SIA10_MOUSE
ID SIA10_MOUSE Reviewed; 329 AA.
AC Q8VIB3; Q3TRN3; Q80UR7; Q9WVG2;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 3.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Type 2 lactosamine alpha-2,3-sialyltransferase;
DE EC=2.4.99.-;
DE AltName: Full=CMP-NeuAc:beta-galactoside alpha-2,3-sialyltransferase VI;
DE AltName: Full=ST3Gal VI;
DE Short=ST3GalVI;
DE AltName: Full=Sialyltransferase 10;
GN Name=St3gal6; Synonyms=Siat10;
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].
RC STRAIN=ddY; TISSUE=Hippocampus;
RA Matsuhashi H., Kato K.;
RT "Differential expression of alpha2,3-sialyltransferases in the thalamus of
RT mouse during epileptogenesis.";
RL Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RA Kapitonov D., Yu R.K.;
RT "Sialyltransferases.";
RL Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Bone, and Colon;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C3H/He; TISSUE=Mesenchymal stem cell;
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: Involved in the synthesis of sialyl-paragloboside, a
CC precursor of sialyl-Lewis X determinant. Has a alpha-2,3-
CC sialyltransferase activity toward Gal-beta1,4-GlcNAc structure on
CC glycoproteins and glycolipids. Has a restricted substrate specificity,
CC it utilizes Gal-beta1,4-GlcNAc on glycoproteins, and
CC neolactotetraosylceramide and neolactohexaosylceramide, but not
CC lactotetraosylceramide, lactosylceramide or asialo-GM1 (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000305}; Single-
CC pass type II membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 29 family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase; Note=ST3Gal
CC VI;
CC URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_mou_647";
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DR EMBL; AB063326; BAB79494.1; -; mRNA.
DR EMBL; AF119390; AAD39130.1; -; mRNA.
DR EMBL; AK033562; BAC28360.1; -; mRNA.
DR EMBL; AK162619; BAE36994.1; -; mRNA.
DR EMBL; BC052338; AAH52338.1; -; mRNA.
DR CCDS; CCDS28230.1; -.
DR RefSeq; NP_061254.1; NM_018784.2.
DR RefSeq; XP_006522450.1; XM_006522387.2.
DR RefSeq; XP_006522451.1; XM_006522388.2.
DR RefSeq; XP_011244273.1; XM_011245971.1.
DR RefSeq; XP_011244274.1; XM_011245972.2.
DR RefSeq; XP_011244275.1; XM_011245973.2.
DR RefSeq; XP_011244276.1; XM_011245974.2.
DR RefSeq; XP_017172572.1; XM_017317083.1.
DR AlphaFoldDB; Q8VIB3; -.
DR SMR; Q8VIB3; -.
DR STRING; 10090.ENSMUSP00000115756; -.
DR CAZy; GT29; Glycosyltransferase Family 29.
DR GlyGen; Q8VIB3; 4 sites.
DR PhosphoSitePlus; Q8VIB3; -.
DR MaxQB; Q8VIB3; -.
DR PaxDb; Q8VIB3; -.
DR PeptideAtlas; Q8VIB3; -.
DR PRIDE; Q8VIB3; -.
DR ProteomicsDB; 261229; -.
DR Antibodypedia; 35151; 60 antibodies from 23 providers.
DR DNASU; 54613; -.
DR Ensembl; ENSMUST00000114357; ENSMUSP00000109997; ENSMUSG00000022747.
DR Ensembl; ENSMUST00000114358; ENSMUSP00000109998; ENSMUSG00000022747.
DR Ensembl; ENSMUST00000137035; ENSMUSP00000115756; ENSMUSG00000022747.
DR GeneID; 54613; -.
DR KEGG; mmu:54613; -.
DR UCSC; uc007znt.2; mouse.
DR CTD; 10402; -.
DR MGI; MGI:1888707; St3gal6.
DR VEuPathDB; HostDB:ENSMUSG00000022747; -.
DR eggNOG; KOG2692; Eukaryota.
DR GeneTree; ENSGT00940000161415; -.
DR HOGENOM; CLU_032020_1_1_1; -.
DR InParanoid; Q8VIB3; -.
DR OMA; LYWISFY; -.
DR OrthoDB; 891104at2759; -.
DR PhylomeDB; Q8VIB3; -.
DR TreeFam; TF354325; -.
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 BioGRID-ORCS; 54613; 4 hits in 75 CRISPR screens.
DR PRO; PR:Q8VIB3; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q8VIB3; protein.
DR Bgee; ENSMUSG00000022747; Expressed in parotid gland and 243 other tissues.
DR ExpressionAtlas; Q8VIB3; baseline and differential.
DR Genevisible; Q8VIB3; MM.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0052798; F:beta-galactoside alpha-2,3-sialyltransferase activity; ISS:UniProtKB.
DR GO; GO:0008373; F:sialyltransferase activity; ISO:MGI.
DR GO; GO:0071354; P:cellular response to interleukin-6; ISS:UniProtKB.
DR GO; GO:0006664; P:glycolipid metabolic process; ISS:UniProtKB.
DR GO; GO:0009311; P:oligosaccharide metabolic process; ISS:UniProtKB.
DR GO; GO:0006486; P:protein glycosylation; IBA:GO_Central.
DR GO; GO:0036211; P:protein modification process; ISS:UniProtKB.
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 2: Evidence at transcript level;
KW Glycoprotein; Glycosyltransferase; Golgi apparatus; Membrane;
KW Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..329
FT /note="Type 2 lactosamine alpha-2,3-sialyltransferase"
FT /id="PRO_0000149306"
FT TOPO_DOM 1..4
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 5..25
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 26..329
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT CARBOHYD 129
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 181
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 295
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 308
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 78
FT /note="T -> I (in Ref. 1; BAB79494)"
FT /evidence="ECO:0000305"
FT CONFLICT 137
FT /note="D -> N (in Ref. 4; AAH52338)"
FT /evidence="ECO:0000305"
FT CONFLICT 234
FT /note="T -> I (in Ref. 1; BAB79494)"
FT /evidence="ECO:0000305"
FT CONFLICT 329
FT /note="T -> TQN (in Ref. 1; BAB79494)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 329 AA; 37854 MW; AD38A825253F6352 CRC64;
MKGYLVAIFL SSIFLYYVLY CILWGTNGYW FPAEEMRTRN NVNNCFKKPA FANLLRFPQL
YPFLCRADFI KVAAMSGTNN FPLPYGIKTF ETYFSSALSK LQSCDLFDEF DRVPCKRCVV
VGNGGVLKNK TLGATIDSYD VIIRMNNGPV LGHEEEVGTR TTFRLFYPES VFSDSSHYDP
NTTAVLVVFK PQDLRWLVEI LLGKKINTQG FWKTPALKLI YKQYQIRILD PYITSEAAFQ
MLRFPRVFPK DQKPKHPTTG IIAITMAFHI CSEVHLAGFK YNFYSPNSPL HYYGNATMSL
MKQNAYHNLT AEQLFLNDII KKKMVINLT
