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O95395 (GCNT3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 101. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase 3

EC=2.4.1.102
EC=2.4.1.150
Alternative name(s):
C2GnT-mucin type
Short name=C2GnT-M
Short name=hC2GnT-M
Core 2/core 4 beta-1,6-N-acetylglucosaminyltransferase
Short name=C2/4GnT
Gene names
Name:GCNT3
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length438 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Glycosyltransferase that can synthesize all known mucin beta 6 N-acetylglucosaminides. Mediates core 2 and core 4 O-glycan branching, 2 important steps in mucin-type biosynthesis. Has also I-branching enzyme activity by converting linear into branched poly-N-acetyllactosaminoglycans, leading to introduce the blood group I antigen during embryonic development. Ref.1

Catalytic activity

UDP-N-acetyl-D-glucosamine + beta-D-galactosyl-1,3-N-acetyl-D-galactosaminyl-R = UDP + beta-D-galactosyl-1,3-(N-acetyl-beta-D-glucosaminyl-1,6)-N-acetyl-D-galactosaminyl-R. Ref.1

UDP-N-acetyl-D-glucosamine + beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-R = UDP + N-acetyl-beta-D-glucosaminyl-1,6-beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-R.

Pathway

Protein modification; protein glycosylation.

Subcellular location

Golgi apparatus membrane; Single-pass type II membrane protein By similarity.

Tissue specificity

Primarily expressed in mucus-secreting tissues. Expressed in colon, kidney, small intestine, trachea, and stomach, where mucin is produced. Ref.1 Ref.3

Induction

By all-trans retinoic acid (ATRA), TNF and IL13/interleukin-13. Strongly down-regulated in colorectal cancer. Ref.3 Ref.5 Ref.6

Post-translational modification

N-glycosylated By similarity.

Sequence similarities

Belongs to the glycosyltransferase 14 family.

Ontologies

Keywords
   Cellular componentGolgi apparatus
Membrane
   DomainSignal-anchor
Transmembrane
Transmembrane helix
   Molecular functionGlycosyltransferase
Transferase
   PTMDisulfide bond
Glycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processO-glycan processing

Traceable author statement. Source: Reactome

carbohydrate metabolic process

Non-traceable author statement Ref.2. Source: ProtInc

cellular protein metabolic process

Traceable author statement. Source: Reactome

immunoglobulin production in mucosal tissue

Inferred from electronic annotation. Source: Ensembl

intestinal absorption

Inferred from electronic annotation. Source: Ensembl

kidney morphogenesis

Inferred from electronic annotation. Source: Ensembl

post-translational protein modification

Traceable author statement. Source: Reactome

protein O-linked glycosylation

Traceable author statement Ref.2. Source: ProtInc

tissue morphogenesis

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentGolgi membrane

Traceable author statement. Source: Reactome

extracellular vesicular exosome

Inferred from direct assay PubMed 19199708. Source: UniProt

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

membrane

Traceable author statement Ref.2. Source: ProtInc

   Molecular_functionN-acetyllactosaminide beta-1,6-N-acetylglucosaminyltransferase activity

Traceable author statement Ref.2. Source: ProtInc

acetylgalactosaminyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase activity

Inferred from electronic annotation. Source: Ensembl

beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 438438Beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase 3
PRO_0000288545

Regions

Topological domain1 – 66Cytoplasmic Potential
Transmembrane7 – 2620Helical; Signal-anchor for type II membrane protein; Potential
Topological domain27 – 438412Lumenal Potential

Amino acid modifications

Glycosylation2891N-linked (GlcNAc...) Potential
Disulfide bond70 ↔ 227 By similarity
Disulfide bond161 ↔ 382 By similarity
Disulfide bond182 ↔ 209 By similarity
Disulfide bond391 ↔ 423 By similarity

Sequences

Sequence LengthMass (Da)Tools
O95395 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: 1FF0A7B451C88407

FASTA43850,864
        10         20         30         40         50         60 
MVQWKRLCQL HYLWALGCYM LLATVALKLS FRLKCDSDHL GLESRESQSQ YCRNILYNFL 

        70         80         90        100        110        120 
KLPAKRSINC SGVTRGDQEA VLQAILNNLE VKKKREPFTD THYLSLTRDC EHFKAERKFI 

       130        140        150        160        170        180 
QFPLSKEEVE FPIAYSMVIH EKIENFERLL RAVYAPQNIY CVHVDEKSPE TFKEAVKAII 

       190        200        210        220        230        240 
SCFPNVFIAS KLVRVVYASW SRVQADLNCM EDLLQSSVPW KYFLNTCGTD FPIKSNAEMV 

       250        260        270        280        290        300 
QALKMLNGRN SMESEVPPKH KETRWKYHFE VVRDTLHLTN KKKDPPPYNL TMFTGNAYIV 

       310        320        330        340        350        360 
ASRDFVQHVL KNPKSQQLIE WVKDTYSPDE HLWATLQRAR WMPGSVPNHP KYDISDMTSI 

       370        380        390        400        410        420 
ARLVKWQGHE GDIDKGAPYA PCSGIHQRAI CVYGAGDLNW MLQNHHLLAN KFDPKVDDNA 

       430 
LQCLEEYLRY KAIYGTEL 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning and expression of a novel beta-1, 6-N-acetylglucosaminyltransferase that forms core 2, core 4, and I branches."
Yeh J.-C., Ong E., Fukuda M.
J. Biol. Chem. 274:3215-3221(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, ENZYME ACTIVITY, TISSUE SPECIFICITY.
Tissue: Brain.
[2]"Control of O-glycan branch formation. Molecular cloning of human cDNA encoding a novel beta1,6-N-acetylglucosaminyltransferase forming core 2 and core 4."
Schwientek T., Nomoto M., Levery S.B., Merkx G., van Kessel A.G., Bennett E.P., Hollingsworth M.A., Clausen H.
J. Biol. Chem. 274:4504-4512(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Mucin biosynthesis: identification of the cis-regulatory elements of human C2GnT-M gene."
Tan S., Cheng P.-W.
Am. J. Respir. Cell Mol. Biol. 36:737-745(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, INDUCTION.
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Colon.
[5]"Regulation of sialyl-Lewis x epitope expression by TNF-alpha and EGF in an airway carcinoma cell line."
Ishibashi Y., Inouye Y., Okano T., Taniguchi A.
Glycoconj. J. 22:53-62(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION.
[6]"C2GnT-M is downregulated in colorectal cancer and its re-expression causes growth inhibition of colon cancer cells."
Huang M.-C., Chen H.-Y., Huang H.-C., Huang J., Liang J.-T., Shen T.-L., Lin N.-Y., Ho C.-C., Cho I.-M., Hsu S.-M.
Oncogene 25:3267-3276(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION.
+Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology
GGDB

GlycoGene database

Functional Glycomics Gateway - GTase

Core 2/core 4 beta-1,6-N-acetylglucosaminyltransferase

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF102542 mRNA. Translation: AAD10824.1.
AF038650 mRNA. Translation: AAD21525.1.
EF152283 mRNA. Translation: ABM21534.1.
BC017032 mRNA. Translation: AAH17032.1.
RefSeqNP_004742.1. NM_004751.2.
UniGeneHs.194710.

3D structure databases

ProteinModelPortalO95395.
SMRO95395. Positions 67-433.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114671. 4 interactions.
IntActO95395. 4 interactions.
STRING9606.ENSP00000267857.

Protein family/group databases

CAZyGT14. Glycosyltransferase Family 14.

PTM databases

PhosphoSiteO95395.

Proteomic databases

PaxDbO95395.
PRIDEO95395.

Protocols and materials databases

DNASU9245.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000396065; ENSP00000379377; ENSG00000140297.
ENST00000560585; ENSP00000452741; ENSG00000140297.
GeneID9245.
KEGGhsa:9245.
UCSCuc002agd.3. human.

Organism-specific databases

CTD9245.
GeneCardsGC15P059903.
HGNCHGNC:4205. GCNT3.
HPAHPA011154.
MIM606836. gene.
neXtProtNX_O95395.
PharmGKBPA28620.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG253565.
HOGENOMHOG000293251.
HOVERGENHBG051711.
InParanoidO95395.
KOK09662.
OMAPCSGIHQ.
PhylomeDBO95395.
TreeFamTF315534.

Enzyme and pathway databases

ReactomeREACT_17015. Metabolism of proteins.
SignaLinkO95395.
UniPathwayUPA00378.

Gene expression databases

ArrayExpressO95395.
BgeeO95395.
CleanExHS_GCNT3.
GenevestigatorO95395.

Family and domain databases

InterProIPR003406. Glyco_trans_14.
[Graphical view]
PfamPF02485. Branch. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSGCNT3. human.
GenomeRNAi9245.
NextBio34657.
PROO95395.
SOURCESearch...

Entry information

Entry nameGCNT3_HUMAN
AccessionPrimary (citable) accession number: O95395
Entry history
Integrated into UniProtKB/Swiss-Prot: May 29, 2007
Last sequence update: May 1, 1999
Last modified: April 16, 2014
This is version 101 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 15

Human chromosome 15: entries, gene names and cross-references to MIM