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Q6P6V1 (GLT11_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 86. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Polypeptide N-acetylgalactosaminyltransferase 11

EC=2.4.1.41
Alternative name(s):
Polypeptide GalNAc transferase 11
Short name=GalNAc-T11
Short name=pp-GaNTase 11
Protein-UDP acetylgalactosaminyltransferase 11
UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 11
Gene names
Name:Galnt11
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length608 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Polypeptide N-acetylgalactosaminyltransferase that catalyzes the initiation of protein O-linked glycosylation and is involved in left/right asymmetry by mediating O-glycosylation of NOTCH1. O-glycosylation of NOTCH1 promotes activation of NOTCH1, modulating the balance between motile and immotile (sensory) cilia at the left-right organiser (LRO). Polypeptide N-acetylgalactosaminyltransferases catalyze the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. Displays the same enzyme activity toward MUC1, MUC4, and EA2 than GALNT1. Not involved in glycosylation of erythropoietin (EPO) By similarity.

Catalytic activity

UDP-N-acetyl-alpha-D-galactosamine + polypeptide = UDP + N-acetyl-alpha-D-galactosaminyl-polypeptide.

Cofactor

Manganese By similarity.

Pathway

Protein modification; protein glycosylation.

Subunit structure

Interacts with NOTCH1 By similarity.

Subcellular location

Golgi apparatus membrane; Single-pass type II membrane protein By similarity.

Domain

There are two conserved domains in the glycosyltransferase region: the N-terminal domain (domain A, also called GT1 motif), which is probably involved in manganese coordination and substrate binding and the C-terminal domain (domain B, also called Gal/GalNAc-T motif), which is probably involved in catalytic reaction and UDP-Gal binding By similarity.

The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity By similarity.

Sequence similarities

Belongs to the glycosyltransferase 2 family. GalNAc-T subfamily.

Contains 1 ricin B-type lectin domain.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 608608Polypeptide N-acetylgalactosaminyltransferase 11
PRO_0000059127

Regions

Topological domain1 – 66Cytoplasmic Potential
Transmembrane7 – 2923Helical; Signal-anchor for type II membrane protein; Potential
Topological domain30 – 608579Lumenal Potential
Domain476 – 607132Ricin B-type lectin
Region150 – 261112Catalytic subdomain A
Region319 – 38163Catalytic subdomain B

Sites

Metal binding2451Manganese By similarity
Metal binding2471Manganese By similarity
Metal binding3781Manganese By similarity
Binding site1911Substrate By similarity
Binding site2221Substrate By similarity
Binding site2461Substrate By similarity
Binding site3501Substrate By similarity
Binding site3811Substrate By similarity
Binding site3861Substrate By similarity

Amino acid modifications

Glycosylation4281N-linked (GlcNAc...) Potential
Disulfide bond141 ↔ 373 By similarity
Disulfide bond364 ↔ 441 By similarity
Disulfide bond493 ↔ 512 By similarity
Disulfide bond536 ↔ 553 By similarity
Disulfide bond578 ↔ 596 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6P6V1 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: ED1295AC1EB35751

FASTA60869,039
        10         20         30         40         50         60 
MGSVTIRYFC YGCLFTSATW TVLLFIYFNF SEVTQPLRNV PIKGSGPHGP FPKKFYPRFT 

        70         80         90        100        110        120 
RGPGRVLEPQ FKANRMDDLM NNNIEDPDKG LSKSSSELGM IFNERDQELR DLGYQKHAFN 

       130        140        150        160        170        180 
MLISNRLGYH RDVPDTRNAE CRGKSYPTDL PTASVVICFY NEAFSALLRT VHSVVDRTPA 

       190        200        210        220        230        240 
HLLHEIILVD DSSDFDDLKG ELDEYIQRYL PAKVKVIRNM KREGLIRGRM IGAAHATGEV 

       250        260        270        280        290        300 
LVFLDSHCEV NVMWLQPLLA IILEDPHTVV CPVIDIISAD TLAYSSSPVV RGGFNWGLHF 

       310        320        330        340        350        360 
KWDLVPVSDL GGADSATAPI RSPTMAGGLF AMNRQYFNDL GQYDSGMDIW GGENLEISFR 

       370        380        390        400        410        420 
IWMCGGKLFI IPCSRVGHIF RKRRPYGSPE GQDTMTHNSL RLAHVWLDEY KEQYFSLRPD 

       430        440        450        460        470        480 
LKTKSFGNIS ERVELRKKLG CQSFKWYLDN VYPEMQVSGP KARLQQPVFI NRGPKRPRVL 

       490        500        510        520        530        540 
LRGRLYHLQT NKCLVAQGRS SQKGGLVLLK ACDYGDPTQV WIYNEEHELI LNNLLCLDMS 

       550        560        570        580        590        600 
ETRSSDPPRL MKCHGSGGSQ QWTFGKNNRL YQVSVGQCLR VVDQMDQKGY VGMAICDGSS 


SQQWRLEG 

« Hide

References

[1]"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].
Tissue: Prostate.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BC062004 mRNA. Translation: AAH62004.1.
RefSeqNP_001258248.1. NM_001271319.1.
NP_955425.2. NM_199393.2.
XP_006235984.1. XM_006235922.1.
XP_006235985.1. XM_006235923.1.
UniGeneRn.211885.

3D structure databases

ProteinModelPortalQ6P6V1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

MINTMINT-4576490.
STRING10116.ENSRNOP00000011815.

Protein family/group databases

CAZyCBM13. Carbohydrate-Binding Module Family 13.
GT27. Glycosyltransferase Family 27.

PTM databases

PhosphoSiteQ6P6V1.

Proteomic databases

PRIDEQ6P6V1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000011814; ENSRNOP00000011815; ENSRNOG00000008117.
GeneID311952.
KEGGrno:311952.

Organism-specific databases

CTD63917.
RGD735097. Galnt11.

Phylogenomic databases

eggNOGNOG239675.
GeneTreeENSGT00740000115054.
HOGENOMHOG000038227.
HOVERGENHBG051699.
InParanoidQ6P6V1.
KOK00710.
OMAMIFNERD.
OrthoDBEOG7J9VP2.
PhylomeDBQ6P6V1.
TreeFamTF313267.

Enzyme and pathway databases

UniPathwayUPA00378.

Gene expression databases

GenevestigatorQ6P6V1.

Family and domain databases

Gene3D3.90.550.10. 1 hit.
InterProIPR027791. Galactosyl_T_C.
IPR001173. Glyco_trans_2-like.
IPR029044. Nucleotide-diphossugar_trans.
IPR000772. Ricin_B_lectin.
[Graphical view]
PfamPF02709. Glyco_transf_7C. 1 hit.
PF00535. Glycos_transf_2. 1 hit.
PF00652. Ricin_B_lectin. 1 hit.
[Graphical view]
SMARTSM00458. RICIN. 1 hit.
[Graphical view]
SUPFAMSSF50370. SSF50370. 2 hits.
SSF53448. SSF53448. 1 hit.
PROSITEPS50231. RICIN_B_LECTIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio664505.
PROQ6P6V1.

Entry information

Entry nameGLT11_RAT
AccessionPrimary (citable) accession number: Q6P6V1
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: July 5, 2004
Last modified: June 11, 2014
This is version 86 of the entry and version 1 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