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Q8MRC9 (GALT9_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 104. 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Putative polypeptide N-acetylgalactosaminyltransferase 9

Short name=pp-GaNTase 9
EC=2.4.1.41
Alternative name(s):
Protein-UDP acetylgalactosaminyltransferase 9
UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 9
Gene names
Name:pgant9
ORF Names:CG30463
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length650 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.

Tissue specificity

During embryonic stages 9-11, expressed in the developing anterior midgut and amnioserosa. Expressed in the salivary glands from embryonic stage 12 onwards. During embryonic stages 12-13, still expressed in the amnioserosa region. In third instar larvae, expressed ubiquitously in wing, with increased expression in the notum and ventral wing pouch, leg and haltere imaginal disks. In eye-antennal imaginal disk, expressed in the presumptive eye region only. Ref.5

Developmental stage

Expressed both maternally and zygotically. Expressed through embryonic and larval stages. 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 caution

The sequence ABL75647.1 differs from that shown. Reason: Intron retention.

The sequence ABL75689.1 differs from that shown. Reason: Intron retention.

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform A (identifier: Q8MRC9-1)

Also known as: D;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Note: No experimental confirmation available.
Isoform B (identifier: Q8MRC9-2)

Also known as: C;

The sequence of this isoform differs from the canonical sequence as follows:
     526-556: RNLGYGGRTCLDAPAGKKHQKKAVGTYPCHR → ANVPNGMCLDAKEKSEEETPVSIYECHG
Note: No experimental confirmation available.
Isoform E (identifier: Q8MRC9-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-383: Missing.
     526-556: RNLGYGGRTCLDAPAGKKHQKKAVGTYPCHR → ANVPNGMCLDAKEKSEEETPVSIYECHG
Note: No experimental confirmation available.
Isoform F (identifier: Q8MRC9-4)

The sequence of this isoform differs from the canonical sequence as follows:
     2-22: AFIWRRRSTTIVKLVAFALAI → NFYLSSWHCQVTQSGLVAGLE
     23-273: Missing.
     526-556: RNLGYGGRTCLDAPAGKKHQKKAVGTYPCHR → ANVPNGMCLDAKEKSEEETPVSIYECHG
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 650650Putative polypeptide N-acetylgalactosaminyltransferase 9
PRO_0000059163

Regions

Topological domain1 – 1111Cytoplasmic Potential
Transmembrane12 – 3120Helical; Signal-anchor for type II membrane protein; Potential
Topological domain32 – 650619Lumenal Potential
Domain521 – 643123Ricin B-type lectin
Region208 – 317110Catalytic subdomain A
Region378 – 44063Catalytic subdomain B
Compositional bias43 – 9048Gly-rich

Sites

Metal binding3011Manganese By similarity
Metal binding3031Manganese By similarity
Metal binding4371Manganese By similarity
Binding site2491Substrate By similarity
Binding site2781Substrate By similarity
Binding site3021Substrate By similarity
Binding site4091Substrate By similarity
Binding site4401Substrate By similarity
Binding site4451Substrate By similarity

Amino acid modifications

Glycosylation3211N-linked (GlcNAc...) Potential
Glycosylation3731N-linked (GlcNAc...) Potential
Disulfide bond198 ↔ 432 By similarity
Disulfide bond423 ↔ 499 By similarity
Disulfide bond535 ↔ 554 By similarity
Disulfide bond577 ↔ 590 By similarity
Disulfide bond616 ↔ 631 By similarity

Natural variations

Alternative sequence1 – 383383Missing in isoform E.
VSP_034632
Alternative sequence2 – 2221AFIWR…FALAI → NFYLSSWHCQVTQSGLVAGL E in isoform F.
VSP_034633
Alternative sequence23 – 273251Missing in isoform F.
VSP_034634
Alternative sequence526 – 55631RNLGY…YPCHR → ANVPNGMCLDAKEKSEEETP VSIYECHG in isoform B, isoform E and isoform F.
VSP_034635

Experimental info

Sequence conflict1451N → D in AAM51988. Ref.3
Sequence conflict4541L → P in AAM51988. Ref.3
Sequence conflict4721Y → C in AAM51988. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Isoform A (D) [UniParc].

Last modified August 16, 2004. Version 2.
Checksum: AC847736AD1C07CA

FASTA65073,193
        10         20         30         40         50         60 
MAFIWRRRST TIVKLVAFAL AIWFCIAFLV YTDDTRRRAA QEGAGASGAG SAPGVGGGAG 

        70         80         90        100        110        120 
GLGDPIALAL RNEPAGEDFG INGNVIGGGG QKQAHDEADI PPTVGKHKAD LQAERMRKKA 

       130        140        150        160        170        180 
AEQPKKKPQE DSKKVIDPPA NFEENPGELG KPVRLPKEMS DEMKKAVDDG WTKNAFNQYV 

       190        200        210        220        230        240 
SDLISVHRTL PDPRDAWCKD EARYLTNLPK TDVIICFHNE AWTVLLRTVH SVLDRSPEHL 

       250        260        270        280        290        300 
IGKIILVDDY SDMPHLKRQL EDYFAAYPKV QIIRGQKREG LIRARILGAN HAKSPVLTYL 

       310        320        330        340        350        360 
DSHCECTEGW LEPLLDRIAR NSTTVVCPVI DVISDETLEY HYRDSGGVNV GGFDWNLQFS 

       370        380        390        400        410        420 
WHPVPERERK RHNSTAEPVY SPTMAGGLFS IDREFFDRLG TYDSGFDIWG GENLELSFKT 

       430        440        450        460        470        480 
WMCGGTLEIV PCSHVGHIFR KRSPYKWRSG VNVLKKNSVR LAEVWMDEYS QYYYHRIGND 

       490        500        510        520        530        540 
KGDWGDVSDR RKLRNDLKCK SFKWYLDNIY PELFIPGDSV AHGEIRNLGY GGRTCLDAPA 

       550        560        570        580        590        600 
GKKHQKKAVG TYPCHRQGGN QYWMLSKAGE IRRDDSCLDY AGKDVTLFGC HGGKGNQFWT 

       610        620        630        640        650 
YRENTKQLHH GTSGKCLAIS ESKDKLLMEE CSASLSRQQW TLENYDSSKL 

« Hide

Isoform B (C) [UniParc].

Checksum: A25855E919100BFE
Show »

FASTA64772,860
Isoform E [UniParc].

Checksum: 06D95D4D4B3D00E8
Show »

FASTA26430,256
Isoform F [UniParc].

Checksum: 8AB540EC2C239DF6
Show »

FASTA39645,208

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, ALTERNATIVE SPLICING.
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] (ISOFORM A).
Strain: Berkeley.
Tissue: Embryo.
[4]Stapleton M., Carlson J.W., Frise E., Kapadia B., Park S., Wan K.H., Yu C., Celniker S.E.
Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM F).
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE013599 Genomic DNA. Translation: AAF57964.3.
AE013599 Genomic DNA. Translation: AAF57966.2.
AE013599 Genomic DNA. Translation: ABV53822.1.
AE013599 Genomic DNA. Translation: ABV53823.1.
AE013599 Genomic DNA. Translation: ABV53824.1.
AY121661 mRNA. Translation: AAM51988.1.
BT029588 mRNA. Translation: ABL75647.1. Sequence problems.
BT029630 mRNA. Translation: ABL75689.1. Sequence problems.
RefSeqNP_001097341.1. NM_001103871.1. [Q8MRC9-2]
NP_001097342.1. NM_001103872.1. [Q8MRC9-1]
NP_001097343.1. NM_001103873.1. [Q8MRC9-3]
NP_725602.1. NM_166188.1. [Q8MRC9-1]
NP_725603.2. NM_166189.2. [Q8MRC9-2]
UniGeneDm.24533.

3D structure databases

ProteinModelPortalQ8MRC9.
SMRQ8MRC9. Positions 147-650.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid73174. 1 interaction.
IntActQ8MRC9. 1 interaction.
MINTMINT-964044.

Protein family/group databases

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

Proteomic databases

PaxDbQ8MRC9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0087112; FBpp0086258; FBgn0050463. [Q8MRC9-1]
FBtr0113380; FBpp0112292; FBgn0050463. [Q8MRC9-1]
GeneID246627.
KEGGdme:Dmel_CG30463.
UCSCCG30463-RA. d. melanogaster. [Q8MRC9-1]

Organism-specific databases

FlyBaseFBgn0050463. CG30463.

Phylogenomic databases

eggNOGNOG239675.
GeneTreeENSGT00750000117385.
InParanoidQ8MRC9.
KOK00710.
OMAYNENLPR.
OrthoDBEOG7J9VP2.
PhylomeDBQ8MRC9.

Enzyme and pathway databases

UniPathwayUPA00378.

Gene expression databases

BgeeQ8MRC9.

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

ChiTaRSCG30463. drosophila.
GenomeRNAi246627.
NextBio843268.
PROQ8MRC9.

Entry information

Entry nameGALT9_DROME
AccessionPrimary (citable) accession number: Q8MRC9
Secondary accession number(s): A1A6R7 expand/collapse secondary AC list , A1A6V9, A8DYG1, A8DYG2, A8DYG3, Q0E950, Q9V7T0
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: August 16, 2004
Last modified: July 9, 2014
This is version 104 of the entry and version 2 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