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Protein

Polypeptide N-acetylgalactosaminyltransferase 2

Gene

pgant2

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript 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 the monoglycosylated Muc5AC-3 as substrate.

Catalytic activityi

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

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 sitei242SubstrateBy similarity1
Binding sitei267SubstrateBy similarity1
Metal bindingi290ManganeseBy similarity1
Binding sitei291SubstrateBy similarity1
Metal bindingi292ManganeseBy similarity1
Binding sitei397SubstrateBy similarity1
Metal bindingi425ManganeseBy similarity1
Binding sitei428SubstrateBy similarity1
Binding sitei431SubstrateBy similarity1
Binding sitei433SubstrateBy similarity1

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

BRENDAi2.4.1.41. 1994.
ReactomeiR-DME-6811436. COPI-independent Golgi-to-ER retrograde traffic.
R-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:
Polypeptide N-acetylgalactosaminyltransferase 2 (EC:2.4.1.41)
Short name:
pp-GaNTase 2
Alternative name(s):
Protein-UDP acetylgalactosaminyltransferase 2
UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 2
Gene namesi
Name:pgant2
ORF Names:CG3254
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 2L

Organism-specific databases

FlyBaseiFBgn0031530. pgant2.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 4CytoplasmicSequence analysis4
Transmembranei5 – 25Helical; Signal-anchor for type II membrane proteinSequence analysisAdd BLAST21
Topological domaini26 – 633LumenalSequence analysisAdd BLAST608

GO - Cellular componenti

  • 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)DescriptionActionsGraphical viewLength
ChainiPRO_00000591561 – 633Polypeptide N-acetylgalactosaminyltransferase 2Add BLAST633

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi192 ↔ 420PROSITE-ProRule annotation
Disulfide bondi411 ↔ 489PROSITE-ProRule annotation
Disulfide bondi521 ↔ 538PROSITE-ProRule annotation
Disulfide bondi561 ↔ 578PROSITE-ProRule annotation
Disulfide bondi602 ↔ 618PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiQ6WV19.
PRIDEiQ6WV19.

Expressioni

Tissue specificityi

Expressed in developing oocytes and egg chambers. No expression observed during embryonic stages 9-11. During embryonic stages 12-13, specific expression is observed in the developing tracheal branches and brain. During embryonic stages 14-17, expression is restricted to the dorsal longitudinal trachea. In third instar larvae imaginal wing disk, expressed in clusters of cells in the presumptive pleura and notum. In eye-antennal imaginal disk, shows a very distinct band of expression at the morphogenetic furrow and weaker expression in the presumptive eye posterior to the furrow, no expression is detected in the presumptive antennal or head region anterior to the furrow. No expression observed in leg or haltere imaginal disks.2 Publications

Developmental stagei

Expressed both maternally and zygotically. Expressed during embryonic, larval, pupal and adult stages. Weakly expressed in the male and female body and correspondingly low levels during early embryonic stages. Significantly expressed from embryonic stage 8-12 hours and reaches maximal levels in the pupae and male head.2 Publications

Gene expression databases

BgeeiFBgn0031530.
GenevisibleiQ6WV19. DM.

Interactioni

Protein-protein interaction databases

STRINGi7227.FBpp0292961.

Structurei

3D structure databases

ProteinModelPortaliQ6WV19.
SMRiQ6WV19.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini508 – 630Ricin B-type lectinPROSITE-ProRule annotationAdd BLAST123

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni201 – 306Catalytic subdomain AAdd BLAST106
Regioni366 – 428Catalytic subdomain BAdd BLAST63

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi67 – 141Gly-richAdd BLAST75

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

eggNOGiKOG3738. Eukaryota.
ENOG410XPRX. LUCA.
GeneTreeiENSGT00760000118828.
HOGENOMiHOG000281220.
InParanoidiQ6WV19.
KOiK00710.
OMAiGKVRWPD.
OrthoDBiEOG091G085O.
PhylomeDBiQ6WV19.

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.

Q6WV19-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRRNIKLIVF VSIIWMFVMV YYFQSSTEKV ENRALRLREV ATAMQQYQDD
60 70 80 90 100
SSSAAAASTA RQWAPAGGGA GPGAAAGAAG SGADDPGGNV ILIGSVKDFE
110 120 130 140 150
RNAVHGLKLN GIVALEETSQ GLSGGTGGPG GRLPVAPSGR GTEVEYFNEA
160 170 180 190 200
GYIRAGALRN GEDPYIRNRF NQEASDALPS NRDIPDTRNP MCRTKKYRED
210 220 230 240 250
LPETSVIITF HNEARSTLLR TIVSVLNRSP EHLIREIVLV DDYSDHPEDG
260 270 280 290 300
LELAKIDKVR VIRNDKREGL VRSRVKGADA AVSSVLTFLD SHVECNEMWL
310 320 330 340 350
EPLLERVRED PTRVVCPVID VISMDNFQYI GASADLRGGF DWNLIFKWEY
360 370 380 390 400
LSPSERAMRH NDPTTAIRTP MIAGGLFVID KAYFNKLGKY DMKMDVWGGE
410 420 430 440 450
NLEISFRVWQ CGGSLEIIPC SRVGHVFRKR HPYTFPGGSG NVFARNTRRA
460 470 480 490 500
AEVWMDDYKQ HYYNAVPLAK NIPFGNIDDR LALKEKLHCK PFKWYLENVY
510 520 530 540 550
PDLQAPDPQE VGQFRQDSTE CLDTMGHLID GTVGIFPCHN TGGNQEWAFT
560 570 580 590 600
KRGEIKHDDL CLTLVTFARG SQVVLKACDD SENQRWIMRE GGLVRHYKIN
610 620 630
VCLDSRDQSQ QGVSAQHCNS ALGTQRWSFG KYA
Length:633
Mass (Da):70,736
Last modified:August 16, 2004 - v2
Checksum:i8DA64F627BCB08DB
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti134P → L in AAQ56700 (PubMed:12829714).Curated1
Sequence conflicti617H → R in AAQ22499 (Ref. 3) Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014134 Genomic DNA. Translation: AAF51113.3.
BT010030 mRNA. Translation: AAQ22499.1.
AY268064 mRNA. Translation: AAQ56700.1.
RefSeqiNP_608773.2. NM_134929.4.
NP_995625.2. NM_205903.3.

Genome annotation databases

EnsemblMetazoaiFBtr0077592; FBpp0099799; FBgn0031530.
FBtr0303992; FBpp0292961; FBgn0031530.
GeneIDi33556.
KEGGidme:Dmel_CG3254.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014134 Genomic DNA. Translation: AAF51113.3.
BT010030 mRNA. Translation: AAQ22499.1.
AY268064 mRNA. Translation: AAQ56700.1.
RefSeqiNP_608773.2. NM_134929.4.
NP_995625.2. NM_205903.3.

3D structure databases

ProteinModelPortaliQ6WV19.
SMRiQ6WV19.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi7227.FBpp0292961.

Protein family/group databases

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

Proteomic databases

PaxDbiQ6WV19.
PRIDEiQ6WV19.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0077592; FBpp0099799; FBgn0031530.
FBtr0303992; FBpp0292961; FBgn0031530.
GeneIDi33556.
KEGGidme:Dmel_CG3254.

Organism-specific databases

CTDi33556.
FlyBaseiFBgn0031530. pgant2.

Phylogenomic databases

eggNOGiKOG3738. Eukaryota.
ENOG410XPRX. LUCA.
GeneTreeiENSGT00760000118828.
HOGENOMiHOG000281220.
InParanoidiQ6WV19.
KOiK00710.
OMAiGKVRWPD.
OrthoDBiEOG091G085O.
PhylomeDBiQ6WV19.

Enzyme and pathway databases

UniPathwayiUPA00378.
BRENDAi2.4.1.41. 1994.
ReactomeiR-DME-6811436. COPI-independent Golgi-to-ER retrograde traffic.
R-DME-913709. O-linked glycosylation of mucins.

Miscellaneous databases

GenomeRNAii33556.
PROiQ6WV19.

Gene expression databases

BgeeiFBgn0031530.
GenevisibleiQ6WV19. 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 nameiGALT2_DROME
AccessioniPrimary (citable) accession number: Q6WV19
Secondary accession number(s): Q7KU27, Q7YU21, Q9VQQ2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: August 16, 2004
Last modified: November 2, 2016
This is version 100 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.