Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9Y117 (GALT3_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 101. 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:
Polypeptide N-acetylgalactosaminyltransferase 3

Short name=pp-GaNTase 3
EC=2.4.1.41
Alternative name(s):
Protein-UDP acetylgalactosaminyltransferase 3
UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 3
Gene names
Name:pgant3
ORF Names:CG4445
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length667 AA.
Sequence statusComplete.
Protein existenceEvidence at protein 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. It can both act as a peptide transferase that transfers GalNAc onto unmodified peptide substrates, and as a glycopeptide transferase that requires the prior addition of a GalNAc on a peptide before adding additional GalNAc moieties. Prefers EA2 as substrate. Has weak activity toward Muc5AC-3, -13 and -3/13 substrates. Plays a critical role in the regulation of integrin-mediated cell adhesion during wing development by influencing, via glycosylation, the secretion and localization of the integrin ligand Tig to the basal cell layer interface. Ref.6 Ref.7

Catalytic activity

UDP-N-acetyl-alpha-D-galactosamine + polypeptide = UDP + N-acetyl-alpha-D-galactosaminyl-polypeptide. Ref.4

Cofactor

Manganese By similarity.

Pathway

Protein modification; protein glycosylation.

Subcellular location

Golgi apparatus membrane; Single-pass type II membrane protein Ref.7.

Tissue specificity

Expressed in developing oocytes and egg chambers. During embryonic stages 9-11, expressed in the primordiums of the foregut, midgut and hindgut. During embryonic stages 12-13, expression is found uniquely in the posterior spiracle. During embryonic stages 14-17, expressed in the pharynx, esophagus and posterior spiracles. Expression observed in the epidermis during embryonic stages 16-17. In third instar larvae, expressed ubiquitously in wing, with increased expression in pleura and notum, eye-antennal, leg and haltere imaginal disks. Ref.4 Ref.5

Developmental stage

Expressed both maternally and zygotically. Expressed throughout embryonic, larval, pupal and adult stages. Ref.4 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.

Disruption phenotype

Mutant larval wing disks show a decrease in thickness and in the content of O-glycoproteins specifically along the basal surface of the columnar epithelial cells. Adult mutants display blistered wings. Ref.6 Ref.7

Sequence similarities

Belongs to the glycosyltransferase 2 family. GalNAc-T subfamily.

Contains 1 ricin B-type lectin domain.

Ontologies

Keywords
   Cellular componentGolgi apparatus
Membrane
   DomainSignal-anchor
Transmembrane
Transmembrane helix
   LigandLectin
Manganese
Metal-binding
   Molecular functionGlycosyltransferase
Transferase
   PTMDisulfide bond
Glycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processO-glycan processing

Inferred from direct assay Ref.6. Source: FlyBase

cell-substrate adhesion

Inferred from mutant phenotype Ref.7. Source: FlyBase

extracellular matrix constituent secretion

Inferred from mutant phenotype Ref.7. Source: FlyBase

oligosaccharide biosynthetic process

Inferred from direct assay Ref.4. Source: UniProtKB

protein O-linked glycosylation

Inferred from direct assay Ref.6. Source: FlyBase

regulation of cell adhesion mediated by integrin

Inferred from mutant phenotype Ref.6. Source: FlyBase

   Cellular_componentGolgi apparatus

Inferred from direct assay Ref.7. Source: FlyBase

Golgi membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

Golgi stack

Non-traceable author statement Ref.4. Source: UniProtKB

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionacetylgalactosaminyltransferase activity

Inferred from direct assay Ref.6. Source: FlyBase

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

polypeptide N-acetylgalactosaminyltransferase activity

Inferred from direct assay Ref.4. Source: UniProtKB

transferase activity, transferring glycosyl groups

Inferred from direct assay Ref.7. Source: FlyBase

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 667667Polypeptide N-acetylgalactosaminyltransferase 3
PRO_0000059157

Regions

Topological domain1 – 1212Cytoplasmic Potential
Transmembrane13 – 3523Helical; Signal-anchor for type II membrane protein; Potential
Topological domain36 – 667632Lumenal Potential
Domain513 – 661149Ricin B-type lectin
Region149 – 259111Catalytic subdomain A
Region321 – 38363Catalytic subdomain B

Sites

Metal binding2431Manganese By similarity
Metal binding2451Manganese By similarity
Metal binding3801Manganese By similarity
Binding site1901Substrate By similarity
Binding site2201Substrate By similarity
Binding site3521Substrate By similarity
Binding site3831Substrate By similarity
Binding site3881Substrate By similarity

Amino acid modifications

Glycosylation751N-linked (GlcNAc...) Potential
Glycosylation1291N-linked (GlcNAc...) Potential
Glycosylation2791N-linked (GlcNAc...) Potential
Glycosylation3131N-linked (GlcNAc...) Potential
Glycosylation4331N-linked (GlcNAc...) Potential
Glycosylation5901N-linked (GlcNAc...) Potential
Disulfide bond140 ↔ 375 By similarity
Disulfide bond366 ↔ 446 By similarity
Disulfide bond526 ↔ 547 By similarity
Disulfide bond572 ↔ 601 By similarity
Disulfide bond626 ↔ 649 By similarity

Experimental info

Mutagenesis1301R → C: Does not affect subcellular location. Loss of catalytic activity. Ref.7

Sequences

Sequence LengthMass (Da)Tools
Q9Y117 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: B8C6924AA8E19805

FASTA66776,807
        10         20         30         40         50         60 
MGLRFQQLKK LWLLYLFLLF FAFFMFAISI NLYVASIQGG DAEMRHPKPP PKRRSLWPHK 

        70         80         90        100        110        120 
NIVAHYIGKG DIFGNMTADD YNINLFQPIN GEGADGRPVV VPPRDRFRMQ RFFRLNSFNL 

       130        140        150        160        170        180 
LASDRIPLNR TLKDYRTPEC RDKKYASGLP STSVIIVFHN EAWSVLLRTI TSVINRSPRH 

       190        200        210        220        230        240 
LLKEIILVDD ASDRSYLKRQ LESYVKVLAV PTRIFRMKKR SGLVPARLLG AENARGDVLT 

       250        260        270        280        290        300 
FLDAHCECSR GWLEPLLSRI KESRKVVICP VIDIISDDNF SYTKTFENHW GAFNWQLSFR 

       310        320        330        340        350        360 
WFSSDRKRQT AGNSSKDSTD PIATPGMAGG LFAIDRKYFY EMGSYDSNMR VWGGENVEMS 

       370        380        390        400        410        420 
FRIWQCGGRV EISPCSHVGH VFRSSTPYTF PGGMSEVLTD NLARAATVWM DDWQYFIMLY 

       430        440        450        460        470        480 
TSGLTLGAKD KVNVTERVAL RERLQCKPFS WYLENIWPEH FFPAPDRFFG KIIWLDGETE 

       490        500        510        520        530        540 
CAQAYSKHMK NLPGRALSRE WKRAFEEIDS KAEELMALID LERDKCLRPL KEDVPRSSLS 

       550        560        570        580        590        600 
AVTVGDCTSH AQSMDMFVIT PKGQIMTNDN VCLTYRQQKL GVIKMLKNRN ATTSNVMLAQ 

       610        620        630        640        650        660 
CASDSSQLWT YDMDTQQISH RDTKLCLTLK AATNSRLQKV EKVVLSMECD FKDITQKWGF 


IPLPWRM 

« 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.
[4]"Functional characterization and expression analysis of members of the UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase family from Drosophila melanogaster."
Ten Hagen K.G., Tran D.T., Gerken T.A., Stein D.S., Zhang Z.
J. Biol. Chem. 278:35039-35048(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: ENZYME ACTIVITY, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
[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.
[6]"A mucin-type O-glycosyltransferase modulates cell adhesion during Drosophila development."
Zhang L., Zhang Y., Hagen K.G.
J. Biol. Chem. 283:34076-34086(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE.
[7]"An O-glycosyltransferase promotes cell adhesion during development by influencing secretion of an extracellular matrix integrin ligand."
Zhang L., Tran D.T., Ten Hagen K.G.
J. Biol. Chem. 285:19491-19501(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, MUTAGENESIS OF ARG-130.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE013599 Genomic DNA. Translation: AAF59298.1.
AF145655 mRNA. Translation: AAD38630.1.
RefSeqNP_610256.1. NM_136412.3.
UniGeneDm.3144.

3D structure databases

ProteinModelPortalQ9Y117.
SMRQ9Y117. Positions 91-663.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid61516. 5 interactions.
IntActQ9Y117. 1 interaction.
MINTMINT-336298.
STRING7227.FBpp0088130.

Protein family/group databases

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

Proteomic databases

PaxDbQ9Y117.
PRIDEQ9Y117.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0089061; FBpp0088130; FBgn0027558.
GeneID35627.
KEGGdme:Dmel_CG4445.

Organism-specific databases

CTD35627.
FlyBaseFBgn0027558. pgant3.

Phylogenomic databases

eggNOGNOG285975.
GeneTreeENSGT00750000117385.
InParanoidQ9Y117.
KOK00710.
OMAMFAISIN.
OrthoDBEOG7J9VP2.
PhylomeDBQ9Y117.

Enzyme and pathway databases

BRENDA2.4.1.41. 1994.
UniPathwayUPA00378.

Gene expression databases

BgeeQ9Y117.

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

GenomeRNAi35627.
NextBio794347.

Entry information

Entry nameGALT3_DROME
AccessionPrimary (citable) accession number: Q9Y117
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: November 1, 1999
Last modified: April 16, 2014
This is version 101 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