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Reviewed, UniProtKB/Swiss-Prot Q6P6V1 (GLT11_RAT)

Last modified November 3, 2009. Version 46. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

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

Protein attributes

Sequence length608 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at transcript level.

General annotation (Comments)

Function

Catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, 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, Muc4.1, and EA2 than GALNT1. Does not appear to be involved in glycosylation of erythropoietin By similarity.

Catalytic activity

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

Cofactor

Manganese By similarity.

Calcium By similarity.

Pathway

Protein modification; protein glycosylation.

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 608608Polypeptide N-acetylgalactosaminyltransferase 11
PRO_0000059127

Regions

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

Amino acid modifications

Disulfide bond493 ↔ 512 By similarity
Disulfide bond536 ↔ 553 By similarity
Disulfide bond578 ↔ 596 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6P6V1-1 [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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Prostate.
+Additional computationally mapped references.

Cross-references

Sequence databases

BC062004 mRNA. Translation: AAH62004.1.
IPIIPI00400738.
RefSeqNP_955425.1.
UniGeneRn.211885

3D structure databases

ModBaseSearch...

Protein family/group databases

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

Proteomic databases

PRIDEQ6P6V1.

Genome annotation databases

EnsemblENSRNOT00000011814; ENSRNOP00000011815; ENSRNOG00000008117; Rattus norvegicus. [Genome view]
GeneID311952.
KEGGrno:311952.
UCSCNM_199393. rat.

Organism-specific databases

CTD311952.
RGD735097. Galnt11.

Phylogenomic databases

HOVERGENQ6P6V1.
OMAGMIFNER.

Enzyme and pathway databases

BRENDA2.4.1.41. 248.

Gene expression databases

ArrayExpressQ6P6V1.
GenevestigatorQ6P6V1.
GermOnlineENSRNOG00000008117. Rattus norvegicus.

Family and domain databases

InterProIPR001173. Glyco_trans_2.
IPR000772. Ricin_B_lectin.
[Graphical view]
PfamPF00535. Glycos_transf_2. 1 hit.
PF00652. Ricin_B_lectin. 1 hit.
[Graphical view]
SMARTSM00458. RICIN. 1 hit.
[Graphical view]
PROSITEPS50231. RICIN_B_LECTIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio664505.

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: November 3, 2009
This is version 46 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents