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

Contribute

Send feedback

Read comments (?) or add your own

Q8CH87 (GCNT3_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 66. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

text xml rdf/xml gff fasta

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

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
dI/C2/C4GnT
Short name=dIGnT

Gene names

Name:

Gcnt3

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	437 AA.
Sequence status	Complete.
Protein existence	Evidence at protein 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.
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.
Biophysicochemical properties	pH dependence: Optimum pH is 7-8.5. Ref.1

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 Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	immunoglobulin production in mucosal tissue Inferred from electronic annotation. Source: Compara intestinal absorption Inferred from electronic annotation. Source: Compara kidney morphogenesis Inferred from electronic annotation. Source: Compara protein glycosylation Inferred from electronic annotation. Source: UniProtKB-UniPathway tissue morphogenesis Inferred from electronic annotation. Source: Compara
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 direct assay Ref.1. Source: RGD acetylgalactosaminyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase activity Inferred from electronic annotation. Source: Compara 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_0000288547

Regions

Topological domain

1 – 6

Cytoplasmic Potential

Transmembrane

7 – 27

Helical; Signal-anchor for type II membrane protein; Potential

Topological domain

28 – 437

410

Lumenal Potential

Amino acid modifications

Glycosylation

288

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

Sequences

Sequence

Length

Mass (Da)

Tools

Q8CH87 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: 94CA5C1B883A1D82
Show »

FASTA

437

50,642

        10         20         30         40         50         60 
MVSWRRFCWH YHGWTLGCYM LLAIIALKLS LRLKCDFDVM DLDSKEFQSQ YCRDLLYKTL 

        70         80         90        100        110        120 
ELPAKSSINC SGVIRGEQKA VTQALLNNLE LKRKRQSFTE ADYLSMTADC EHFKTQRKFI 

       130        140        150        160        170        180 
QVPLSKEEAN FPIAYSMVIH EKIENFERLL RAVYTPQNIY CVHVDQKSSE TFQQAVRAIV 

       190        200        210        220        230        240 
SCFPNVFIAN KLVSVVYASW SRVQADLNCM EDLLQSPVPW EYLLNTCGTD FPIKTNAEMV 

       250        260        270        280        290        300 
KALKLLNGQN SMESEVPPPH KTFRWKYHYE VADTLYRTSK EKTPPPNNIT MFTGNAYMVA 

       310        320        330        340        350        360 
SRDFIEHVLS NSKARQLIEW VKDTYSPDEH LWATLQRASW MPGSDPLHPK FDLSDMRSIA 

       370        380        390        400        410        420 
RLTKWQDHEG DIENGAPYTS CSGIHQRAIC VYGSGDLHWI LQNHHLLANK FDPKVDDNVL 

       430 
QCLEEYLRHK AIYGTEL

« Hide

References

[1]

"Purification and cDNA cloning of UDP-GlcNAc:GlcNAcbeta1-3Galbeta1-4Glc(NAc)-R [GlcNAc to Gal]beta1,6N-acetylglucosaminyltransferase from rat small intestine: a major carrier of dIGnT activity in rat small intestine."
Korekane H., Taguchi T., Sakamoto Y., Honke K., Dohmae N., Salminen H., Toivonen S., Helin J., Takio K., Renkonen O., Taniguchi N.
Glycobiology 13:387-400(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 118-126; 266-280 AND 313-324, BIOPHYSICOCHEMICAL PROPERTIES.

Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB098520 mRNA. Translation: BAC53607.1.
IPI	IPI00192585.
RefSeq	NP_775434.1. NM_173312.2.
UniGene	Rn.43518.
3D structure databases
ProteinModelPortal	Q8CH87.
SMR	Q8CH87. Positions 67-432.
ModBase	Search...
Protein-protein interaction databases
STRING	10116.ENSRNOP00000014727.
Protein family/group databases
CAZy	GT14. Glycosyltransferase Family 14.
PTM databases
PhosphoSite	Q8CH87.
Proteomic databases
PRIDE	Q8CH87.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSRNOT00000014727; ENSRNOP00000014727; ENSRNOG00000011086.
GeneID	286976.
KEGG	rno:286976.
UCSC	RGD:631333. rat.
Organism-specific databases
CTD	9245.
RGD	631333. Gcnt3.
Phylogenomic databases
eggNOG	NOG253565.
GeneTree	ENSGT00690000102117.
HOGENOM	HOG000293251.
HOVERGEN	HBG051711.
InParanoid	Q8CH87.
KO	K09662.
OMA	CADESLW.
OrthoDB	EOG4X6C8B.
Enzyme and pathway databases
BRENDA	2.4.1.164. 5301.
UniPathway	UPA00378.
Gene expression databases
Genevestigator	Q8CH87.
Family and domain databases
InterPro	IPR003406. Glyco_trans_14. [Graphical view]
Pfam	PF02485. Branch. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	625213.

Entry information

Entry name

GCNT3_RAT

Accession

Primary (citable) accession number: Q8CH87

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 29, 2007
Last sequence update:	March 1, 2003
Last modified:	April 3, 2013
This is version 66 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents