GCNT3_RAT
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 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=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.ENSRNOP00000014727; -.
DR CAZy; GT14; Glycosyltransferase Family 14.
DR GlyGen; Q8CH87; 1 site.
DR PhosphoSitePlus; Q8CH87; -.
DR PaxDb; Q8CH87; -.
DR PRIDE; Q8CH87; -.
DR Ensembl; ENSRNOT00000079815; ENSRNOP00000071784; ENSRNOG00000059540.
DR Ensembl; ENSRNOT00000104989; ENSRNOP00000094498; ENSRNOG00000059540.
DR Ensembl; ENSRNOT00000106219; ENSRNOP00000093903; ENSRNOG00000059540.
DR Ensembl; ENSRNOT00000109431; ENSRNOP00000096892; ENSRNOG00000059540.
DR Ensembl; ENSRNOT00000112837; ENSRNOP00000081773; ENSRNOG00000059540.
DR GeneID; 286976; -.
DR KEGG; rno:286976; -.
DR UCSC; RGD:631333; rat.
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; IHQRAVC; -.
DR OrthoDB; 868849at2759; -.
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 tissues.
DR Genevisible; Q8CH87; RN.
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; 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 Pfam; PF02485; Branch; 1.
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 beta-
FT 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
