing; IBA:GO_Central.
DR   GO; GO:0009311; P:oligosaccharide metabolic process; IBA:GO_Central.
DR   GO; GO:0006486; P:protein glycosylation; IBA:GO_Central.
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..375
FT                   /note="Alpha-2,8-sialyltransferase 8B"
FT                   /id="PRO_0000149287"
FT   TOPO_DOM        1..6
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        7..23
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        24..375
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        346
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:O43173"
FT   BINDING         185
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:O43173"
FT   BINDING         206..208
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:O43173"
FT   BINDING         294..296
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:O43173"
FT   BINDING         329..330
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:O43173"
FT   CARBOHYD        60
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        72
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        89
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        134
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        219
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        234
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        157..307
FT                   /evidence="ECO:0000250|UniProtKB:O43173"
FT   DISULFID        171..371
FT                   /evidence="ECO:0000250|UniProtKB:O43173"
SQ   SEQUENCE   375 AA;  42357 MW;  717A94FC6EA57131 CRC64;
     MQLQFRSWML AALTLLVVFL IFADISEIEE EIGNSGGRGT IRSAVNSLHS KSNRAEVVIN
     GSSSPAVVDR SNESIKHNIQ PASSKWRHNQ TLSLRIRKQI LKFLDAEKDI SVLKGTLKPG
     DIIHYIFDRD STMNVSQNLY ELLPRTSPLK NKHFGTCAIV GNSGVLLNSG CGQEIDAHSF
     VIRCNLAPVQ EYARDVGLKT DLVTMNPSVI QRAFEDLVNA TWREKLLQRL HSLNGSILWI
     PAFMARGGKE RVEWVNELIL KHHVNVRTAY PSLPLLHAVR GYWLTNKVHI KRPTTGLLMY
     TLATRFCNQI YLYGFWPFPL DQNQNPVKYH YYDSLKYGYT SQASPHTMPL EFKALKSLHE
     QGALKLTVGQ CDGAT