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 05-DEC-2018, entry version 146. 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; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; OC Muroidea; Muridae; 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., RA Tsuji S.; RT "Two step single primer mediated polymerase chain reaction. RT Application to cloning of putative mouse, beta-galactoside alpha 2,6- RT sialyltransferase 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., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA 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., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA 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 RT project: 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 RT positions 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 CC N-acetyl-alpha-neuraminyl-(2->6)-beta-D-galactosyl derivative + CC CMP + H(+); Xref=Rhea:RHEA:52104, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:28034, ChEBI:CHEBI:57812, ChEBI:CHEBI:60377, CC ChEBI:CHEBI:136398; EC=2.4.99.1; CC 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 CC protein. Secreted. Note=Membrane-bound form in trans cisternae of CC Golgi. Secreted into the body fluid. CC -!- PTM: The soluble form derives from the membrane form by CC proteolytic 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; CC Note=ST6Gal I; CC URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_mou_648"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 UniGene; Mm.149029; -. DR UniGene; Mm.489708; -. DR ProteinModelPortal; Q64685; -. DR SMR; Q64685; -. DR STRING; 10090.ENSMUSP00000023601; -. DR CAZy; GT29; Glycosyltransferase Family 29. DR iPTMnet; Q64685; -. DR PhosphoSitePlus; Q64685; -. DR EPD; Q64685; -. DR MaxQB; Q64685; -. DR PaxDb; Q64685; -. DR PeptideAtlas; Q64685; -. DR PRIDE; Q64685; -. 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 eggNOG; KOG2692; Eukaryota. DR eggNOG; ENOG410XT8P; LUCA. DR GeneTree; ENSGT00940000157053; -. DR HOGENOM; HOG000013206; -. DR HOVERGEN; HBG052853; -. DR InParanoid; Q64685; -. DR KO; K00778; -. DR OMA; ICVWKER; -. DR OrthoDB; EOG091G07C7; -. 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 ChiTaRS; St6gal1; mouse. DR PRO; PR:Q64685; -. DR Proteomes; UP000000589; Chromosome 16. DR Bgee; ENSMUSG00000022885; Expressed in 289 organ(s), highest expression level in metanephric ureteric bud. DR CleanEx; MM_ST6GAL1; -. 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: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: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 Complete proteome; Disulfide bond; Glycoprotein; Glycosyltransferase; KW Golgi apparatus; Membrane; Phosphoprotein; Reference proteome; KW Secreted; Signal-anchor; Transferase; Transmembrane; KW Transmembrane helix. FT CHAIN 1 403 Beta-galactoside alpha-2,6- FT sialyltransferase 1. FT /FTId=PRO_0000149250. FT TOPO_DOM 1 9 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 10 26 Helical; Signal-anchor for type II FT membrane protein. {ECO:0000255}. FT TOPO_DOM 27 403 Lumenal. {ECO:0000255}. FT REGION 319 321 Substrate binding. FT {ECO:0000250|UniProtKB:P15907}. FT BINDING 186 186 Substrate; via amide nitrogen. FT {ECO:0000250|UniProtKB:P15907}. FT BINDING 209 209 Substrate. FT {ECO:0000250|UniProtKB:P15907}. FT BINDING 230 230 Substrate. FT {ECO:0000250|UniProtKB:P15907}. FT BINDING 350 350 Substrate; via carbonyl oxygen. FT {ECO:0000250|UniProtKB:P15907}. FT BINDING 351 351 Substrate. FT {ECO:0000250|UniProtKB:P15907}. FT BINDING 362 362 Substrate. FT {ECO:0000250|UniProtKB:P15907}. FT BINDING 366 366 Substrate. {ECO:0000250}. FT BINDING 367 367 Substrate. FT {ECO:0000250|UniProtKB:P15907}. FT BINDING 373 373 Substrate. FT {ECO:0000250|UniProtKB:P15907}. FT MOD_RES 366 366 Phosphotyrosine. FT {ECO:0000250|UniProtKB:P15907}. FT CARBOHYD 146 146 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 158 158 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT DISULFID 139 403 {ECO:0000269|PubMed:22039275}. FT DISULFID 181 332 {ECO:0000269|PubMed:22039275}. FT DISULFID 350 361 {ECO:0000269|PubMed:22039275}. FT MUTAGEN 139 139 C->A,S: No effect on enzyme activity. FT {ECO:0000269|PubMed:22039275}. FT MUTAGEN 181 181 C->S: Loss of enzyme activity. FT {ECO:0000269|PubMed:22039275}. FT MUTAGEN 350 350 C->A,S: Loss of enzyme activity. FT {ECO:0000269|PubMed:22039275}. FT CONFLICT 131 131 K -> R (in Ref. 1; BAA03680). FT {ECO:0000305}. FT CONFLICT 136 136 A -> G (in Ref. 1; BAA03680). FT {ECO:0000305}. FT CONFLICT 155 155 F -> S (in Ref. 1; BAA03680). FT {ECO:0000305}. FT CONFLICT 170 170 N -> T (in Ref. 1; BAA03680). FT {ECO:0000305}. FT CONFLICT 178 179 WH -> CT (in Ref. 1; BAA03680). FT {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 //