SIAT6_MOUSE
ID SIAT6_MOUSE Reviewed; 374 AA.
AC P97325; Q922X5;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=CMP-N-acetylneuraminate-beta-1,4-galactoside alpha-2,3-sialyltransferase;
DE EC=2.4.99.6 {ECO:0000269|PubMed:9184827};
DE AltName: Full=Beta-galactoside alpha-2,3-sialyltransferase 3;
DE Short=Alpha 2,3-ST 3;
DE AltName: Full=Gal beta-1,3(4) GlcNAc alpha-2,3 sialyltransferase;
DE AltName: Full=N-acetyllactosaminide alpha-2,3-sialyltransferase;
DE AltName: Full=ST3Gal III;
DE Short=ST3GalIII;
DE AltName: Full=ST3N;
DE AltName: Full=Sialyltransferase 6;
GN Name=St3gal3; Synonyms=Siat3, Siat6;
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, TISSUE
RP SPECIFICITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC TISSUE=Brain;
RX PubMed=9184827; DOI=10.1093/glycob/7.4.469;
RA Kono M., Ohyama Y., Lee Y.-C., Hamamoto T., Kojima N., Tsuji S.;
RT "Mouse beta-galactoside alpha2,3-sialyltransferases: comparison of in vitro
RT substrate specificities and tissue specific expression.";
RL Glycobiology 7:469-479(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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: Catalyzes the formation of the NeuAc-alpha-2,3-Gal-beta-1,4-
CC GlcNAc-, NeuAc-alpha-2,3-Gal-beta-1,3-GlcNAc- and NeuAc-alpha-2,3-Gal-
CC beta-1,3-GalNAc- sequences found in terminal carbohydrate groups of
CC glycoproteins and glycolipids. The highest activity is toward Gal-beta-
CC 1,3-GlcNAc and the lowest toward Gal-beta-1,3-GalNAc.
CC {ECO:0000269|PubMed:9184827}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl
CC derivative + CMP-N-acetyl-beta-neuraminate = an N-acetyl-alpha-
CC neuraminyl-(2->3)-beta-D-galactosyl-(1->4)-N-acetyl-beta-D-
CC glucosaminyl derivative + CMP + H(+); Xref=Rhea:RHEA:52316,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57812, ChEBI:CHEBI:60377,
CC ChEBI:CHEBI:133507, ChEBI:CHEBI:136545; EC=2.4.99.6;
CC Evidence={ECO:0000269|PubMed:9184827};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.32 mM for Gal-beta-1,3-GlcNAc {ECO:0000269|PubMed:9184827};
CC KM=3.0 mM for Gal-beta-1,4-GlcNAc {ECO:0000269|PubMed:9184827};
CC KM=2.2 mM for Gal-beta-1,3-GalNAc {ECO:0000269|PubMed:9184827};
CC Note=Relative Vmax is 4:2:1 for Gal-beta-1,3-GlcNAc, Gal-beta-1,4-
CC GlcNAc and Gal-beta-1,3-GalNAc as substrate, respectively.
CC {ECO:0000269|PubMed:9184827};
CC pH dependence:
CC Optimum pH is 6.4. {ECO:0000269|PubMed:9184827};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type II membrane protein.
CC Golgi apparatus, Golgi stack membrane; Single-pass type II membrane
CC protein.
CC -!- TISSUE SPECIFICITY: Found in all tissues tested. High expression found
CC in brain, liver, kidney, colon, heart and spleen.
CC {ECO:0000269|PubMed:9184827}.
CC -!- DEVELOPMENTAL STAGE: Developmental regulation only occurs in liver,
CC heart, kidney and spleen.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 29 family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase; Note=ST3Gal
CC III;
CC URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_mou_644";
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DR EMBL; X84234; CAA59013.1; -; mRNA.
DR EMBL; AL611952; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL626764; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL627128; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466552; EDL30520.1; -; Genomic_DNA.
DR EMBL; CH466552; EDL30522.1; -; Genomic_DNA.
DR EMBL; BC006710; AAH06710.1; -; mRNA.
DR CCDS; CCDS18544.1; -.
DR RefSeq; NP_001155246.1; NM_001161774.2.
DR RefSeq; NP_001272449.1; NM_001285520.1.
DR RefSeq; NP_033202.3; NM_009176.5.
DR AlphaFoldDB; P97325; -.
DR SMR; P97325; -.
DR STRING; 10090.ENSMUSP00000030263; -.
DR CAZy; GT29; Glycosyltransferase Family 29.
DR GlyGen; P97325; 2 sites.
DR iPTMnet; P97325; -.
DR PhosphoSitePlus; P97325; -.
DR MaxQB; P97325; -.
DR PaxDb; P97325; -.
DR PRIDE; P97325; -.
DR ProteomicsDB; 257245; -.
DR Antibodypedia; 32385; 166 antibodies from 26 providers.
DR DNASU; 20441; -.
DR Ensembl; ENSMUST00000030263; ENSMUSP00000030263; ENSMUSG00000028538.
DR Ensembl; ENSMUST00000106410; ENSMUSP00000102018; ENSMUSG00000028538.
DR GeneID; 20441; -.
DR KEGG; mmu:20441; -.
DR UCSC; uc008ujk.3; mouse.
DR CTD; 6487; -.
DR MGI; MGI:1316659; St3gal3.
DR VEuPathDB; HostDB:ENSMUSG00000028538; -.
DR eggNOG; KOG2692; Eukaryota.
DR GeneTree; ENSGT00940000157285; -.
DR InParanoid; P97325; -.
DR OMA; NDINVGR; -.
DR OrthoDB; 891104at2759; -.
DR PhylomeDB; P97325; -.
DR TreeFam; TF354325; -.
DR BRENDA; 2.4.99.2; 3474.
DR BRENDA; 2.4.99.6; 3474.
DR BRENDA; 2.4.99.8; 3474.
DR Reactome; R-MMU-2022854; Keratan sulfate biosynthesis.
DR Reactome; R-MMU-4085001; Sialic acid metabolism.
DR Reactome; R-MMU-9037629; Lewis blood group biosynthesis.
DR Reactome; R-MMU-977068; Termination of O-glycan biosynthesis.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 20441; 7 hits in 74 CRISPR screens.
DR ChiTaRS; St3gal3; mouse.
DR PRO; PR:P97325; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; P97325; protein.
DR Bgee; ENSMUSG00000028538; Expressed in hindlimb stylopod muscle and 242 other tissues.
DR ExpressionAtlas; P97325; baseline and differential.
DR Genevisible; P97325; MM.
DR GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0003836; F:beta-galactoside (CMP) alpha-2,3-sialyltransferase activity; IDA:MGI.
DR GO; GO:0008118; F:N-acetyllactosaminide alpha-2,3-sialyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0008373; F:sialyltransferase activity; IBA:GO_Central.
DR GO; GO:0010706; P:ganglioside biosynthetic process via lactosylceramide; IMP:UniProtKB.
DR GO; GO:0006486; P:protein glycosylation; IDA:MGI.
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 Membrane; Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..374
FT /note="CMP-N-acetylneuraminate-beta-1,4-galactoside alpha-
FT 2,3-sialyltransferase"
FT /id="PRO_0000149267"
FT TOPO_DOM 1..8
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 9..28
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 29..374
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT CARBOHYD 79
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 170
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 159..313
FT /evidence="ECO:0000250"
FT CONFLICT 78
FT /note="A -> P (in Ref. 1; CAA59013)"
FT /evidence="ECO:0000305"
FT CONFLICT 350
FT /note="N -> S (in Ref. 1; CAA59013)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 374 AA; 42132 MW; 9E776305912CECDC CRC64;
MGLLVFVRNL LLALCLFLVL GFLYYSAWKL HLLQWEDSNS LLLSLDSAGQ TLGTEYDRLG
FLLKLDSKLP AELATKYANF SEGACKPGYA SAMMTAIFPR FSKPAPMFLD DSFRKWARIR
EFVPPFGIKG QDNLIKAILS VTKEYRLTPA LDSLHCRRCI IVGNGGVLAN KSLGSRIDDY
DIVIRLNSAP VKGFERDVGS KTTLRITYPE GAMQRPEQYE RDSLFVLAGF KWQDFKWLKY
IVYKERVSAS DGFWKSVATR VPKEPPEIRI LNPYFIQEAA FTLIGLPFNN GLMGRGNIPT
LGSVAVTMAL HGCDEVAVAG FGYDMNTPNA PLHYYETVRM AAIKESWTHN IQREKEFLRK
LVKARVITDL SSGI
