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Q925R7 (GLT10_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 89. 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 10

EC=2.4.1.41
Alternative name(s):
Polypeptide GalNAc transferase 10
Short name=GalNAc-T10
Short name=pp-GaNTase 10
Protein-UDP acetylgalactosaminyltransferase 10
UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 10
Gene names
Name:Galnt10
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length603 AA.
Sequence statusComplete.
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. Has activity toward Muc5Ac and EA2 peptide substrates.

Catalytic activity

UDP-N-acetyl-alpha-D-galactosamine + polypeptide = UDP + N-acetyl-alpha-D-galactosaminyl-polypeptide. Ref.1

Cofactor

Manganese By similarity.

Pathway

Protein modification; protein glycosylation.

Subcellular location

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

Tissue specificity

Highly expressed in the sublingual gland, testis, small intestine, colon and ovary. Expressed at intermediate level in heart, brain, spleen, lung, stomach, cervix and uterus. Ref.1

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.

Caution

According to Ref.1, this enzyme is unable to transfer GalNAc onto serine or threonine residue on the protein receptor, but instead requires the prior addition of a GalNAc on a peptide before adding additional GalNAc moieties, thereby acting as a glycopeptide transferase.

Was originally (Ref.1) termed Galnt9/pp-GaNTase 9.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 603603Polypeptide N-acetylgalactosaminyltransferase 10
PRO_0000059124

Regions

Topological domain1 – 1111Cytoplasmic Potential
Transmembrane12 – 3120Helical; Signal-anchor for type II membrane protein; Potential
Topological domain32 – 603572Lumenal Potential
Domain458 – 590133Ricin B-type lectin
Region144 – 253110Catalytic subdomain A
Region311 – 37363Catalytic subdomain B
Region373 – 38412Flexible loop By similarity

Sites

Metal binding2371Manganese By similarity
Metal binding2391Manganese By similarity
Metal binding3701Manganese By similarity
Binding site1851Substrate By similarity
Binding site2141Substrate By similarity
Binding site2381Substrate By similarity
Binding site3421Substrate By similarity
Binding site3731Substrate By similarity
Binding site3781Substrate By similarity

Amino acid modifications

Glycosylation1241N-linked (GlcNAc...) Potential
Glycosylation1461N-linked (GlcNAc...) Potential
Glycosylation5931N-linked (GlcNAc...) Potential
Disulfide bond135 ↔ 365 By similarity
Disulfide bond356 ↔ 432 By similarity
Disulfide bond471 ↔ 488 By similarity
Disulfide bond523 ↔ 538 By similarity
Disulfide bond563 ↔ 578 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q925R7 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: 194EDEAA626A4BBF

FASTA60369,117
        10         20         30         40         50         60 
MRRKEKRLLQ AVALALAALV LLPNVGLWAL YRERQPDGSP GGSGAAVAPE AIQELHSRQK 

        70         80         90        100        110        120 
KTLFLGAEQR LKDWHNKEAI RRDAQRVGNG EQGKPYPMTD AERVDQAYRE NGFNIYVSDK 

       130        140        150        160        170        180 
ISLNRSLPDI RHPNCNSKLY LETLPNTSII IPFHNEGWSS LLRTVHSVLN RSPPELVAEI 

       190        200        210        220        230        240 
VLVDDFSDRE HLKKPLEDYM ALFPSVRILR TKKREGLIRT RMLGASAATG DVITFLDSHC 

       250        260        270        280        290        300 
EANVNWLPPL LDRIARNRKT IVCPMIDVID HDDFRYETQA GDAMRGAFDW EMYYKRIPIP 

       310        320        330        340        350        360 
PELQKADPSD PFESPVMAGG LFAVDRKWFW ELGGYDPGLE IWGGEQYEIS FKVWMCGGRM 

       370        380        390        400        410        420 
EDIPCSRVGH IYRKYVPYKV PAGVSLARNL KRVAEVWMDE YAEYIYQRRP EYRHLSAGDV 

       430        440        450        460        470        480 
VAQKKLRGSL NCKSFKWFMT KIAWDLPKFY PPVEPPAAAW GEIRNVGTGL CTDTKHGTLG 

       490        500        510        520        530        540 
SPLRLETCIR GRGEAAWNSM QVFTFTWRED IRPGDPQHTK KFCFDAVSHT SPVTLYDCHS 

       550        560        570        580        590        600 
MKGNQLWKYR KDKTLYHPVS GSCMDCSESD HRIFMNTCNP SSLTQQWLFE HTNSTVLENF 


NRN 

« Hide

References

[1]"Cloning and characterization of a ninth member of the UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase family, ppGaNTase-T9."
Ten Hagen K.G., Bedi G.S., Tetaert D., Kingsley P.D., Hagen F.K., Balys M.M., Beres T.M., Degand P., Tabak L.A.
J. Biol. Chem. 276:17395-17404(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], ENZYME ACTIVITY, TISSUE SPECIFICITY.
Tissue: Sublingual gland.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF241241 mRNA. Translation: AAK54498.1.
RefSeqNP_570098.1. NM_130742.1.
UniGeneRn.60224.

3D structure databases

ProteinModelPortalQ925R7.
SMRQ925R7. Positions 69-603.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000003447.

Protein family/group databases

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

Proteomic databases

PaxDbQ925R7.
PRIDEQ925R7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000003447; ENSRNOP00000003447; ENSRNOG00000002488.
GeneID170501.
KEGGrno:170501.
UCSCRGD:69409. rat.

Organism-specific databases

CTD55568.
RGD69409. Galnt10.

Phylogenomic databases

eggNOGNOG239675.
GeneTreeENSGT00740000115054.
HOGENOMHOG000038227.
HOVERGENHBG051699.
InParanoidQ925R7.
KOK00710.
OMAQKKTFFL.
OrthoDBEOG7J9VP2.
PhylomeDBQ925R7.
TreeFamTF313267.

Enzyme and pathway databases

UniPathwayUPA00378.

Gene expression databases

GenevestigatorQ925R7.

Family and domain databases

InterProIPR001173. Glyco_trans_2-like.
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]
SUPFAMSSF50370. SSF50370. 1 hit.
PROSITEPS50231. RICIN_B_LECTIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio621001.
PROQ925R7.

Entry information

Entry nameGLT10_RAT
AccessionPrimary (citable) accession number: Q925R7
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: December 1, 2001
Last modified: April 16, 2014
This is version 89 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