SIA4B_MOUSE
ID SIA4B_MOUSE Reviewed; 350 AA.
AC Q11204; Q8BPL0;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase 2;
DE Short=Alpha 2,3-ST 2;
DE Short=Beta-galactoside alpha-2,3-sialyltransferase 2;
DE EC=2.4.99.4 {ECO:0000269|PubMed:8144500, ECO:0000269|PubMed:9184827};
DE AltName: Full=Gal-NAc6S;
DE AltName: Full=Gal-beta-1,3-GalNAc-alpha-2,3-sialyltransferase {ECO:0000303|PubMed:8144500};
DE AltName: Full=Monosialoganglioside sialyltransferase;
DE EC=2.4.99.2 {ECO:0000305|PubMed:8144500};
DE AltName: Full=ST3Gal II;
DE Short=ST3GalII;
DE AltName: Full=ST3GalA.2;
DE AltName: Full=Sialyltransferase 4B;
DE Short=SIAT4-B;
GN Name=St3gal2 {ECO:0000303|PubMed:22735313, ECO:0000312|MGI:MGI:99427};
GN Synonyms=Siat4b, Siat5;
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, SUBSTRATE
RP SPECIFICITY, TISSUE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP PATHWAY.
RC TISSUE=Brain;
RX PubMed=8144500; DOI=10.1016/s0021-9258(17)36985-5;
RA Lee Y.-C., Kojima N., Wada E., Kurosawa N., Nakaoka T., Hamamoto T.,
RA Tsuji S.;
RT "Cloning and expression of cDNA for a new type of Gal beta 1,3GalNAc alpha
RT 2,3-sialyltransferase.";
RL J. Biol. Chem. 269:10028-10033(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Cerebellum, and Eye;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, AND BIOPHYSICOCHEMICAL
RP 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 [6]
RP FUNCTION, PATHWAY, AND DISRUPTION PHENOTYPE.
RX PubMed=22735313; DOI=10.1093/glycob/cws103;
RA Sturgill E.R., Aoki K., Lopez P.H., Colacurcio D., Vajn K., Lorenzini I.,
RA Majic S., Yang W.H., Heffer M., Tiemeyer M., Marth J.D., Schnaar R.L.;
RT "Biosynthesis of the major brain gangliosides GD1a and GT1b.";
RL Glycobiology 22:1289-1301(2012).
RN [7]
RP FUNCTION, TISSUE SPECIFICITY, INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=32030804; DOI=10.15252/embj.2019102214;
RA Lim H., Lee J., You B., Oh J.H., Mok H.J., Kim Y.S., Yoon B.E., Kim B.G.,
RA Back S.K., Park J.S., Kim K.P., Schnaar R.L., Lee S.J.;
RT "GT1b functions as a novel endogenous agonist of toll-like receptor 2
RT inducing neuropathic pain.";
RL EMBO J. 39:e102214-e102214(2020).
CC -!- FUNCTION: A beta-galactoside alpha2-3 sialyltransferase primarily
CC involved in terminal sialylation of ganglio and globo series
CC glycolipids (PubMed:8144500, PubMed:9184827). Catalyzes the transfer of
CC sialic acid (N-acetyl-neuraminic acid; Neu5Ac) from the nucleotide
CC sugar donor CMP-Neu5Ac onto acceptor Galbeta-(1->3)-GalNAc-terminated
CC glycoconjugates through an alpha2-3 linkage. Sialylates GM1/GM1a,
CC GA1/asialo-GM1 and GD1b gangliosides to form GD1a, GM1b and GT1b,
CC respectively (PubMed:8144500, PubMed:9184827). Together with ST3GAL3,
CC primarily responsible for biosynthesis of brain GD1a and GT1b that
CC function as ligands for myelin-associated glycoprotein MAG on axons,
CC regulating MAG expression and axonal myelin stability and regeneration
CC (PubMed:22735313). Via GT1b regulates TLR2 signaling in spinal cord
CC microglia in response to nerve injury (PubMed:32030804). Responsible
CC for the sialylation of the pluripotent stem cell- and cancer stem cell-
CC associated antigen SSEA3, forming SSEA4 (By similarity). Sialylates
CC with low efficiency asialofetuin, presumably onto O-glycosidically
CC linked Galbeta-(1->3)-GalNAc-O-Ser (PubMed:8144500).
CC {ECO:0000250|UniProtKB:Q16842, ECO:0000269|PubMed:22735313,
CC ECO:0000269|PubMed:32030804, ECO:0000269|PubMed:8144500,
CC ECO:0000269|PubMed:9184827}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a beta-D-galactosyl-(1->3)-N-acetyl-alpha-D-galactosaminyl
CC derivative + CMP-N-acetyl-beta-neuraminate = an N-acetyl-alpha-
CC neuraminyl-(2->3)-beta-D-galactosyl-(1->3)-N-acetyl-alpha-D-
CC galactosaminyl derivative + CMP + H(+); Xref=Rhea:RHEA:21616,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57812, ChEBI:CHEBI:60377,
CC ChEBI:CHEBI:133470, ChEBI:CHEBI:139596; EC=2.4.99.4;
CC Evidence={ECO:0000269|PubMed:8144500, ECO:0000269|PubMed:9184827};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21617;
CC Evidence={ECO:0000305|PubMed:8144500, ECO:0000305|PubMed:9184827};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CMP-N-acetyl-beta-neuraminate + ganglioside GM1 (d18:1(4E)) =
CC CMP + ganglioside GD1a (d18:1(4E)) + H(+); Xref=Rhea:RHEA:18021,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57812, ChEBI:CHEBI:60377,
CC ChEBI:CHEBI:77709, ChEBI:CHEBI:78445; EC=2.4.99.2;
CC Evidence={ECO:0000305|PubMed:8144500};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18022;
CC Evidence={ECO:0000305|PubMed:8144500};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CMP-N-acetyl-beta-neuraminate + ganglioside GM1
CC (d18:1(4E)/18:0) = CMP + ganglioside GD1a (18:1(4E)/18:0) + H(+);
CC Xref=Rhea:RHEA:48248, ChEBI:CHEBI:15378, ChEBI:CHEBI:57812,
CC ChEBI:CHEBI:60377, ChEBI:CHEBI:73110, ChEBI:CHEBI:90153;
CC Evidence={ECO:0000269|PubMed:8144500};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48249;
CC Evidence={ECO:0000305|PubMed:8144500};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CMP-N-acetyl-beta-neuraminate + ganglioside GA1 = CMP +
CC ganglioside GM1b + H(+); Xref=Rhea:RHEA:48244, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57812, ChEBI:CHEBI:60377, ChEBI:CHEBI:88069,
CC ChEBI:CHEBI:90151; Evidence={ECO:0000269|PubMed:8144500,
CC ECO:0000269|PubMed:9184827};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48245;
CC Evidence={ECO:0000305|PubMed:8144500, ECO:0000305|PubMed:9184827};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CMP-N-acetyl-beta-neuraminate + ganglioside GA1 (d18:1(4E)) =
CC CMP + ganglioside GM1b (d18:1(4E)) + H(+); Xref=Rhea:RHEA:47560,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:27938, ChEBI:CHEBI:57812,
CC ChEBI:CHEBI:60377, ChEBI:CHEBI:78568;
CC Evidence={ECO:0000305|PubMed:8144500};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47561;
CC Evidence={ECO:0000305|PubMed:8144500};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CMP-N-acetyl-beta-neuraminate + ganglioside GD1b = CMP +
CC ganglioside GT1b + H(+); Xref=Rhea:RHEA:48240, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57812, ChEBI:CHEBI:60377, ChEBI:CHEBI:82939,
CC ChEBI:CHEBI:82940; Evidence={ECO:0000269|PubMed:8144500};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48241;
CC Evidence={ECO:0000305|PubMed:8144500};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CMP-N-acetyl-beta-neuraminate + ganglioside GD1b (d18:1(4E)) =
CC CMP + ganglioside GT1b (d18:1(4E)) + H(+); Xref=Rhea:RHEA:47572,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57812, ChEBI:CHEBI:60377,
CC ChEBI:CHEBI:78452, ChEBI:CHEBI:87785;
CC Evidence={ECO:0000305|PubMed:8144500};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47573;
CC Evidence={ECO:0000305|PubMed:8144500};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CMP-N-acetyl-beta-neuraminate + globoside GalGb4Cer = CMP +
CC globoside MSGG + H(+); Xref=Rhea:RHEA:65372, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57812, ChEBI:CHEBI:60377, ChEBI:CHEBI:140623,
CC ChEBI:CHEBI:140691; Evidence={ECO:0000250|UniProtKB:Q16842};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65373;
CC Evidence={ECO:0000250|UniProtKB:Q16842};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.3 mM for Gal-beta-1,3-GlcNAc {ECO:0000269|PubMed:9184827};
CC KM=0.16 mM for Gal-beta-1,3-GalNAc {ECO:0000269|PubMed:9184827};
CC KM=0.63 mM for Gal-beta-1,3-GalNAc {ECO:0000269|PubMed:8144500};
CC KM=0.83 mM for GM1 {ECO:0000269|PubMed:8144500};
CC KM=0.67 mM for asialo-GM1 {ECO:0000269|PubMed:8144500};
CC Note=Vmax is 10 fold higher with Gal-beta-1,3-GalNAc than with Gal-
CC beta-1,3-GlcNAc as substrate. {ECO:0000269|PubMed:9184827};
CC pH dependence:
CC Optimum pH is 6.4. {ECO:0000269|PubMed:9184827};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000305|PubMed:8144500}.
CC -!- PATHWAY: Glycolipid biosynthesis. {ECO:0000305|PubMed:22735313,
CC ECO:0000305|PubMed:8144500}.
CC -!- SUBUNIT: Homodimer; disulfide-linked. Homodimer formation occurs in the
CC endoplasmic reticulum. {ECO:0000250|UniProtKB:Q16842}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane
CC {ECO:0000250|UniProtKB:Q16842}; Single-pass type II membrane protein.
CC Secreted. Note=Membrane-bound form distributed along the Golgi
CC cisternae, mainly in proximal compartments (By similarity). Secreted
CC into the body fluid. {ECO:0000250|UniProtKB:Q16842}.
CC -!- TISSUE SPECIFICITY: Strongly expressed in brain and liver and to a
CC lesser extent in heart and kidney. Scarcely detectable in lung,
CC pancreas, spleen and submaxillary gland (PubMed:8144500). Expressed in
CC L5 dorsal root ganglion (DRG) neurons (at protein level)
CC (PubMed:32030804). {ECO:0000269|PubMed:32030804,
CC ECO:0000269|PubMed:8144500}.
CC -!- INDUCTION: Up-regulated in DRG neurons in response to nerve injury.
CC {ECO:0000269|PubMed:32030804}.
CC -!- PTM: The soluble form derives from the membrane form by proteolytic
CC processing.
CC -!- PTM: N-glycosylated; necessary for proper exit from endoplasmic
CC reticulum and trafficking to the Golgi apparatus.
CC {ECO:0000250|UniProtKB:Q16842}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under physiological
CC conditions; due to the redundancy with ST3GAL3. Simultaneous knockdown
CC of ST3GAL2 and ST3GAL3 results in markedly fewer offspring and impaired
CC nervous system function at weaning (PubMed:22735313). Knockout mice
CC show reduced nerve injury-induced neuropathic pain in response to
CC noxious stimuli (hyperalgesia) and to normally innocuous stimuli
CC (allodynia) (PubMed:32030804). {ECO:0000269|PubMed:22735313,
CC ECO:0000269|PubMed:32030804}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 29 family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase; Note=ST3Gal
CC II;
CC URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_mou_643";
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DR EMBL; X76989; CAA54294.1; -; mRNA.
DR EMBL; AK053827; BAC35543.1; -; mRNA.
DR EMBL; AK131653; BAE20742.1; -; mRNA.
DR EMBL; CH466525; EDL11478.1; -; Genomic_DNA.
DR EMBL; BC066064; AAH66064.1; -; mRNA.
DR CCDS; CCDS22667.1; -.
DR PIR; A54420; A54420.
DR RefSeq; NP_033205.2; NM_009179.3.
DR RefSeq; XP_006530849.1; XM_006530786.2.
DR RefSeq; XP_006530850.1; XM_006530787.2.
DR RefSeq; XP_006530851.1; XM_006530788.1.
DR RefSeq; XP_017168113.1; XM_017312624.1.
DR AlphaFoldDB; Q11204; -.
DR SMR; Q11204; -.
DR STRING; 10090.ENSMUSP00000034197; -.
DR SwissLipids; SLP:000001389; -.
DR CAZy; GT29; Glycosyltransferase Family 29.
DR GlyGen; Q11204; 1 site.
DR PhosphoSitePlus; Q11204; -.
DR MaxQB; Q11204; -.
DR PaxDb; Q11204; -.
DR PRIDE; Q11204; -.
DR ProteomicsDB; 257232; -.
DR Antibodypedia; 2529; 144 antibodies from 25 providers.
DR DNASU; 20444; -.
DR Ensembl; ENSMUST00000034197; ENSMUSP00000034197; ENSMUSG00000031749.
DR GeneID; 20444; -.
DR KEGG; mmu:20444; -.
DR UCSC; uc009nlk.2; mouse.
DR CTD; 6483; -.
DR MGI; MGI:99427; St3gal2.
DR VEuPathDB; HostDB:ENSMUSG00000031749; -.
DR eggNOG; KOG2692; Eukaryota.
DR GeneTree; ENSGT00940000156356; -.
DR HOGENOM; CLU_032020_2_0_1; -.
DR InParanoid; Q11204; -.
DR OMA; ISPVWTK; -.
DR OrthoDB; 891104at2759; -.
DR PhylomeDB; Q11204; -.
DR TreeFam; TF354325; -.
DR BRENDA; 2.4.99.2; 3474.
DR Reactome; R-MMU-2022854; Keratan sulfate biosynthesis.
DR Reactome; R-MMU-4085001; Sialic acid metabolism.
DR Reactome; R-MMU-977068; Termination of O-glycan biosynthesis.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 20444; 0 hits in 75 CRISPR screens.
DR ChiTaRS; St3gal2; mouse.
DR PRO; PR:Q11204; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q11204; protein.
DR Bgee; ENSMUSG00000031749; Expressed in cerebellar vermis and 233 other tissues.
DR ExpressionAtlas; Q11204; baseline and differential.
DR Genevisible; Q11204; MM.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0003836; F:beta-galactoside (CMP) alpha-2,3-sialyltransferase activity; IDA:UniProtKB.
DR GO; GO:0047288; F:monosialoganglioside sialyltransferase activity; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0008373; F:sialyltransferase activity; ISO:MGI.
DR GO; GO:0010706; P:ganglioside biosynthetic process via lactosylceramide; IDA:UniProtKB.
DR GO; GO:0010707; P:globoside biosynthetic process via lactosylceramide; ISS:UniProtKB.
DR GO; GO:0009247; P:glycolipid biosynthetic process; ISO:MGI.
DR GO; GO:0009101; P:glycoprotein biosynthetic process; ISO:MGI.
DR GO; GO:0030259; P:lipid glycosylation; ISO:MGI.
DR GO; GO:0009312; P:oligosaccharide biosynthetic process; ISO:MGI.
DR GO; GO:0006486; P:protein glycosylation; IDA:MGI.
DR GO; GO:1990743; P:protein sialylation; ISO:MGI.
DR GO; GO:0097503; P:sialylation; ISO: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 Lipid metabolism; Membrane; Reference proteome; Secreted; Signal-anchor;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..350
FT /note="CMP-N-acetylneuraminate-beta-galactosamide-alpha-
FT 2,3-sialyltransferase 2"
FT /id="PRO_0000149259"
FT TOPO_DOM 1..6
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 7..27
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 28..350
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT BINDING 116
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 157
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 180
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 240
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 276
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 280
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 300
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 309
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 326
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CARBOHYD 211
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 70..75
FT /evidence="ECO:0000250"
FT DISULFID 72..149
FT /evidence="ECO:0000250"
FT DISULFID 152..291
FT /evidence="ECO:0000250"
FT CONFLICT 309..310
FT /note="HY -> RH (in Ref. 1; CAA54294)"
FT /evidence="ECO:0000305"
SQ 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
