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Q6WV19

- GALT2_DROME

UniProt

Q6WV19 - GALT2_DROME

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Protein

Polypeptide N-acetylgalactosaminyltransferase 2

Gene
pgant2, CG3254
Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - 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

Manganese By similarity.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei242 – 2421Substrate By similarity
Binding sitei267 – 2671Substrate By similarity
Metal bindingi290 – 2901Manganese By similarity
Binding sitei291 – 2911Substrate By similarity
Metal bindingi292 – 2921Manganese By similarity
Binding sitei397 – 3971Substrate By similarity
Metal bindingi425 – 4251Manganese By similarity
Binding sitei428 – 4281Substrate By similarity
Binding sitei431 – 4311Substrate By similarity
Binding sitei433 – 4331Substrate By similarity

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. polypeptide N-acetylgalactosaminyltransferase activity Source: UniProtKB

GO - Biological processi

  1. oligosaccharide biosynthetic process Source: UniProtKB
  2. 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.
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
ProteomesiUP000000803: Chromosome 2L

Organism-specific databases

FlyBaseiFBgn0031530. pgant2.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 44Cytoplasmic Reviewed prediction
Transmembranei5 – 2521Helical; Signal-anchor for type II membrane protein; Reviewed predictionAdd
BLAST
Topological domaini26 – 633608Lumenal Reviewed predictionAdd
BLAST

GO - Cellular componenti

  1. Golgi membrane Source: UniProtKB-SubCell
  2. Golgi stack Source: UniProtKB
  3. 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 – 633633Polypeptide N-acetylgalactosaminyltransferase 2PRO_0000059156Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi192 ↔ 420 By similarity
Disulfide bondi411 ↔ 489 By similarity
Disulfide bondi521 ↔ 538 By similarity
Disulfide bondi561 ↔ 578 By similarity
Disulfide bondi602 ↔ 618 By similarity

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

BgeeiQ6WV19.

Structurei

3D structure databases

ProteinModelPortaliQ6WV19.
SMRiQ6WV19. Positions 170-629.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini508 – 630123Ricin B-type lectinAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni201 – 306106Catalytic subdomain AAdd
BLAST
Regioni366 – 42863Catalytic subdomain BAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi67 – 14175Gly-richAdd
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

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG239675.
GeneTreeiENSGT00750000117385.
HOGENOMiHOG000281220.
InParanoidiQ6WV19.
KOiK00710.
OMAiDDYSDNP.
OrthoDBiEOG7J9VP2.
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

MRRNIKLIVF VSIIWMFVMV YYFQSSTEKV ENRALRLREV ATAMQQYQDD    50
SSSAAAASTA RQWAPAGGGA GPGAAAGAAG SGADDPGGNV ILIGSVKDFE 100
RNAVHGLKLN GIVALEETSQ GLSGGTGGPG GRLPVAPSGR GTEVEYFNEA 150
GYIRAGALRN GEDPYIRNRF NQEASDALPS NRDIPDTRNP MCRTKKYRED 200
LPETSVIITF HNEARSTLLR TIVSVLNRSP EHLIREIVLV DDYSDHPEDG 250
LELAKIDKVR VIRNDKREGL VRSRVKGADA AVSSVLTFLD SHVECNEMWL 300
EPLLERVRED PTRVVCPVID VISMDNFQYI GASADLRGGF DWNLIFKWEY 350
LSPSERAMRH NDPTTAIRTP MIAGGLFVID KAYFNKLGKY DMKMDVWGGE 400
NLEISFRVWQ CGGSLEIIPC SRVGHVFRKR HPYTFPGGSG NVFARNTRRA 450
AEVWMDDYKQ HYYNAVPLAK NIPFGNIDDR LALKEKLHCK PFKWYLENVY 500
PDLQAPDPQE VGQFRQDSTE CLDTMGHLID GTVGIFPCHN TGGNQEWAFT 550
KRGEIKHDDL CLTLVTFARG SQVVLKACDD SENQRWIMRE GGLVRHYKIN 600
VCLDSRDQSQ QGVSAQHCNS ALGTQRWSFG KYA 633
Length:633
Mass (Da):70,736
Last modified:August 16, 2004 - v2
Checksum:i8DA64F627BCB08DB
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti134 – 1341P → L in AAQ56700. 1 Publication
Sequence conflicti617 – 6171H → R in AAQ22499. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE014134 Genomic DNA. Translation: AAF51113.3.
BT010030 mRNA. Translation: AAQ22499.1.
AY268064 mRNA. Translation: AAQ56700.1.
RefSeqiNP_608773.2. NM_134929.3.
NP_995625.2. NM_205903.2.
UniGeneiDm.11992.

Genome annotation databases

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

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE014134 Genomic DNA. Translation: AAF51113.3 .
BT010030 mRNA. Translation: AAQ22499.1 .
AY268064 mRNA. Translation: AAQ56700.1 .
RefSeqi NP_608773.2. NM_134929.3.
NP_995625.2. NM_205903.2.
UniGenei Dm.11992.

3D structure databases

ProteinModelPortali Q6WV19.
SMRi Q6WV19. Positions 170-629.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

CAZyi CBM13. Carbohydrate-Binding Module Family 13.
GT27. Glycosyltransferase Family 27.

Proteomic databases

PaxDbi Q6WV19.
PRIDEi Q6WV19.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblMetazoai FBtr0077592 ; FBpp0099799 ; FBgn0031530 .
FBtr0303992 ; FBpp0292961 ; FBgn0031530 .
GeneIDi 33556.
KEGGi dme:Dmel_CG3254.

Organism-specific databases

CTDi 33556.
FlyBasei FBgn0031530. pgant2.

Phylogenomic databases

eggNOGi NOG239675.
GeneTreei ENSGT00750000117385.
HOGENOMi HOG000281220.
InParanoidi Q6WV19.
KOi K00710.
OMAi DDYSDNP.
OrthoDBi EOG7J9VP2.
PhylomeDBi Q6WV19.

Enzyme and pathway databases

UniPathwayi UPA00378 .
BRENDAi 2.4.1.41. 1994.

Miscellaneous databases

GenomeRNAii 33556.
NextBioi 784182.
PROi Q6WV19.

Gene expression databases

Bgeei Q6WV19.

Family and domain databases

Gene3Di 3.90.550.10. 1 hit.
InterProi IPR001173. Glyco_trans_2-like.
IPR029044. Nucleotide-diphossugar_trans.
IPR000772. Ricin_B_lectin.
[Graphical view ]
Pfami PF00535. Glycos_transf_2. 1 hit.
PF00652. Ricin_B_lectin. 1 hit.
[Graphical view ]
SMARTi SM00458. RICIN. 1 hit.
[Graphical view ]
SUPFAMi SSF50370. SSF50370. 1 hit.
SSF53448. SSF53448. 1 hit.
PROSITEi PS50231. RICIN_B_LECTIN. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: Embryo.
  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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 19-633, ENZYME ACTIVITY, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
    Strain: Canton-S.
    Tissue: Embryo.
  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(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.

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: July 9, 2014
This is version 86 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