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Q9VUT6 (GALT8_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 94. 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 8

Short name=pp-GaNTase 8
EC=2.4.1.41
Alternative name(s):
Protein-UDP acetylgalactosaminyltransferase 8
UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 8
Gene names
Name:pgant8
ORF Names:CG7297
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length590 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 both EA2 and the diglycosylated Muc5AC-3/13 as substrates, albeit at very low levels fro Muc5AC-3/13.

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. 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. Ref.4 Ref.5

Developmental stage

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. 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 – 590590Polypeptide N-acetylgalactosaminyltransferase 8
PRO_0000059162

Regions

Topological domain1 – 1111Cytoplasmic Potential
Transmembrane12 – 3120Helical; Signal-anchor for type II membrane protein; Potential
Topological domain32 – 590559Lumenal Potential
Domain446 – 573128Ricin B-type lectin
Region127 – 236110Catalytic subdomain A
Region291 – 35363Catalytic subdomain B

Sites

Metal binding2201Manganese By similarity
Metal binding2221Manganese By similarity
Metal binding3501Manganese By similarity
Binding site1681Substrate By similarity
Binding site2211Substrate By similarity
Binding site3221Substrate By similarity
Binding site3531Substrate By similarity

Amino acid modifications

Glycosylation771N-linked (GlcNAc...) Potential
Glycosylation2411N-linked (GlcNAc...) Potential
Disulfide bond117 ↔ 345 By similarity
Disulfide bond336 ↔ 419 By similarity
Disulfide bond459 ↔ 475 By similarity
Disulfide bond502 ↔ 517 By similarity
Disulfide bond546 ↔ 561 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9VUT6 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: B18B759A9FC2B021

FASTA59068,100
        10         20         30         40         50         60 
MCLDIWRHKK KVLPLLLLMA IGSIIYYLYT LKLEGERDES ATSTTSRLER DIRDLQAVFE 

        70         80         90        100        110        120 
SEVIPDLGAL GRPARGNWTE EQLEAIAKSQ RETGYNAWLS KRISPERSLY DMRHRSCKKL 

       130        140        150        160        170        180 
KYPMEKLPSV SVVITYHNEE ASVLLRTLSS LRSRTPIQLL REVILVDDGS TQADEKLNDF 

       190        200        210        220        230        240 
IKIKFLNMVQ HRRITTQVGL MHARVVGAEL ALADVLVFLD SHVEVTKGWL EPLIAPILED 

       250        260        270        280        290        300 
NRTCTTPIID TIDFDNFAYR RGKPSRGFFN WEFNYIQLPL LKEEAVAMPA PHKNPIMNGG 

       310        320        330        340        350        360 
LFAIGREWFS ELGGYDKGLK IWGAEQFELS LKLWLCGGQI LEVPCSRVGH LFRDGNFQIR 

       370        380        390        400        410        420 
YTNKDKNSEK KLISRNYRRV AEIWLDEYKD KLFANMPHLT VIPVGNLAEQ RDLKNRLHCK 

       430        440        450        460        470        480 
PFKWFLDNLA TDFLNLYPIL DPAEYASGVL QSISSPKLCL DRKDPSHGQP KLAPCSSDHV 

       490        500        510        520        530        540 
FPSPEQYWSL TNHRELRSGF YCLEVRNHGV NVHIYQCHGQ SGNQFWSFDS KTHQVISGQQ 

       550        560        570        580        590 
QNFRHCLEAQ PELNAVTSSV CDPKNHKQQW KFGYLNSQRL QHFWDNVKTQ 

« 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]"A Drosophila full-length cDNA resource."
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E.
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE014296 Genomic DNA. Translation: AAF49587.1.
AY070966 mRNA. Translation: AAL48588.1.
RefSeqNP_648800.1. NM_140543.4.
UniGeneDm.6188.

3D structure databases

ProteinModelPortalQ9VUT6.
SMRQ9VUT6. Positions 50-586.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING7227.FBpp0075331.

Protein family/group databases

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

Proteomic databases

PaxDbQ9VUT6.
PRIDEQ9VUT6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0075578; FBpp0075331; FBgn0036529.
GeneID39715.
KEGGdme:Dmel_CG7297.

Organism-specific databases

CTD39715.
FlyBaseFBgn0036529. pgant8.

Phylogenomic databases

eggNOGNOG259651.
GeneTreeENSGT00740000115054.
InParanoidQ9VUT6.
KOK00710.
OMAHRSCKKL.
OrthoDBEOG7J9VP2.
PhylomeDBQ9VUT6.

Enzyme and pathway databases

UniPathwayUPA00378.

Gene expression databases

BgeeQ9VUT6.

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

GenomeRNAi39715.
NextBio815013.

Entry information

Entry nameGALT8_DROME
AccessionPrimary (citable) accession number: Q9VUT6
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: May 1, 2000
Last modified: July 9, 2014
This is version 94 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