SIAT1_MOUSE
ID SIAT1_MOUSE Reviewed; 403 AA.
AC Q64685; Q8K1L1;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Beta-galactoside alpha-2,6-sialyltransferase 1;
DE Short=Alpha 2,6-ST 1;
DE EC=2.4.99.1 {ECO:0000269|PubMed:22039275};
DE AltName: Full=CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,6-sialyltransferase 1;
DE AltName: Full=ST6Gal I;
DE Short=ST6GalI;
DE AltName: Full=Sialyltransferase 1;
GN Name=St6gal1; Synonyms=Siat1;
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 TISSUE=Brain, and Liver;
RX PubMed=8081843; DOI=10.1016/s0968-0896(00)82111-2;
RA Hamamoto T., Kawasaki M., Kurosawa N., Nakaoka T., Lee Y.-C., Tsuji S.;
RT "Two step single primer mediated polymerase chain reaction. Application to
RT cloning of putative mouse, beta-galactoside alpha 2,6-sialyltransferase
RT cDNA.";
RL Bioorg. Med. Chem. 1:141-145(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Spinal ganglion;
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, and 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).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, DISULFIDE BONDS, IDENTIFICATION BY MASS
RP SPECTROMETRY, AND MUTAGENESIS OF CYS-139; CYS-181 AND CYS-350.
RX PubMed=22039275; DOI=10.1093/jb/mvr133;
RA Hirano Y., Suzuki T., Matsumoto T., Ishihara Y., Takaki Y., Kono M.,
RA Dohmae N., Tsuji S.;
RT "Disulfide linkage in mouse ST6Gal I: Determination of linkage positions
RT and mutant analysis.";
RL J. Biochem. 151:197-203(2012).
CC -!- FUNCTION: Transfers sialic acid from CMP-sialic acid to galactose-
CC containing acceptor substrates. {ECO:0000269|PubMed:22039275}.
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:0000250|UniProtKB:P15907,
CC ECO:0000269|PubMed:22039275};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000269|PubMed:22039275}.
CC -!- SUBUNIT: Monomer and homodimer. {ECO:0000250|UniProtKB:P15907}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane
CC {ECO:0000250|UniProtKB:P15907}; Single-pass type II membrane protein.
CC Secreted. Note=Membrane-bound form in trans cisternae of Golgi.
CC Secreted into the body fluid.
CC -!- PTM: The soluble form derives from the membrane form by proteolytic
CC processing. {ECO:0000250|UniProtKB:P13721}.
CC -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:P13721}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 29 family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase; Note=ST6Gal I;
CC URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_mou_648";
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DR EMBL; D16106; BAA03680.1; -; mRNA.
DR EMBL; AK084124; BAC39120.1; -; mRNA.
DR EMBL; CH466521; EDK97666.1; -; Genomic_DNA.
DR EMBL; CH466521; EDK97667.1; -; Genomic_DNA.
DR EMBL; BC027833; AAH27833.1; -; mRNA.
DR EMBL; BC092222; AAH92222.1; -; mRNA.
DR EMBL; BC096026; AAH96026.1; -; mRNA.
DR CCDS; CCDS28077.1; -.
DR RefSeq; NP_001239434.1; NM_001252505.1.
DR RefSeq; NP_001239435.1; NM_001252506.1.
DR RefSeq; NP_666045.1; NM_145933.4.
DR RefSeq; XP_006521936.1; XM_006521873.3.
DR RefSeq; XP_006521937.1; XM_006521874.1.
DR RefSeq; XP_006521938.1; XM_006521875.3.
DR RefSeq; XP_006521939.1; XM_006521876.3.
DR RefSeq; XP_011244150.1; XM_011245848.1.
DR AlphaFoldDB; Q64685; -.
DR SMR; Q64685; -.
DR STRING; 10090.ENSMUSP00000023601; -.
DR CAZy; GT29; Glycosyltransferase Family 29.
DR GlyGen; Q64685; 2 sites.
DR iPTMnet; Q64685; -.
DR PhosphoSitePlus; Q64685; -.
DR EPD; Q64685; -.
DR MaxQB; Q64685; -.
DR PaxDb; Q64685; -.
DR PeptideAtlas; Q64685; -.
DR PRIDE; Q64685; -.
DR ProteomicsDB; 261039; -.
DR Antibodypedia; 4243; 574 antibodies from 38 providers.
DR DNASU; 20440; -.
DR Ensembl; ENSMUST00000023601; ENSMUSP00000023601; ENSMUSG00000022885.
DR Ensembl; ENSMUST00000115335; ENSMUSP00000110992; ENSMUSG00000022885.
DR Ensembl; ENSMUST00000178797; ENSMUSP00000136206; ENSMUSG00000022885.
DR GeneID; 20440; -.
DR KEGG; mmu:20440; -.
DR UCSC; uc007yto.2; mouse.
DR CTD; 6480; -.
DR MGI; MGI:108470; St6gal1.
DR VEuPathDB; HostDB:ENSMUSG00000022885; -.
DR eggNOG; KOG2692; Eukaryota.
DR GeneTree; ENSGT00940000157053; -.
DR HOGENOM; CLU_038334_0_0_1; -.
DR InParanoid; Q64685; -.
DR OMA; ICVWKER; -.
DR OrthoDB; 494294at2759; -.
DR PhylomeDB; Q64685; -.
DR TreeFam; TF323961; -.
DR BRENDA; 2.4.99.1; 3474.
DR Reactome; R-MMU-4085001; Sialic acid metabolism.
DR Reactome; R-MMU-975577; N-Glycan antennae elongation.
DR Reactome; R-MMU-977068; Termination of O-glycan biosynthesis.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 20440; 1 hit in 71 CRISPR screens.
DR ChiTaRS; St6gal1; mouse.
DR PRO; PR:Q64685; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q64685; protein.
DR Bgee; ENSMUSG00000022885; Expressed in metanephric ureteric bud and 250 other tissues.
DR ExpressionAtlas; Q64685; baseline and differential.
DR Genevisible; Q64685; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005797; C:Golgi medial cisterna; ISO:MGI.
DR GO; GO:0000139; C:Golgi membrane; ISS:UniProtKB.
DR GO; GO:0000138; C:Golgi trans cisterna; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0003835; F:beta-galactoside alpha-2,6-sialyltransferase activity; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0008373; F:sialyltransferase activity; IDA:MGI.
DR GO; GO:0006054; P:N-acetylneuraminate metabolic process; ISS:UniProtKB.
DR GO; GO:0050922; P:negative regulation of chemotaxis; ISO:MGI.
DR GO; GO:2000110; P:negative regulation of macrophage apoptotic process; ISO:MGI.
DR GO; GO:0032946; P:positive regulation of mononuclear cell proliferation; ISO:MGI.
DR GO; GO:0006486; P:protein glycosylation; IMP:MGI.
DR GO; GO:0018279; P:protein N-linked glycosylation via asparagine; IDA:UniProtKB.
DR GO; GO:1990743; P:protein sialylation; ISO:MGI.
DR GO; GO:1900024; P:regulation of substrate adhesion-dependent cell spreading; ISO:MGI.
DR GO; GO:0045471; P:response to ethanol; IEA:Ensembl.
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 Membrane; Phosphoprotein; Reference proteome; Secreted; Signal-anchor;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..403
FT /note="Beta-galactoside alpha-2,6-sialyltransferase 1"
FT /id="PRO_0000149250"
FT TOPO_DOM 1..9
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 10..26
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 27..403
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT BINDING 186
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P15907"
FT BINDING 209
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P15907"
FT BINDING 230
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P15907"
FT BINDING 319..321
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P15907"
FT BINDING 350
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P15907"
FT BINDING 351
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P15907"
FT BINDING 362
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P15907"
FT BINDING 366
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 367
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P15907"
FT BINDING 373
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P15907"
FT MOD_RES 366
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P15907"
FT CARBOHYD 146
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 158
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 139..403
FT /evidence="ECO:0000269|PubMed:22039275"
FT DISULFID 181..332
FT /evidence="ECO:0000269|PubMed:22039275"
FT DISULFID 350..361
FT /evidence="ECO:0000269|PubMed:22039275"
FT MUTAGEN 139
FT /note="C->A,S: No effect on enzyme activity."
FT /evidence="ECO:0000269|PubMed:22039275"
FT MUTAGEN 181
FT /note="C->S: Loss of enzyme activity."
FT /evidence="ECO:0000269|PubMed:22039275"
FT MUTAGEN 350
FT /note="C->A,S: Loss of enzyme activity."
FT /evidence="ECO:0000269|PubMed:22039275"
FT CONFLICT 131
FT /note="K -> R (in Ref. 1; BAA03680)"
FT /evidence="ECO:0000305"
FT CONFLICT 136
FT /note="A -> G (in Ref. 1; BAA03680)"
FT /evidence="ECO:0000305"
FT CONFLICT 155
FT /note="F -> S (in Ref. 1; BAA03680)"
FT /evidence="ECO:0000305"
FT CONFLICT 170
FT /note="N -> T (in Ref. 1; BAA03680)"
FT /evidence="ECO:0000305"
FT CONFLICT 178..179
FT /note="WH -> CT (in Ref. 1; BAA03680)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 403 AA; 46586 MW; ABBD86D8B13D3E04 CRC64;
MIHTNLKRKF SCFVLVFLLF AIICVWKKGS DYEALTLQAK VFQMPKSQEK VAVGPAPQAV
FSNSKQDPKE GVQILSYPRV TAKVKPQPSL QVWDKDSTYS KLNPRLLKIW RNYLNMNKYK
VSYKGPGPGV KFSVEALRCH LRDHVNVSMI EATDFPFNTT EWEGYLPKEN FRTKAGPWHK
CAVVSSAGSL KNSQLGREID NHDAVLRFNG APTDNFQQDV GTKTTIRLVN SQLVTTEKRF
LKDSLYTEGI LILWDPSVYH ADIPQWYQKP DYNFFETYKS YRRLHPSQPF YILKPQMPWE
LWDIIQEISP DLIQPNPPSS GMLGIIIMMT LCDQVDIYEF LPSKRKTDVC YYHQKFFDSA
CTMGAYHPLL FEKNMVKHLN EGTDEDIYLF GKATLSGFRN NRC
