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Q8IA41

- GLT11_DROME

UniProt

Q8IA41 - GLT11_DROME

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Protein
Putative polypeptide N-acetylgalactosaminyltransferase 11
Gene
pgant11, CG7579
Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 4 out of 5 - Protein inferred from homologyi

Functioni

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 activityi

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

Cofactori

Manganese By similarity.

Pathwayi

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

UniPathwayiUPA00378.

Protein family/group databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
Putative polypeptide N-acetylgalactosaminyltransferase 11 (EC:2.4.1.41)
Short name:
pp-GaNTase 11
Alternative name(s):
Protein-UDP acetylgalactosaminyltransferase 11
UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 11
Gene namesi
Name:pgant11
ORF Names:CG7579
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803: Chromosome 3L

Organism-specific databases

FlyBaseiFBgn0036528. CG7579.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 44Cytoplasmic Reviewed prediction
Transmembranei5 – 2723Helical; Signal-anchor for type II membrane protein; Reviewed prediction
Add
BLAST
Topological domaini28 – 557530Lumenal Reviewed prediction
Add
BLAST

GO - Cellular componenti

  1. Golgi membrane Source: UniProtKB-SubCell
  2. 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 – 557557Putative polypeptide N-acetylgalactosaminyltransferase 11
PRO_0000059165Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi33 – 331N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi99 ↔ 325 By similarity
Glycosylationi103 – 1031N-linked (GlcNAc...) Reviewed prediction
Glycosylationi220 – 2201N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi316 ↔ 397 By similarity
Glycosylationi379 – 3791N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi437 ↔ 450 By similarity
Disulfide bondi472 ↔ 486 By similarity
Disulfide bondi511 ↔ 526 By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PRIDEiQ8IA41.

Expressioni

Gene expression databases

BgeeiQ8IA41.

Interactioni

Protein-protein interaction databases

STRINGi7227.FBpp0075334.

Structurei

3D structure databases

ProteinModelPortaliQ8IA41.
SMRiQ8IA41. Positions 65-537.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini456 – 557102Ricin B-type lectin
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni109 – 215107Catalytic subdomain A
Add
BLAST
Regioni271 – 33363Catalytic subdomain B
Add
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

eggNOGiKOG3736.
InParanoidiQ8IA41.
KOiK00710.
OrthoDBiEOG7R56S5.
PhylomeDBiQ8IA41.

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.

Q8IA41-1 [UniParc]FASTAAdd to Basket

« Hide

MKSLLFGTPC SCAIFILVYC IITLFIWFLY TDNLSNAIVD FEYFSIKNLG    50
ELGKEAHLQM TETDLVDAQL QNEKYQYNAW LSERIPLKRT LEDYRDPQCL 100
KINYSSEKTV TVSIVIAIQQ EHPHTLLRGI YSVITQTSPY LLKEIVLVHD 150
GHPDLDLIRH IHHKLPIVIQ LEMESSKGII HARLTGAGVA TGDILVFLNG 200
HMEVTRGWLP PLLEPILLNN QTVTEPIVDA ISRESFAYRK LVEPEQLAFD 250
WQLDHIFLPL DQHSWNSLPK PYPSSQLEGR VFAIDRKWFW HLGGWDEGLR 300
DYGGDALELS LKVWQCGGLI LAVPCSRVGI IYKRDELEAQ MAPNRNPSLQ 350
VQKNFKRVVD VWLDEYKLHF YRYNPKLRNL TAESLDKPRD LRRRLNCKSF 400
EWYRSQVAPQ IRNHFLHAGL TNYPIGKIMP FVAPHFCLSI KGGFPVIRKC 450
HSTNFEDWTL TSRCQLKHGN MCLDVDYKNN VRATKCTKKL SKNPWHYNYQ 500
HSSFVSNGNK CLQIDVNKVG LILSACDSDV TEQRWMFTKV QDFKLDHMRD 550
ICLSVNH 557
Length:557
Mass (Da):64,539
Last modified:March 1, 2003 - v1
Checksum:iB6F58FBAF8DB5F75
GO

Sequence cautioni

The sequence AAF49588.1 differs from that shown. Reason: Erroneous initiation.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF326979 Genomic DNA. Translation: AAO13781.1.
AE014296 Genomic DNA. Translation: AAF49588.1. Different initiation.
RefSeqiNP_648799.1. NM_140542.2.
UniGeneiDm.27150.

Genome annotation databases

GeneIDi39714.
KEGGidme:Dmel_CG7579.
UCSCiCG7579-RA. d. melanogaster.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF326979 Genomic DNA. Translation: AAO13781.1 .
AE014296 Genomic DNA. Translation: AAF49588.1 . Different initiation.
RefSeqi NP_648799.1. NM_140542.2.
UniGenei Dm.27150.

3D structure databases

ProteinModelPortali Q8IA41.
SMRi Q8IA41. Positions 65-537.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 7227.FBpp0075334.

Protein family/group databases

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

Proteomic databases

PRIDEi Q8IA41.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 39714.
KEGGi dme:Dmel_CG7579.
UCSCi CG7579-RA. d. melanogaster.

Organism-specific databases

FlyBasei FBgn0036528. CG7579.

Phylogenomic databases

eggNOGi KOG3736.
InParanoidi Q8IA41.
KOi K00710.
OrthoDBi EOG7R56S5.
PhylomeDBi Q8IA41.

Enzyme and pathway databases

UniPathwayi UPA00378 .

Miscellaneous databases

GenomeRNAii 39714.
NextBioi 815008.

Gene expression databases

Bgeei Q8IA41.

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. "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 [GENOMIC DNA].
  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.
    , 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. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.

Entry informationi

Entry nameiGLT11_DROME
AccessioniPrimary (citable) accession number: Q8IA41
Secondary accession number(s): Q9VUT5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: March 1, 2003
Last modified: July 9, 2014
This is version 84 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Caution

Although strongly related to polypeptide N-acetylgalactosaminyltransferase proteins, it lacks the conserved Asp-Xaa-His motif in positions 199-201 and the conserved His residue in position 330. This suggests that it may have lost its activity.

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