SIAT9_RAT
ID SIAT9_RAT Reviewed; 387 AA.
AC Q68G12; O88830;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 112.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RA Ishii A., Saito M.;
RT "Rat GM3 synthase cDNA.";
RL Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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=BAA33492.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB018049; BAA33492.1; ALT_INIT; mRNA.
DR EMBL; BC078798; AAH78798.1; -; mRNA.
DR RefSeq; NP_112627.2; NM_031337.2.
DR RefSeq; XP_006236739.1; XM_006236677.1.
DR RefSeq; XP_006236741.1; XM_006236679.3.
DR RefSeq; XP_008761218.1; XM_008762996.1.
DR AlphaFoldDB; Q68G12; -.
DR SMR; Q68G12; -.
DR STRING; 10116.ENSRNOP00000042426; -.
DR CAZy; GT29; Glycosyltransferase Family 29.
DR GlyGen; Q68G12; 2 sites.
DR PaxDb; Q68G12; -.
DR PRIDE; Q68G12; -.
DR Ensembl; ENSRNOT00000050249; ENSRNOP00000042426; ENSRNOG00000010284.
DR GeneID; 83505; -.
DR KEGG; rno:83505; -.
DR UCSC; RGD:620875; rat.
DR CTD; 8869; -.
DR RGD; 620875; St3gal5.
DR eggNOG; KOG2692; Eukaryota.
DR GeneTree; ENSGT00940000157929; -.
DR InParanoid; Q68G12; -.
DR OMA; GQTMHNV; -.
DR OrthoDB; 891104at2759; -.
DR PhylomeDB; Q68G12; -.
DR Reactome; R-RNO-4085001; Sialic acid metabolism.
DR PRO; PR:Q68G12; -.
DR Proteomes; UP000002494; Chromosome 4.
DR Bgee; ENSRNOG00000010284; Expressed in heart and 19 other tissues.
DR ExpressionAtlas; Q68G12; baseline and differential.
DR Genevisible; Q68G12; RN.
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..387
FT /note="Lactosylceramide alpha-2,3-sialyltransferase"
FT /id="PRO_0000334618"
FT TOPO_DOM 1..33
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 34..54
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 55..387
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT CARBOHYD 58
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 208
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 167..325
FT /evidence="ECO:0000250"
SQ SEQUENCE 387 AA; 44640 MW; BF53342B7E8C06EA CRC64;
MPNEFTSAKL RSDCSRTSLQ WYTQTQHKMR RPSLLLKDIL KCMLVVFGVW LLYILKLNYT
AEECDMKKLN YVDPARIKRA HRNTQEVFQK ECRPGHAKKT MDLLFKGKYS MDLEPFVQKI
PTASEAELKY DPPFGFRKFS SKVQSLLDML PEHDFPEHLR AKHCKRCVVI GNGGILHGLE
LGHALNQFDV VIRLNSAPIE GYSEHVGNKT TIRMTYPEGA PLSDAEYYAN DLFVAVLFKS
VDFKWLQAMV KNESLPFWIR LFFWKQVAEK IPLQPKHFRI LNPVIIKETA FDILQYSEPQ
SRFWGHDKNI PTIGIIAIVL ATHLCDEVSL AGFGYDLSQP RTPLHYFDSQ CMGAMNWQVM
HNVTTETQFL QKLIKEGVVQ DLSGGIH
