GCNT3_MOUSE
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 03-AUG-2022, entry version 119.
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";
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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 GlyGen; Q5JCT0; 1 site.
DR PhosphoSitePlus; Q5JCT0; -.
DR MaxQB; Q5JCT0; -.
DR PaxDb; Q5JCT0; -.
DR PeptideAtlas; Q5JCT0; -.
DR PRIDE; Q5JCT0; -.
DR ProteomicsDB; 268859; -.
DR Antibodypedia; 2476; 401 antibodies from 32 providers.
DR DNASU; 72077; -.
DR Ensembl; ENSMUST00000034751; ENSMUSP00000034751; ENSMUSG00000032226.
DR GeneID; 72077; -.
DR KEGG; mmu:72077; -.
DR UCSC; uc009qnt.1; mouse.
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; IHQRAVC; -.
DR OrthoDB; 868849at2759; -.
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; 3 hits in 75 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 44 other tissues.
DR Genevisible; Q5JCT0; MM.
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: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 Pfam; PF02485; Branch; 1.
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 beta-
FT 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
