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Q8IA44 (GLT12_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 85. 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:
Putative polypeptide N-acetylgalactosaminyltransferase 12

Short name=pp-GaNTase 12
EC=2.4.1.41
Alternative name(s):
Protein-UDP acetylgalactosaminyltransferase 12
UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 12
Gene names
Name:pgant12
ORF Names:CG7304
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length563 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

May catalyze 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 By similarity.

Catalytic activity

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

Cofactor

Manganese By similarity.

Pathway

Protein modification; protein glycosylation.

Subcellular location

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

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.

Caution

Although strongly related to polypeptide N-acetylgalactosaminyltransferase proteins, it lacks the conserved Asp-Xaa-His motif in positions 209-211 and the conserved His residue in position 211. This suggests that it may have lost its activity.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 563563Putative polypeptide N-acetylgalactosaminyltransferase 12
PRO_0000059166

Regions

Topological domain1 – 66Cytoplasmic Potential
Transmembrane7 – 2923Helical; Signal-anchor for type II membrane protein; Potential
Topological domain30 – 563534Lumenal Potential
Domain433 – 549117Ricin B-type lectin
Region109 – 225117Catalytic subdomain A
Region280 – 34263Catalytic subdomain B

Amino acid modifications

Glycosylation501N-linked (GlcNAc...) Potential
Glycosylation3891N-linked (GlcNAc...) Potential
Glycosylation4281N-linked (GlcNAc...) Potential
Glycosylation4641N-linked (GlcNAc...) Potential
Glycosylation4691N-linked (GlcNAc...) Potential
Glycosylation5521N-linked (GlcNAc...) Potential
Disulfide bond97 ↔ 334 By similarity
Disulfide bond446 ↔ 461 By similarity
Disulfide bond485 ↔ 499 By similarity
Disulfide bond523 ↔ 537 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8IA44 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: F56D71430BD88B36

FASTA56365,108
        10         20         30         40         50         60 
MEVFASVLNC CFKYIVLPVW IFIVLLLLHR DLSSWDGLMG PLSHPGLGEN GSASYLSVPS 

        70         80         90        100        110        120 
WEIDEYTQGW RYYLYNSWLA ERIPLRRSLP DLRDHRCQKL EYDEDSDEMK PASIIMIFRN 

       130        140        150        160        170        180 
EQLVVLLRTL HSLVERTPKY LYIELILVND HSDTDFWNDK LSLIFFDNYV HRYIHPKARI 

       190        200        210        220        230        240 
LHLPEQVGLI KARNLAASEA KAENLVFVDA QVEFTNGWLS PLLDTIAEQS YTLATPILDN 

       250        260        270        280        290        300 
LDEQTLAYQR SIERRGMYDW SLTRREVPLS RARRSHLPWP YEVAAVRTSV FAIPAVWFQD 

       310        320        330        340        350        360 
ISNFDNNLRG FGAAELELSF KVWCTGGRIV QVPCSRVGHL QPKDEDYLKR YGDLHKMGEQ 

       370        380        390        400        410        420 
KSRNLKRIIE VWTGDLKSAI YKYQPHLLNI SEGDLNEPRK LYKQNECQSF KEFINDITPG 

       430        440        450        460        470        480 
LNHVAALNRT DYASGHVKTL EFPKKCLTIN AKSQNLFLER CSTNNTLQNW TLTYVKDLRV 

       490        500        510        520        530        540 
AGNICAEVRP NLRLGYSFCH SLGGRQSWHY DSVSNQLMSN TKCLEFTDEL NIFLAICDAA 

       550        560 
NGKQRWILDN INLSVMQSAN ILV 

« Hide

References

« Hide 'large scale' references
[1]"Functional conservation of subfamilies of putative UDP-N-acetylgalactosamine:polypeptide N-acetylgalactosaminyltransferases in Drosophila, Caenorhabditis elegans, and mammals. One subfamily composed of l(2)35Aa is essential in Drosophila."
Schwientek T., Bennett E.P., Flores C., Thacker J., Hollmann M., Reis C.A., Behrens J., Mandel U., Keck B., Schaefer M.A., Haselmann K., Zubarev R., Roepstorff P., Burchell J.M., Taylor-Papadimitriou J., Hollingsworth M.A., Clausen H.
J. Biol. Chem. 277:22623-22638(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"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.
[3]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF324750 mRNA. Translation: AAN75749.1.
AE014296 Genomic DNA. Translation: AAS64999.1.
RefSeqNP_996098.1. NM_206376.1.
UniGeneDm.14885.

3D structure databases

ProteinModelPortalQ8IA44.
SMRQ8IA44. Positions 46-560.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING7227.FBpp0075329.

Protein family/group databases

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

Proteomic databases

PRIDEQ8IA44.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0075577; FBpp0075330; FBgn0036527.
GeneID39713.
KEGGdme:Dmel_CG7304.
UCSCCG7304-RA. d. melanogaster.

Organism-specific databases

FlyBaseFBgn0036527. CG7304.

Phylogenomic databases

eggNOGNOG252016.
GeneTreeENSGT00670000097647.
InParanoidQ8IA44.
KOK00710.
OMAQVPCSRV.
OrthoDBEOG79CXZ1.
PhylomeDBQ8IA44.

Enzyme and pathway databases

UniPathwayUPA00378.

Gene expression databases

BgeeQ8IA44.

Family and domain databases

Gene3D3.90.550.10. 1 hit.
InterProIPR001173. Glyco_trans_2-like.
IPR029044. Nucleotide-diphossugar_trans.
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.
SSF53448. SSF53448. 1 hit.
PROSITEPS50231. RICIN_B_LECTIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi39713.
NextBio815001.

Entry information

Entry nameGLT12_DROME
AccessionPrimary (citable) accession number: Q8IA44
Secondary accession number(s): Q9VUT4
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: March 1, 2003
Last modified: July 9, 2014
This is version 85 of the entry and version 1 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