Q5JCT0 (GCNT3_MOUSE) Reviewed, UniProtKB/Swiss-Prot

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):
C2GnT-mucin type
Short name=C2GnT-M
Mucus-type core 2 beta-1,6-N-acetylglucosaminyltransferase

Gene names

Name:

Gcnt3

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	437 AA.
Sequence status	Complete.
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 By similarity.
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. 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.
Post-translational modification	N-glycosylated By similarity.
Sequence similarities	Belongs to the glycosyltransferase 14 family.
Sequence caution	The sequence AAH18297.1 differs from that shown. Reason: Erroneous initiation. The sequence BAB25548.1 differs from that shown. Reason: Erroneous termination at position 35. Translated as Cys.

Ontologies

Keywords
Cellular component	Golgi apparatus Membrane
Domain	Signal-anchor Transmembrane Transmembrane helix
Molecular function	Glycosyltransferase Transferase
PTM	Disulfide bond Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	immunoglobulin production in mucosal tissue Inferred from mutant phenotype. Source: MGI intestinal absorption Inferred from mutant phenotype. Source: MGI
Cellular component	Golgi membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	N-acetyllactosaminide beta-1,6-N-acetylglucosaminyltransferase activity Inferred from electronic annotation. Source: EC acetylgalactosaminyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase activity Inferred from mutant phenotype. Source: MGI 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 – 437	437	Beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase 3		PRO_0000288546
Regions
	Topological domain	1 – 12	12	Cytoplasmic Potential
	Transmembrane	13 – 30	18	Helical; Signal-anchor for type II membrane protein; Potential
	Topological domain	31 – 437	407	Lumenal Potential
Amino acid modifications
	Glycosylation	288	1	N-linked (GlcNAc...) Potential
	Disulfide bond	70 ↔ 227		By similarity
	Disulfide bond	161 ↔ 381		By similarity
	Disulfide bond	182 ↔ 209		By similarity
	Disulfide bond	390 ↔ 422		By similarity
Experimental info
	Sequence conflict	101	1	A → G in AAK72480. Ref.1
	Sequence conflict	353	1	L → M in BAB25548. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Q5JCT0 [UniParc]. Last modified May 29, 2007. Version 2. Checksum: FF0C1EC8F25320F1	FASTA	437	50,698
	10 20 30 40 50 60 MTSWQRLCWH YRLWTLGCYM LLAILALKLS LRLKCDFDAM DLDSEEFQSQ YCRDLLYKTL 70 80 90 100 110 120 KLPAKSSINC SGVIRGEQKA VTQALLNNLE IKKKQQLFTE ADYLRMTADC EHFKTKRKFI 130 140 150 160 170 180 QVPLSKEEAS FPIAYSMVVH EKIENFERLL RAVYTPQNVY CVHMDQKSSE PFKQAVRAIV 190 200 210 220 230 240 SCFPNVFIAS KLVSVVYASW SRVQADLNCM EDLLQSPVPW KYLLNTCGTD FPIKTNAEMV 250 260 270 280 290 300 KALKLLKGQN SMESEVPPPH KKSRWKYHYE VTDTLHMTSK RKTPPPNNLT MFTGNAYMVA 310 320 330 340 350 360 SRDFIEHVFS NSKARQLIEW VKDTYSPDEH LWATLQRASW MPGSDPLHRK FDLSDMRAIA 370 380 390 400 410 420 RLTKWYDHEG DIENGAPYTS CSGIHQRAVC VYGSGDLHWI LQNHHLLANK FDPKVDDNVL 430 QCLEEYLRHK AIYGTEL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Core 2 beta-1,6-N-acetylglucosaminyltransferase II (Core2-GlcNAcT-II)." Yeh J.-C., Ong E., Fukuda M. Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Mucin biosynthesis: molecular cloning and expression of mouse mucus-type core 2 beta-1,6 N-acetylglucosaminyltransferase." Hashimoto M., Tan S., Mori N., Cheng H., Cheng P.-W. Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: C57BL/6. Tissue: Colon.
[3]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Small intestine.
[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]. Strain: FVB/N. Tissue: Colon.
+	Additional computationally mapped references.

Web resources

Functional Glycomics Gateway - GTase

core 2 beta 6 GlcNAc T3

Cross-references

Sequence databases
EMBL GenBank DDBJ	AY039027 mRNA. Translation: AAK72480.1. EF202835 mRNA. Translation: ABM91120.1. AK008234 mRNA. Translation: BAB25548.1. Sequence problems. BC018297 mRNA. Translation: AAH18297.1. Different initiation.
IPI	IPI00111289.
RefSeq	NP_082363.2. NM_028087.2.
UniGene	Mm.195555.
3D structure databases
ProteinModelPortal	Q5JCT0.
SMR	Q5JCT0. Positions 62-432.
ModBase	Search...
Protein-protein interaction databases
STRING	Q5JCT0.
Protein family/group databases
CAZy	GT14. Glycosyltransferase Family 14.
Proteomic databases
PRIDE	Q5JCT0.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000034751; ENSMUSP00000034751; ENSMUSG00000032226.
GeneID	72077.
KEGG	mmu:72077.
UCSC	uc009qnt.1. mouse.
Organism-specific databases
CTD	9245.
MGI	MGI:1919327. Gcnt3.
Phylogenomic databases
eggNOG	maNOG07131.
GeneTree	ENSGT00550000074330.
HOGENOM	HBG446687.
HOVERGEN	HBG051711.
InParanoid	Q5JCT0.
OMA	GQNSMES.
OrthoDB	EOG4X6C8B.
Gene expression databases
ArrayExpress	Q5JCT0.
Bgee	Q5JCT0.
CleanEx	MM_GCNT3.
Genevestigator	Q5JCT0.
Family and domain databases
InterPro	IPR003406. Glyco_trans_14. [Graphical view]
KO	K09662.
Pfam	PF02485. Branch. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	335378.
SOURCE	Search...

Entry information

Entry name

GCNT3_MOUSE

Accession

Primary (citable) accession number: Q5JCT0
Secondary accession number(s): A2TIK7, Q8VCX9, Q9D8A3

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 29, 2007
Last sequence update:	May 29, 2007
Last modified:	November 16, 2011
This is version 55 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program