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Protein

N-acetylgalactosaminyltransferase 7

Gene

GalNAc-T2

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

Functioni

Glycopeptide transferase involved in O-linked oligosaccharide biosynthesis, which catalyzes the transfer of an N-acetyl-D-galactosamine residue to an already glycosylated peptide. In contrast to other proteins of the family, it does not act as a peptide transferase that transfers GalNAc onto serine or threonine residue on the protein receptor, but instead requires the prior addition of a GalNAc on a peptide before adding additional GalNAc moieties. Some peptide transferase activity is however not excluded, considering that its appropriate peptide substrate may remain unidentified. Prefers the monoglycosylated Muc5AC-3 as substrate.

Cofactori

Mn2+By similarity

Pathwayi: 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 sitei182 – 1821SubstrateBy similarity
Binding sitei212 – 2121SubstrateBy similarity
Metal bindingi235 – 2351ManganeseBy similarity
Metal bindingi237 – 2371ManganeseBy similarity
Binding sitei344 – 3441SubstrateBy similarity
Metal bindingi372 – 3721ManganeseBy similarity
Binding sitei375 – 3751SubstrateBy similarity
Binding sitei380 – 3801SubstrateBy similarity

GO - Molecular functioni

GO - Biological processi

  • oligosaccharide biosynthetic process Source: UniProtKB
  • protein glycosylation Source: UniProtKB-UniPathway
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:
N-acetylgalactosaminyltransferase 7 (EC:2.4.1.-)
Alternative name(s):
Protein-UDP acetylgalactosaminyltransferase 7
UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 7
Short name:
pp-GaNTase 7
dGalNAc-T2
Gene namesi
Name:GalNAc-T2
Synonyms:pgant7
ORF Names:CG6394
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome X

Organism-specific databases

FlyBaseiFBgn0030930. GalNAc-T2.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1111CytoplasmicSequence analysisAdd
BLAST
Transmembranei12 – 2918Helical; Signal-anchor for type II membrane proteinSequence analysisAdd
BLAST
Topological domaini30 – 591562LumenalSequence analysisAdd
BLAST

GO - Cellular componenti

  • endomembrane system Source: FlyBase
  • Golgi membrane Source: UniProtKB-SubCell
  • Golgi stack Source: UniProtKB
  • integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 591591N-acetylgalactosaminyltransferase 7PRO_0000059161Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi30 – 301N-linked (GlcNAc...)Sequence analysis
Disulfide bondi132 ↔ 367PROSITE-ProRule annotation
Disulfide bondi358 ↔ 441PROSITE-ProRule annotation
Disulfide bondi479 ↔ 496PROSITE-ProRule annotation
Disulfide bondi519 ↔ 532PROSITE-ProRule annotation
Disulfide bondi558 ↔ 573PROSITE-ProRule annotation
Glycosylationi576 – 5761N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ8MV48.
PRIDEiQ8MV48.

Expressioni

Tissue specificityi

Expressed in developing oocytes and egg chambers. During embryonic stages 9-11, expressed in the primordium of the foregut, midgut and hindgut. Expressed in the salivary glands from embryonic stage 12 onwards. During embryonic stages 12-13, expressed in the posterior midgut and hindgut. During embryonic stages 14-15, expression continues in the hindgut. During embryonic stages 16-17, expressed in the antennomaxillary complex. In third instar larvae, ubiquitously expressed in wing, with increased expression in the notum and ventral wing pouch, eye-antennal, leg and haltere imaginal disks.2 Publications

Developmental stagei

Expressed both maternally and zygotically. Expressed throughout embryonic, larval, pupal and adult stages, with increasing levels during larval development.2 Publications

Gene expression databases

BgeeiFBgn0030930.
ExpressionAtlasiQ8MV48. differential.
GenevisibleiQ8MV48. DM.

Interactioni

Protein-protein interaction databases

BioGridi59149. 4 interactions.
IntActiQ8MV48. 4 interactions.
MINTiMINT-325977.
STRINGi7227.FBpp0074396.

Structurei

3D structure databases

ProteinModelPortaliQ8MV48.
SMRiQ8MV48. Positions 115-584.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini466 – 585120Ricin B-type lectinPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni141 – 251111Catalytic subdomain AAdd
BLAST
Regioni313 – 37563Catalytic 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

eggNOGiKOG3736. Eukaryota.
ENOG410XPMK. LUCA.
InParanoidiQ8MV48.
KOiK00710.
OMAiFDDTHKE.
OrthoDBiEOG091G085O.
PhylomeDBiQ8MV48.

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.

Q8MV48-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRVSTIRSGR ICRLALCLLV LLPLLYLLAN WSDHHKRVQE AYHTRFGGPK
60 70 80 90 100
FAHQRLEGRP REVPKLVDGL GNFEPKDVKP RSGPGENGEA HSLSPDKKHM
110 120 130 140 150
SDASEMEYGM NIACSDEISM HRSVRDTRLE ECRHWDYPFD LPRTSVIIVF
160 170 180 190 200
HNEGFSVLMR TVHSVIDRSP THMLHEIILV DDFSDKENLR SQLDEYVLQF
210 220 230 240 250
KGLVKVIRNK EREGLIRTRS RGAMEATGEV IVFLDAHCEV NTNWLPPLLA
260 270 280 290 300
PIYRDRTVMT VPIIDGIDHK NFEYRPVYGT DNHFRGIFEW GMLYKENEVP
310 320 330 340 350
RREQRRRAHN SEPYRSPTHA GGLFAINREY FLELGAYDPG LLVWGGENFE
360 370 380 390 400
LSFKIWQCGG SIEWVPCSRV GHVYRGFMPY NFGKLASKKK GPLITINYKR
410 420 430 440 450
VIETWFDDTH KEYFYTREPL ARYLDMGDIS EQLALKKRLN CKSFQWFMDH
460 470 480 490 500
IAYDVYDKFP GLPANLHWGE LRSVASDGCL DSMGHQPPAI MGLTYCHGGG
510 520 530 540 550
NNQLVRLNAA GQLGVGERCV EADRQGIKLA VCRLGTVDGP WQYNEHTKHL
560 570 580 590
MHRVHKKCMA LHPATQQLSL GHCDVNDSYQ QWWFKEIRPR W
Length:591
Mass (Da):68,333
Last modified:August 16, 2004 - v2
Checksum:i6CC2F7DC38E4CF17
GO

Sequence cautioni

The sequence AAL13889 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAL28887 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti84 – 841P → S in AAM62412 (PubMed:11925450).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF493067 mRNA. Translation: AAM62412.1.
AY268068 mRNA. Translation: AAQ56704.1.
AE014298 Genomic DNA. Translation: AAF48851.1.
AE014298 Genomic DNA. Translation: AAN09470.1.
BT016123 mRNA. Translation: AAV37008.1.
AY058660 mRNA. Translation: AAL13889.1. Different initiation.
AY061339 mRNA. Translation: AAL28887.1. Different initiation.
RefSeqiNP_001285406.1. NM_001298477.1.
NP_573301.2. NM_133073.3.
NP_728178.1. NM_167623.2.
UniGeneiDm.7692.

Genome annotation databases

EnsemblMetazoaiFBtr0074624; FBpp0074395; FBgn0030930.
FBtr0074625; FBpp0074396; FBgn0030930.
FBtr0346082; FBpp0311917; FBgn0030930.
GeneIDi32836.
KEGGidme:Dmel_CG6394.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF493067 mRNA. Translation: AAM62412.1.
AY268068 mRNA. Translation: AAQ56704.1.
AE014298 Genomic DNA. Translation: AAF48851.1.
AE014298 Genomic DNA. Translation: AAN09470.1.
BT016123 mRNA. Translation: AAV37008.1.
AY058660 mRNA. Translation: AAL13889.1. Different initiation.
AY061339 mRNA. Translation: AAL28887.1. Different initiation.
RefSeqiNP_001285406.1. NM_001298477.1.
NP_573301.2. NM_133073.3.
NP_728178.1. NM_167623.2.
UniGeneiDm.7692.

3D structure databases

ProteinModelPortaliQ8MV48.
SMRiQ8MV48. Positions 115-584.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi59149. 4 interactions.
IntActiQ8MV48. 4 interactions.
MINTiMINT-325977.
STRINGi7227.FBpp0074396.

Protein family/group databases

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

Proteomic databases

PaxDbiQ8MV48.
PRIDEiQ8MV48.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0074624; FBpp0074395; FBgn0030930.
FBtr0074625; FBpp0074396; FBgn0030930.
FBtr0346082; FBpp0311917; FBgn0030930.
GeneIDi32836.
KEGGidme:Dmel_CG6394.

Organism-specific databases

CTDi32836.
FlyBaseiFBgn0030930. GalNAc-T2.

Phylogenomic databases

eggNOGiKOG3736. Eukaryota.
ENOG410XPMK. LUCA.
InParanoidiQ8MV48.
KOiK00710.
OMAiFDDTHKE.
OrthoDBiEOG091G085O.
PhylomeDBiQ8MV48.

Enzyme and pathway databases

UniPathwayiUPA00378.

Miscellaneous databases

GenomeRNAii32836.
PROiQ8MV48.

Gene expression databases

BgeeiFBgn0030930.
ExpressionAtlasiQ8MV48. differential.
GenevisibleiQ8MV48. 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.
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...

Entry informationi

Entry nameiGALT7_DROME
AccessioniPrimary (citable) accession number: Q8MV48
Secondary accession number(s): A4V4R2
, Q5U0W9, Q95RJ3, Q95TN2, Q9VWT6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: August 16, 2004
Last modified: September 7, 2016
This is version 112 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

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 one 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.