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   24-JAN-2024, entry version 171.
DE   RecName: Full=Beta-galactoside alpha-2,6-sialyltransferase 1;
DE            Short=Alpha 2,6-ST 1;
DE            EC=2.4.3.1 {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; EC=2.4.3.1;
CC         Evidence={ECO:0000250|UniProtKB:P15907, 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   GlyCosmos; Q64685; 2 sites, No reported glycans.
DR   GlyGen; Q64685; 2 sites.
DR   iPTMnet; Q64685; -.
DR   PhosphoSitePlus; Q64685; -.
DR   EPD; Q64685; -.
DR   MaxQB; Q64685; -.
DR   PaxDb; 10090-ENSMUSP00000023601; -.
DR   PeptideAtlas; Q64685; -.
DR   ProteomicsDB; 261039; -.
DR   Antibodypedia; 4243; 627 antibodies from 38 providers.
DR   DNASU; 20440; -.
DR   Ensembl; ENSMUST00000023601.14; ENSMUSP00000023601.8; ENSMUSG00000022885.17.
DR   Ensembl; ENSMUST00000115335.2; ENSMUSP00000110992.2; ENSMUSG00000022885.17.
DR   Ensembl; ENSMUST00000178797.8; ENSMUSP00000136206.2; ENSMUSG00000022885.17.
DR   GeneID; 20440; -.
DR   KEGG; mmu:20440; -.
DR   UCSC; uc007yto.2; mouse.
DR   AGR; MGI:108470; -.
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; HCHLRDH; -.
DR   OrthoDB; 5348004at2759; -.
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 76 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 253 other cell types or tissues.
DR   ExpressionAtlas; Q64685; baseline and differential.
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: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: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; Glycosyl transferase family 29; 1.
DR   InterPro; IPR001675; Glyco_trans_29.
DR   InterPro; IPR038578; GT29-like_sf.
DR   InterPro; IPR012163; Sialyl_trans.
DR   PANTHER; PTHR46059; BETA-GALACTOSIDE ALPHA-2,6-SIALYLTRANSFERASE; 1.
DR   PANTHER; PTHR46059:SF2; BETA-GALACTOSIDE ALPHA-2,6-SIALYLTRANSFERASE 1; 1.
DR   Pfam; PF00777; Glyco_transf_29; 1.
DR   PIRSF; PIRSF005557; Sialyl_trans; 1.
DR   Genevisible; Q64685; MM.
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
//