ID   SIAT9_PANTR             Reviewed;         362 AA.
AC   Q6KB55;
DT   15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   24-JAN-2024, entry version 102.
DE   RecName: Full=Lactosylceramide alpha-2,3-sialyltransferase;
DE            EC=2.4.3.9 {ECO:0000250|UniProtKB:Q9UNP4};
DE   AltName: Full=CMP-NeuAc:lactosylceramide alpha-2,3-sialyltransferase;
DE   AltName: Full=Ganglioside GM3 synthase;
DE   AltName: Full=ST3Gal V;
DE            Short=ST3GalV;
DE   AltName: Full=Sialyltransferase 9;
GN   Name=ST3GAL5; Synonyms=SIAT9;
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 (JUN-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Transfers the sialyl group (N-acetyl-alpha-neuraminyl or
CC       NeuAc) from CMP-NeuAc to the non-reducing terminal galactose (Gal) of
CC       glycosphingolipids forming gangliosides (important molecules involved
CC       in the regulation of multiple cellular processes, including cell
CC       proliferation and differentiation, apoptosis, embryogenesis,
CC       development, and oncogenesis). Mainly involved in the biosynthesis of
CC       ganglioside GM3 but can also use different glycolipids as substrate
CC       acceptors such as D-galactosylceramide (GalCer), asialo-GM2 (GA2) and
CC       asialo-GM1 (GA1), although less preferentially than beta-D-Gal-(1->4)-
CC       beta-D-Glc-(1<->1)-Cer (LacCer). {ECO:0000250|UniProtKB:Q9UNP4}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a beta-D-Gal-(1->4)-beta-D-Glc-(1<->1)-Cer(d18:1(4E)) + CMP-N-
CC         acetyl-beta-neuraminate = a ganglioside GM3 (d18:1(4E)) + CMP + H(+);
CC         Xref=Rhea:RHEA:18417, ChEBI:CHEBI:15378, ChEBI:CHEBI:17950,
CC         ChEBI:CHEBI:57812, ChEBI:CHEBI:60065, ChEBI:CHEBI:60377; EC=2.4.3.9;
CC         Evidence={ECO:0000250|UniProtKB:Q9UNP4};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18418;
CC         Evidence={ECO:0000250|UniProtKB:Q9UNP4};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=CMP-N-acetyl-beta-neuraminate + ganglioside GA2
CC         (d18:1(4E)/18:0) = CMP + ganglioside GM2 (d18:1(4E)/18:0) + H(+);
CC         Xref=Rhea:RHEA:41776, ChEBI:CHEBI:15378, ChEBI:CHEBI:57812,
CC         ChEBI:CHEBI:60377, ChEBI:CHEBI:78485, ChEBI:CHEBI:78486;
CC         Evidence={ECO:0000250|UniProtKB:Q9UNP4};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41777;
CC         Evidence={ECO:0000250|UniProtKB:Q9UNP4};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=beta-D-Gal-(1<->1')-Cer + CMP-N-acetyl-beta-neuraminate = CMP
CC         + H(+) + N-acetyl-alpha-neuraminosyl-(2->3)-beta-D-galactosyl-
CC         (1<->1')-ceramide; Xref=Rhea:RHEA:41780, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57812, ChEBI:CHEBI:60377, ChEBI:CHEBI:82643,
CC         ChEBI:CHEBI:143593; Evidence={ECO:0000250|UniProtKB:Q9UNP4};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41781;
CC         Evidence={ECO:0000250|UniProtKB:Q9UNP4};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=CMP-N-acetyl-beta-neuraminate + ganglioside GA1
CC         (d18:1(4E)/18:0) = CMP + ganglioside GM1 (d18:1(4E)/18:0) + H(+);
CC         Xref=Rhea:RHEA:41784, ChEBI:CHEBI:15378, ChEBI:CHEBI:57812,
CC         ChEBI:CHEBI:60377, ChEBI:CHEBI:73110, ChEBI:CHEBI:78484;
CC         Evidence={ECO:0000250|UniProtKB:Q9UNP4};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41785;
CC         Evidence={ECO:0000250|UniProtKB:Q9UNP4};
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; AJ744807; CAG32843.1; -; mRNA.
DR   RefSeq; NP_001032378.1; NM_001037301.1.
DR   AlphaFoldDB; Q6KB55; -.
DR   SMR; Q6KB55; -.
DR   STRING; 9598.ENSPTRP00000087081; -.
DR   CAZy; GT29; Glycosyltransferase Family 29.
DR   GlyCosmos; Q6KB55; 4 sites, No reported glycans.
DR   PaxDb; 9598-ENSPTRP00000020834; -.
DR   GeneID; 459371; -.
DR   KEGG; ptr:459371; -.
DR   CTD; 8869; -.
DR   eggNOG; KOG2692; Eukaryota.
DR   HOGENOM; CLU_032020_3_2_1; -.
DR   InParanoid; Q6KB55; -.
DR   OrthoDB; 5404317at2759; -.
DR   TreeFam; TF352819; -.
DR   Proteomes; UP000002277; Unplaced.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0047291; F:lactosylceramide alpha-2,3-sialyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006486; P:protein glycosylation; IBA:GO_Central.
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; PTHR13713:SF60; LACTOSYLCERAMIDE ALPHA-2,3-SIALYLTRANSFERASE; 1.
DR   PANTHER; PTHR13713; 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 metabolism; Membrane; Reference proteome; Signal-anchor; Transferase;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..362
FT                   /note="Lactosylceramide alpha-2,3-sialyltransferase"
FT                   /id="PRO_0000149304"
FT   TOPO_DOM        1..5
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        6..26
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        27..362
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        30
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        180
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        224
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        334
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        139..297
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   362 AA;  41714 MW;  4DD19605E1AB76AD CRC64;
     MRRPSLLLKD ILKCTLLVFG VWILYILKLN YTTEECDMKK MHYVDPDRVK RAQTYAQQVL
     QKECRPKFAK TSMALLFEHR YSVDLLPFVQ KAPKDSEAES KYDPPFGFRK FSSKVQTLLE
     LLPEHDLPEH LKAKTCRRCV VIGSGGILHG LELGHTLNQF DVVIRLNSAP VEGYSEHVGN
     KTTIRMTYPE GAPLSDLEYY SNDLFVAVLF KSVDFNWLQA MVKNETLPFW VRLFFWKQVA
     EKIPLQPKHF RILNPVIIKE TAFDILQYSE PQSRFWGRDK NVPTIGVIAV VLATHLCDEV
     SLAGFGYDLS QPRTPLHYFD NQCMAAMNFQ TMHNVTTETK FLLKLVKEGV VKDLSGGIDR
     EF
//