SIA7B_MOUSE
ID SIA7B_MOUSE Reviewed; 373 AA.
AC P70277; Q3UWG0; Q9DC24;
DT 11-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 2.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase 2;
DE EC=2.4.99.3 {ECO:0000269|PubMed:8662927};
DE AltName: Full=Gal-beta-1,3-GalNAc alpha-2,6-sialyltransferase;
DE AltName: Full=GalNAc alpha-2,6-sialyltransferase II;
DE AltName: Full=ST6GalNAc II;
DE Short=ST6GalNAcII;
DE AltName: Full=Sialyltransferase 7B;
DE Short=SIAT7-B;
GN Name=St6galnac2; Synonyms=Siat7, Siat7b;
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 / MRNA], CATALYTIC ACTIVITY, FUNCTION,
RP PATHWAY, AND TISSUE SPECIFICITY.
RC STRAIN=ICR; TISSUE=Submandibular gland;
RX PubMed=8662927; DOI=10.1074/jbc.271.25.15109;
RA Kurosawa N., Inoue M., Yoshida Y., Tsuji S.;
RT "Molecular cloning and genomic analysis of mouse Galbeta1, 3GalNAc-specific
RT GalNAc alpha2,6-sialyltransferase.";
RL J. Biol. Chem. 271:15109-15116(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Lung;
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 MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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: Catalyzes the transfer of N-acetylneuraminyl groups onto
CC glycan chains in glycoproteins (PubMed:8662927). Shows a preference for
CC N-acetylgalactosamine (GalNAc) residues already modified by the
CC addition of galactose or galactose followed by sialic acid in alpha-2,3
CC linkage (PubMed:8662927). {ECO:0000269|PubMed:8662927}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a beta-D-galactosyl-(1->3)-N-acetyl-alpha-D-galactosaminyl
CC derivative + CMP-N-acetyl-beta-neuraminate = a beta-D-galactosyl-
CC (1->3)-[N-acetyl-alpha-neuraminyl-(2->6)]-N-acetyl-alpha-D-
CC galactosaminyl derivative + CMP + H(+); Xref=Rhea:RHEA:11136,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57812, ChEBI:CHEBI:60377,
CC ChEBI:CHEBI:133470, ChEBI:CHEBI:140764; EC=2.4.99.3;
CC Evidence={ECO:0000269|PubMed:8662927};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11137;
CC Evidence={ECO:0000269|PubMed:8662927};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000269|PubMed:8662927}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000305}; Single-
CC pass type II membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Highly expressed in lactating mammary gland and
CC adult testis. Lower levels in kidney. {ECO:0000269|PubMed:8662927}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 29 family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase; Note=ST6GalNAc
CC II;
CC URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_mou_651";
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DR EMBL; X93999; CAA63821.1; -; mRNA.
DR EMBL; X94000; CAA63822.1; -; Genomic_DNA.
DR EMBL; AK004613; BAB23410.1; -; mRNA.
DR EMBL; AK136381; BAE22955.1; -; mRNA.
DR EMBL; BC010208; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS36379.1; -.
DR RefSeq; NP_033206.2; NM_009180.3.
DR AlphaFoldDB; P70277; -.
DR SMR; P70277; -.
DR STRING; 10090.ENSMUSP00000078501; -.
DR CAZy; GT29; Glycosyltransferase Family 29.
DR GlyGen; P70277; 2 sites.
DR PhosphoSitePlus; P70277; -.
DR MaxQB; P70277; -.
DR PaxDb; P70277; -.
DR PRIDE; P70277; -.
DR ProteomicsDB; 261359; -.
DR Antibodypedia; 32441; 106 antibodies from 19 providers.
DR DNASU; 20446; -.
DR Ensembl; ENSMUST00000079545; ENSMUSP00000078501; ENSMUSG00000057286.
DR GeneID; 20446; -.
DR KEGG; mmu:20446; -.
DR UCSC; uc007mma.1; mouse.
DR CTD; 10610; -.
DR MGI; MGI:107553; St6galnac2.
DR VEuPathDB; HostDB:ENSMUSG00000057286; -.
DR eggNOG; KOG2692; Eukaryota.
DR GeneTree; ENSGT00940000160433; -.
DR HOGENOM; CLU_032020_0_1_1; -.
DR InParanoid; P70277; -.
DR OMA; LHYIFIP; -.
DR OrthoDB; 891104at2759; -.
DR PhylomeDB; P70277; -.
DR TreeFam; TF354325; -.
DR Reactome; R-MMU-4085001; Sialic acid metabolism.
DR Reactome; R-MMU-977068; Termination of O-glycan biosynthesis.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 20446; 3 hits in 71 CRISPR screens.
DR ChiTaRS; St6galnac2; mouse.
DR PRO; PR:P70277; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; P70277; protein.
DR Bgee; ENSMUSG00000057286; Expressed in seminiferous tubule of testis and 185 other tissues.
DR Genevisible; P70277; 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:0001665; F:alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase activity; ISS:UniProtKB.
DR GO; GO:0016740; F:transferase activity; IBA:GO_Central.
DR GO; GO:0006486; P:protein glycosylation; ISO:MGI.
DR GO; GO:0006493; P:protein O-linked glycosylation; ISS:UniProtKB.
DR GO; GO:1990743; P:protein sialylation; 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 1: Evidence at protein level;
KW Disulfide bond; Glycoprotein; Glycosyltransferase; Golgi apparatus;
KW Membrane; Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..373
FT /note="Alpha-N-acetylgalactosaminide alpha-2,6-
FT sialyltransferase 2"
FT /id="PRO_0000149273"
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..373
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT BINDING 155
FT /ligand="CMP-N-acetyl-beta-neuraminate"
FT /ligand_id="ChEBI:CHEBI:57812"
FT /evidence="ECO:0000250|UniProtKB:Q9UJ37"
FT BINDING 178
FT /ligand="CMP-N-acetyl-beta-neuraminate"
FT /ligand_id="ChEBI:CHEBI:57812"
FT /evidence="ECO:0000250|UniProtKB:Q9UJ37"
FT BINDING 303
FT /ligand="CMP-N-acetyl-beta-neuraminate"
FT /ligand_id="ChEBI:CHEBI:57812"
FT /evidence="ECO:0000250|UniProtKB:Q9UJ37"
FT BINDING 335
FT /ligand="CMP-N-acetyl-beta-neuraminate"
FT /ligand_id="ChEBI:CHEBI:57812"
FT /evidence="ECO:0000250|UniProtKB:Q9UJ37"
FT CARBOHYD 103
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 160
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 65..147
FT /evidence="ECO:0000250|UniProtKB:Q9UJ37"
FT DISULFID 150..316
FT /evidence="ECO:0000250|UniProtKB:Q9UJ37"
FT CONFLICT 184
FT /note="G -> A (in Ref. 1; CAA63821)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 373 AA; 42482 MW; 4C1E6AE9AE618450 CRC64;
MDLPRRWLFR MLLLVATSSG ILLMLYSSAG QQSPETQVPA RNMAYPRAFF DPKPPNSENR
KSRLCQHSLS LAIQKDRRFR SLFDLSTPVL LWEGLFTQEL WNNLSQHKVP YGWQGLSHEV
IASTLRLLKS PESGELFGAP RKLPLSCIRC AVVGNGGILN GSRQGQKIDA HDYVFRLNGA
ITEGFERDVG TKTSFYGFTV NTMKNSLISY AKLGFTSVPQ GQNLRYIFIP SSIRDYLMLR
SAILGVPVPE GPDKGDRPHT YFGPETSASK FKLLHPDFIS YLTERFLKSK LINTRFGDMY
MPSTGALMLL TALHTCDQVS AYGFITNNYQ KYSDHYFERE KKPLIFYANH DLSLEASLWR
DLHNAGILWL YQR
