Reviewed, UniProtKB/Swiss-Prot O95395 (GCNT3_HUMAN)

Names and origin

Protein names

Recommended 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):
    Core 2/core 4 beta-1,6-N-acetylglucosaminyltransferase
      Short name=C2/4GnT
    C2GnT-mucin type
      Short name=hC2GnT-M
      Short name=C2GnT-M

Gene names

Name:

GCNT3

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	438 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence 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-alpha and IL13. 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 component	Golgi apparatus Membrane
Domain	Signal-anchor Transmembrane
Molecular function	Glycosyltransferase Transferase
PTM	Disulfide bond Glycoprotein
Gene Ontology (GO)
Biological process	protein amino acid O-linked glycosylation Ref.2 Traceable author statement. Source: ProtInc
Cellular component	Golgi membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW membrane fraction Ref.2 Traceable author statement. Source: ProtInc
Molecular function	N-acetyllactosaminide beta-1,6-N-acetylglucosaminyltransferase activity Ref.2 Traceable author statement. Source: ProtInc beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 438	438	Beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase 3		PRO_0000288545
Regions
	Topological domain	1 – 6	6	Cytoplasmic Potential
	Transmembrane	7 – 26	20	Signal-anchor for type II membrane Potential
	Topological domain	27 – 438	412	Lumenal Potential
Amino acid modifications
	Glycosylation	289	1	N-linked (GlcNAc...) Potential
	Disulfide bond	70 ↔ 227		By similarity
	Disulfide bond	161 ↔ 382		By similarity
	Disulfide bond	182 ↔ 209		By similarity
	Disulfide bond	391 ↔ 423		By similarity

Sequences

	Sequence		Length	Mass (Da)
	O95395-1 [UniParc]. Last modified May 1, 1999. Version 1. Checksum: 1FF0A7B451C88407	FASTA	438	50,864
	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

References

	« Hide 'large scale' referencesShow '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: 9915862] [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: 9988682] [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: 17303715] [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: 15489334] [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: 15864435] [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: 16418723] [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
EMBLGenBankDDBJ	AF102542 mRNA. Translation: AAD10824.1. AF038650 mRNA. Translation: AAD21525.1. EF152283 mRNA. Translation: ABM21534.1. BC017032 mRNA. Translation: AAH17032.1.
IPI	IPI00006248.
RefSeq	NP_004742.1.
UniGene	Hs.194710
3D structure databases
ModBase	Search...
Protein family/group databases
CAZy	GT14. Glycosyltransferase Family 14.
Proteomic databases
PRIDE	O95395.
Genome annotation databases
Ensembl	ENSG00000140297. Homo sapiens. [Contig view]
GeneID	9245.
KEGG	hsa:9245.
Organism-specific databases
GeneCards	GC15P057691.
HGNC	HGNC:4205. GCNT3.
HPA	HPA011154.
MIM	606836. gene.
PharmGKB	PA28620.
GenAtlas	Search...
Phylogenomic databases
HOGENOM	O95395.
HOVERGEN	O95395.
OMA	O95395. NNLEVKK.
Enzyme and pathway databases
BRENDA	2.4.1.102. 247. 2.4.1.150. 247.
Gene expression databases
ArrayExpress	O95395.
Bgee	O95395.
CleanEx	HS_GCNT3.
Family and domain databases
InterPro	IPR003406. Glyco_trans_14. [Graphical view]
PANTHER	PTHR19297. Glyco_trans_14. 1 hit.
Pfam	PF02485. Branch. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	34657.
SOURCE	Search...

Entry information

Entry name

GCNT3_HUMAN

Accession

Primary (citable) accession number: O95395

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 29, 2007
Last sequence update:	May 1, 1999
Last modified:	June 16, 2009
This is version 56 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)