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Q8MYY6 (GLT13_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 86. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:
Putative polypeptide N-acetylgalactosaminyltransferase 13

Short name=pp-GaNTase 13
EC=2.4.1.41
Alternative name(s):
Protein-UDP acetylgalactosaminyltransferase 13
UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 13
Gene names
Name:pgant13
ORF Names:CG10000
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length558 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

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.

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.

Subcellular location

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

Tissue specificity

During embryonic stages 16-17, very weak expression in the midgut.

Developmental stage

Transcripts first detected during embryonic stages 16-17.

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 – 558558Putative polypeptide N-acetylgalactosaminyltransferase 13
PRO_0000059167

Regions

Topological domain1 – 1212Cytoplasmic Potential
Transmembrane13 – 3220Helical; Signal-anchor for type II membrane protein; Potential
Topological domain33 – 558526Lumenal Potential
Domain422 – 556135Ricin B-type lectin
Region109 – 225117Catalytic subdomain A
Region281 – 34363Catalytic subdomain B

Sites

Metal binding2091Manganese By similarity
Metal binding2111Manganese By similarity
Metal binding3401Manganese By similarity
Binding site1501Substrate By similarity
Binding site1861Substrate By similarity
Binding site2101Substrate By similarity
Binding site3121Substrate By similarity
Binding site3431Substrate By similarity
Binding site3461Substrate By similarity

Amino acid modifications

Glycosylation481N-linked (GlcNAc...) Potential
Glycosylation1111N-linked (GlcNAc...) Potential
Glycosylation5011N-linked (GlcNAc...) Potential
Disulfide bond97 ↔ 335 By similarity
Disulfide bond326 ↔ 412 By similarity
Disulfide bond445 ↔ 460 By similarity
Disulfide bond484 ↔ 498 By similarity
Disulfide bond525 ↔ 539 By similarity

Experimental info

Sequence conflict1711G → E in AAM29489. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q8MYY6 [UniParc].

Last modified August 16, 2004. Version 2.
Checksum: B9CB8EDB60F8D245

FASTA55864,626
        10         20         30         40         50         60 
MHAGGKYCGP RHCSFYIIAF LICQLFFLVI FIRNDDASSA NELLSFMNES EESDHLDWRV 

        70         80         90        100        110        120 
FISHTPETSE DFYQYNIHLS NALGLIRKLP VTRHHSCTTR NSILPAPLEA NVSVVISFHN 

       130        140        150        160        170        180 
EARSMLLRTI VSLLSRSPED YLHELILVDD GSQRDVTLLD DLKRWMGGVF GSRYRLGLTF 

       190        200        210        220        230        240 
LRNQERMGLI WSRNRGASLA SGRYVLFLDS HCEVNEGWLE PLLERLALNT NLAVSPLLDP 

       250        260        270        280        290        300 
IDPTTLSYRK GNELLKGGFD WSLHFHWLKR QLTNQESLEM PYQSPAFAGG VLMMSREWFL 

       310        320        330        340        350        360 
KLGSFNPYLK IWGGESIELA IKLWLCGGQI EIVPCSRIGH IFRRRHAFDF PPQSDRQLSP 

       370        380        390        400        410        420 
AQETYLHNSK IIAESWLDEY KNMFYALRPA ARRIPLDHTY DELQRMRKER RCHPFEWYLR 

       430        440        450        460        470        480 
HVSPELRMHF DELSATGTLR NEDRCVHARQ KDSQPILASC YLSDITQWSM LRQSGQLSTH 

       490        500        510        520        530        540 
RELCLAVGFG MRIALEPCGR NETVRRSQRW VRLGTHLLHA ESHLCLDNPL KDRLEMSTCR 

       550 
SHAVSQSFQF ALEMEGQT 

« Hide

References

« Hide 'large scale' references
[1]"The genome sequence of Drosophila melanogaster."
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. expand/collapse author list , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Berkeley.
[2]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. expand/collapse author list , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: Berkeley.
[3]"A Drosophila full-length cDNA resource."
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E.
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Berkeley.
Tissue: Head.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE014297 Genomic DNA. Translation: AAF56810.2.
AY113484 mRNA. Translation: AAM29489.1.
RefSeqNP_651630.3. NM_143373.3.
UniGeneDm.13252.

3D structure databases

ProteinModelPortalQ8MYY6.
SMRQ8MYY6. Positions 74-552.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING7227.FBpp0084684.

Protein family/group databases

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

Proteomic databases

PaxDbQ8MYY6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0085315; FBpp0084684; FBgn0039596.
GeneID43394.
KEGGdme:Dmel_CG10000.
UCSCCG10000-RA. d. melanogaster.

Organism-specific databases

FlyBaseFBgn0039596. CG10000.

Phylogenomic databases

eggNOGNOG81400.
GeneTreeENSGT00670000097647.
InParanoidQ8MYY6.
KOK00710.
OMAWGGESIE.
OrthoDBEOG7QVM26.
PhylomeDBQ8MYY6.

Enzyme and pathway databases

UniPathwayUPA00378.

Gene expression databases

BgeeQ8MYY6.

Family and domain databases

Gene3D3.90.550.10. 1 hit.
InterProIPR001173. Glyco_trans_2-like.
IPR029044. Nucleotide-diphossugar_trans.
IPR000772. Ricin_B_lectin.
[Graphical view]
PfamPF00535. Glycos_transf_2. 1 hit.
[Graphical view]
SUPFAMSSF50370. SSF50370. 1 hit.
SSF53448. SSF53448. 1 hit.
PROSITEPS50231. RICIN_B_LECTIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi43394.
NextBio833701.

Entry information

Entry nameGLT13_DROME
AccessionPrimary (citable) accession number: Q8MYY6
Secondary accession number(s): Q9VAT9
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: August 16, 2004
Last modified: July 9, 2014
This is version 86 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase