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Q9VUT6

- GALT8_DROME

UniProt

Q9VUT6 - GALT8_DROME

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Protein

Polypeptide N-acetylgalactosaminyltransferase 8

Gene

pgant8

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 both EA2 and the diglycosylated Muc5AC-3/13 as substrates, albeit at very low levels fro Muc5AC-3/13.

Catalytic activityi

UDP-N-acetyl-alpha-D-galactosamine + polypeptide = UDP + N-acetyl-alpha-D-galactosaminyl-polypeptide.1 Publication

Cofactori

Mn2+By similarity

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei168 – 1681SubstrateBy similarity
Metal bindingi220 – 2201ManganeseBy similarity
Binding sitei221 – 2211SubstrateBy similarity
Metal bindingi222 – 2221ManganeseBy similarity
Binding sitei322 – 3221SubstrateBy similarity
Metal bindingi350 – 3501ManganeseBy similarity
Binding sitei353 – 3531SubstrateBy 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:
Polypeptide N-acetylgalactosaminyltransferase 8 (EC:2.4.1.41)
Short name:
pp-GaNTase 8
Alternative name(s):
Protein-UDP acetylgalactosaminyltransferase 8
UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 8
Gene namesi
Name:pgant8
ORF Names:CG7297
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803: Chromosome 3L

Organism-specific databases

FlyBaseiFBgn0036529. pgant8.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1111CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei12 – 3120Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST
Topological domaini32 – 590559LumenalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. Golgi stack Source: UniProtKB
  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 – 590590Polypeptide N-acetylgalactosaminyltransferase 8PRO_0000059162Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi77 – 771N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi117 ↔ 345PROSITE-ProRule annotation
Glycosylationi241 – 2411N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi336 ↔ 419PROSITE-ProRule annotation
Disulfide bondi459 ↔ 475PROSITE-ProRule annotation
Disulfide bondi502 ↔ 517PROSITE-ProRule annotation
Disulfide bondi546 ↔ 561PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ9VUT6.
PRIDEiQ9VUT6.

Expressioni

Tissue specificityi

Expressed in developing oocytes and egg chambers. During embryonic stages 9-11, expressed in the primordium of the foregut, midgut and hindgut. During embryonic stages 12-13, expressed in the posterior midgut and hindgut. During embryonic stages 14-15, expression continues in the hindgut. No expression detected during embryonic stages 16-17 or in third instar larvae imaginal disks.2 Publications

Developmental stagei

Expressed both maternally and zygotically. Weakly expressed during early embryonic stages but increases during 12-24 hours of embryogenesis through larval development and continues to be expressed throughout adulthood, albeit at slightly lower levels in males than females.2 Publications

Gene expression databases

BgeeiQ9VUT6.

Interactioni

Protein-protein interaction databases

STRINGi7227.FBpp0075331.

Structurei

3D structure databases

ProteinModelPortaliQ9VUT6.
SMRiQ9VUT6. Positions 50-586.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini446 – 573128Ricin B-type lectinPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni127 – 236110Catalytic subdomain AAdd
BLAST
Regioni291 – 35363Catalytic 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

eggNOGiNOG259651.
GeneTreeiENSGT00670000097647.
InParanoidiQ9VUT6.
KOiK00710.
OMAiHRSCKKL.
OrthoDBiEOG7J9VP2.
PhylomeDBiQ9VUT6.

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.

Q9VUT6-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MCLDIWRHKK KVLPLLLLMA IGSIIYYLYT LKLEGERDES ATSTTSRLER
60 70 80 90 100
DIRDLQAVFE SEVIPDLGAL GRPARGNWTE EQLEAIAKSQ RETGYNAWLS
110 120 130 140 150
KRISPERSLY DMRHRSCKKL KYPMEKLPSV SVVITYHNEE ASVLLRTLSS
160 170 180 190 200
LRSRTPIQLL REVILVDDGS TQADEKLNDF IKIKFLNMVQ HRRITTQVGL
210 220 230 240 250
MHARVVGAEL ALADVLVFLD SHVEVTKGWL EPLIAPILED NRTCTTPIID
260 270 280 290 300
TIDFDNFAYR RGKPSRGFFN WEFNYIQLPL LKEEAVAMPA PHKNPIMNGG
310 320 330 340 350
LFAIGREWFS ELGGYDKGLK IWGAEQFELS LKLWLCGGQI LEVPCSRVGH
360 370 380 390 400
LFRDGNFQIR YTNKDKNSEK KLISRNYRRV AEIWLDEYKD KLFANMPHLT
410 420 430 440 450
VIPVGNLAEQ RDLKNRLHCK PFKWFLDNLA TDFLNLYPIL DPAEYASGVL
460 470 480 490 500
QSISSPKLCL DRKDPSHGQP KLAPCSSDHV FPSPEQYWSL TNHRELRSGF
510 520 530 540 550
YCLEVRNHGV NVHIYQCHGQ SGNQFWSFDS KTHQVISGQQ QNFRHCLEAQ
560 570 580 590
PELNAVTSSV CDPKNHKQQW KFGYLNSQRL QHFWDNVKTQ
Length:590
Mass (Da):68,100
Last modified:May 1, 2000 - v1
Checksum:iB18B759A9FC2B021
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014296 Genomic DNA. Translation: AAF49587.1.
AY070966 mRNA. Translation: AAL48588.1.
RefSeqiNP_648800.1. NM_140543.4.
UniGeneiDm.6188.

Genome annotation databases

EnsemblMetazoaiFBtr0075578; FBpp0075331; FBgn0036529.
GeneIDi39715.
KEGGidme:Dmel_CG7297.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014296 Genomic DNA. Translation: AAF49587.1 .
AY070966 mRNA. Translation: AAL48588.1 .
RefSeqi NP_648800.1. NM_140543.4.
UniGenei Dm.6188.

3D structure databases

ProteinModelPortali Q9VUT6.
SMRi Q9VUT6. Positions 50-586.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 7227.FBpp0075331.

Protein family/group databases

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

Proteomic databases

PaxDbi Q9VUT6.
PRIDEi Q9VUT6.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblMetazoai FBtr0075578 ; FBpp0075331 ; FBgn0036529 .
GeneIDi 39715.
KEGGi dme:Dmel_CG7297.

Organism-specific databases

CTDi 39715.
FlyBasei FBgn0036529. pgant8.

Phylogenomic databases

eggNOGi NOG259651.
GeneTreei ENSGT00670000097647.
InParanoidi Q9VUT6.
KOi K00710.
OMAi HRSCKKL.
OrthoDBi EOG7J9VP2.
PhylomeDBi Q9VUT6.

Enzyme and pathway databases

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

Miscellaneous databases

GenomeRNAii 39715.
NextBioi 815013.

Gene expression databases

Bgeei Q9VUT6.

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: ENZYME ACTIVITY, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
  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 nameiGALT8_DROME
AccessioniPrimary (citable) accession number: Q9VUT6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: May 1, 2000
Last modified: November 26, 2014
This is version 97 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