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Q9Y117

- GALT3_DROME

UniProt

Q9Y117 - GALT3_DROME

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Protein
Polypeptide N-acetylgalactosaminyltransferase 3
Gene
pgant3, CG4445
Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.2 Publications

Catalytic activityi

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

Cofactori

Manganese By similarity.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei190 – 1901Substrate By similarity
Binding sitei220 – 2201Substrate By similarity
Metal bindingi243 – 2431Manganese By similarity
Metal bindingi245 – 2451Manganese By similarity
Binding sitei352 – 3521Substrate By similarity
Metal bindingi380 – 3801Manganese By similarity
Binding sitei383 – 3831Substrate By similarity
Binding sitei388 – 3881Substrate By similarity

GO - Molecular functioni

  1. acetylgalactosaminyltransferase activity Source: FlyBase
  2. metal ion binding Source: UniProtKB-KW
  3. polypeptide N-acetylgalactosaminyltransferase activity Source: UniProtKB
  4. transferase activity, transferring glycosyl groups Source: FlyBase
Complete GO annotation...

GO - Biological processi

  1. O-glycan processing Source: FlyBase
  2. cell-substrate adhesion Source: FlyBase
  3. extracellular matrix constituent secretion Source: FlyBase
  4. oligosaccharide biosynthetic process Source: UniProtKB
  5. protein O-linked glycosylation Source: FlyBase
  6. regulation of cell adhesion mediated by integrin Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Ligandi

Lectin, Manganese, Metal-binding

Enzyme and pathway databases

BRENDAi2.4.1.41. 1994.
UniPathwayiUPA00378.

Protein family/group databases

CAZyiCBM13. Carbohydrate-Binding Module Family 13.
GT27. Glycosyltransferase Family 27.

Names & Taxonomyi

Protein namesi
Recommended name:
Polypeptide N-acetylgalactosaminyltransferase 3 (EC:2.4.1.41)
Short name:
pp-GaNTase 3
Alternative name(s):
Protein-UDP acetylgalactosaminyltransferase 3
UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 3
Gene namesi
Name:pgant3
ORF Names:CG4445
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803: Chromosome 2R

Organism-specific databases

FlyBaseiFBgn0027558. pgant3.

Subcellular locationi

Golgi apparatus membrane; Single-pass type II membrane protein 1 Publication

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1212Cytoplasmic Reviewed prediction
Add
BLAST
Transmembranei13 – 3523Helical; Signal-anchor for type II membrane protein; Reviewed prediction
Add
BLAST
Topological domaini36 – 667632Lumenal Reviewed prediction
Add
BLAST

GO - Cellular componenti

  1. Golgi apparatus Source: FlyBase
  2. Golgi membrane Source: UniProtKB-SubCell
  3. Golgi stack Source: UniProtKB
  4. integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane

Pathology & Biotechi

Disruption phenotypei

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.2 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi130 – 1301R → C: Does not affect subcellular location. Loss of catalytic activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 667667Polypeptide N-acetylgalactosaminyltransferase 3
PRO_0000059157Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi75 – 751N-linked (GlcNAc...) Reviewed prediction
Glycosylationi129 – 1291N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi140 ↔ 375 By similarity
Glycosylationi279 – 2791N-linked (GlcNAc...) Reviewed prediction
Glycosylationi313 – 3131N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi366 ↔ 446 By similarity
Glycosylationi433 – 4331N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi526 ↔ 547 By similarity
Disulfide bondi572 ↔ 601 By similarity
Glycosylationi590 – 5901N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi626 ↔ 649 By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ9Y117.
PRIDEiQ9Y117.

Expressioni

Tissue specificityi

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.2 Publications

Developmental stagei

Expressed both maternally and zygotically. Expressed throughout embryonic, larval, pupal and adult stages.2 Publications

Gene expression databases

BgeeiQ9Y117.

Interactioni

Protein-protein interaction databases

BioGridi61516. 5 interactions.
IntActiQ9Y117. 1 interaction.
MINTiMINT-336298.
STRINGi7227.FBpp0088130.

Structurei

3D structure databases

ProteinModelPortaliQ9Y117.
SMRiQ9Y117. Positions 91-472.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini513 – 661149Ricin B-type lectin
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni149 – 259111Catalytic subdomain A
Add
BLAST
Regioni321 – 38363Catalytic subdomain B
Add
BLAST

Domaini

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 similaritiesi

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG285975.
GeneTreeiENSGT00750000117385.
InParanoidiQ9Y117.
KOiK00710.
OMAiMFAISIN.
OrthoDBiEOG7J9VP2.
PhylomeDBiQ9Y117.

Family and domain databases

Gene3Di3.90.550.10. 1 hit.
InterProiIPR001173. Glyco_trans_2-like.
IPR029044. Nucleotide-diphossugar_trans.
IPR000772. Ricin_B_lectin.
[Graphical view]
PfamiPF00535. Glycos_transf_2. 1 hit.
PF00652. Ricin_B_lectin. 1 hit.
[Graphical view]
SMARTiSM00458. RICIN. 1 hit.
[Graphical view]
SUPFAMiSSF50370. SSF50370. 1 hit.
SSF53448. SSF53448. 1 hit.
PROSITEiPS50231. RICIN_B_LECTIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9Y117-1 [UniParc]FASTAAdd to Basket

« Hide

MGLRFQQLKK LWLLYLFLLF FAFFMFAISI NLYVASIQGG DAEMRHPKPP    50
PKRRSLWPHK NIVAHYIGKG DIFGNMTADD YNINLFQPIN GEGADGRPVV 100
VPPRDRFRMQ RFFRLNSFNL LASDRIPLNR TLKDYRTPEC RDKKYASGLP 150
STSVIIVFHN EAWSVLLRTI TSVINRSPRH LLKEIILVDD ASDRSYLKRQ 200
LESYVKVLAV PTRIFRMKKR SGLVPARLLG AENARGDVLT FLDAHCECSR 250
GWLEPLLSRI KESRKVVICP VIDIISDDNF SYTKTFENHW GAFNWQLSFR 300
WFSSDRKRQT AGNSSKDSTD PIATPGMAGG LFAIDRKYFY EMGSYDSNMR 350
VWGGENVEMS FRIWQCGGRV EISPCSHVGH VFRSSTPYTF PGGMSEVLTD 400
NLARAATVWM DDWQYFIMLY TSGLTLGAKD KVNVTERVAL RERLQCKPFS 450
WYLENIWPEH FFPAPDRFFG KIIWLDGETE CAQAYSKHMK NLPGRALSRE 500
WKRAFEEIDS KAEELMALID LERDKCLRPL KEDVPRSSLS AVTVGDCTSH 550
AQSMDMFVIT PKGQIMTNDN VCLTYRQQKL GVIKMLKNRN ATTSNVMLAQ 600
CASDSSQLWT YDMDTQQISH RDTKLCLTLK AATNSRLQKV EKVVLSMECD 650
FKDITQKWGF IPLPWRM 667
Length:667
Mass (Da):76,807
Last modified:November 1, 1999 - v1
Checksum:iB8C6924AA8E19805
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE013599 Genomic DNA. Translation: AAF59298.1.
AF145655 mRNA. Translation: AAD38630.1.
RefSeqiNP_610256.1. NM_136412.3.
UniGeneiDm.3144.

Genome annotation databases

EnsemblMetazoaiFBtr0089061; FBpp0088130; FBgn0027558.
GeneIDi35627.
KEGGidme:Dmel_CG4445.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE013599 Genomic DNA. Translation: AAF59298.1 .
AF145655 mRNA. Translation: AAD38630.1 .
RefSeqi NP_610256.1. NM_136412.3.
UniGenei Dm.3144.

3D structure databases

ProteinModelPortali Q9Y117.
SMRi Q9Y117. Positions 91-472.
ModBasei Search...

Protein-protein interaction databases

BioGridi 61516. 5 interactions.
IntActi Q9Y117. 1 interaction.
MINTi MINT-336298.
STRINGi 7227.FBpp0088130.

Protein family/group databases

CAZyi CBM13. Carbohydrate-Binding Module Family 13.
GT27. Glycosyltransferase Family 27.

Proteomic databases

PaxDbi Q9Y117.
PRIDEi Q9Y117.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblMetazoai FBtr0089061 ; FBpp0088130 ; FBgn0027558 .
GeneIDi 35627.
KEGGi dme:Dmel_CG4445.

Organism-specific databases

CTDi 35627.
FlyBasei FBgn0027558. pgant3.

Phylogenomic databases

eggNOGi NOG285975.
GeneTreei ENSGT00750000117385.
InParanoidi Q9Y117.
KOi K00710.
OMAi MFAISIN.
OrthoDBi EOG7J9VP2.
PhylomeDBi Q9Y117.

Enzyme and pathway databases

UniPathwayi UPA00378 .
BRENDAi 2.4.1.41. 1994.

Miscellaneous databases

GenomeRNAii 35627.
NextBioi 794347.

Gene expression databases

Bgeei Q9Y117.

Family and domain databases

Gene3Di 3.90.550.10. 1 hit.
InterProi IPR001173. Glyco_trans_2-like.
IPR029044. Nucleotide-diphossugar_trans.
IPR000772. Ricin_B_lectin.
[Graphical view ]
Pfami PF00535. Glycos_transf_2. 1 hit.
PF00652. Ricin_B_lectin. 1 hit.
[Graphical view ]
SMARTi SM00458. RICIN. 1 hit.
[Graphical view ]
SUPFAMi SSF50370. SSF50370. 1 hit.
SSF53448. SSF53448. 1 hit.
PROSITEi PS50231. RICIN_B_LECTIN. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  3. 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.

Entry informationi

Entry nameiGALT3_DROME
AccessioniPrimary (citable) accession number: Q9Y117
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: November 1, 1999
Last modified: July 9, 2014
This is version 103 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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