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Q8MRC9

- GALT9_DROME

UniProt

Q8MRC9 - GALT9_DROME

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Protein

Putative polypeptide N-acetylgalactosaminyltransferase 9

Gene

pgant9

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

Manganese.By similarity

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei249 – 2491SubstrateBy similarity
Binding sitei278 – 2781SubstrateBy similarity
Metal bindingi301 – 3011ManganeseBy similarity
Binding sitei302 – 3021SubstrateBy similarity
Metal bindingi303 – 3031ManganeseBy similarity
Binding sitei409 – 4091SubstrateBy similarity
Metal bindingi437 – 4371ManganeseBy similarity
Binding sitei440 – 4401SubstrateBy similarity
Binding sitei445 – 4451SubstrateBy similarity

GO - Molecular functioni

  1. carbohydrate binding Source: UniProtKB-KW
  2. metal ion binding Source: UniProtKB-KW
  3. polypeptide N-acetylgalactosaminyltransferase activity Source: UniProtKB-EC

GO - Biological processi

  1. multicellular organism reproduction Source: FlyBase
  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 9 (EC:2.4.1.41)
Short name:
pp-GaNTase 9
Alternative name(s):
Protein-UDP acetylgalactosaminyltransferase 9
UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 9
Gene namesi
Name:pgant9
ORF Names:CG30463
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803: Chromosome 2R

Organism-specific databases

FlyBaseiFBgn0050463. CG30463.

Subcellular locationi

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 – 650650Putative polypeptide N-acetylgalactosaminyltransferase 9PRO_0000059163Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi198 ↔ 432PROSITE-ProRule annotation
Glycosylationi321 – 3211N-linked (GlcNAc...)Sequence Analysis
Glycosylationi373 – 3731N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi423 ↔ 499PROSITE-ProRule annotation
Disulfide bondi535 ↔ 554PROSITE-ProRule annotation
Disulfide bondi577 ↔ 590PROSITE-ProRule annotation
Disulfide bondi616 ↔ 631PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ8MRC9.

Expressioni

Tissue specificityi

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.1 Publication

Developmental stagei

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

Gene expression databases

BgeeiQ8MRC9.

Interactioni

Protein-protein interaction databases

BioGridi73174. 1 interaction.
IntActiQ8MRC9. 1 interaction.
MINTiMINT-964044.

Structurei

3D structure databases

ProteinModelPortaliQ8MRC9.
SMRiQ8MRC9. Positions 187-644.
ModBaseiSearch...
MobiDBiSearch...

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1111CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini32 – 650619LumenalSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei12 – 3120Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini521 – 643123Ricin B-type lectinPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni208 – 317110Catalytic subdomain AAdd
BLAST
Regioni378 – 44063Catalytic subdomain BAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi43 – 9048Gly-richAdd
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

eggNOGiNOG239675.
GeneTreeiENSGT00760000118828.
InParanoidiQ8MRC9.
KOiK00710.
OMAiYNENLPR.
OrthoDBiEOG7J9VP2.
PhylomeDBiQ8MRC9.

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]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. Align

Isoform A (identifier: Q8MRC9-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MAFIWRRRST TIVKLVAFAL AIWFCIAFLV YTDDTRRRAA QEGAGASGAG
60 70 80 90 100
SAPGVGGGAG GLGDPIALAL RNEPAGEDFG INGNVIGGGG QKQAHDEADI
110 120 130 140 150
PPTVGKHKAD LQAERMRKKA AEQPKKKPQE DSKKVIDPPA NFEENPGELG
160 170 180 190 200
KPVRLPKEMS DEMKKAVDDG WTKNAFNQYV SDLISVHRTL PDPRDAWCKD
210 220 230 240 250
EARYLTNLPK TDVIICFHNE AWTVLLRTVH SVLDRSPEHL IGKIILVDDY
260 270 280 290 300
SDMPHLKRQL EDYFAAYPKV QIIRGQKREG LIRARILGAN HAKSPVLTYL
310 320 330 340 350
DSHCECTEGW LEPLLDRIAR NSTTVVCPVI DVISDETLEY HYRDSGGVNV
360 370 380 390 400
GGFDWNLQFS WHPVPERERK RHNSTAEPVY SPTMAGGLFS IDREFFDRLG
410 420 430 440 450
TYDSGFDIWG GENLELSFKT WMCGGTLEIV PCSHVGHIFR KRSPYKWRSG
460 470 480 490 500
VNVLKKNSVR LAEVWMDEYS QYYYHRIGND KGDWGDVSDR RKLRNDLKCK
510 520 530 540 550
SFKWYLDNIY PELFIPGDSV AHGEIRNLGY GGRTCLDAPA GKKHQKKAVG
560 570 580 590 600
TYPCHRQGGN QYWMLSKAGE IRRDDSCLDY AGKDVTLFGC HGGKGNQFWT
610 620 630 640 650
YRENTKQLHH GTSGKCLAIS ESKDKLLMEE CSASLSRQQW TLENYDSSKL

Note: No experimental confirmation available.

Length:650
Mass (Da):73,193
Last modified:August 16, 2004 - v2
Checksum:iAC847736AD1C07CA
GO
Isoform B (identifier: Q8MRC9-2) [UniParc]FASTAAdd to Basket

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.

Show »
Length:647
Mass (Da):72,860
Checksum:iA25855E919100BFE
GO
Isoform E (identifier: Q8MRC9-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-383: Missing.
     526-556: RNLGYGGRTCLDAPAGKKHQKKAVGTYPCHR → ANVPNGMCLDAKEKSEEETPVSIYECHG

Note: No experimental confirmation available.

Show »
Length:264
Mass (Da):30,256
Checksum:i06D95D4D4B3D00E8
GO
Isoform F (identifier: Q8MRC9-4) [UniParc]FASTAAdd to Basket

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.

Show »
Length:396
Mass (Da):45,208
Checksum:i8AB540EC2C239DF6
GO

Sequence cautioni

The sequence ABL75647.1 differs from that shown. Reason: Intron retention.
The sequence ABL75689.1 differs from that shown. Reason: Intron retention.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti145 – 1451N → D in AAM51988. (PubMed:12537569)Curated
Sequence conflicti454 – 4541L → P in AAM51988. (PubMed:12537569)Curated
Sequence conflicti472 – 4721Y → C in AAM51988. (PubMed:12537569)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 383383Missing in isoform E. CuratedVSP_034632Add
BLAST
Alternative sequencei2 – 2221AFIWR…FALAI → NFYLSSWHCQVTQSGLVAGL E in isoform F. 1 PublicationVSP_034633Add
BLAST
Alternative sequencei23 – 273251Missing in isoform F. 1 PublicationVSP_034634Add
BLAST
Alternative sequencei526 – 55631RNLGY…YPCHR → ANVPNGMCLDAKEKSEEETP VSIYECHG in isoform B, isoform E and isoform F. 1 PublicationVSP_034635Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
RefSeqiNP_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_166188.2. [Q8MRC9-1]
NP_725603.2. NM_166189.2. [Q8MRC9-2]
UniGeneiDm.24533.

Genome annotation databases

EnsemblMetazoaiFBtr0087112; FBpp0086258; FBgn0050463. [Q8MRC9-1]
FBtr0113380; FBpp0112292; FBgn0050463. [Q8MRC9-1]
GeneIDi246627.
KEGGidme:Dmel_CG30463.
UCSCiCG30463-RA. d. melanogaster. [Q8MRC9-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
RefSeqi NP_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_166188.2. [Q8MRC9-1 ]
NP_725603.2. NM_166189.2. [Q8MRC9-2 ]
UniGenei Dm.24533.

3D structure databases

ProteinModelPortali Q8MRC9.
SMRi Q8MRC9. Positions 187-644.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 73174. 1 interaction.
IntActi Q8MRC9. 1 interaction.
MINTi MINT-964044.

Protein family/group databases

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

Proteomic databases

PaxDbi Q8MRC9.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblMetazoai FBtr0087112 ; FBpp0086258 ; FBgn0050463 . [Q8MRC9-1 ]
FBtr0113380 ; FBpp0112292 ; FBgn0050463 . [Q8MRC9-1 ]
GeneIDi 246627.
KEGGi dme:Dmel_CG30463.
UCSCi CG30463-RA. d. melanogaster. [Q8MRC9-1 ]

Organism-specific databases

FlyBasei FBgn0050463. CG30463.

Phylogenomic databases

eggNOGi NOG239675.
GeneTreei ENSGT00760000118828.
InParanoidi Q8MRC9.
KOi K00710.
OMAi YNENLPR.
OrthoDBi EOG7J9VP2.
PhylomeDBi Q8MRC9.

Enzyme and pathway databases

UniPathwayi UPA00378 .

Miscellaneous databases

ChiTaRSi CG30463. drosophila.
GenomeRNAii 246627.
NextBioi 843268.
PROi Q8MRC9.

Gene expression databases

Bgeei Q8MRC9.

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, ALTERNATIVE SPLICING.
    Strain: Berkeley.
  3. 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.

Entry informationi

Entry nameiGALT9_DROME
AccessioniPrimary (citable) accession number: Q8MRC9
Secondary accession number(s): A1A6R7
, A1A6V9, A8DYG1, A8DYG2, A8DYG3, Q0E950, Q9V7T0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: August 16, 2004
Last modified: October 29, 2014
This is version 106 of the entry and version 2 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