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Q8IA43

- GLT10_DROME

UniProt

Q8IA43 - GLT10_DROME

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Protein

Putative polypeptide N-acetylgalactosaminyltransferase 10

Gene

pgant10

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli

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

Mn2+By similarity

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei207 – 2071SubstrateBy similarity
Binding sitei238 – 2381SubstrateBy similarity
Metal bindingi261 – 2611ManganeseBy similarity
Binding sitei262 – 2621SubstrateBy similarity
Metal bindingi263 – 2631ManganeseBy similarity
Binding sitei363 – 3631SubstrateBy similarity
Metal bindingi391 – 3911ManganeseBy similarity

GO - Molecular functioni

  1. carbohydrate binding Source: UniProtKB-KW
  2. metal ion binding Source: UniProtKB-KW
  3. 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

ReactomeiREACT_231871. 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:
Putative polypeptide N-acetylgalactosaminyltransferase 10 (EC:2.4.1.41)
Short name:
pp-GaNTase 10
Alternative name(s):
Protein-UDP acetylgalactosaminyltransferase 10
UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 10
Gene namesi
Name:pgant10
ORF Names:CG31776
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803: Chromosome 2L

Organism-specific databases

FlyBaseiFBgn0051776. CG31776.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 66CytoplasmicSequence Analysis
Transmembranei7 – 2620Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST
Topological domaini27 – 630604LumenalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. Golgi apparatus Source: UniProtKB-KW
  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 – 630630Putative polypeptide N-acetylgalactosaminyltransferase 10PRO_0000059164Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi72 – 721N-linked (GlcNAc...)Sequence Analysis
Glycosylationi84 – 841N-linked (GlcNAc...)Sequence Analysis
Glycosylationi146 – 1461N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi157 ↔ 386PROSITE-ProRule annotation
Glycosylationi168 – 1681N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi377 ↔ 456PROSITE-ProRule annotation
Disulfide bondi496 ↔ 513PROSITE-ProRule annotation
Glycosylationi525 – 5251N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi543 ↔ 559PROSITE-ProRule annotation
Disulfide bondi586 ↔ 606PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PRIDEiQ8IA43.

Expressioni

Tissue specificityi

During embryonic stages 9-11, weakly expressed in the mesoderm. During embryonic stages 12-13, very weak expression is observed in the somatic mesoderm region. No expression detected from stage 14-15. During embryonic stages 16-17, expressed in the epidermis and the antennomaxillary complex. In third instar larvae, expressed ubiquitously in wing, eye-antennal, leg and haltere imaginal disks.1 Publication

Developmental stagei

Expressed both maternally and zygotically. Expressed throughout embryonic and larval stages.1 Publication

Gene expression databases

BgeeiQ8IA43.

Interactioni

Protein-protein interaction databases

STRINGi7227.FBpp0077211.

Structurei

3D structure databases

ProteinModelPortaliQ8IA43.
SMRiQ8IA43. Positions 93-615.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini483 – 618136Ricin B-type lectinPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni166 – 277112Catalytic subdomain AAdd
BLAST
Regioni333 – 39462Catalytic subdomain BAdd
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

Contains 1 ricin B-type lectin domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG254892.
GeneTreeiENSGT00670000097647.
InParanoidiQ8IA43.
KOiK00710.
OMAiNALECKT.
OrthoDBiEOG7J9VP2.
PhylomeDBiQ8IA43.

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.

Q8IA43-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MNVDLRLIVR LLLAILLTSL VTTILMGKQI HRRLVKSMVK TTGEKDSLPA
60 70 80 90 100
RQLPKREISP KVADFPPPLT LNQTELDILK IQRNNSFRLP QQEAIKEWQD
110 120 130 140 150
AIFFKEDSNR RGLGEQGRAV QLPNAKLNPD DFQDFYAELS DRIPLNRSLP
160 170 180 190 200
DTRPISCRKR KYLENLPNVT VIIAFHDEHL SVLLRSITSI INRSPVELLK
210 220 230 240 250
QIVLVDDDSN LPELGQQLEE IVAQNFPKII HILRLPERRG SIKARMEAIR
260 270 280 290 300
VSSCQVLVFL DSHIEVNTNW LPPLLEPIVI NPHIVTRPIL DAISRKTFAY
310 320 330 340 350
AKQNTMTRSG FNWWLESESL PIFPEDKSPD STPYRTPVLS GAMAIDRNYF
360 370 380 390 400
LNLGGFDEQL DTWEAEKFEI SFKVWMCGGM MLYVPCARVG HIGKRPMKSI
410 420 430 440 450
SSPGYHNFLA RNYKRVAEVW MDNYKKYVYD KNPKLYKMAN AGLLFQRKTK
460 470 480 490 500
RNALECKTFD WYMTKVAPDF LKRYLALDSP LVFSGVIESV AFPGFCVDSL
510 520 530 540 550
NCRHTKPVVL ARCTGHNSMP GEHQNWSLTQ DHEIQLTNSK DDCLEAQGLR
560 570 580 590 600
SKSVWLFRCH KNGGNQYWYY NHRHRWIQQG QIWVWCLEAQ LASGHKVGKV
610 620 630
LANKICDKNQ LEQQWKVGRN APYDPQREPH
Length:630
Mass (Da):72,795
Last modified:March 1, 2003 - v1
Checksum:i7E2748165A9293CA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF324751 mRNA. Translation: AAN75750.1.
AE014134 Genomic DNA. Translation: AAF51101.3.
BT022827 mRNA. Translation: AAY55243.1.
RefSeqiNP_722909.2. NM_164538.5.
UniGeneiDm.14884.

Genome annotation databases

EnsemblMetazoaiFBtr0077522; FBpp0077211; FBgn0051776.
GeneIDi33568.
KEGGidme:Dmel_CG31776.
UCSCiCG31776-RA. d. melanogaster.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF324751 mRNA. Translation: AAN75750.1 .
AE014134 Genomic DNA. Translation: AAF51101.3 .
BT022827 mRNA. Translation: AAY55243.1 .
RefSeqi NP_722909.2. NM_164538.5.
UniGenei Dm.14884.

3D structure databases

ProteinModelPortali Q8IA43.
SMRi Q8IA43. Positions 93-615.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 7227.FBpp0077211.

Protein family/group databases

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

Proteomic databases

PRIDEi Q8IA43.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblMetazoai FBtr0077522 ; FBpp0077211 ; FBgn0051776 .
GeneIDi 33568.
KEGGi dme:Dmel_CG31776.
UCSCi CG31776-RA. d. melanogaster.

Organism-specific databases

FlyBasei FBgn0051776. CG31776.

Phylogenomic databases

eggNOGi NOG254892.
GeneTreei ENSGT00670000097647.
InParanoidi Q8IA43.
KOi K00710.
OMAi NALECKT.
OrthoDBi EOG7J9VP2.
PhylomeDBi Q8IA43.

Enzyme and pathway databases

UniPathwayi UPA00378 .
Reactomei REACT_231871. O-linked glycosylation of mucins.

Miscellaneous databases

GenomeRNAii 33568.
NextBioi 784234.

Gene expression databases

Bgeei Q8IA43.

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 [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.
    , 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.
  4. Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M., Park S., Wan K.H., Yu C., Celniker S.E.
    Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
  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 nameiGLT10_DROME
AccessioniPrimary (citable) accession number: Q8IA43
Secondary accession number(s): Q4V529, Q9VQR4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: March 1, 2003
Last modified: November 26, 2014
This is version 86 of the entry and version 1 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