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CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase 1 (Alpha 2,3-ST 1) (Beta-galactoside alpha-2,3-sialyltransferase 1) (EC 2.4.99.4) (Gal-NAc6S) (Gal-beta-1,3-GalNAc-alpha-2,3-sialyltransferase) (ST3Gal I) (ST3GalI) (ST3GalA.1) (ST3O) (Sialyltransferase 4A) (SIAT4-A)

 SIA4A_MOUSE             Reviewed;         337 AA.
P54751; Q11202;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 1.
20-JUN-2018, entry version 143.
RecName: Full=CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase 1;
Short=Alpha 2,3-ST 1;
Short=Beta-galactoside alpha-2,3-sialyltransferase 1;
EC=2.4.99.4 {ECO:0000269|PubMed:8375377, ECO:0000269|PubMed:9184827};
AltName: Full=Gal-NAc6S;
AltName: Full=Gal-beta-1,3-GalNAc-alpha-2,3-sialyltransferase;
AltName: Full=ST3Gal I;
Short=ST3GalI;
AltName: Full=ST3GalA.1;
AltName: Full=ST3O;
AltName: Full=Sialyltransferase 4A;
Short=SIAT4-A;
Name=St3gal1; Synonyms=Siat4, Siat4a;
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, SUBSTRATE
SPECIFICITY, AND TISSUE SPECIFICITY.
TISSUE=Brain;
PubMed=8375377; DOI=10.1111/j.1432-1033.1993.tb18155.x;
Lee Y.-C., Kurosawa N., Hamamoto T., Nakaoka T., Tsuji S.;
"Molecular cloning and expression of Gal beta 1,3GalNAc alpha 2,3-
sialyltransferase from mouse brain.";
Eur. J. Biochem. 216:377-385(1993).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Brain;
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).
[3]
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).
-!- FUNCTION: Responsible for the synthesis of the sequence NeuAc-
alpha-2,3-Gal-beta-1,3-GalNAc- found on sugar chains O-linked to
Thr or Ser and also as a terminal sequence on certain
gangliosides. SIAT4A and SIAT4B sialylate the same acceptor
substrates but exhibit different Km values.
{ECO:0000269|PubMed:8375377, ECO:0000269|PubMed:9184827}.
-!- CATALYTIC ACTIVITY: CMP-N-acetylneuraminate + beta-D-galactosyl-
1,3-N-acetyl-alpha-D-galactosaminyl-R = CMP + alpha-N-
acetylneuraminyl-2,3-beta-D-galactosyl-1,3-N-acetyl-alpha-D-
galactosaminyl-R. {ECO:0000269|PubMed:8375377,
ECO:0000269|PubMed:9184827}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=3.2 mM for Gal-beta-1,3-GlcNAc {ECO:0000269|PubMed:9184827};
KM=51 uM for Gal-beta-1,3-GalNAc {ECO:0000269|PubMed:9184827};
KM=0.11 mM for Gal-beta-1,3-GalNAc {ECO:0000269|PubMed:8375377};
KM=0.03 mM for CMP-N-acetyl-beta-neuraminate
{ECO:0000269|PubMed:8375377};
KM=1.5 mM for GM1 {ECO:0000269|PubMed:8375377};
KM=0.37 mM for asialo-GM1 {ECO:0000269|PubMed:8375377};
Note=Vmax is 4 fold higher with Gal-beta-1,3-GalNAc than with
Gal-beta-1,3-GlcNAc as substrate. {ECO:0000269|PubMed:9184827};
pH dependence:
Optimum pH is 6.4. {ECO:0000269|PubMed:8375377};
-!- PATHWAY: Protein modification; protein glycosylation.
-!- SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane;
Single-pass type II membrane protein. Secreted. Note=Membrane-
bound form in trans cisternae of Golgi. Secreted into the body
fluid.
-!- TISSUE SPECIFICITY: Highly expressed in submaxillary gland and to
a much lesser extent in liver, lung, kidney, heart and brain.
{ECO:0000269|PubMed:8375377}.
-!- PTM: The soluble form derives from the membrane form by
proteolytic processing.
-!- SIMILARITY: Belongs to the glycosyltransferase 29 family.
{ECO:0000305}.
-!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase;
Note=ST3Gal I;
URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_mou_642";
-----------------------------------------------------------------------
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EMBL; X73523; CAA51919.1; -; mRNA.
EMBL; BC084730; AAH84730.1; -; mRNA.
CCDS; CCDS27511.1; -.
PIR; S36824; S36824.
RefSeq; NP_033203.1; NM_009177.4.
RefSeq; XP_006520727.1; XM_006520664.3.
RefSeq; XP_006520728.1; XM_006520665.3.
RefSeq; XP_011243831.1; XM_011245529.2.
UniGene; Mm.248334; -.
UniGene; Mm.442417; -.
UniGene; Mm.461082; -.
ProteinModelPortal; P54751; -.
SMR; P54751; -.
IntAct; P54751; 1.
MINT; P54751; -.
STRING; 10090.ENSMUSP00000090307; -.
SwissLipids; SLP:000001413; -.
CAZy; GT29; Glycosyltransferase Family 29.
iPTMnet; P54751; -.
PhosphoSitePlus; P54751; -.
EPD; P54751; -.
PaxDb; P54751; -.
PeptideAtlas; P54751; -.
PRIDE; P54751; -.
Ensembl; ENSMUST00000092640; ENSMUSP00000090307; ENSMUSG00000013846.
Ensembl; ENSMUST00000229028; ENSMUSP00000154853; ENSMUSG00000013846.
Ensembl; ENSMUST00000229213; ENSMUSP00000155359; ENSMUSG00000013846.
GeneID; 20442; -.
KEGG; mmu:20442; -.
UCSC; uc007wba.1; mouse.
CTD; 6482; -.
MGI; MGI:98304; St3gal1.
eggNOG; KOG2692; Eukaryota.
eggNOG; ENOG410XT8P; LUCA.
GeneTree; ENSGT00760000119095; -.
HOGENOM; HOG000126811; -.
HOVERGEN; HBG054227; -.
InParanoid; P54751; -.
KO; K00780; -.
OMA; TWFPKQM; -.
OrthoDB; EOG091G08DE; -.
PhylomeDB; P54751; -.
TreeFam; TF354325; -.
BRENDA; 2.4.99.4; 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; St3gal1; mouse.
PRO; PR:P54751; -.
Proteomes; UP000000589; Chromosome 15.
Bgee; ENSMUSG00000013846; -.
ExpressionAtlas; P54751; baseline and differential.
Genevisible; P54751; MM.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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:0006054; P:N-acetylneuraminate metabolic process; ISS:UniProtKB.
GO; GO:0009311; P:oligosaccharide metabolic process; IBA:GO_Central.
GO; GO:0006486; P:protein glycosylation; IDA:MGI.
GO; GO:0006487; P:protein N-linked glycosylation; ISS:UniProtKB.
GO; GO:0018279; P:protein N-linked glycosylation via asparagine; IBA:GO_Central.
GO; GO:0006468; P:protein phosphorylation; IDA:MGI.
GO; GO:0097503; P:sialylation; ISS:UniProtKB.
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; Secreted;
Signal-anchor; Transferase; Transmembrane; Transmembrane helix.
CHAIN 1 337 CMP-N-acetylneuraminate-beta-
galactosamide-alpha-2,3-sialyltransferase
1.
/FTId=PRO_0000149254.
TOPO_DOM 1 4 Cytoplasmic. {ECO:0000255}.
TRANSMEM 5 25 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 26 337 Lumenal. {ECO:0000255}.
BINDING 102 102 Substrate. {ECO:0000250}.
BINDING 144 144 Substrate. {ECO:0000250}.
BINDING 167 167 Substrate. {ECO:0000250}.
BINDING 227 227 Substrate. {ECO:0000250}.
BINDING 263 263 Substrate. {ECO:0000250}.
BINDING 267 267 Substrate; via amide nitrogen.
{ECO:0000250}.
BINDING 287 287 Substrate; via amide nitrogen.
{ECO:0000250}.
BINDING 296 296 Substrate. {ECO:0000250}.
BINDING 313 313 Substrate. {ECO:0000250}.
CARBOHYD 76 76 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 109 109 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 320 320 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 56 61 {ECO:0000250}.
DISULFID 58 136 {ECO:0000250}.
DISULFID 139 278 {ECO:0000250}.
SEQUENCE 337 AA; 39073 MW; CB54929D1EC047D1 CRC64;
MRRKTLKYLT FFLLFIFLTS FVLNYSNTGV PSAWFPKQML LELSENFRRF IKSQPCTCRH
CISQDKVSYW FDQRFNKTMQ PLLTVHNALM EEDTYRWWLR LQRERKPNNL SDTVKELFRL
VPGNVDPMLN KRLVGCRRCA VVGNSGNLKD SSYGPEIDSH DFVLRMNKAP TVGFEADVGS
RTTHHLVYPE SFRELGENVN MVLVPFKTTD LQWVISATTT GTITHTYVPV PPKIKVKQEK
ILIYHPAFIK YVFDNWLQGH GRYPSTGILS IIFSIHICDE VDLYGFGADS KGNWHHYWEN
NPSAGAFRKT GVHDGDFEYN ITTTLAAINK IRIFKGR


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