SIA7E_MOUSE
ID SIA7E_MOUSE Reviewed; 336 AA.
AC Q9QYJ1; Q9R0K6;
DT 11-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 135.
DE RecName: Full=Alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase 5;
DE EC=2.4.99.- {ECO:0000269|PubMed:10521438, ECO:0000305|PubMed:10601645};
DE AltName: Full=GD1 alpha synthase;
DE AltName: Full=GalNAc alpha-2,6-sialyltransferase V;
DE AltName: Full=ST6GalNAc V {ECO:0000303|PubMed:10521438, ECO:0000303|PubMed:10601645};
DE Short=ST6GalNAcV;
DE AltName: Full=Sialyltransferase 7E;
DE Short=SIAT7-E;
GN Name=St6galnac5; Synonyms=Siat7e;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND TISSUE
RP SPECIFICITY.
RC STRAIN=C3H/HeN, C57BL/6J, and C57BL/6N; TISSUE=Brain;
RX PubMed=10601645; DOI=10.1016/s0014-5793(99)01605-1;
RA Ikehara Y., Shimizu N., Kono M., Nishihara S., Nakanishi H., Kitamura T.,
RA Narimatsu H., Tsuji S., Tatematsu M.;
RT "A novel glycosyltransferase with a polyglutamine repeat; a new candidate
RT for GD1alpha synthase (ST6GalNAc V).";
RL FEBS Lett. 463:92-96(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND TISSUE
RP SPECIFICITY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=10521438; DOI=10.1074/jbc.274.43.30557;
RA Okajima T., Fukumoto S., Ito H., Kiso M., Hirabayashi Y., Urano T.,
RA Furukawa K.;
RT "Molecular cloning of brain specific GD1alpha synthase (ST6GalNAc V)
RT containing CAG/glutamine repeats.";
RL J. Biol. Chem. 274:30557-30562(1999).
RN [3]
RP FUNCTION.
RX PubMed=9157980;
RA Taki T., Ishikawa D., Ogura M., Nakajima M., Handa S.;
RT "Ganglioside GD1alpha functions in the adhesion of metastatic tumor cells
RT to endothelial cells of the target tissue.";
RL Cancer Res. 57:1882-1888(1997).
CC -!- FUNCTION: Predominantly catalyzes the biosynthesis of ganglioside
CC GD1alpha from GM1b in the brain, by transferring the sialyl group (N-
CC acetyl-alpha-neuraminyl or NeuAc) from CMP-NeuAc to the GalNAc residue
CC on the NeuAc-alpha-2,3-Gal-beta-1,3-GalNAc sequence of GM1b
CC (PubMed:10601645, PubMed:10521438). GD1alpha is a critical molecule in
CC the communication and interaction between neuronal cells and their
CC supportive cells, particularly in brain tissues, and functions as an
CC adhesion molecule in the process of metastasis (PubMed:9157980). Also
CC shows activity towards sialyl Lc4Cer (N-acetyl-alpha-neuraminosyl-
CC (2->3)-beta-D-galactosyl-(1->3)-N-acetyl-beta-D-glucosaminyl-(1->3)-
CC beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1')-N-acyl-sphing-4-
CC enine) generating disialyl Lc4Cer, which can lead to the synthesis of
CC disialyl Lewis a (Le(a)), suggested to be a cancer-associated antigen
CC (By similarity). {ECO:0000250|UniProtKB:Q9BVH7,
CC ECO:0000269|PubMed:10521438, ECO:0000269|PubMed:10601645,
CC ECO:0000269|PubMed:9157980}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CMP-N-acetyl-beta-neuraminate + ganglioside GM1b (d18:1(4E)) =
CC a ganglioside GD1alpha (d18:1(4E)) + CMP + H(+);
CC Xref=Rhea:RHEA:41968, ChEBI:CHEBI:15378, ChEBI:CHEBI:57812,
CC ChEBI:CHEBI:60377, ChEBI:CHEBI:78568, ChEBI:CHEBI:78569;
CC Evidence={ECO:0000269|PubMed:10521438, ECO:0000305|PubMed:10601645};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41969;
CC Evidence={ECO:0000305|PubMed:10521438, ECO:0000305|PubMed:10601645};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CMP-N-acetyl-beta-neuraminate + N-acetyl-alpha-neuraminosyl-
CC (2->3)-beta-D-galactosyl-(1->3)-N-acetyl-beta-D-glucosaminyl-(1->3)-
CC beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1')-N-acyl-sphing-4-
CC enine = CMP + H(+) + N-acetyl-alpha-neuraminosyl-(2->3)-beta-D-
CC galactosyl-(1->3)-[N-acetyl-alpha-neuraminosyl-(2->6)]-N-acetyl-beta-
CC D-glucosaminyl-(1->3)-beta-D-galactosyl-(1->4)-beta-D-glucosyl-
CC (1<->1')-N-acyl-sphing-4-enine; Xref=Rhea:RHEA:47884,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57812, ChEBI:CHEBI:60377,
CC ChEBI:CHEBI:88073, ChEBI:CHEBI:88079;
CC Evidence={ECO:0000250|UniProtKB:Q9BVH7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47885;
CC Evidence={ECO:0000250|UniProtKB:Q9BVH7};
CC -!- PATHWAY: Glycolipid biosynthesis. {ECO:0000305|PubMed:10521438,
CC ECO:0000305|PubMed:10601645}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane; Single-pass type II
CC membrane protein.
CC -!- TISSUE SPECIFICITY: High expression in forebrain and to a lesser extent
CC in cerebellum. No expression in salivary gland, intestine, liver,
CC kidney, heart, lung, thymus and spleen. {ECO:0000269|PubMed:10521438,
CC ECO:0000269|PubMed:10601645}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 29 family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase; Note=ST6GalNAc
CC V;
CC URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_mou_654";
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DR EMBL; AB028840; BAA89292.1; -; mRNA.
DR EMBL; AB030836; BAA85747.1; -; mRNA.
DR RefSeq; NP_036158.3; NM_012028.4.
DR AlphaFoldDB; Q9QYJ1; -.
DR STRING; 10090.ENSMUSP00000036227; -.
DR SwissLipids; SLP:000000784; -.
DR CAZy; GT29; Glycosyltransferase Family 29.
DR GlyGen; Q9QYJ1; 2 sites.
DR iPTMnet; Q9QYJ1; -.
DR PhosphoSitePlus; Q9QYJ1; -.
DR PaxDb; Q9QYJ1; -.
DR PRIDE; Q9QYJ1; -.
DR ProteomicsDB; 261231; -.
DR DNASU; 26938; -.
DR GeneID; 26938; -.
DR KEGG; mmu:26938; -.
DR CTD; 81849; -.
DR MGI; MGI:1349471; St6galnac5.
DR eggNOG; KOG2692; Eukaryota.
DR InParanoid; Q9QYJ1; -.
DR OrthoDB; 817470at2759; -.
DR PhylomeDB; Q9QYJ1; -.
DR Reactome; R-MMU-4085001; Sialic acid metabolism.
DR BioGRID-ORCS; 26938; 3 hits in 75 CRISPR screens.
DR ChiTaRS; St6galnac5; mouse.
DR PRO; PR:Q9QYJ1; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q9QYJ1; protein.
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:0001665; F:alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase activity; IDA:BHF-UCL.
DR GO; GO:0008373; F:sialyltransferase activity; IDA:BHF-UCL.
DR GO; GO:0001574; P:ganglioside biosynthetic process; IBA:GO_Central.
DR GO; GO:0006688; P:glycosphingolipid biosynthetic process; IDA:BHF-UCL.
DR GO; GO:0009312; P:oligosaccharide biosynthetic process; IDA:BHF-UCL.
DR GO; GO:0009311; P:oligosaccharide metabolic process; IBA:GO_Central.
DR GO; GO:0006486; P:protein glycosylation; IEA:InterPro.
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 1: Evidence at protein level;
KW Disulfide bond; Glycoprotein; Glycosyltransferase; Golgi apparatus;
KW Lipid metabolism; Membrane; Reference proteome; Sialic acid; Signal-anchor;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..336
FT /note="Alpha-N-acetylgalactosaminide alpha-2,6-
FT sialyltransferase 5"
FT /id="PRO_0000149281"
FT TOPO_DOM 1..8
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 9..29
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 30..336
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 34..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..65
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 137
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 161
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 96..245
FT /evidence="ECO:0000250"
FT VARIANT 48..49
FT /note="Missing (in strain: C57BL/6J)"
FT VARIANT 49
FT /note="Missing (in strain: C57BL/6N and C57BL/6J)"
SQ SEQUENCE 336 AA; 38430 MW; 128516E3815985E6 CRC64;
MKTLMRHGLA VCLVLTTMCT SLLLVYSSLG SQKERPPQQQ QQQQQQQQQA ATATGSTQLV
ESSPQPRRTA PAGPRQLEGY LGVADHKPLK MHCKDCALVT SSGHLLRSQQ GPHIDQTECV
IRMNDAPTRG YGLDVGNRTS LRVIAHSSIQ RILRNRHDLL NVSQGTVFIF WGPSSYMRRD
GKGQAYNNLQ LLSQVLPRLK AFMITRHRML QFDELFKQET GKDRKISNTW LSTGWFTMTI
ALELCDRIDV YGMVPPDFCR DPKHPSVPYH YYEPSGPDEC TMYLSHERGR KGSHHRFITE
KRVFKNWART FNIHFFQPDW KPESPAVNHA EGKPVF
