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 31-OCT-2012, entry version 100. DE RecName: Full=Beta-galactoside alpha-2,6-sialyltransferase 1; DE Short=Alpha 2,6-ST 1; DE EC=2.4.99.1; 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; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Brain, and Liver; RX MEDLINE=94363344; 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/6, 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 DISULFIDE BONDS. 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 the donor of substrate CMP- CC sialic acid to galactose containing acceptor substrates. CC -!- CATALYTIC ACTIVITY: CMP-N-acetylneuraminate + beta-D-galactosyl- CC 1,4-N-acetyl-beta-D-glucosamine = CMP + alpha-N-acetylneuraminyl- CC 2,6-beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosamine. CC -!- PATHWAY: Protein modification; protein glycosylation. CC -!- SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane; CC Single-pass type II membrane protein. Secreted. Note=Membrane- CC bound form in trans cisternae of Golgi. Secreted into the body CC fluid. CC -!- PTM: The soluble form derives from the membrane form by CC proteolytic processing. CC -!- SIMILARITY: Belongs to the glycosyltransferase 29 family. 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 IPI; IPI00136942; -. 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 UniGene; Mm.149029; -. DR UniGene; Mm.489708; -. DR ProteinModelPortal; Q64685; -. DR SMR; Q64685; 175-389. DR STRING; Q64685; -. DR CAZy; GT29; Glycosyltransferase Family 29. DR PhosphoSite; 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 CTD; 6480; -. DR MGI; MGI:108470; St6gal1. DR eggNOG; NOG249416; -. DR GeneTree; ENSGT00550000074444; -. DR HOGENOM; HOG000013206; -. DR HOVERGEN; HBG052853; -. DR InParanoid; Q8K1L1; -. DR KO; K00778; -. DR OMA; NIRTKAG; -. DR OrthoDB; EOG4M0F1Q; -. DR BRENDA; 2.4.99.1; 3474. DR UniPathway; UPA00378; -. DR NextBio; 298476; -. DR PMAP-CutDB; Q8K1L1; -. DR ArrayExpress; Q64685; -. DR Bgee; Q64685; -. DR CleanEx; MM_ST6GAL1; -. DR Genevestigator; Q64685; -. DR GermOnline; ENSMUSG00000022885; Mus musculus. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell. DR GO; GO:0030173; C:integral to Golgi membrane; IEA:InterPro. DR GO; GO:0003835; F:beta-galactoside alpha-2,6-sialyltransferase activity; IMP:MGI. DR GO; GO:0006486; P:protein glycosylation; IMP:MGI. DR InterPro; IPR001675; Glyco_trans_29. 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 (Potential). FT TRANSMEM 10 26 Helical; Signal-anchor for type II FT membrane protein; (Potential). FT TOPO_DOM 27 403 Lumenal (Potential). FT MOD_RES 366 366 Phosphotyrosine (By similarity). FT CARBOHYD 146 146 N-linked (GlcNAc...) (Potential). FT CARBOHYD 158 158 N-linked (GlcNAc...) (Potential). FT DISULFID 139 403 FT DISULFID 181 332 FT DISULFID 350 361 FT CONFLICT 131 131 K -> R (in Ref. 1; BAA03680). FT CONFLICT 136 136 A -> G (in Ref. 1; BAA03680). FT CONFLICT 155 155 F -> S (in Ref. 1; BAA03680). FT CONFLICT 170 170 N -> T (in Ref. 1; BAA03680). FT CONFLICT 178 179 WH -> CT (in Ref. 1; BAA03680). 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 //