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

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Q7YQE1 (GCNT3_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 60. History...

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

Documents (2) |

Third-party data

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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
Mucus-type core 2 beta-1,6-N-acetylglucosaminyltransferase
bC2GnT-M
Short name=C2GnT-M

Gene names

Name:

GCNT3

Organism

Bos taurus (Bovine) [Reference proteome]

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length	440 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 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.
Tissue specificity	Primarily expressed in mucus-secreting tissues.
Post-translational modification	N-glycosylated Probable. Ref.3
Sequence similarities	Belongs to the glycosyltransferase 14 family.

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 electronic annotation. Source: EC 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 – 440

440

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

PRO_0000288543

Regions

Topological domain

1 – 12

Cytoplasmic Potential

Transmembrane

13 – 30

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

Topological domain

31 – 440

410

Lumenal Potential

Amino acid modifications

Glycosylation

N-linked (GlcNAc...) Potential

Glycosylation

108

N-linked (GlcNAc...) Potential

Disulfide bond

Disulfide bond

Disulfide bond

Disulfide bond

Experimental info

Sequence conflict

N → S in AAO22165. Ref.1

Sequence conflict

263

Y → S in AAP76324. Ref.2

Sequence conflict

263

Y → S in AAP76326. Ref.2

Sequences

Sequence

Length

Mass (Da)

Tools

Q7YQE1 [UniParc].

Last modified October 1, 2003. Version 1.
Checksum: 94D0EF6A08D9DA10
Show »

FASTA

440

50,953

        10         20         30         40         50         60 
MKMTGWKKKL CRGHHLWALG CYMLLAVVAL RLSLRLKCDV DSLDLESRDF QSQRCRDVLY 

        70         80         90        100        110        120 
KNLKLPAKRS INCSGITRGD QEAVVQALLD NLEVKKKRLP FTDTYYLNIT RDCEQFKAQR 

       130        140        150        160        170        180 
KFIQFPLSKE ELDFPIAYSM VVHEKIENFE RLLRAVYAPQ NIYCVHVDVK SPETFKEAVK 

       190        200        210        220        230        240 
AIISCFPNVF MASKLVPVVY ASWSRVQADL NCMEDLLQSS VPWKYLLNTC GTDFPIKTNA 

       250        260        270        280        290        300 
EMVLALKMLN GKNSMESEIP SEYKKNRWKY RYEVTDRLYL TSKMKDPPPD NLPMFTGNAY 

       310        320        330        340        350        360 
FVASRAFVQH VLENPKSQRL IEWVKDTYSP DEHLWATLQR APWMPGSVPY HPKYHISDMT 

       370        380        390        400        410        420 
AIARLVKWQG HEGDVSMGAP YAPCSGIHQR AICIYGAGDL HWILQNHHLL ANKFDPRVDD 

       430        440 
NVLQCLEEYL RHKAIYGTEL

« Hide

References

[1]	"The core 2 beta-1,6-N-acetylglucosaminyltransferase-mucin encoded by bovine herpesvirus 4 was acquired from an ancestor of the African buffalo." Markine-Goriaynoff N., Georgin J.-P., Goltz M., Zimmermann W., Broll H., Wamwayi H.M., Pastoret P.-P., Sharp P.M., Vanderplasschen A. J. Virol. 77:1784-1792(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Mucin biosynthesis: bovine C2GnT-M gene, tissue-specific expression, and herpes virus-4 homologue." Choi K.H., Osorio F.A., Cheng P.-W. Am. J. Respir. Cell Mol. Biol. 30:710-719(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. Tissue: Colon and Tracheal epithelium.
[3]	"Identification of disulfide bonds among the nine core 2 N-acetylglucosaminyltransferase-M cysteines conserved in the mucin beta6-N-acetylglucosaminyltransferase family." Singh J., Khan G.A., Kinarsky L., Cheng H., Wilken J., Choi K.H., Bedows E., Sherman S., Cheng P.-W. J. Biol. Chem. 279:38969-38977(2004) [PubMed] [Europe PMC] [Abstract] Cited for: PARTIAL PROTEIN SEQUENCE, DISULFIDE BONDS, GLYCOSYLATION.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF465338 Genomic DNA. Translation: AAO22165.1. AY283763 mRNA. Translation: AAP76324.1. AY283764 mRNA. Translation: AAP76325.1. AY283765 mRNA. Translation: AAP76326.1. AY283766 mRNA. Translation: AAP76327.1. AY283767 Genomic DNA. Translation: AAP76328.1.
IPI	IPI00712843.
RefSeq	NP_991378.1. NM_205809.1.
UniGene	Bt.51854.
3D structure databases
ProteinModelPortal	Q7YQE1.
SMR	Q7YQE1. Positions 70-435.
ModBase	Search...
Protein family/group databases
CAZy	GT14. Glycosyltransferase Family 14.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSBTAT00000012427; ENSBTAP00000012427; ENSBTAG00000009443.
GeneID	404167.
KEGG	bta:404167.
Organism-specific databases
CTD	9245.
Phylogenomic databases
eggNOG	NOG253565.
GeneTree	ENSGT00690000102117.
HOGENOM	HOG000293251.
HOVERGEN	HBG051711.
InParanoid	Q7YQE1.
KO	K09662.
OMA	PCSGIHQ.
OrthoDB	EOG4X6C8B.
Enzyme and pathway databases
UniPathway	UPA00378.
Family and domain databases
InterPro	IPR003406. Glyco_trans_14. [Graphical view]
Pfam	PF02485. Branch. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	20817599.

Entry information

Entry name

GCNT3_BOVIN

Accession

Primary (citable) accession number: Q7YQE1
Secondary accession number(s): Q7YQF8, Q866Z3

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 29, 2007
Last sequence update:	October 1, 2003
Last modified:	April 3, 2013
This is version 60 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

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein family/group databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Other

Entry information

Relevant documents