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CMP-N-acetylneuraminate-beta-1,4-galactoside alpha-2,3-sialyltransferase (EC 2.4.99.6) (Beta-galactoside alpha-2,3-sialyltransferase 3) (Alpha 2,3-ST 3) (Gal beta-1,3(4) GlcNAc alpha-2,3 sialyltransferase) (N-acetyllactosaminide alpha-2,3-sialyltransferase) (ST3Gal III) (ST3GalIII) (ST3N) (Sialyltransferase 6)

 SIAT6_MOUSE             Reviewed;         374 AA.
P97325; Q922X5;
27-APR-2001, integrated into UniProtKB/Swiss-Prot.
27-JUL-2011, sequence version 2.
28-MAR-2018, entry version 139.
RecName: Full=CMP-N-acetylneuraminate-beta-1,4-galactoside alpha-2,3-sialyltransferase;
EC=2.4.99.6 {ECO:0000269|PubMed:9184827};
AltName: Full=Beta-galactoside alpha-2,3-sialyltransferase 3;
Short=Alpha 2,3-ST 3;
AltName: Full=Gal beta-1,3(4) GlcNAc alpha-2,3 sialyltransferase;
AltName: Full=N-acetyllactosaminide alpha-2,3-sialyltransferase;
AltName: Full=ST3Gal III;
Short=ST3GalIII;
AltName: Full=ST3N;
AltName: Full=Sialyltransferase 6;
Name=St3gal3; Synonyms=Siat3, Siat6;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, TISSUE
SPECIFICITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
TISSUE=Brain;
PubMed=9184827; DOI=10.1093/glycob/7.4.469;
Kono M., Ohyama Y., Lee Y.-C., Hamamoto T., Kojima N., Tsuji S.;
"Mouse beta-galactoside alpha2,3-sialyltransferases: comparison of in
vitro substrate specificities and tissue specific expression.";
Glycobiology 7:469-479(1997).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N; TISSUE=Mammary tumor;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
-!- FUNCTION: Catalyzes the formation of the NeuAc-alpha-2,3-Gal-beta-
1,4-GlcNAc-, NeuAc-alpha-2,3-Gal-beta-1,3-GlcNAc- and NeuAc-alpha-
2,3-Gal-beta-1,3-GalNAc- sequences found in terminal carbohydrate
groups of glycoproteins and glycolipids. The highest activity is
toward Gal-beta-1,3-GlcNAc and the lowest toward Gal-beta-1,3-
GalNAc. {ECO:0000269|PubMed:9184827}.
-!- CATALYTIC ACTIVITY: CMP-N-acetyl-beta-neuraminate + beta-D-
galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-R = CMP + N-acetyl-
alpha-neuraminyl-(2->3)-beta-D-galactosyl-(1->4)-N-acetyl-beta-D-
glucosaminyl-R. {ECO:0000269|PubMed:9184827}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.32 mM for Gal-beta-1,3-GlcNAc {ECO:0000269|PubMed:9184827};
KM=3.0 mM for Gal-beta-1,4-GlcNAc {ECO:0000269|PubMed:9184827};
KM=2.2 mM for Gal-beta-1,3-GalNAc {ECO:0000269|PubMed:9184827};
Note=Relative Vmax is 4:2:1 for Gal-beta-1,3-GlcNAc, Gal-beta-
1,4-GlcNAc and Gal-beta-1,3-GalNAc as substrate, respectively.
{ECO:0000269|PubMed:9184827};
pH dependence:
Optimum pH is 6.4. {ECO:0000269|PubMed:9184827};
-!- PATHWAY: Protein modification; protein glycosylation.
-!- SUBCELLULAR LOCATION: Membrane; Single-pass type II membrane
protein. Golgi apparatus, Golgi stack membrane; Single-pass type
II membrane protein.
-!- TISSUE SPECIFICITY: Found in all tissues tested. High expression
found in brain, liver, kidney, colon, heart and spleen.
{ECO:0000269|PubMed:9184827}.
-!- DEVELOPMENTAL STAGE: Developmental regulation only occurs in
liver, heart, kidney and spleen.
-!- SIMILARITY: Belongs to the glycosyltransferase 29 family.
{ECO:0000305}.
-!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase;
Note=ST3Gal III;
URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_mou_644";
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; X84234; CAA59013.1; -; mRNA.
EMBL; AL627128; CAM14710.1; -; Genomic_DNA.
EMBL; AL611952; CAM14710.1; JOINED; Genomic_DNA.
EMBL; AL626764; CAM14710.1; JOINED; Genomic_DNA.
EMBL; AL611952; CAM26721.1; -; Genomic_DNA.
EMBL; AL626764; CAM26721.1; JOINED; Genomic_DNA.
EMBL; AL627128; CAM26721.1; JOINED; Genomic_DNA.
EMBL; AL626764; CAM27383.1; -; Genomic_DNA.
EMBL; AL611952; CAM27383.1; JOINED; Genomic_DNA.
EMBL; AL627128; CAM27383.1; JOINED; Genomic_DNA.
EMBL; CH466552; EDL30520.1; -; Genomic_DNA.
EMBL; CH466552; EDL30522.1; -; Genomic_DNA.
EMBL; BC006710; AAH06710.1; -; mRNA.
CCDS; CCDS18544.1; -.
RefSeq; NP_001155246.1; NM_001161774.2.
RefSeq; NP_001272449.1; NM_001285520.1.
RefSeq; NP_033202.3; NM_009176.5.
UniGene; Mm.251002; -.
ProteinModelPortal; P97325; -.
STRING; 10090.ENSMUSP00000030263; -.
CAZy; GT29; Glycosyltransferase Family 29.
iPTMnet; P97325; -.
PhosphoSitePlus; P97325; -.
MaxQB; P97325; -.
PaxDb; P97325; -.
PRIDE; P97325; -.
Ensembl; ENSMUST00000030263; ENSMUSP00000030263; ENSMUSG00000028538.
Ensembl; ENSMUST00000106410; ENSMUSP00000102018; ENSMUSG00000028538.
GeneID; 20441; -.
KEGG; mmu:20441; -.
UCSC; uc008ujk.3; mouse.
CTD; 6487; -.
MGI; MGI:1316659; St3gal3.
eggNOG; KOG2692; Eukaryota.
eggNOG; ENOG410XT8P; LUCA.
GeneTree; ENSGT00760000119095; -.
HOGENOM; HOG000000682; -.
HOVERGEN; HBG056676; -.
InParanoid; P97325; -.
KO; K00781; -.
OMA; PHEIRIL; -.
OrthoDB; EOG091G098L; -.
TreeFam; TF354325; -.
BRENDA; 2.4.99.4; 3474.
BRENDA; 2.4.99.6; 3474.
BRENDA; 2.4.99.8; 3474.
Reactome; R-MMU-2022854; Keratan sulfate biosynthesis.
Reactome; R-MMU-4085001; Sialic acid metabolism.
Reactome; R-MMU-977068; Termination of O-glycan biosynthesis.
UniPathway; UPA00378; -.
ChiTaRS; St3gal3; mouse.
PRO; PR:P97325; -.
Proteomes; UP000000589; Chromosome 4.
Bgee; ENSMUSG00000028538; -.
ExpressionAtlas; P97325; baseline and differential.
Genevisible; P97325; MM.
GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
GO; GO:0000139; C:Golgi membrane; IBA:GO_Central.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0003836; F:beta-galactoside (CMP) alpha-2,3-sialyltransferase activity; IDA:MGI.
GO; GO:0008118; F:N-acetyllactosaminide alpha-2,3-sialyltransferase activity; IBA:GO_Central.
GO; GO:0009311; P:oligosaccharide metabolic process; IBA:GO_Central.
GO; GO:0006486; P:protein glycosylation; IDA:MGI.
GO; GO:0018279; P:protein N-linked glycosylation via asparagine; IBA:GO_Central.
Gene3D; 3.90.1480.20; -; 1.
InterPro; IPR001675; Glyco_trans_29.
InterPro; IPR038578; GT29-like_sf.
InterPro; IPR012163; Sialyl_trans.
Pfam; PF00777; Glyco_transf_29; 1.
PIRSF; PIRSF005557; Sialyl_trans; 1.
1: Evidence at protein level;
Complete proteome; Disulfide bond; Glycoprotein; Glycosyltransferase;
Golgi apparatus; Membrane; Reference proteome; Signal-anchor;
Transferase; Transmembrane; Transmembrane helix.
CHAIN 1 374 CMP-N-acetylneuraminate-beta-1,4-
galactoside alpha-2,3-sialyltransferase.
/FTId=PRO_0000149267.
TOPO_DOM 1 8 Cytoplasmic. {ECO:0000255}.
TRANSMEM 9 28 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 29 374 Lumenal. {ECO:0000255}.
CARBOHYD 79 79 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 170 170 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 159 313 {ECO:0000250}.
CONFLICT 78 78 A -> P (in Ref. 1; CAA59013).
{ECO:0000305}.
CONFLICT 350 350 N -> S (in Ref. 1; CAA59013).
{ECO:0000305}.
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


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