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Q6WV19 (GALT2_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 84. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Polypeptide N-acetylgalactosaminyltransferase 2

Short name=pp-GaNTase 2
EC=2.4.1.41
Alternative name(s):
Protein-UDP acetylgalactosaminyltransferase 2
UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 2
Gene names
Name:pgant2
ORF Names:CG3254
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length633 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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 activity

UDP-N-acetyl-alpha-D-galactosamine + polypeptide = UDP + N-acetyl-alpha-D-galactosaminyl-polypeptide. Ref.4

Cofactor

Manganese By similarity.

Pathway

Protein modification; protein glycosylation.

Subcellular location

Golgi apparatus membrane; Single-pass type II membrane protein By similarity.

Tissue specificity

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. Ref.4 Ref.5

Developmental stage

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. Ref.4 Ref.5

Domain

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 similarities

Belongs to the glycosyltransferase 2 family. GalNAc-T subfamily.

Contains 1 ricin B-type lectin domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 633633Polypeptide N-acetylgalactosaminyltransferase 2
PRO_0000059156

Regions

Topological domain1 – 44Cytoplasmic Potential
Transmembrane5 – 2521Helical; Signal-anchor for type II membrane protein; Potential
Topological domain26 – 633608Lumenal Potential
Domain508 – 630123Ricin B-type lectin
Region201 – 306106Catalytic subdomain A
Region366 – 42863Catalytic subdomain B
Compositional bias67 – 14175Gly-rich

Sites

Metal binding2901Manganese By similarity
Metal binding2921Manganese By similarity
Metal binding4251Manganese By similarity
Binding site2421Substrate By similarity
Binding site2671Substrate By similarity
Binding site2911Substrate By similarity
Binding site3971Substrate By similarity
Binding site4281Substrate By similarity
Binding site4311Substrate By similarity
Binding site4331Substrate By similarity

Amino acid modifications

Disulfide bond192 ↔ 420 By similarity
Disulfide bond411 ↔ 489 By similarity
Disulfide bond521 ↔ 538 By similarity
Disulfide bond561 ↔ 578 By similarity
Disulfide bond602 ↔ 618 By similarity

Experimental info

Sequence conflict1341P → L in AAQ56700. Ref.4
Sequence conflict6171H → R in AAQ22499. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q6WV19 [UniParc].

Last modified August 16, 2004. Version 2.
Checksum: 8DA64F627BCB08DB

FASTA63370,736
        10         20         30         40         50         60 
MRRNIKLIVF VSIIWMFVMV YYFQSSTEKV ENRALRLREV ATAMQQYQDD SSSAAAASTA 

        70         80         90        100        110        120 
RQWAPAGGGA GPGAAAGAAG SGADDPGGNV ILIGSVKDFE RNAVHGLKLN GIVALEETSQ 

       130        140        150        160        170        180 
GLSGGTGGPG GRLPVAPSGR GTEVEYFNEA GYIRAGALRN GEDPYIRNRF NQEASDALPS 

       190        200        210        220        230        240 
NRDIPDTRNP MCRTKKYRED LPETSVIITF HNEARSTLLR TIVSVLNRSP EHLIREIVLV 

       250        260        270        280        290        300 
DDYSDHPEDG LELAKIDKVR VIRNDKREGL VRSRVKGADA AVSSVLTFLD SHVECNEMWL 

       310        320        330        340        350        360 
EPLLERVRED PTRVVCPVID VISMDNFQYI GASADLRGGF DWNLIFKWEY LSPSERAMRH 

       370        380        390        400        410        420 
NDPTTAIRTP MIAGGLFVID KAYFNKLGKY DMKMDVWGGE NLEISFRVWQ CGGSLEIIPC 

       430        440        450        460        470        480 
SRVGHVFRKR HPYTFPGGSG NVFARNTRRA AEVWMDDYKQ HYYNAVPLAK NIPFGNIDDR 

       490        500        510        520        530        540 
LALKEKLHCK PFKWYLENVY PDLQAPDPQE VGQFRQDSTE CLDTMGHLID GTVGIFPCHN 

       550        560        570        580        590        600 
TGGNQEWAFT KRGEIKHDDL CLTLVTFARG SQVVLKACDD SENQRWIMRE GGLVRHYKIN 

       610        620        630 
VCLDSRDQSQ QGVSAQHCNS ALGTQRWSFG KYA 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. expand/collapse author list , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: Berkeley.
[3]Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M., Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A., Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A. expand/collapse author list , Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S., Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.
Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE014134 Genomic DNA. Translation: AAF51113.3.
BT010030 mRNA. Translation: AAQ22499.1.
AY268064 mRNA. Translation: AAQ56700.1.
RefSeqNP_608773.2. NM_134929.3.
NP_995625.2. NM_205903.2.
UniGeneDm.11992.

3D structure databases

ProteinModelPortalQ6WV19.
SMRQ6WV19. Positions 170-629.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyCBM13. Carbohydrate-Binding Module Family 13.
GT27. Glycosyltransferase Family 27.

Proteomic databases

PaxDbQ6WV19.
PRIDEQ6WV19.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0077592; FBpp0099799; FBgn0031530.
FBtr0303992; FBpp0292961; FBgn0031530.
GeneID33556.
KEGGdme:Dmel_CG3254.

Organism-specific databases

CTD33556.
FlyBaseFBgn0031530. pgant2.

Phylogenomic databases

eggNOGNOG239675.
GeneTreeENSGT00750000117385.
HOGENOMHOG000281220.
InParanoidQ6WV19.
KOK00710.
OMADDYSDNP.
OrthoDBEOG7J9VP2.
PhylomeDBQ6WV19.

Enzyme and pathway databases

BRENDA2.4.1.41. 1994.
UniPathwayUPA00378.

Gene expression databases

BgeeQ6WV19.

Family and domain databases

InterProIPR001173. Glyco_trans_2-like.
IPR000772. Ricin_B_lectin.
[Graphical view]
PfamPF00535. Glycos_transf_2. 1 hit.
PF00652. Ricin_B_lectin. 1 hit.
[Graphical view]
SMARTSM00458. RICIN. 1 hit.
[Graphical view]
SUPFAMSSF50370. SSF50370. 1 hit.
PROSITEPS50231. RICIN_B_LECTIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi33556.
NextBio784182.
PROQ6WV19.

Entry information

Entry nameGALT2_DROME
AccessionPrimary (citable) accession number: Q6WV19
Secondary accession number(s): Q7KU27, Q7YU21, Q9VQQ2
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: August 16, 2004
Last modified: April 16, 2014
This is version 84 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase