SIAT9_PANTR
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 03-AUG-2022, entry version 96.
DE RecName: Full=Lactosylceramide alpha-2,3-sialyltransferase;
DE EC=2.4.99.9 {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 = CMP + ganglioside GM3 (d18:1(4E)) + H(+);
CC Xref=Rhea:RHEA:18417, ChEBI:CHEBI:15378, ChEBI:CHEBI:17950,
CC ChEBI:CHEBI:57812, ChEBI:CHEBI:60065, ChEBI:CHEBI:60377; EC=2.4.99.9;
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.ENSPTRP00000020834; -.
DR CAZy; GT29; Glycosyltransferase Family 29.
DR PaxDb; Q6KB55; -.
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 TreeFam; TF352819; -.
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:0047291; F:lactosylceramide alpha-2,3-sialyltransferase activity; ISS:UniProtKB.
DR GO; GO:0008373; F:sialyltransferase activity; IBA:GO_Central.
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; -; 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 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
