ID   SIA8A_PANTR             Reviewed;         356 AA.
AC   P61642;
DT   07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2004, sequence version 1.
DT   27-MAR-2024, entry version 95.
DE   RecName: Full=Alpha-N-acetylneuraminide alpha-2,8-sialyltransferase {ECO:0000250|UniProtKB:Q92185};
DE            EC=2.4.3.8 {ECO:0000250|UniProtKB:Q92185};
DE   AltName: Full=Alpha-2,8-sialyltransferase 8A;
DE   AltName: Full=Ganglioside GD3 synthase;
DE   AltName: Full=Ganglioside GT3 synthase;
DE   AltName: Full=Sialyltransferase 8A;
DE            Short=SIAT8-A;
DE   AltName: Full=Sialyltransferase St8Sia I;
DE            Short=ST8SiaI;
GN   Name=ST8SIA1 {ECO:0000250|UniProtKB:Q92185}; Synonyms=SIAT8A;
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].
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 addition of sialic acid in alpha 2,8-linkage to
CC       the sialic acid moiety of the ganglioside GM3 to form ganglioside GD3;
CC       gangliosides are a subfamily of complex glycosphingolipds that contain
CC       one or more residues of sialic acid (By similarity). Can catalyze the
CC       addition of a second alpha-2,8- sialic acid to GD3 to form GT3 (By
CC       similarity). Can use GM1b, GD1a and GT1b as acceptor substrates to
CC       synthesize GD1c, GT1a and GQ1b respectively (By similarity).
CC       {ECO:0000250|UniProtKB:Q92185}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an N-acetyl-alpha-neuraminyl-(2->3)-beta-D-galactosyl
CC         derivative + CMP-N-acetyl-beta-neuraminate = an N-acetyl-alpha-
CC         neuraminyl-(2->8)-N-acetyl-alpha-neuraminyl-(2->3)-beta-D-galactosyl
CC         derivative + CMP + H(+); Xref=Rhea:RHEA:19313, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57812, ChEBI:CHEBI:60377, ChEBI:CHEBI:140308,
CC         ChEBI:CHEBI:140309; EC=2.4.3.8;
CC         Evidence={ECO:0000250|UniProtKB:Q92185};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a ganglioside GM3 (d18:1(4E)) + CMP-N-acetyl-beta-neuraminate
CC         = a ganglioside GD3 (d18:1(4E)) + CMP + H(+); Xref=Rhea:RHEA:41760,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57812, ChEBI:CHEBI:60065,
CC         ChEBI:CHEBI:60377, ChEBI:CHEBI:78436;
CC         Evidence={ECO:0000250|UniProtKB:Q92185};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41761;
CC         Evidence={ECO:0000250|UniProtKB:Q92185};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a ganglioside GD3 (d18:1(4E)) + CMP-N-acetyl-beta-neuraminate
CC         = a ganglioside GT3 (d18:1(4E)) + CMP + H(+); Xref=Rhea:RHEA:41764,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57812, ChEBI:CHEBI:60377,
CC         ChEBI:CHEBI:78436, ChEBI:CHEBI:78438;
CC         Evidence={ECO:0000250|UniProtKB:Q92185};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41765;
CC         Evidence={ECO:0000250|UniProtKB:Q92185};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a ganglioside GD1a (d18:1(4E)) + CMP-N-acetyl-beta-neuraminate
CC         = a ganglioside GT1a (d18:1(4E)) + CMP + H(+); Xref=Rhea:RHEA:41768,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57812, ChEBI:CHEBI:60377,
CC         ChEBI:CHEBI:78445, ChEBI:CHEBI:78447;
CC         Evidence={ECO:0000250|UniProtKB:Q92185};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41769;
CC         Evidence={ECO:0000250|UniProtKB:Q92185};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a ganglioside GT1b (d18:1(4E)) + CMP-N-acetyl-beta-neuraminate
CC         = a ganglioside GQ1b (d18:1(4E)) + CMP + H(+); Xref=Rhea:RHEA:41772,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57812, ChEBI:CHEBI:60377,
CC         ChEBI:CHEBI:78452, ChEBI:CHEBI:78455;
CC         Evidence={ECO:0000250|UniProtKB:Q92185};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41773;
CC         Evidence={ECO:0000250|UniProtKB:Q92185};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a ganglioside GM1b (d18:1(4E)) + CMP-N-acetyl-beta-neuraminate
CC         = a ganglioside GD1c (d18:1(4E)) + CMP + H(+); Xref=Rhea:RHEA:47576,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57812, ChEBI:CHEBI:60377,
CC         ChEBI:CHEBI:78568, ChEBI:CHEBI:87787;
CC         Evidence={ECO:0000250|UniProtKB:Q92185};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47577;
CC         Evidence={ECO:0000250|UniProtKB:Q92185};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a ganglioside GD3 + CMP-N-acetyl-beta-neuraminate = a
CC         ganglioside GT3 + CMP + H(+); Xref=Rhea:RHEA:77295,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57812, ChEBI:CHEBI:60377,
CC         ChEBI:CHEBI:79214, ChEBI:CHEBI:79216;
CC         Evidence={ECO:0000250|UniProtKB:Q92185};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77296;
CC         Evidence={ECO:0000250|UniProtKB:Q92185};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[alpha-N-acetylneuraminyl-(2->8)](n)-alpha-N-acetylneuraminyl-
CC         (2->8)-alpha-N-acetylneuraminyl-(2->3)-beta-D-galactosyl-(1->4)-beta-
CC         D-glucosyl-(1<->1)-ceramide + CMP-N-acetyl-beta-neuraminate = [alpha-
CC         N-acetylneuraminyl-(2->8)](n+1)-alpha-N-acetylneuraminyl-(2->8)-
CC         alpha-N-acetylneuraminyl-(2->3)-beta-D-galactosyl-(1->4)-beta-D-
CC         glucosyl-(1<->1)-ceramide + CMP + H(+); Xref=Rhea:RHEA:77371,
CC         Rhea:RHEA-COMP:18881, Rhea:RHEA-COMP:18935, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57812, ChEBI:CHEBI:60377, ChEBI:CHEBI:197322;
CC         Evidence={ECO:0000250|UniProtKB:Q92185};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77372;
CC         Evidence={ECO:0000250|UniProtKB:Q92185};
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC   -!- PATHWAY: Lipid metabolism; sphingolipid metabolism.
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; AJ697658; CAG26896.1; -; mRNA.
DR   RefSeq; NP_001032380.1; NM_001037303.1.
DR   AlphaFoldDB; P61642; -.
DR   SMR; P61642; -.
DR   STRING; 9598.ENSPTRP00000090869; -.
DR   CAZy; GT29; Glycosyltransferase Family 29.
DR   GlyCosmos; P61642; 4 sites, No reported glycans.
DR   PaxDb; 9598-ENSPTRP00000008136; -.
DR   GeneID; 465341; -.
DR   KEGG; ptr:465341; -.
DR   CTD; 6489; -.
DR   eggNOG; KOG2692; Eukaryota.
DR   InParanoid; P61642; -.
DR   OrthoDB; 5348004at2759; -.
DR   UniPathway; UPA00222; -.
DR   UniPathway; UPA00378; -.
DR   Proteomes; UP000002277; Unplaced.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0003828; F:alpha-N-acetylneuraminate alpha-2,8-sialyltransferase activity; ISS:UniProtKB.
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   GO; GO:0006665; P:sphingolipid metabolic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.90.1480.20; Glycosyl transferase family 29; 1.
DR   InterPro; IPR001675; Glyco_trans_29.
DR   InterPro; IPR038578; GT29-like_sf.
DR   InterPro; IPR012163; Sialyl_trans.
DR   PANTHER; PTHR11987; ALPHA-2,8-SIALYLTRANSFERASE; 1.
DR   PANTHER; PTHR11987:SF3; ALPHA-N-ACETYLNEURAMINIDE ALPHA-2,8-SIALYLTRANSFERASE; 1.
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   Lipid biosynthesis; Lipid metabolism; Membrane; Reference proteome;
KW   Signal-anchor; Sphingolipid metabolism; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..356
FT                   /note="Alpha-N-acetylneuraminide alpha-2,8-
FT                   sialyltransferase"
FT                   /id="PRO_0000149284"
FT   TOPO_DOM        1..29
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        30..48
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        49..356
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        322
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:O43173"
FT   BINDING         143
FT                   /ligand="CMP-N-acetyl-beta-neuraminate"
FT                   /ligand_id="ChEBI:CHEBI:57812"
FT                   /evidence="ECO:0000250|UniProtKB:O43173"
FT   BINDING         166
FT                   /ligand="CMP-N-acetyl-beta-neuraminate"
FT                   /ligand_id="ChEBI:CHEBI:57812"
FT                   /evidence="ECO:0000250|UniProtKB:O43173"
FT   BINDING         274
FT                   /ligand="CMP-N-acetyl-beta-neuraminate"
FT                   /ligand_id="ChEBI:CHEBI:57812"
FT                   /evidence="ECO:0000250|UniProtKB:O43173"
FT   BINDING         275
FT                   /ligand="CMP-N-acetyl-beta-neuraminate"
FT                   /ligand_id="ChEBI:CHEBI:57812"
FT                   /evidence="ECO:0000250|UniProtKB:O43173"
FT   BINDING         276
FT                   /ligand="CMP-N-acetyl-beta-neuraminate"
FT                   /ligand_id="ChEBI:CHEBI:57812"
FT                   /evidence="ECO:0000250|UniProtKB:O43173"
FT   BINDING         296
FT                   /ligand="CMP-N-acetyl-beta-neuraminate"
FT                   /ligand_id="ChEBI:CHEBI:57812"
FT                   /evidence="ECO:0000250|UniProtKB:O43173"
FT   BINDING         310
FT                   /ligand="CMP-N-acetyl-beta-neuraminate"
FT                   /ligand_id="ChEBI:CHEBI:57812"
FT                   /evidence="ECO:0000250|UniProtKB:O43173"
FT   CARBOHYD        71
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        214
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        245
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        138..287
FT                   /evidence="ECO:0000250|UniProtKB:O43173"
FT   DISULFID        152..347
FT                   /evidence="ECO:0000250|UniProtKB:O43173"
SQ   SEQUENCE   356 AA;  40592 MW;  452FE2C313964395 CRC64;
     MSPCGRARRQ TSRGAMAVLA WKFPRTRLPM GASALCVVVL CWLYIFPVYR LPNEKEIVQG
     VLQQGTAWRR NQTAARAFRK QMEDCCDPAH LFAMTKMNSP MGKSMWYDGE FLYSFTIDNS
     TYSLFPQATP FQLPLKKCAV VGNGGILKKS GCGRQIDEAN FVMRCNLPPL SSEYTKDVGS
     KSQLVTANPS IIRQRFQNLL WSRKTFVDNM KIYNHSYIYM PAFSMKTGTE PSLRVYYTLS
     DVGANQTVLF ANPNFLRSIG KFWKSRGIHA KRLSTGLFLV SAALGLCEEV AIYGFWPFSV
     NMHEQPISHH YYDNVLPFSG FHAMPEEFLQ LWYLHKIGAL RMQLERCEDT SLQPTS
//