ID GCNT3_RAT Reviewed; 437 AA. AC Q8CH87; DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2003, sequence version 1. DT 24-JAN-2024, entry version 125. 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=dI/C2/C4GnT; DE Short=dIGnT; GN Name=Gcnt3; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 118-126; 266-280 AND RP 313-324, AND BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=12626393; DOI=10.1093/glycob/cwg044; RA Korekane H., Taguchi T., Sakamoto Y., Honke K., Dohmae N., Salminen H., RA Toivonen S., Helin J., Takio K., Renkonen O., Taniguchi N.; RT "Purification and cDNA cloning of UDP-GlcNAc:GlcNAcbeta1-3Galbeta1- RT 4Glc(NAc)-R [GlcNAc to Gal]beta1,6N-acetylglucosaminyltransferase from rat RT small intestine: a major carrier of dIGnT activity in rat small RT intestine."; RL Glycobiology 13:387-400(2003). 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. 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 -!- BIOPHYSICOCHEMICAL PROPERTIES: CC pH dependence: CC Optimum pH is 7-8.5. {ECO:0000269|PubMed:12626393}; 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 --------------------------------------------------------------------------- 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; AB098520; BAC53607.1; -; mRNA. DR RefSeq; NP_775434.1; NM_173312.2. DR RefSeq; XP_006243428.1; XM_006243366.3. DR RefSeq; XP_008764442.1; XM_008766220.2. DR RefSeq; XP_017450987.1; XM_017595498.1. DR RefSeq; XP_017450988.1; XM_017595499.1. DR AlphaFoldDB; Q8CH87; -. DR SMR; Q8CH87; -. DR STRING; 10116.ENSRNOP00000071784; -. DR CAZy; GT14; Glycosyltransferase Family 14. DR GlyCosmos; Q8CH87; 1 site, No reported glycans. DR GlyGen; Q8CH87; 1 site. DR PhosphoSitePlus; Q8CH87; -. DR PaxDb; 10116-ENSRNOP00000014727; -. DR Ensembl; ENSRNOT00000079815.2; ENSRNOP00000071784.1; ENSRNOG00000059540.2. DR Ensembl; ENSRNOT00000104989.1; ENSRNOP00000094498.1; ENSRNOG00000059540.2. DR Ensembl; ENSRNOT00000106219.1; ENSRNOP00000093903.1; ENSRNOG00000059540.2. DR Ensembl; ENSRNOT00000109431.1; ENSRNOP00000096892.1; ENSRNOG00000059540.2. DR Ensembl; ENSRNOT00000112837.1; ENSRNOP00000081773.1; ENSRNOG00000059540.2. DR Ensembl; ENSRNOT00055011668; ENSRNOP00055009198; ENSRNOG00055007060. DR Ensembl; ENSRNOT00055011672; ENSRNOP00055009202; ENSRNOG00055007060. DR Ensembl; ENSRNOT00055011675; ENSRNOP00055009205; ENSRNOG00055007060. DR Ensembl; ENSRNOT00055011678; ENSRNOP00055009208; ENSRNOG00055007060. DR Ensembl; ENSRNOT00055011679; ENSRNOP00055009209; ENSRNOG00055007060. DR Ensembl; ENSRNOT00060029012; ENSRNOP00060023362; ENSRNOG00060016982. DR Ensembl; ENSRNOT00060029020; ENSRNOP00060023366; ENSRNOG00060016982. DR Ensembl; ENSRNOT00060029035; ENSRNOP00060023379; ENSRNOG00060016982. DR Ensembl; ENSRNOT00060029048; ENSRNOP00060023390; ENSRNOG00060016982. DR Ensembl; ENSRNOT00060029061; ENSRNOP00060023400; ENSRNOG00060016982. DR Ensembl; ENSRNOT00065027023; ENSRNOP00065021235; ENSRNOG00065016244. DR Ensembl; ENSRNOT00065027030; ENSRNOP00065021238; ENSRNOG00065016244. DR Ensembl; ENSRNOT00065027038; ENSRNOP00065021246; ENSRNOG00065016244. DR Ensembl; ENSRNOT00065027047; ENSRNOP00065021252; ENSRNOG00065016244. DR Ensembl; ENSRNOT00065027050; ENSRNOP00065021255; ENSRNOG00065016244. DR GeneID; 286976; -. DR KEGG; rno:286976; -. DR UCSC; RGD:631333; rat. DR AGR; RGD:631333; -. DR CTD; 9245; -. DR RGD; 631333; Gcnt3. DR eggNOG; KOG0799; Eukaryota. DR GeneTree; ENSGT00940000159331; -. DR HOGENOM; CLU_032341_1_2_1; -. DR InParanoid; Q8CH87; -. DR OMA; CRDILYK; -. DR OrthoDB; 5403607at2759; -. DR PhylomeDB; Q8CH87; -. DR TreeFam; TF315534; -. DR BRENDA; 2.4.1.150; 5301. DR Reactome; R-RNO-913709; O-linked glycosylation of mucins. DR UniPathway; UPA00378; -. DR PRO; PR:Q8CH87; -. DR Proteomes; UP000002494; Chromosome 8. DR Bgee; ENSRNOG00000059540; Expressed in stomach and 10 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; ISO:RGD. 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; IBA:GO_Central. 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; IDA:RGD. DR GO; GO:0050892; P:intestinal absorption; ISO:RGD. DR GO; GO:0060993; P:kidney morphogenesis; ISO:RGD. DR GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway. DR GO; GO:0048729; P:tissue morphogenesis; ISO:RGD. 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; Q8CH87; RN. PE 1: Evidence at protein level; KW Direct protein sequencing; Disulfide bond; Glycoprotein; KW Glycosyltransferase; Golgi apparatus; Membrane; Reference proteome; KW Signal-anchor; Transferase; Transmembrane; 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_0000288547" FT TOPO_DOM 1..6 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 7..27 FT /note="Helical; Signal-anchor for type II membrane protein" FT /evidence="ECO:0000255" FT TOPO_DOM 28..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" SQ SEQUENCE 437 AA; 50642 MW; 94CA5C1B883A1D82 CRC64; MVSWRRFCWH YHGWTLGCYM LLAIIALKLS LRLKCDFDVM DLDSKEFQSQ YCRDLLYKTL ELPAKSSINC SGVIRGEQKA VTQALLNNLE LKRKRQSFTE ADYLSMTADC EHFKTQRKFI QVPLSKEEAN FPIAYSMVIH EKIENFERLL RAVYTPQNIY CVHVDQKSSE TFQQAVRAIV SCFPNVFIAN KLVSVVYASW SRVQADLNCM EDLLQSPVPW EYLLNTCGTD FPIKTNAEMV KALKLLNGQN SMESEVPPPH KTFRWKYHYE VADTLYRTSK EKTPPPNNIT MFTGNAYMVA SRDFIEHVLS NSKARQLIEW VKDTYSPDEH LWATLQRASW MPGSDPLHPK FDLSDMRSIA RLTKWQDHEG DIENGAPYTS CSGIHQRAIC VYGSGDLHWI LQNHHLLANK FDPKVDDNVL QCLEEYLRHK AIYGTEL //