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Protein

Polypeptide N-acetylgalactosaminyltransferase 3

Gene

pgant3

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: 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

Mn2+By similarity

Pathwayi

Sites

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

GO - Molecular functioni

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

GO - Biological processi

  1. cell-substrate adhesion Source: FlyBase
  2. extracellular matrix constituent secretion Source: FlyBase
  3. O-glycan processing 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 Componenti: Chromosome 2R

Organism-specific databases

FlyBaseiFBgn0027558. pgant3.

Subcellular locationi

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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1212CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei13 – 3523Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST
Topological domaini36 – 667632LumenalSequence AnalysisAdd
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 3PRO_0000059157Add
BLAST

Amino acid modifications

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

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. 2 interactions.
MINTiMINT-336298.
STRINGi7227.FBpp0088130.

Structurei

3D structure databases

ProteinModelPortaliQ9Y117.
SMRiQ9Y117. Positions 129-463.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini513 – 661149Ricin B-type lectinPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni149 – 259111Catalytic subdomain AAdd
BLAST
Regioni321 – 38363Catalytic subdomain BAdd
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

Contains 1 ricin B-type lectin domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG285975.
GeneTreeiENSGT00760000118828.
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

        10         20         30         40         50
MGLRFQQLKK LWLLYLFLLF FAFFMFAISI NLYVASIQGG DAEMRHPKPP
60 70 80 90 100
PKRRSLWPHK NIVAHYIGKG DIFGNMTADD YNINLFQPIN GEGADGRPVV
110 120 130 140 150
VPPRDRFRMQ RFFRLNSFNL LASDRIPLNR TLKDYRTPEC RDKKYASGLP
160 170 180 190 200
STSVIIVFHN EAWSVLLRTI TSVINRSPRH LLKEIILVDD ASDRSYLKRQ
210 220 230 240 250
LESYVKVLAV PTRIFRMKKR SGLVPARLLG AENARGDVLT FLDAHCECSR
260 270 280 290 300
GWLEPLLSRI KESRKVVICP VIDIISDDNF SYTKTFENHW GAFNWQLSFR
310 320 330 340 350
WFSSDRKRQT AGNSSKDSTD PIATPGMAGG LFAIDRKYFY EMGSYDSNMR
360 370 380 390 400
VWGGENVEMS FRIWQCGGRV EISPCSHVGH VFRSSTPYTF PGGMSEVLTD
410 420 430 440 450
NLARAATVWM DDWQYFIMLY TSGLTLGAKD KVNVTERVAL RERLQCKPFS
460 470 480 490 500
WYLENIWPEH FFPAPDRFFG KIIWLDGETE CAQAYSKHMK NLPGRALSRE
510 520 530 540 550
WKRAFEEIDS KAEELMALID LERDKCLRPL KEDVPRSSLS AVTVGDCTSH
560 570 580 590 600
AQSMDMFVIT PKGQIMTNDN VCLTYRQQKL GVIKMLKNRN ATTSNVMLAQ
610 620 630 640 650
CASDSSQLWT YDMDTQQISH RDTKLCLTLK AATNSRLQKV EKVVLSMECD
660
FKDITQKWGF IPLPWRM
Length:667
Mass (Da):76,807
Last modified:November 1, 1999 - v1
Checksum:iB8C6924AA8E19805
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE013599 Genomic DNA. Translation: AAF59298.1.
AF145655 mRNA. Translation: AAD38630.1.
RefSeqiNP_610256.1. NM_136412.4.
UniGeneiDm.3144.

Genome annotation databases

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

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE013599 Genomic DNA. Translation: AAF59298.1.
AF145655 mRNA. Translation: AAD38630.1.
RefSeqiNP_610256.1. NM_136412.4.
UniGeneiDm.3144.

3D structure databases

ProteinModelPortaliQ9Y117.
SMRiQ9Y117. Positions 129-463.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi61516. 5 interactions.
IntActiQ9Y117. 2 interactions.
MINTiMINT-336298.
STRINGi7227.FBpp0088130.

Protein family/group databases

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

Proteomic databases

PaxDbiQ9Y117.
PRIDEiQ9Y117.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi35627.
FlyBaseiFBgn0027558. pgant3.

Phylogenomic databases

eggNOGiNOG285975.
GeneTreeiENSGT00760000118828.
InParanoidiQ9Y117.
KOiK00710.
OMAiMFAISIN.
OrthoDBiEOG7J9VP2.
PhylomeDBiQ9Y117.

Enzyme and pathway databases

UniPathwayiUPA00378.
BRENDAi2.4.1.41. 1994.

Miscellaneous databases

ChiTaRSipgant3. fly.
GenomeRNAii35627.
NextBioi794347.

Gene expression databases

BgeeiQ9Y117.

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]
ProtoNetiSearch...

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(1999) [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(2002) [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(2005) [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(2007) [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(2009) [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: April 1, 2015
This is version 108 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.