SIAT9_BOVIN
ID SIAT9_BOVIN Reviewed; 420 AA.
AC Q70D51;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 2.
DT 03-AUG-2022, entry version 93.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford;
RX PubMed=19390049; DOI=10.1126/science.1169588;
RG The bovine genome sequencing and analysis consortium;
RT "The genome sequence of taurine cattle: a window to ruminant biology and
RT evolution.";
RL Science 324:522-528(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 20-420.
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: 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAE51392.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AAFC03040697; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAFC03065753; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AJ585768; CAE51392.1; ALT_INIT; mRNA.
DR RefSeq; NP_991376.2; NM_205807.3.
DR AlphaFoldDB; Q70D51; -.
DR SMR; Q70D51; -.
DR STRING; 9913.ENSBTAP00000015414; -.
DR CAZy; GT29; Glycosyltransferase Family 29.
DR PaxDb; Q70D51; -.
DR PRIDE; Q70D51; -.
DR GeneID; 404164; -.
DR KEGG; bta:404164; -.
DR CTD; 8869; -.
DR eggNOG; KOG2692; Eukaryota.
DR InParanoid; Q70D51; -.
DR OrthoDB; 891104at2759; -.
DR Proteomes; UP000009136; 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..420
FT /note="Lactosylceramide alpha-2,3-sialyltransferase"
FT /id="PRO_0000334617"
FT TOPO_DOM 1..67
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 68..88
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 89..420
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 238
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 197..355
FT /evidence="ECO:0000250"
SQ SEQUENCE 420 AA; 48263 MW; B8E51833DB069032 CRC64;
MRKKAAGGAE RRPLKPRTEA AAAAPAGRAM PSDHSRMKLR RDCSRPSLQW YTRAQNKMRR
PNLLLKDILK CTLLLFGVWI LFYILKLNHT TEECDMKRMP YMDPDRIKRA QQYAQQVLQK
ECRPQFAKRS MAQLFGSRYS LDLPPFVTKV PAESEAEYKY DPPFGFRKFS GKVQTLLELL
PEHDFPEHLR AKSCKHCVVI GSGGILHGLE MGHALNQFDV VIRLNNAPVE GYSEHVGNKT
TIRMTYPEGA PLSDLEYYSS DLFVTVLFKS VDFNWLQAMV KNETLPFWVR LFFWKQVAEK
IPLQPKQFRI LNPVIIKETA FDILQYSEPQ SRFWGRDKNV PTIGVIAVVL ATHLCDEVSL
AGFSYALNQP RTPLHYFDNL CMAAMNFQTM HNVTTETNFL LKLVREGVVR DLSGGIHSEF
