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Q5JCT0 (GCNT3_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 70. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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
Mucus-type core 2 beta-1,6-N-acetylglucosaminyltransferase
Gene names
Name:Gcnt3
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length437 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 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 437437Beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase 3
PRO_0000288546

Regions

Topological domain1 – 1212Cytoplasmic Potential
Transmembrane13 – 3018Helical; Signal-anchor for type II membrane protein; Potential
Topological domain31 – 437407Lumenal Potential

Amino acid modifications

Glycosylation2881N-linked (GlcNAc...) Potential
Disulfide bond70 ↔ 227 By similarity
Disulfide bond161 ↔ 381 By similarity
Disulfide bond182 ↔ 209 By similarity
Disulfide bond390 ↔ 422 By similarity

Experimental info

Sequence conflict1011A → G in AAK72480. Ref.1
Sequence conflict3531L → M in BAB25548. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q5JCT0 [UniParc].

Last modified May 29, 2007. Version 2.
Checksum: FF0C1EC8F25320F1

FASTA43750,698
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: FVB/N.
Tissue: Colon.
+Additional computationally mapped references.

Web resources

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.
RefSeqNP_082363.2. NM_028087.2.
XP_006511526.1. XM_006511463.1.
XP_006511527.1. XM_006511464.1.
XP_006511528.1. XM_006511465.1.
UniGeneMm.195555.

3D structure databases

ProteinModelPortalQ5JCT0.
SMRQ5JCT0. Positions 67-432.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGT14. Glycosyltransferase Family 14.

PTM databases

PhosphoSiteQ5JCT0.

Proteomic databases

PRIDEQ5JCT0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000034751; ENSMUSP00000034751; ENSMUSG00000032226.
GeneID72077.
KEGGmmu:72077.
UCSCuc009qnt.1. mouse.

Organism-specific databases

CTD9245.
MGIMGI:1919327. Gcnt3.

Phylogenomic databases

eggNOGNOG253565.
GeneTreeENSGT00750000117608.
HOGENOMHOG000293251.
HOVERGENHBG051711.
InParanoidQ5JCT0.
KOK09662.
OMACADESLW.
OrthoDBEOG74N5HW.
PhylomeDBQ5JCT0.
TreeFamTF315534.

Enzyme and pathway databases

UniPathwayUPA00378.

Gene expression databases

BgeeQ5JCT0.
CleanExMM_GCNT3.
GenevestigatorQ5JCT0.

Family and domain databases

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

Other

NextBio335378.
PROQ5JCT0.
SOURCESearch...

Entry information

Entry nameGCNT3_MOUSE
AccessionPrimary (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: April 16, 2014
This is version 70 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot