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CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase 2 (Alpha 2,3-ST 2) (Beta-galactoside alpha-2,3-sialyltransferase 2) (EC 2.4.99.4) (Gal-NAc6S) (Gal-beta-1,3-GalNAc-alpha-2,3-sialyltransferase) (ST3Gal II) (ST3GalII) (ST3GalA.2) (Sialyltransferase 4B) (SIAT4-B)

 SIA4B_MOUSE             Reviewed;         350 AA.
Q11204; Q8BPL0;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
27-JUL-2011, sequence version 2.
20-JUN-2018, entry version 135.
RecName: Full=CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase 2;
Short=Alpha 2,3-ST 2;
Short=Beta-galactoside alpha-2,3-sialyltransferase 2;
EC=2.4.99.4 {ECO:0000269|PubMed:9184827};
AltName: Full=Gal-NAc6S;
AltName: Full=Gal-beta-1,3-GalNAc-alpha-2,3-sialyltransferase;
AltName: Full=ST3Gal II;
Short=ST3GalII;
AltName: Full=ST3GalA.2;
AltName: Full=Sialyltransferase 4B;
Short=SIAT4-B;
Name=St3gal2; Synonyms=Siat4b, Siat5;
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, TISSUE SPECIFICITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
TISSUE=Brain;
PubMed=8144500;
Lee Y.-C., Kojima N., Wada E., Kurosawa N., Nakaoka T., Hamamoto T.,
Tsuji S.;
"Cloning and expression of cDNA for a new type of Gal beta 1,3GalNAc
alpha 2,3-sialyltransferase.";
J. Biol. Chem. 269:10028-10033(1994).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Cerebellum, and Eye;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[4]
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).
[5]
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 in terminal carbohydrate
groups of certain glycoproteins, oligosaccharides and glycolipids.
SIAT4A and SIAT4B sialylate the same acceptor substrates but
exhibit different Km values. {ECO:0000269|PubMed:8144500,
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:8144500,
ECO:0000269|PubMed:9184827}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=2.3 mM for Gal-beta-1,3-GlcNAc {ECO:0000269|PubMed:9184827};
KM=0.16 mM for Gal-beta-1,3-GalNAc {ECO:0000269|PubMed:9184827};
KM=0.63 mM for Gal-beta-1,3-GalNAc {ECO:0000269|PubMed:8144500};
KM=0.83 mM for GM1 {ECO:0000269|PubMed:8144500};
KM=0.67 mM for asialo-GM1 {ECO:0000269|PubMed:8144500};
Note=Vmax is 10 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:9184827};
-!- 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: Strongly expressed in brain and liver and to a
lesser extent in heart and kidney. Scarcely detectable in lung,
pancreas, spleen and submaxillary gland.
{ECO:0000269|PubMed:8144500}.
-!- 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 II;
URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_mou_643";
-----------------------------------------------------------------------
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EMBL; X76989; CAA54294.1; -; mRNA.
EMBL; AK053827; BAC35543.1; -; mRNA.
EMBL; AK131653; BAE20742.1; -; mRNA.
EMBL; CH466525; EDL11478.1; -; Genomic_DNA.
EMBL; BC066064; AAH66064.1; -; mRNA.
CCDS; CCDS22667.1; -.
PIR; A54420; A54420.
RefSeq; NP_033205.2; NM_009179.3.
RefSeq; XP_006530849.1; XM_006530786.2.
RefSeq; XP_006530850.1; XM_006530787.2.
RefSeq; XP_006530851.1; XM_006530788.1.
RefSeq; XP_017168113.1; XM_017312624.1.
UniGene; Mm.200388; -.
ProteinModelPortal; Q11204; -.
SMR; Q11204; -.
STRING; 10090.ENSMUSP00000034197; -.
SwissLipids; SLP:000001389; -.
CAZy; GT29; Glycosyltransferase Family 29.
PhosphoSitePlus; Q11204; -.
MaxQB; Q11204; -.
PaxDb; Q11204; -.
PRIDE; Q11204; -.
Ensembl; ENSMUST00000034197; ENSMUSP00000034197; ENSMUSG00000031749.
GeneID; 20444; -.
KEGG; mmu:20444; -.
UCSC; uc009nlk.2; mouse.
CTD; 6483; -.
MGI; MGI:99427; St3gal2.
eggNOG; KOG2692; Eukaryota.
eggNOG; ENOG410XT8P; LUCA.
GeneTree; ENSGT00760000119095; -.
HOGENOM; HOG000126811; -.
HOVERGEN; HBG054227; -.
InParanoid; Q11204; -.
KO; K03368; -.
OMA; CACRRCM; -.
OrthoDB; EOG091G08DE; -.
TreeFam; TF354325; -.
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; -.
PRO; PR:Q11204; -.
Proteomes; UP000000589; Chromosome 8.
Bgee; ENSMUSG00000031749; -.
ExpressionAtlas; Q11204; baseline and differential.
Genevisible; Q11204; 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:0047288; F:monosialoganglioside sialyltransferase activity; ISO:MGI.
GO; GO:0008373; F:sialyltransferase activity; ISO:MGI.
GO; GO:0009247; P:glycolipid biosynthetic process; ISO:MGI.
GO; GO:0009101; P:glycoprotein biosynthetic process; ISO:MGI.
GO; GO:0030259; P:lipid glycosylation; ISO:MGI.
GO; GO:0009312; P:oligosaccharide biosynthetic process; ISO:MGI.
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.
GO; GO:1990743; P:protein sialylation; ISO:MGI.
GO; GO:0097503; P:sialylation; ISO:MGI.
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 1 350 CMP-N-acetylneuraminate-beta-
galactosamide-alpha-2,3-sialyltransferase
2.
/FTId=PRO_0000149259.
TOPO_DOM 1 6 Cytoplasmic. {ECO:0000255}.
TRANSMEM 7 27 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 28 350 Lumenal. {ECO:0000255}.
BINDING 116 116 Substrate. {ECO:0000250}.
BINDING 157 157 Substrate. {ECO:0000250}.
BINDING 180 180 Substrate. {ECO:0000250}.
BINDING 240 240 Substrate. {ECO:0000250}.
BINDING 276 276 Substrate. {ECO:0000250}.
BINDING 280 280 Substrate; via amide nitrogen.
{ECO:0000250}.
BINDING 300 300 Substrate; via amide nitrogen.
{ECO:0000250}.
BINDING 309 309 Substrate. {ECO:0000250}.
BINDING 326 326 Substrate. {ECO:0000250}.
CARBOHYD 92 92 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 211 211 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 70 75 {ECO:0000250}.
DISULFID 72 149 {ECO:0000250}.
DISULFID 152 291 {ECO:0000250}.
CONFLICT 309 310 HY -> RH (in Ref. 1; CAA54294).
{ECO:0000305}.
SEQUENCE 350 AA; 40130 MW; 3C59FA39E6A03E4D CRC64;
MKCSLRVWFL SMAFLLVFIM SLLFTYSHHS MATLPYLDSG ALGGTHRVKL VPGYSGLQRL
GKEGLLGRNC ACSRCMGDAS TSEWFDSHFD GNISPVWTRD NMNLPPDVQR WWMMLQPQFK
SHNTNEVLEK LFQIVPGENP YRFRDPQQCR RCAVVGNSGN LRGSGYGQEV DSHNFIMRMN
QAPTVGFEKD VGSRTTHHFM YPESAKNLPA NVSFVLVPFK ALDLMWIASA LSTGQIRFTY
APVKSFLRVD KEKVQIYNPA FFKYIHDRWT EHHGRYPSTG MLVLFFALHV CDEVNVYGFG
ADSRGNWHHY WENNRYAGEF RKTGVHDADF EAHIIDMLAK ASKIEVYRGN


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