ID GCNT1_MOUSE Reviewed; 428 AA. AC Q09324; O35981; Q8BRB2; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 27-JUL-2011, sequence version 2. DT 16-SEP-2015, entry version 136. DE RecName: Full=Beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase; DE EC=2.4.1.102; DE AltName: Full=Core 2-branching enzyme; DE AltName: Full=Core2-GlcNAc-transferase; DE Short=C2GNT; GN Name=Gcnt1; 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 STRAIN=DBA/2; RA Warren C.E., Smookler D.S., Dennis J.W.; RL Submitted (DEC-1994) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY. RC STRAIN=BALB/c; TISSUE=Kidney, and Submandibular gland; RX PubMed=9341170; DOI=10.1074/jbc.272.43.27246; RA Sekine M., Nara K., Suzuki A.; RT "Tissue-specific regulation of mouse core 2 beta-1,6-N- RT acetylglucosaminyltransferase."; RL J. Biol. Chem. 272:27246-27252(1997). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Embryo; 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 [4] RP PROTEIN SEQUENCE OF 62-72; 109-116; 225-232 AND 258-265, AND FUNCTION. RC TISSUE=Kidney; RX PubMed=7983056; RA Sekine M., Hashimoto Y., Suzuki M., Inagaki F., Takio K., Suzuki A.; RT "Purification and characterization of UDP-GlcNAc:IV3 beta Gal-Gb4Cer RT beta-1,6-GlcNAc transferase from mouse kidney."; RL J. Biol. Chem. 269:31143-31148(1994). RN [5] RP DISULFIDE BONDS. RX PubMed=12954635; DOI=10.1074/jbc.M303851200; RA Yen T.Y., Macher B.A., Bryson S., Chang X., Tvaroska I., Tse R., RA Takeshita S., Lew A.M., Datti A.; RT "Highly conserved cysteines of mouse core 2 beta1,6-N- RT acetylglucosaminyltransferase I form a network of disulfide bonds and RT include a thiol that affects enzyme activity."; RL J. Biol. Chem. 278:45864-45881(2003). RN [6] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Kidney, and Pancreas; RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and RT expression."; RL Cell 143:1174-1189(2010). RN [7] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 38-428 ALONE AND IN COMPLEX RP WITH GALBETA1-3GALNAC, DISULFIDE BOND, ACTIVE SITE, AND GLYCOSYLATION RP AT ASN-58 AND ASN-95. RX PubMed=16829524; DOI=10.1074/jbc.M603534200; RA Pak J.E., Arnoux P., Zhou S., Sivarajah P., Satkunarajah M., Xing X., RA Rini J.M.; RT "X-ray crystal structure of leukocyte type core 2 beta1,6-N- RT acetylglucosaminyltransferase. Evidence for a convergence of metal RT ion-independent glycosyltransferase mechanism."; RL J. Biol. Chem. 281:26693-26701(2006). CC -!- FUNCTION: Glycosyltransferase that catalyzes the transfer of an N- CC acetylglucosamine moiety onto mucin-type core 1 O-glycan to form CC the branched mucin-type core 2 O-glycan. Mucin-type core 2 O- CC glycans play an important role in leukocyte extravasation as they CC serve as scaffolds for the display of the selectin ligand sialyl CC Lewis X by leukocytes. {ECO:0000269|PubMed:7983056}. CC -!- CATALYTIC ACTIVITY: UDP-N-acetyl-D-glucosamine + beta-D- CC galactosyl-1,3-N-acetyl-D-galactosaminyl-R = UDP + beta-D- CC galactosyl-1,3-(N-acetyl-beta-D-glucosaminyl-1,6)-N-acetyl-D- CC galactosaminyl-R. CC -!- PATHWAY: Protein modification; protein glycosylation. CC -!- SUBUNIT: Interacts with GOLPH3; may control GCNT1 retention in the CC Golgi. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; CC Single-pass type II membrane protein {ECO:0000250}. Note=Also CC detected in the trans-Golgi network. {ECO:0000250}. CC -!- TISSUE SPECIFICITY: Expressed in kidney, liver, stomach, spleen, CC lung and brain. {ECO:0000269|PubMed:9341170}. CC -!- SIMILARITY: Belongs to the glycosyltransferase 14 family. CC {ECO:0000305}. CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase; Note=core CC 2 beta 6 GlcNAc T1; CC URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_mou_574"; 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; U19265; AAA60948.1; -; mRNA. DR EMBL; D87332; BAA22998.1; -; mRNA. DR EMBL; D87333; BAA22999.1; -; mRNA. DR EMBL; AK045216; BAC32265.1; -; mRNA. DR CCDS; CCDS29687.1; -. DR RefSeq; NP_001129956.3; NM_001136484.3. DR RefSeq; NP_034395.4; NM_010265.5. DR RefSeq; NP_775618.3; NM_173442.5. DR UniGene; Mm.244825; -. DR PDB; 2GAK; X-ray; 2.00 A; A/B=38-428. DR PDB; 2GAM; X-ray; 2.70 A; A/B/C/D=38-428. DR PDB; 3OTK; X-ray; 2.30 A; A/B/C/D=38-428. DR PDBsum; 2GAK; -. DR PDBsum; 2GAM; -. DR PDBsum; 3OTK; -. DR ProteinModelPortal; Q09324; -. DR SMR; Q09324; 56-424. DR STRING; 10090.ENSMUSP00000069023; -. DR CAZy; GT14; Glycosyltransferase Family 14. DR PhosphoSite; Q09324; -. DR MaxQB; Q09324; -. DR PaxDb; Q09324; -. DR PRIDE; Q09324; -. DR Ensembl; ENSMUST00000169897; ENSMUSP00000127835; ENSMUSG00000038843. DR Ensembl; ENSMUST00000174236; ENSMUSP00000133935; ENSMUSG00000038843. DR GeneID; 14537; -. DR KEGG; mmu:14537; -. DR UCSC; uc008gxm.2; mouse. DR CTD; 2650; -. DR MGI; MGI:95676; Gcnt1. DR eggNOG; NOG253565; -. DR GeneTree; ENSGT00760000119183; -. DR HOGENOM; HOG000293251; -. DR HOVERGEN; HBG051711; -. DR InParanoid; Q09324; -. DR KO; K00727; -. DR OMA; THVRSIC; -. DR BRENDA; 2.4.1.102; 3474. DR Reactome; R-MMU-913709; O-linked glycosylation of mucins. DR UniPathway; UPA00378; -. DR ChiTaRS; Gcnt1; mouse. DR EvolutionaryTrace; Q09324; -. DR NextBio; 286198; -. DR PRO; PR:Q09324; -. DR Proteomes; UP000000589; Chromosome 19. DR Bgee; Q09324; -. DR CleanEx; MM_GCNT1; -. DR Genevisible; Q09324; MM. DR GO; GO:0005615; C:extracellular space; IEA:Ensembl. DR GO; GO:0031985; C:Golgi cisterna; ISS:UniProtKB. DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005802; C:trans-Golgi network; ISO:MGI. DR GO; GO:0003829; F:beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0060352; P:cell adhesion molecule production; ISS:UniProtKB. DR GO; GO:0009101; P:glycoprotein biosynthetic process; ISS:UniProtKB. DR GO; GO:0060993; P:kidney morphogenesis; IGI:MGI. DR GO; GO:0050901; P:leukocyte tethering or rolling; ISS:UniProtKB. DR GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway. DR GO; GO:0032868; P:response to insulin; IEA:Ensembl. DR GO; GO:0048729; P:tissue morphogenesis; IGI:MGI. DR InterPro; IPR003406; Glyco_trans_14. DR Pfam; PF02485; Branch; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Direct protein sequencing; KW Disulfide bond; Glycoprotein; Glycosyltransferase; Golgi apparatus; KW Membrane; Reference proteome; Signal-anchor; Transferase; KW Transmembrane; Transmembrane helix. FT CHAIN 1 428 Beta-1,3-galactosyl-O-glycosyl- FT glycoprotein beta-1,6-N- FT acetylglucosaminyltransferase. FT /FTId=PRO_0000191396. FT TOPO_DOM 1 9 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 10 32 Helical; Signal-anchor for type II FT membrane protein. {ECO:0000255}. FT TOPO_DOM 33 428 Lumenal. {ECO:0000255}. FT REGION 5 9 Mediates interaction with GOLPH3 and is FT necessary and sufficent for localization FT to the Golgi. {ECO:0000250}. FT REGION 33 121 Stem region. FT REGION 122 428 Catalytic. FT ACT_SITE 320 320 {ECO:0000269|PubMed:16829524}. FT CARBOHYD 58 58 N-linked (GlcNAc...). FT {ECO:0000269|PubMed:16829524}. FT CARBOHYD 95 95 N-linked (GlcNAc...). FT {ECO:0000269|PubMed:16829524}. FT DISULFID 59 413 FT DISULFID 100 172 FT DISULFID 151 199 FT DISULFID 372 381 FT CONFLICT 88 88 R -> W (in Ref. 1; AAA60948 and 2; FT BAA22998/BAA22999). {ECO:0000305}. FT CONFLICT 191 191 S -> T (in Ref. 1; AAA60948). FT {ECO:0000305}. FT CONFLICT 238 238 G -> A (in Ref. 2; BAA22998/BAA22999). FT {ECO:0000305}. FT CONFLICT 260 260 T -> A (in Ref. 1; AAA60948 and 2; FT BAA22998/BAA22999). {ECO:0000305}. FT CONFLICT 362 362 H -> D (in Ref. 1; AAA60948 and 2; FT BAA22998/BAA22999). {ECO:0000305}. FT CONFLICT 404 404 M -> I (in Ref. 2; BAA22998/BAA22999). FT {ECO:0000305}. FT CONFLICT 420 420 H -> R (in Ref. 1; AAA60948 and 2; FT BAA22998/BAA22999). {ECO:0000305}. FT HELIX 59 63 {ECO:0000244|PDB:2GAK}. FT HELIX 67 78 {ECO:0000244|PDB:2GAK}. FT HELIX 80 83 {ECO:0000244|PDB:2GAK}. FT HELIX 90 96 {ECO:0000244|PDB:2GAK}. FT HELIX 100 107 {ECO:0000244|PDB:2GAK}. FT HELIX 116 119 {ECO:0000244|PDB:2GAK}. FT STRAND 123 129 {ECO:0000244|PDB:2GAK}. FT HELIX 133 143 {ECO:0000244|PDB:2GAK}. FT STRAND 148 154 {ECO:0000244|PDB:2GAK}. FT HELIX 160 171 {ECO:0000244|PDB:2GAK}. FT STRAND 176 178 {ECO:0000244|PDB:2GAK}. FT HELIX 190 206 {ECO:0000244|PDB:2GAK}. FT STRAND 212 217 {ECO:0000244|PDB:2GAK}. FT STRAND 221 224 {ECO:0000244|PDB:2GAK}. FT HELIX 226 235 {ECO:0000244|PDB:2GAK}. FT TURN 236 238 {ECO:0000244|PDB:2GAK}. FT STRAND 244 246 {ECO:0000244|PDB:2GAK}. FT HELIX 249 251 {ECO:0000244|PDB:2GAK}. FT HELIX 253 256 {ECO:0000244|PDB:2GAK}. FT STRAND 257 262 {ECO:0000244|PDB:2GAK}. FT STRAND 265 272 {ECO:0000244|PDB:2GAK}. FT STRAND 290 292 {ECO:0000244|PDB:2GAK}. FT HELIX 293 301 {ECO:0000244|PDB:2GAK}. FT HELIX 303 312 {ECO:0000244|PDB:2GAK}. FT STRAND 315 317 {ECO:0000244|PDB:2GAK}. FT HELIX 318 320 {ECO:0000244|PDB:2GAK}. FT HELIX 322 326 {ECO:0000244|PDB:2GAK}. FT HELIX 340 342 {ECO:0000244|PDB:2GAK}. FT TURN 346 348 {ECO:0000244|PDB:2GAK}. FT STRAND 349 354 {ECO:0000244|PDB:2GAK}. FT TURN 357 359 {ECO:0000244|PDB:2GAK}. FT HELIX 363 365 {ECO:0000244|PDB:2GAK}. FT STRAND 373 377 {ECO:0000244|PDB:2GAK}. FT STRAND 380 382 {ECO:0000244|PDB:2GAK}. FT HELIX 385 387 {ECO:0000244|PDB:2GAK}. FT HELIX 388 391 {ECO:0000244|PDB:2GAK}. FT STRAND 397 400 {ECO:0000244|PDB:2GAK}. FT TURN 404 406 {ECO:0000244|PDB:2GAK}. FT HELIX 408 423 {ECO:0000244|PDB:2GAK}. SQ SEQUENCE 428 AA; 49839 MW; 57E54F07AFFE640B CRC64; MLRNLFRRRL FSCPTKYYFM LLVLSLITFS VLRIHQKPEF FSVRHLELAG DDPYSNVNCT KILQGDPEEI QKVKLEILTV QFKKRPRRTP HDYINMTRDC ASFIRTRKYI VEPLTKEEVG FPIAYSIVVH HKIEMLDRLL RAIYMPQNFY CIHVDRKAEE SFLAAVQGIA SCFDNVFVAS QLESVVYASW SRVKADLNCM KDLYRMNANW KYLINLCGMD FPIKTNLEIV RKLKCSTGEN NLETEKMPPN KEERWKKRYT VVDGKLTNTG IVKAPPPLKT PLFSGSAYFV VTREYVGYVL ENENIQKLME WAQDTYSPDE FLWATIQRIP EVPGSFPSSN KYDLSDMNAI ARFVKWQYFE GHVSNGAPYP PCSGVHVRSV CVFGAGDLSW MLRQHHLFAN KFDMDVDPFA IQCLDEHLRH KALENLEH //