Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

N-acetylgalactosaminyltransferase 7

Gene

GalNAc-T2

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: -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)DescriptionActionsGraphical viewLength
Binding sitei182SubstrateBy similarity1
Binding sitei212SubstrateBy similarity1
Metal bindingi235ManganeseBy similarity1
Metal bindingi237ManganeseBy similarity1
Binding sitei344SubstrateBy similarity1
Metal bindingi372ManganeseBy similarity1
Binding sitei375SubstrateBy similarity1
Binding sitei380SubstrateBy similarity1

GO - Molecular functioni

GO - Biological processi

  • oligosaccharide biosynthetic process Source: UniProtKB
  • protein glycosylation Source: UniProtKB-UniPathway

Keywordsi

Molecular functionGlycosyltransferase, Transferase
LigandLectin, Manganese, Metal-binding

Enzyme and pathway databases

ReactomeiR-DME-913709 O-linked glycosylation of mucins
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 lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraHolometabolaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome X

Organism-specific databases

FlyBaseiFBgn0030930 GalNAc-T2

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 11CytoplasmicSequence analysisAdd BLAST11
Transmembranei12 – 29Helical; Signal-anchor for type II membrane proteinSequence analysisAdd BLAST18
Topological domaini30 – 591LumenalSequence analysisAdd BLAST562

Keywords - Cellular componenti

Golgi apparatus, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000591611 – 591N-acetylgalactosaminyltransferase 7Add BLAST591

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi30N-linked (GlcNAc...) asparagineSequence analysis1
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
Glycosylationi576N-linked (GlcNAc...) asparagineSequence analysis1

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 baseline and differential
GenevisibleiQ8MV48 DM

Interactioni

Protein-protein interaction databases

BioGridi59149, 4 interactors
IntActiQ8MV48, 4 interactors
STRINGi7227.FBpp0074396

Structurei

3D structure databases

ProteinModelPortaliQ8MV48
SMRiQ8MV48
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini466 – 585Ricin B-type lectinPROSITE-ProRule annotationAdd BLAST120

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni141 – 251Catalytic subdomain AAdd BLAST111
Regioni313 – 375Catalytic subdomain BAdd BLAST63

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

eggNOGiKOG3736 Eukaryota
ENOG410XPMK LUCA
InParanoidiQ8MV48
KOiK00710
OMAiNFEYRPV
OrthoDBiEOG091G085O
PhylomeDBiQ8MV48

Family and domain databases

CDDicd00161 RICIN, 1 hit
Gene3Di3.90.550.10, 1 hit
InterProiView protein in InterPro
IPR001173 Glyco_trans_2-like
IPR029044 Nucleotide-diphossugar_trans
IPR035992 Ricin_B-like_lectins
IPR000772 Ricin_B_lectin
PfamiView protein in Pfam
PF00535 Glycos_transf_2, 1 hit
PF00652 Ricin_B_lectin, 1 hit
SMARTiView protein in SMART
SM00458 RICIN, 1 hit
SUPFAMiSSF50370 SSF50370, 1 hit
SSF53448 SSF53448, 1 hit
PROSITEiView protein in PROSITE
PS50231 RICIN_B_LECTIN, 1 hit

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)DescriptionActionsGraphical viewLength
Sequence conflicti84P → S in AAM62412 (PubMed:11925450).Curated1

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
UCSCiCG6394-RB d. melanogaster

Similar proteinsi

Entry informationi

Entry nameiGALT7_DROME
AccessioniPrimary (citable) accession number: Q8MV48
Secondary accession number(s): A4V4R2
, Q5U0W9, Q95RJ3, Q95TN2, Q9VWT6
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: August 16, 2004
Last modified: May 23, 2018
This is version 126 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health