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A8Y236 (GLT10_CAEBR) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 38. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Putative polypeptide N-acetylgalactosaminyltransferase 10
Short name=pp-GaNTase 10
EC=2.4.1.41
Alternative name(s):
Protein-UDP acetylgalactosaminyltransferase 10
UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 10
Gene names
Name:gly-10
ORF Names:CBG22373
OrganismCaenorhabditis briggsae [Reference proteome]
Taxonomic identifier6238 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Ecdysozoa › Nematoda › Chromadorea › Rhabditida › Rhabditoidea › Rhabditidae › Peloderinae › Caenorhabditis

Protein attributes

Sequence length629 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

May catalyze 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 By similarity. UniProtKB Q86SR1

Catalytic activity

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

Cofactor

Manganese By similarity. UniProtKB Q10472

Calcium By similarity. UniProtKB Q10472

Pathway

Protein modification; protein glycosylation. UniProtKB Q86SR1

Subcellular location

Golgi apparatus membrane; Single-pass type II membrane protein By similarity UniProtKB Q10472.

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. UniProtKB O08912

The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity By similarity. UniProtKB Q10473

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 – 629629Putative polypeptide N-acetylgalactosaminyltransferase 10
PRO_0000328999

Regions

Topological domain1 – 1212Cytoplasmic Potential
Transmembrane13 – 3321Helical; Signal-anchor for type II membrane protein
Topological domain34 – 629596Lumenal Potential
Domain526 – 629104Ricin B-type lectin
Region163 – 275113Catalytic subdomain A
Region331 – 39363Catalytic subdomain B
Region393 – 40614Flexible loop By similarity

Sites

Metal binding2591Manganese By similarity
Metal binding2611Manganese By similarity
Metal binding3901Manganese By similarity
Binding site2041Substrate By similarity
Binding site2591Substrate By similarity

Amino acid modifications

Glycosylation1431N-linked (GlcNAc...) Potential
Glycosylation1771N-linked (GlcNAc...) Potential
Disulfide bond154 ↔ 385 By similarity
Disulfide bond376 ↔ 454 By similarity
Disulfide bond493 ↔ 510 By similarity
Disulfide bond539 ↔ 556 By similarity
Disulfide bond582 ↔ 598 By similarity

Sequences

Sequence LengthMass (Da)Tools
A8Y236 [UniParc].

Last modified October 13, 2009. Version 2.
Checksum: FCD8FD9F61829238

FASTA62973,008
        10         20         30         40         50         60 
MGLSRYLSRR HHWVIQYCAL LLFLYFIYSY VAVSNDAPRL NEEIPVFREF SEDLPQGSRK 

        70         80         90        100        110        120 
FPEQKPAAAL GDEALDPFEK YRGHEKIKWE DEVAYEKDKA REGPGEWGKP VKLPDDKETE 

       130        140        150        160        170        180 
KEALSLYKAN GYNAYISDMI SLNRSIKDIR HKECKKMTYS AKLPTVSVIF PFHEEHNSTL 

       190        200        210        220        230        240 
LRSVYSVINR SPPELLKEII LVDDFSEKPA LRQPLEDFLK KNKIDHIVKI LRTKKREGLI 

       250        260        270        280        290        300 
RGRQLGAQEA TGEILIFLDA HSECNYNWLP PLLDPIADDY RTVVCPFVDV IDCETYEIRP 

       310        320        330        340        350        360 
QDEGARGSFD WAFNYKRLPL TKKDRENPTK PFDSPVMAGG YFAISAKWFW ELGGYDEGLD 

       370        380        390        400        410        420 
IWGGEQYELS FKVWQCHGKM VDAPCSRVAH IYRCKYAPFK NAGMGDFVSR NYKRVAEVWM 

       430        440        450        460        470        480 
DEYKETLYKH RPGIGNADAG DLKLMKGIRE KLQCKSFDWF MKEIAFDQDK YYPAIEPKAS 

       490        500        510        520        530        540 
AEGEIRHVAS NLCIDTQFKE QNQRFGLRKC ASEDKDGGGE QDLRLTRWHD IRPKGRKICF 

       550        560        570        580        590        600 
DVSTSVDKAP IILFDCHSMK GNQLFKYRMP QKQIYHPVSG QCLTADENGK GFLHMKKCDS 

       610        620 
SSKLQQWAWQ TIDQELLDQR QANEHKELE

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		HE600912 Genomic DNA. Translation: CAP38976.1.

3D structure databases

ProteinModelPortalA8Y236.
ModBaseSearch...

Protein-protein interaction databases

STRING6238.CBG22373.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaCBG22373; CBG22373; CBG22373.

Organism-specific databases

WormBaseCBG22373; CBP28929; WBGene00040946; Cbr-gly-10.

Phylogenomic databases

eggNOGNOG239675.

Enzyme and pathway databases

UniPathwayUPA00378.

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]
SUPFAMSSF50370. RicinB_like. 1 hit.
PROSITEPS50231. RICIN_B_LECTIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGLT10_CAEBR
AccessionPrimary (citable) accession number: A8Y236
Entry history
Integrated into UniProtKB/Swiss-Prot: April 8, 2008
Last sequence update: October 13, 2009
Last modified: April 3, 2013
This is version 38 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programCaenorhabditis annotation project

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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