SIA7A_MOUSE
ID SIA7A_MOUSE Reviewed; 526 AA.
AC Q9QZ39; A2AA23; Q9JJP5;
DT 11-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase 1;
DE EC=2.4.99.3 {ECO:0000269|PubMed:10788794};
DE AltName: Full=GalNAc alpha-2,6-sialyltransferase I {ECO:0000303|PubMed:10788794};
DE AltName: Full=ST6GalNAc I {ECO:0000303|PubMed:10788794};
DE Short=ST6GalNAcI {ECO:0000303|PubMed:10788794};
DE AltName: Full=Sialyltransferase 7A;
DE Short=SIAT7-A;
GN Name=St6galnac1 {ECO:0000312|MGI:MGI:1341826}; Synonyms=Siat7a;
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], FUNCTION, CATALYTIC ACTIVITY, AND
RP TISSUE SPECIFICITY.
RC TISSUE=Submandibular gland;
RX PubMed=10788794; DOI=10.1093/oxfordjournals.jbchem.a022678;
RA Kurosawa N., Takashima S., Kono M., Ikehara Y., Inoue M., Tachida Y.,
RA Narimatsu H., Tsuji S.;
RT "Molecular cloning and genomic analysis of mouse GalNAc alpha-2,6-
RT sialyltransferase (ST6GalNAc I).";
RL J. Biochem. 127:845-854(2000).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [4]
RP FUNCTION, AND MUTAGENESIS OF ARG-319.
RX PubMed=35303419; DOI=10.1016/j.cell.2022.02.013;
RA Yao Y., Kim G., Shafer S., Chen Z., Kubo S., Ji Y., Luo J., Yang W.,
RA Perner S.P., Kanellopoulou C., Park A.Y., Jiang P., Li J., Baris S.,
RA Aydiner E.K., Ertem D., Mulder D.J., Warner N., Griffiths A.M.,
RA Topf-Olivestone C., Kori M., Werner L., Ouahed J., Field M., Liu C.,
RA Schwarz B., Bosio C.M., Ganesan S., Song J., Urlaub H., Oellerich T.,
RA Malaker S.A., Zheng L., Bertozzi C.R., Zhang Y., Matthews H.,
RA Montgomery W., Shih H.Y., Jiang J., Jones M., Baras A., Shuldiner A.,
RA Gonzaga-Jauregui C., Snapper S.B., Muise A.M., Shouval D.S., Ozen A.,
RA Pan K.T., Wu C., Lenardo M.J.;
RT "Mucus sialylation determines intestinal host-commensal homeostasis.";
RL Cell 0:0-0(2022).
CC -!- FUNCTION: Protein sialyltransferase specifically expressed in goblet
CC cells that plays a key role in intestinal host-commensal homeostasis
CC (PubMed:35303419). Conjugates sialic acid with an alpha-2-6 linkage to
CC N-acetylgalactosamine (GalNAc) glycan chains linked to serine or
CC threonine in glycoproteins (PubMed:10788794). Catalyzes the formation
CC of the sialyl-Tn (S-Tn) antigen, an antigen found in intestinal goblet
CC cells (PubMed:35303419). Protein sialylation in globlet cells is
CC essential for mucus integrity and is required to protect the intestinal
CC mucus against excessive bacterial proteolytic degradation
CC (PubMed:35303419). {ECO:0000269|PubMed:10788794,
CC ECO:0000269|PubMed:35303419}.
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:10788794};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11137;
CC Evidence={ECO:0000269|PubMed:10788794};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000305|PubMed:10788794}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:Q9NSC7}; Single-pass type II membrane protein
CC {ECO:0000250|UniProtKB:Q9NSC7}.
CC -!- TISSUE SPECIFICITY: Submaxillary gland, mammary gland, spleen and
CC colon. {ECO:0000269|PubMed:10788794}.
CC -!- PTM: Glycosylated; autosialylated. {ECO:0000250|UniProtKB:Q9NSC7}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 29 family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase; Note=ST6GalNAc
CC I;
CC URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_mou_650";
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DR EMBL; Y11274; CAA72137.1; -; mRNA.
DR EMBL; Y10294; CAA71341.1; -; Genomic_DNA.
DR EMBL; AL645542; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC141095; AAI41096.1; -; mRNA.
DR EMBL; BC145373; AAI45374.1; -; mRNA.
DR CCDS; CCDS36380.1; -.
DR PIR; JC7248; JC7248.
DR RefSeq; NP_035501.2; NM_011371.2.
DR AlphaFoldDB; Q9QZ39; -.
DR SMR; Q9QZ39; -.
DR STRING; 10090.ENSMUSP00000009732; -.
DR CAZy; GT29; Glycosyltransferase Family 29.
DR GlyGen; Q9QZ39; 5 sites.
DR iPTMnet; Q9QZ39; -.
DR PhosphoSitePlus; Q9QZ39; -.
DR MaxQB; Q9QZ39; -.
DR PaxDb; Q9QZ39; -.
DR PRIDE; Q9QZ39; -.
DR ProteomicsDB; 261358; -.
DR Antibodypedia; 2230; 141 antibodies from 23 providers.
DR DNASU; 20445; -.
DR Ensembl; ENSMUST00000009732; ENSMUSP00000009732; ENSMUSG00000009588.
DR GeneID; 20445; -.
DR KEGG; mmu:20445; -.
DR UCSC; uc007mme.1; mouse.
DR CTD; 55808; -.
DR MGI; MGI:1341826; St6galnac1.
DR VEuPathDB; HostDB:ENSMUSG00000009588; -.
DR eggNOG; KOG2692; Eukaryota.
DR GeneTree; ENSGT00940000159930; -.
DR HOGENOM; CLU_032020_4_1_1; -.
DR InParanoid; Q9QZ39; -.
DR OMA; WDFEEQY; -.
DR OrthoDB; 891104at2759; -.
DR PhylomeDB; Q9QZ39; -.
DR TreeFam; TF354325; -.
DR Reactome; R-MMU-4085001; Sialic acid metabolism.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 20445; 7 hits in 72 CRISPR screens.
DR ChiTaRS; St6galnac1; mouse.
DR PRO; PR:Q9QZ39; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q9QZ39; protein.
DR Bgee; ENSMUSG00000009588; Expressed in conjunctival fornix and 28 other tissues.
DR Genevisible; Q9QZ39; MM.
DR GO; GO:0000139; C:Golgi membrane; ISS:UniProtKB.
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; IDA:MGI.
DR GO; GO:0016740; F:transferase activity; IBA:GO_Central.
DR GO; GO:0001574; P:ganglioside biosynthetic process; TAS:MGI.
DR GO; GO:0048874; P:host-mediated regulation of intestinal microbiota composition; IMP:UniProtKB.
DR GO; GO:0051851; P:modulation by host of symbiont process; IMP:UniProtKB.
DR GO; GO:0009312; P:oligosaccharide biosynthetic process; IDA:MGI.
DR GO; GO:0006486; P:protein glycosylation; ISS:UniProtKB.
DR Gene3D; 3.90.1480.20; -; 1.
DR InterPro; IPR001675; Glyco_trans_29.
DR InterPro; IPR038578; GT29-like_sf.
DR Pfam; PF00777; Glyco_transf_29; 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..526
FT /note="Alpha-N-acetylgalactosaminide alpha-2,6-
FT sialyltransferase 1"
FT /id="PRO_0000149270"
FT TOPO_DOM 1..12
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 13..33
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 34..526
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 49..182
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 75..108
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 206
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 228
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 259
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 303
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 388
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 207..290
FT /evidence="ECO:0000250|UniProtKB:Q9UJ37"
FT DISULFID 293..461
FT /evidence="ECO:0000250|UniProtKB:Q9UJ37"
FT MUTAGEN 319
FT /note="R->Q: Knockin mice display compromised mucus
FT barriers, dysbiosis with reduced bacterial diversity, as
FT well as susceptibility to intestinal inflammation."
FT /evidence="ECO:0000269|PubMed:35303419"
FT CONFLICT 40
FT /note="C -> R (in Ref. 1; CAA72137)"
FT /evidence="ECO:0000305"
FT CONFLICT 44..45
FT /note="WK -> LN (in Ref. 1; CAA72137)"
FT /evidence="ECO:0000305"
FT CONFLICT 48
FT /note="A -> S (in Ref. 1; CAA72137)"
FT /evidence="ECO:0000305"
FT CONFLICT 53..54
FT /note="NQ -> IL (in Ref. 1; CAA72137)"
FT /evidence="ECO:0000305"
FT CONFLICT 61
FT /note="V -> G (in Ref. 1; CAA72137)"
FT /evidence="ECO:0000305"
FT CONFLICT 75
FT /note="T -> A (in Ref. 1; CAA72137)"
FT /evidence="ECO:0000305"
FT CONFLICT 133
FT /note="L -> V (in Ref. 1; CAA72137)"
FT /evidence="ECO:0000305"
FT CONFLICT 136
FT /note="A -> T (in Ref. 1; CAA72137)"
FT /evidence="ECO:0000305"
FT CONFLICT 378
FT /note="D -> N (in Ref. 1; CAA72137)"
FT /evidence="ECO:0000305"
FT CONFLICT 475
FT /note="Q -> E (in Ref. 1; CAA72137)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 526 AA; 60734 MW; 682A5E35E3C142D6 CRC64;
MTRYCRGLSQ RQAFLLLTVL ALLFILLFVV KDPRAKDSRC QFIWKNDASA QENQQKAEPQ
VPIMTLSPRV HNKETTSVSS KDLKKQEREA VQGEQAEGKE KRKLETIRPA PENPQSKAEP
AAKTPVSEHL DKLPRAPGAL STRKTPMATG AVPAKKKVVQ ATKSPASSPH PTTRRRQRLK
ASEFKSEPRW DFEEEYSLDM SSLQTNCSAS VKIKASKSPW LQNIFLPNIT LFLDSGRFTQ
SEWNRLEHFA PPFGFMELNQ SLVQKVVTRF PPVRQQQLLL ASLPTGYSKC ITCAVVGNGG
ILNDSRVGRE IDSHDYVFRL SGAVIKGYEQ DVGTRTSFYG FTAFSLTQSI LILGRRGFQH
VPLGKDVRYL HFLEGTRDYE WLEAMFLNQT LAKTHLSWFR HRPQEAFRNA LDLDRYLLLH
PDFLRYMKNR FLRSKTLDTA HWRIYRPTTG ALLLLTALHL CDKVSAYGFI TEGHQRFSDH
YYDTSWKRLI FYINHDFRLE RMVWKRLHDE GIIWLYQRPQ SDKAKN
