ID GCNT3_MOUSE Reviewed; 437 AA. AC Q5JCT0; A2TIK7; Q8VCX9; Q9D8A3; DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot. DT 29-MAY-2007, sequence version 2. DT 24-JAN-2024, entry version 127. DE RecName: Full=Beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase 3; DE EC=2.4.1.102 {ECO:0000250|UniProtKB:O95395}; DE EC=2.4.1.148 {ECO:0000250|UniProtKB:O95395}; DE EC=2.4.1.150 {ECO:0000250|UniProtKB:O95395}; DE AltName: Full=C2GnT-mucin type; DE Short=C2GnT-M; DE AltName: Full=Mucus-type core 2 beta-1,6-N-acetylglucosaminyltransferase; GN Name=Gcnt3; 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]. RA Yeh J.-C., Ong E., Fukuda M.; RT "Core 2 beta-1,6-N-acetylglucosaminyltransferase II (Core2-GlcNAcT-II)."; RL Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=C57BL/6J; TISSUE=Colon; RA Hashimoto M., Tan S., Mori N., Cheng H., Cheng P.-W.; RT "Mucin biosynthesis: molecular cloning and expression of mouse mucus-type RT core 2 beta-1,6 N-acetylglucosaminyltransferase."; RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Small intestine; 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Colon; 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). CC -!- FUNCTION: Glycosyltransferase that can synthesize all known mucin beta CC 6 N-acetylglucosaminides. Mediates core 2 and core 4 O-glycan CC branching, 2 important steps in mucin-type biosynthesis. Has also I- CC branching enzyme activity by converting linear into branched poly-N- CC acetyllactosaminoglycans, leading to introduce the blood group I CC antigen during embryonic development. {ECO:0000250|UniProtKB:O95395}. CC -!- CATALYTIC ACTIVITY: CC Reaction=O(3)-[beta-D-galactosyl-(1->3)-N-acetyl-alpha-D- CC galactosaminyl]-L-seryl-[protein] + UDP-N-acetyl-alpha-D-glucosamine CC = 3-O-{beta-D-galactosyl-(1->3)-[N-acetyl-beta-D-glucosaminyl- CC (1->6)]-N-acetyl-alpha-D-galactosaminyl}-L-seryl-[protein] + H(+) + CC UDP; Xref=Rhea:RHEA:56212, Rhea:RHEA-COMP:13922, Rhea:RHEA- CC COMP:14419, ChEBI:CHEBI:15378, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223, CC ChEBI:CHEBI:137949, ChEBI:CHEBI:139605; EC=2.4.1.102; CC Evidence={ECO:0000250|UniProtKB:O95395}; CC -!- CATALYTIC ACTIVITY: CC Reaction=O(3)-[beta-D-galactosyl-(1->3)-N-acetyl-alpha-D- CC galactosaminyl]-L-threonyl-[protein] + UDP-N-acetyl-alpha-D- CC glucosamine = 3-O-{beta-D-galactosyl-(1->3)-[N-acetyl-beta-D- CC glucosaminyl-(1->6)]-N-acetyl-alpha-D-galactosaminyl}-L-threonyl- CC [protein] + H(+) + UDP; Xref=Rhea:RHEA:56216, Rhea:RHEA-COMP:13923, CC Rhea:RHEA-COMP:14420, ChEBI:CHEBI:15378, ChEBI:CHEBI:57705, CC ChEBI:CHEBI:58223, ChEBI:CHEBI:137950, ChEBI:CHEBI:139607; CC EC=2.4.1.102; Evidence={ECO:0000250|UniProtKB:O95395}; CC -!- CATALYTIC ACTIVITY: CC Reaction=a beta-D-Gal-(1->4)-beta-D-GlcNAc-(1->3)-beta-D-Gal-(1->4)- CC beta-D-GlcNAc derivative + UDP-N-acetyl-alpha-D-glucosamine = a beta- CC D-Gal-(1->4)-beta-D-GlcNAc-(1->3)-[beta-D-GlcNAc-(1->6)]-beta-D-Gal- CC (1->4)-N-acetyl-beta-D-glucosaminyl derivative + H(+) + UDP; CC Xref=Rhea:RHEA:54820, ChEBI:CHEBI:15378, ChEBI:CHEBI:57705, CC ChEBI:CHEBI:58223, ChEBI:CHEBI:138371, ChEBI:CHEBI:138372; CC EC=2.4.1.150; Evidence={ECO:0000250|UniProtKB:O95395}; CC -!- CATALYTIC ACTIVITY: CC Reaction=3-O-[N-acetyl-beta-D-glucosaminyl-(1->3)-N-acetyl-alpha-D- CC galactosaminyl]-L-seryl-[protein] + UDP-N-acetyl-alpha-D-glucosamine CC = 3-O-[N-acetyl-beta-D-glucosaminyl-(1->3)-[N-acetyl-beta-D- CC glucosaminyl-(1->6)]-N-acetyl-alpha-D-galactosaminyl]-L-seryl- CC [protein] + H(+) + UDP; Xref=Rhea:RHEA:56188, Rhea:RHEA-COMP:11691, CC Rhea:RHEA-COMP:14412, ChEBI:CHEBI:15378, ChEBI:CHEBI:57705, CC ChEBI:CHEBI:58223, ChEBI:CHEBI:87079, ChEBI:CHEBI:139581; CC EC=2.4.1.148; Evidence={ECO:0000250|UniProtKB:O95395}; CC -!- CATALYTIC ACTIVITY: CC Reaction=3-O-[N-acetyl-beta-D-glucosaminyl-(1->3)-N-acetyl-alpha-D- CC galactosaminyl]-L-threonyl-[protein] + UDP-N-acetyl-alpha-D- CC glucosamine = 3-O-[N-acetyl-beta-D-glucosaminyl-(1->3)-[N-acetyl- CC beta-D-glucosaminyl-(1->6)]-N-acetyl-alpha-D-galactosaminyl]-L- CC threonyl-[protein] + H(+) + UDP; Xref=Rhea:RHEA:56192, Rhea:RHEA- CC COMP:11692, Rhea:RHEA-COMP:14413, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:57705, ChEBI:CHEBI:58223, ChEBI:CHEBI:87080, CC ChEBI:CHEBI:139580; EC=2.4.1.148; CC Evidence={ECO:0000250|UniProtKB:O95395}; CC -!- PATHWAY: Protein modification; protein glycosylation. CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single- CC pass type II membrane protein {ECO:0000250}. CC -!- PTM: N-glycosylated. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the glycosyltransferase 14 family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAH18297.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC Sequence=BAB25548.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305}; CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase; Note=core 2 CC beta 6 GlcNAc T3; CC URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_mou_575"; 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; AY039027; AAK72480.1; -; mRNA. DR EMBL; EF202835; ABM91120.1; -; mRNA. DR EMBL; AK008234; BAB25548.1; ALT_SEQ; mRNA. DR EMBL; BC018297; AAH18297.1; ALT_INIT; mRNA. DR CCDS; CCDS40678.1; -. DR RefSeq; NP_082363.2; NM_028087.2. DR RefSeq; XP_006511526.1; XM_006511463.3. DR RefSeq; XP_006511528.1; XM_006511465.3. DR RefSeq; XP_011241117.1; XM_011242815.2. DR RefSeq; XP_011241118.1; XM_011242816.2. DR RefSeq; XP_011241119.1; XM_011242817.2. DR AlphaFoldDB; Q5JCT0; -. DR SMR; Q5JCT0; -. DR STRING; 10090.ENSMUSP00000034751; -. DR CAZy; GT14; Glycosyltransferase Family 14. DR GlyCosmos; Q5JCT0; 1 site, No reported glycans. DR GlyGen; Q5JCT0; 1 site. DR PhosphoSitePlus; Q5JCT0; -. DR MaxQB; Q5JCT0; -. DR PaxDb; 10090-ENSMUSP00000034751; -. DR PeptideAtlas; Q5JCT0; -. DR ProteomicsDB; 268859; -. DR Antibodypedia; 2476; 420 antibodies from 32 providers. DR DNASU; 72077; -. DR Ensembl; ENSMUST00000034751.6; ENSMUSP00000034751.6; ENSMUSG00000032226.6. DR GeneID; 72077; -. DR KEGG; mmu:72077; -. DR UCSC; uc009qnt.1; mouse. DR AGR; MGI:1919327; -. DR CTD; 9245; -. DR MGI; MGI:1919327; Gcnt3. DR VEuPathDB; HostDB:ENSMUSG00000032226; -. DR eggNOG; KOG0799; Eukaryota. DR GeneTree; ENSGT00940000159331; -. DR HOGENOM; CLU_032341_1_2_1; -. DR InParanoid; Q5JCT0; -. DR OMA; CRDILYK; -. DR OrthoDB; 5403607at2759; -. DR PhylomeDB; Q5JCT0; -. DR TreeFam; TF315534; -. DR BRENDA; 2.4.1.102; 3474. DR BRENDA; 2.4.1.150; 3474. DR Reactome; R-MMU-913709; O-linked glycosylation of mucins. DR UniPathway; UPA00378; -. DR BioGRID-ORCS; 72077; 4 hits in 80 CRISPR screens. DR ChiTaRS; Gcnt3; mouse. DR PRO; PR:Q5JCT0; -. DR Proteomes; UP000000589; Chromosome 9. DR RNAct; Q5JCT0; Protein. DR Bgee; ENSMUSG00000032226; Expressed in epithelium of stomach and 45 other cell types or tissues. DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell. DR GO; GO:0047225; F:acetylgalactosaminyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase activity; IMP:MGI. DR GO; GO:0106325; F:acetylgalactosaminyl-O-glycosyl-seryl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0106326; F:acetylgalactosaminyl-O-glycosyl-threonyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0008375; F:acetylglucosaminyltransferase activity; 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:0008109; F:N-acetyllactosaminide beta-1,6-N-acetylglucosaminyltransferase activity; ISO:MGI. DR GO; GO:0050892; P:intestinal absorption; IMP:MGI. DR GO; GO:0060993; P:kidney morphogenesis; IGI:MGI. DR GO; GO:0006493; P:protein O-linked glycosylation; ISO:MGI. DR GO; GO:0048729; P:tissue morphogenesis; IGI:MGI. DR InterPro; IPR003406; Glyco_trans_14. DR PANTHER; PTHR19297:SF81; BETA-1,3-GALACTOSYL-O-GLYCOSYL-GLYCOPROTEIN BETA-1,6-N-ACETYLGLUCOSAMINYLTRANSFERASE 3; 1. DR PANTHER; PTHR19297; GLYCOSYLTRANSFERASE 14 FAMILY MEMBER; 1. DR Pfam; PF02485; Branch; 1. DR Genevisible; Q5JCT0; MM. PE 2: Evidence at transcript level; KW Disulfide bond; Glycoprotein; Glycosyltransferase; Golgi apparatus; KW Membrane; Reference proteome; Signal-anchor; Transferase; Transmembrane; KW Transmembrane helix. FT CHAIN 1..437 FT /note="Beta-1,3-galactosyl-O-glycosyl-glycoprotein FT beta-1,6-N-acetylglucosaminyltransferase 3" FT /id="PRO_0000288546" FT TOPO_DOM 1..12 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 13..30 FT /note="Helical; Signal-anchor for type II membrane protein" FT /evidence="ECO:0000255" FT TOPO_DOM 31..437 FT /note="Lumenal" FT /evidence="ECO:0000255" FT CARBOHYD 288 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 70..227 FT /evidence="ECO:0000250" FT DISULFID 161..381 FT /evidence="ECO:0000250" FT DISULFID 182..209 FT /evidence="ECO:0000250" FT DISULFID 390..422 FT /evidence="ECO:0000250" FT CONFLICT 101 FT /note="A -> G (in Ref. 1; AAK72480)" FT /evidence="ECO:0000305" FT CONFLICT 353 FT /note="L -> M (in Ref. 3; BAB25548)" FT /evidence="ECO:0000305" SQ SEQUENCE 437 AA; 50698 MW; FF0C1EC8F25320F1 CRC64; MTSWQRLCWH YRLWTLGCYM LLAILALKLS LRLKCDFDAM DLDSEEFQSQ YCRDLLYKTL KLPAKSSINC SGVIRGEQKA VTQALLNNLE IKKKQQLFTE ADYLRMTADC EHFKTKRKFI QVPLSKEEAS FPIAYSMVVH EKIENFERLL RAVYTPQNVY CVHMDQKSSE PFKQAVRAIV SCFPNVFIAS KLVSVVYASW SRVQADLNCM EDLLQSPVPW KYLLNTCGTD FPIKTNAEMV KALKLLKGQN SMESEVPPPH KKSRWKYHYE VTDTLHMTSK RKTPPPNNLT MFTGNAYMVA SRDFIEHVFS NSKARQLIEW VKDTYSPDEH LWATLQRASW MPGSDPLHRK FDLSDMRAIA RLTKWYDHEG DIENGAPYTS CSGIHQRAVC VYGSGDLHWI LQNHHLLANK FDPKVDDNVL QCLEEYLRHK AIYGTEL //