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Protein

Putative polypeptide N-acetylgalactosaminyltransferase 13

Gene

pgant13

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

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 activityi

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

Cofactori

Mn2+By similarity

Pathway: protein glycosylation

This protein is involved in the pathway protein glycosylation, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein glycosylation and in Protein modification.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei150 – 1501SubstrateBy similarity
Binding sitei186 – 1861SubstrateBy similarity
Metal bindingi209 – 2091ManganeseBy similarity
Binding sitei210 – 2101SubstrateBy similarity
Metal bindingi211 – 2111ManganeseBy similarity
Binding sitei312 – 3121SubstrateBy similarity
Metal bindingi340 – 3401ManganeseBy similarity
Binding sitei343 – 3431SubstrateBy similarity
Binding sitei346 – 3461SubstrateBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Ligandi

Lectin, Manganese, Metal-binding

Enzyme and pathway databases

UniPathwayiUPA00378.

Protein family/group databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
Putative polypeptide N-acetylgalactosaminyltransferase 13 (EC:2.4.1.41)
Short name:
pp-GaNTase 13
Alternative name(s):
Protein-UDP acetylgalactosaminyltransferase 13
UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 13
Gene namesi
Name:pgant13
ORF Names:CG10000
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803 Componenti: Chromosome 3R

Organism-specific databases

FlyBaseiFBgn0039596. CG10000.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1212CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei13 – 3220Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST
Topological domaini33 – 558526LumenalSequence AnalysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 558558Putative polypeptide N-acetylgalactosaminyltransferase 13PRO_0000059167Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi48 – 481N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi97 ↔ 335PROSITE-ProRule annotation
Glycosylationi111 – 1111N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi326 ↔ 412PROSITE-ProRule annotation
Disulfide bondi445 ↔ 460PROSITE-ProRule annotation
Disulfide bondi484 ↔ 498PROSITE-ProRule annotation
Glycosylationi501 – 5011N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi525 ↔ 539PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ8MYY6.

Expressioni

Tissue specificityi

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

Developmental stagei

Transcripts first detected during embryonic stages 16-17.

Gene expression databases

BgeeiQ8MYY6.
GenevisibleiQ8MYY6. DM.

Interactioni

Protein-protein interaction databases

STRINGi7227.FBpp0084684.

Structurei

3D structure databases

ProteinModelPortaliQ8MYY6.
SMRiQ8MYY6. Positions 66-554.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini422 – 556135Ricin B-type lectinPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni109 – 225117Catalytic subdomain AAdd
BLAST
Regioni281 – 34363Catalytic 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

eggNOGiNOG81400.
GeneTreeiENSGT00670000097647.
InParanoidiQ8MYY6.
KOiK00710.
OMAiQIEIVPC.
OrthoDBiEOG7QVM26.
PhylomeDBiQ8MYY6.

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.
[Graphical view]
SUPFAMiSSF50370. SSF50370. 1 hit.
SSF53448. SSF53448. 1 hit.
PROSITEiPS50231. RICIN_B_LECTIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8MYY6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MHAGGKYCGP RHCSFYIIAF LICQLFFLVI FIRNDDASSA NELLSFMNES
60 70 80 90 100
EESDHLDWRV FISHTPETSE DFYQYNIHLS NALGLIRKLP VTRHHSCTTR
110 120 130 140 150
NSILPAPLEA NVSVVISFHN EARSMLLRTI VSLLSRSPED YLHELILVDD
160 170 180 190 200
GSQRDVTLLD DLKRWMGGVF GSRYRLGLTF LRNQERMGLI WSRNRGASLA
210 220 230 240 250
SGRYVLFLDS HCEVNEGWLE PLLERLALNT NLAVSPLLDP IDPTTLSYRK
260 270 280 290 300
GNELLKGGFD WSLHFHWLKR QLTNQESLEM PYQSPAFAGG VLMMSREWFL
310 320 330 340 350
KLGSFNPYLK IWGGESIELA IKLWLCGGQI EIVPCSRIGH IFRRRHAFDF
360 370 380 390 400
PPQSDRQLSP AQETYLHNSK IIAESWLDEY KNMFYALRPA ARRIPLDHTY
410 420 430 440 450
DELQRMRKER RCHPFEWYLR HVSPELRMHF DELSATGTLR NEDRCVHARQ
460 470 480 490 500
KDSQPILASC YLSDITQWSM LRQSGQLSTH RELCLAVGFG MRIALEPCGR
510 520 530 540 550
NETVRRSQRW VRLGTHLLHA ESHLCLDNPL KDRLEMSTCR SHAVSQSFQF

ALEMEGQT
Length:558
Mass (Da):64,626
Last modified:August 16, 2004 - v2
Checksum:iB9CB8EDB60F8D245
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti171 – 1711G → E in AAM29489 (PubMed:12537569).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014297 Genomic DNA. Translation: AAF56810.2.
AY113484 mRNA. Translation: AAM29489.1.
RefSeqiNP_651630.3. NM_143373.3.
UniGeneiDm.13252.

Genome annotation databases

EnsemblMetazoaiFBtr0085315; FBpp0084684; FBgn0039596.
GeneIDi43394.
KEGGidme:Dmel_CG10000.
UCSCiCG10000-RA. d. melanogaster.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014297 Genomic DNA. Translation: AAF56810.2.
AY113484 mRNA. Translation: AAM29489.1.
RefSeqiNP_651630.3. NM_143373.3.
UniGeneiDm.13252.

3D structure databases

ProteinModelPortaliQ8MYY6.
SMRiQ8MYY6. Positions 66-554.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi7227.FBpp0084684.

Protein family/group databases

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

Proteomic databases

PaxDbiQ8MYY6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0085315; FBpp0084684; FBgn0039596.
GeneIDi43394.
KEGGidme:Dmel_CG10000.
UCSCiCG10000-RA. d. melanogaster.

Organism-specific databases

FlyBaseiFBgn0039596. CG10000.

Phylogenomic databases

eggNOGiNOG81400.
GeneTreeiENSGT00670000097647.
InParanoidiQ8MYY6.
KOiK00710.
OMAiQIEIVPC.
OrthoDBiEOG7QVM26.
PhylomeDBiQ8MYY6.

Enzyme and pathway databases

UniPathwayiUPA00378.

Miscellaneous databases

GenomeRNAii43394.
NextBioi833701.
PROiQ8MYY6.

Gene expression databases

BgeeiQ8MYY6.
GenevisibleiQ8MYY6. DM.

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.
[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(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.

Entry informationi

Entry nameiGLT13_DROME
AccessioniPrimary (citable) accession number: Q8MYY6
Secondary accession number(s): Q9VAT9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: August 16, 2004
Last modified: June 24, 2015
This is version 93 of the entry and version 2 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.