SIAT2_MOUSE
ID SIAT2_MOUSE Reviewed; 524 AA.
AC Q76K27; A9C434; Q6ZPG5; Q8BUU4;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Beta-galactoside alpha-2,6-sialyltransferase 2;
DE Short=Alpha 2,6-ST 2;
DE EC=2.4.99.1 {ECO:0000269|PubMed:12966079};
DE AltName: Full=CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,6-sialyltransferase 2;
DE AltName: Full=ST6Gal II;
DE Short=ST6GalII;
DE AltName: Full=Sialyltransferase 2;
GN Name=St6gal2; Synonyms=Kiaa1877;
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 [GENOMIC DNA], ENZYME ACTIVITY, AND TISSUE SPECIFICITY.
RX PubMed=12966079; DOI=10.1093/jb/mvg142;
RA Takashima S., Tsuji S., Tsujimoto M.;
RT "Comparison of the enzymatic properties of mouse beta-galactoside alpha2,6-
RT sialyltransferases, ST6Gal I and II.";
RL J. Biochem. 134:287-296(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Cerebellum;
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].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC 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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 310-524 (ISOFORM 1).
RC TISSUE=Embryonic tail;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
CC -!- FUNCTION: Transfers sialic acid from the donor of substrate CMP-sialic
CC acid to galactose containing acceptor substrates. Has alpha-2,6-
CC sialyltransferase activity toward oligosaccharides that have the Gal-
CC beta-1,4-GlcNAc sequence at the non-reducing end of their carbohydrate
CC groups, but it has weak or no activities toward glycoproteins and
CC glycolipids.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a beta-D-galactoside + CMP-N-acetyl-beta-neuraminate = an N-
CC acetyl-alpha-neuraminyl-(2->6)-beta-D-galactosyl derivative + CMP +
CC H(+); Xref=Rhea:RHEA:52104, ChEBI:CHEBI:15378, ChEBI:CHEBI:28034,
CC ChEBI:CHEBI:57812, ChEBI:CHEBI:60377, ChEBI:CHEBI:136398;
CC EC=2.4.99.1; Evidence={ECO:0000269|PubMed:12966079};
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane
CC {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q76K27-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q76K27-2; Sequence=VSP_030357, VSP_030358;
CC -!- TISSUE SPECIFICITY: Mainly expressed in brain and embryo. Very low
CC expression is also detected in spleen, oviduct, lung and skeletal
CC muscle. {ECO:0000269|PubMed:12966079}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 29 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC98272.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase; Note=ST6Gal
CC II;
CC URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_mou_649";
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DR EMBL; AB095093; BAC87752.1; -; Genomic_DNA.
DR EMBL; AK082566; BAC38534.1; -; mRNA.
DR EMBL; CT009635; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC125586; AAI25587.1; -; mRNA.
DR EMBL; AK129462; BAC98272.1; ALT_INIT; mRNA.
DR CCDS; CCDS84324.1; -. [Q76K27-1]
DR RefSeq; NP_001334332.1; NM_001347403.1. [Q76K27-1]
DR RefSeq; NP_766417.1; NM_172829.2.
DR RefSeq; XP_006524330.1; XM_006524267.2. [Q76K27-1]
DR RefSeq; XP_006524331.1; XM_006524268.2. [Q76K27-1]
DR RefSeq; XP_006524332.1; XM_006524269.2. [Q76K27-1]
DR AlphaFoldDB; Q76K27; -.
DR SMR; Q76K27; -.
DR STRING; 10090.ENSMUSP00000084091; -.
DR CAZy; GT29; Glycosyltransferase Family 29.
DR GlyGen; Q76K27; 3 sites.
DR PhosphoSitePlus; Q76K27; -.
DR PaxDb; Q76K27; -.
DR PRIDE; Q76K27; -.
DR ProteomicsDB; 257243; -. [Q76K27-1]
DR ProteomicsDB; 257244; -. [Q76K27-2]
DR Antibodypedia; 2496; 84 antibodies from 18 providers.
DR DNASU; 240119; -.
DR Ensembl; ENSMUST00000025000; ENSMUSP00000025000; ENSMUSG00000024172. [Q76K27-1]
DR Ensembl; ENSMUST00000086878; ENSMUSP00000084091; ENSMUSG00000024172. [Q76K27-2]
DR GeneID; 240119; -.
DR KEGG; mmu:240119; -.
DR CTD; 84620; -.
DR MGI; MGI:2445190; St6gal2.
DR VEuPathDB; HostDB:ENSMUSG00000024172; -.
DR eggNOG; KOG2692; Eukaryota.
DR GeneTree; ENSGT00940000158714; -.
DR HOGENOM; CLU_038334_1_0_1; -.
DR InParanoid; Q76K27; -.
DR OMA; WRQRMLC; -.
DR OrthoDB; 494294at2759; -.
DR PhylomeDB; Q76K27; -.
DR TreeFam; TF323961; -.
DR Reactome; R-MMU-4085001; Sialic acid metabolism.
DR BioGRID-ORCS; 240119; 1 hit in 59 CRISPR screens.
DR ChiTaRS; St6gal2; mouse.
DR PRO; PR:Q76K27; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q76K27; protein.
DR Bgee; ENSMUSG00000024172; Expressed in embryonic brain and 41 other tissues.
DR ExpressionAtlas; Q76K27; baseline and differential.
DR Genevisible; Q76K27; MM.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0003835; F:beta-galactoside alpha-2,6-sialyltransferase activity; ISS:UniProtKB.
DR GO; GO:0008373; F:sialyltransferase activity; IDA:MGI.
DR GO; GO:0006054; P:N-acetylneuraminate metabolic process; IC:MGI.
DR GO; GO:0009311; P:oligosaccharide metabolic process; ISS:UniProtKB.
DR GO; GO:0006486; P:protein glycosylation; IEA:InterPro.
DR GO; GO:0097503; P:sialylation; IBA:GO_Central.
DR Gene3D; 3.90.1480.20; -; 1.
DR InterPro; IPR011330; Glyco_hydro/deAcase_b/a-brl.
DR InterPro; IPR001675; Glyco_trans_29.
DR InterPro; IPR038578; GT29-like_sf.
DR Pfam; PF00777; Glyco_transf_29; 1.
DR SUPFAM; SSF88713; SSF88713; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Disulfide bond; Glycoprotein; Glycosyltransferase;
KW Golgi apparatus; Membrane; Reference proteome; Signal-anchor; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..524
FT /note="Beta-galactoside alpha-2,6-sialyltransferase 2"
FT /id="PRO_0000314786"
FT TOPO_DOM 1..11
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 12..32
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 33..524
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 152..174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 302
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 332
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 520
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 248..514
FT /evidence="ECO:0000250"
FT DISULFID 291..443
FT /evidence="ECO:0000250"
FT DISULFID 461..472
FT /evidence="ECO:0000250"
FT VAR_SEQ 436..438
FT /note="ILI -> TCV (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_030357"
FT VAR_SEQ 439..524
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_030358"
FT CONFLICT 48
FT /note="R -> S (in Ref. 1; BAC87752)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 524 AA; 60192 MW; 9EB27CB3B901124F CRC64;
MKPHLKQWRQ RMLFGIFVWG LLFLAIFIYF TNSNPAAPMP SSFSFLERRG LLPLQGKQRV
IMGALQEPSL PRSLDASKVL LDSHPENPFH PWPGDPQKWD QAPNGFDNGD EFFTSQVGRK
SQSAFYPEED SYFFVADQPE LYHHRQGALE LPSPGETSWR SGPVQPKQKL LHPRRGSLPE
EAYDSDMLSA SMSRAFLYRL WKGAVSSKML NPRLQKAMRY YMSFNKHGVR FRRRGRREAT
RTGPELLCEM RRRVRVRTLD GREAPFSGLG WRPLVPGVPL SQLHPRGLSS CAVVMSAGAI
LNSSLGEEID SHDAVLRFNS APTRGYEKDV GNKTTVRIIN SQILANPSHH FIDSALYKDV
ILVAWDPAPY SANLNLWYKK PDYNLFTPYI QHRRKYPTQP FYILHPKFIW QLWDIIQENT
REKIQPNPPS SGFIGILIMM SMCKEVHVYE YIPSVRQTEL CHYHELYYDA ACTLGAYHPL
LYEKLLVQRL NTGTQADLHH KGKVVLPGFQ TLRCPVTSPN NTHS
