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Q8IA43 (GLT10_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 80. 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 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:pgant10
ORF Names:CG31776
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length630 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 9-11, weakly expressed in the mesoderm. During embryonic stages 12-13, very weak expression is observed in the somatic mesoderm region. No expression detected from stage 14-15. During embryonic stages 16-17, expressed in the epidermis and the antennomaxillary complex. In third instar larvae, expressed ubiquitously in wing, eye-antennal, leg and haltere imaginal disks. Ref.5

Developmental stage

Expressed both maternally and zygotically. Expressed throughout embryonic and larval stages. Ref.5

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 – 630630Putative polypeptide N-acetylgalactosaminyltransferase 10
PRO_0000059164

Regions

Topological domain1 – 66Cytoplasmic Potential
Transmembrane7 – 2620Helical; Signal-anchor for type II membrane protein; Potential
Topological domain27 – 630604Lumenal Potential
Domain483 – 618136Ricin B-type lectin
Region166 – 277112Catalytic subdomain A
Region333 – 39462Catalytic subdomain B

Sites

Metal binding2611Manganese By similarity
Metal binding2631Manganese By similarity
Metal binding3911Manganese By similarity
Binding site2071Substrate By similarity
Binding site2381Substrate By similarity
Binding site2621Substrate By similarity
Binding site3631Substrate By similarity

Amino acid modifications

Glycosylation721N-linked (GlcNAc...) Potential
Glycosylation841N-linked (GlcNAc...) Potential
Glycosylation1461N-linked (GlcNAc...) Potential
Glycosylation1681N-linked (GlcNAc...) Potential
Glycosylation5251N-linked (GlcNAc...) Potential
Disulfide bond157 ↔ 386 By similarity
Disulfide bond377 ↔ 456 By similarity
Disulfide bond496 ↔ 513 By similarity
Disulfide bond543 ↔ 559 By similarity
Disulfide bond586 ↔ 606 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8IA43 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: 7E2748165A9293CA

FASTA63072,795
        10         20         30         40         50         60 
MNVDLRLIVR LLLAILLTSL VTTILMGKQI HRRLVKSMVK TTGEKDSLPA RQLPKREISP 

        70         80         90        100        110        120 
KVADFPPPLT LNQTELDILK IQRNNSFRLP QQEAIKEWQD AIFFKEDSNR RGLGEQGRAV 

       130        140        150        160        170        180 
QLPNAKLNPD DFQDFYAELS DRIPLNRSLP DTRPISCRKR KYLENLPNVT VIIAFHDEHL 

       190        200        210        220        230        240 
SVLLRSITSI INRSPVELLK QIVLVDDDSN LPELGQQLEE IVAQNFPKII HILRLPERRG 

       250        260        270        280        290        300 
SIKARMEAIR VSSCQVLVFL DSHIEVNTNW LPPLLEPIVI NPHIVTRPIL DAISRKTFAY 

       310        320        330        340        350        360 
AKQNTMTRSG FNWWLESESL PIFPEDKSPD STPYRTPVLS GAMAIDRNYF LNLGGFDEQL 

       370        380        390        400        410        420 
DTWEAEKFEI SFKVWMCGGM MLYVPCARVG HIGKRPMKSI SSPGYHNFLA RNYKRVAEVW 

       430        440        450        460        470        480 
MDNYKKYVYD KNPKLYKMAN AGLLFQRKTK RNALECKTFD WYMTKVAPDF LKRYLALDSP 

       490        500        510        520        530        540 
LVFSGVIESV AFPGFCVDSL NCRHTKPVVL ARCTGHNSMP GEHQNWSLTQ DHEIQLTNSK 

       550        560        570        580        590        600 
DDCLEAQGLR SKSVWLFRCH KNGGNQYWYY NHRHRWIQQG QIWVWCLEAQ LASGHKVGKV 

       610        620        630 
LANKICDKNQ LEQQWKVGRN APYDPQREPH 

« Hide

References

« Hide 'large scale' references
[1]"Functional conservation of subfamilies of putative UDP-N-acetylgalactosamine:polypeptide N-acetylgalactosaminyltransferases in Drosophila, Caenorhabditis elegans, and mammals. One subfamily composed of l(2)35Aa is essential in Drosophila."
Schwientek T., Bennett E.P., Flores C., Thacker J., Hollmann M., Reis C.A., Behrens J., Mandel U., Keck B., Schaefer M.A., Haselmann K., Zubarev R., Roepstorff P., Burchell J.M., Taylor-Papadimitriou J., Hollingsworth M.A., Clausen H.
J. Biol. Chem. 277:22623-22638(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"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.
[3]"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.
[4]Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M., Park S., Wan K.H., Yu C., Celniker S.E.
Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Berkeley.
[5]"Expression of the UDP-GalNAc: polypeptide N-acetylgalactosaminyltransferase family is spatially and temporally regulated during Drosophila development."
Tian E., Ten Hagen K.G.
Glycobiology 16:83-95(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF324751 mRNA. Translation: AAN75750.1.
AE014134 Genomic DNA. Translation: AAF51101.3.
BT022827 mRNA. Translation: AAY55243.1.
RefSeqNP_722909.2. NM_164538.4.
UniGeneDm.14884.

3D structure databases

ProteinModelPortalQ8IA43.
SMRQ8IA43. Positions 93-615.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING7227.FBpp0077211.

Protein family/group databases

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

Proteomic databases

PRIDEQ8IA43.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0077522; FBpp0077211; FBgn0051776.
GeneID33568.
KEGGdme:Dmel_CG31776.
UCSCCG31776-RA. d. melanogaster.

Organism-specific databases

FlyBaseFBgn0051776. CG31776.

Phylogenomic databases

eggNOGNOG254892.
GeneTreeENSGT00740000115054.
InParanoidQ8IA43.
KOK00710.
OrthoDBEOG7J9VP2.
PhylomeDBQ8IA43.

Enzyme and pathway databases

UniPathwayUPA00378.

Gene expression databases

BgeeQ8IA43.

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

GenomeRNAi33568.
NextBio784234.

Entry information

Entry nameGLT10_DROME
AccessionPrimary (citable) accession number: Q8IA43
Secondary accession number(s): Q4V529, Q9VQR4
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: March 1, 2003
Last modified: April 16, 2014
This is version 80 of the entry and version 1 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