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Q6WV20

- GALT1_DROME

UniProt

Q6WV20 - GALT1_DROME

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Protein

Polypeptide N-acetylgalactosaminyltransferase 1

Gene

GalNAc-T1

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 the monoglycosylated Muc5AC-3 as substrate.

Catalytic activityi

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

Cofactori

Manganese.By similarity

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei189 – 1891SubstrateBy similarity
Binding sitei221 – 2211SubstrateBy similarity
Metal bindingi244 – 2441ManganeseBy similarity
Metal bindingi246 – 2461ManganeseBy similarity
Binding sitei358 – 3581SubstrateBy similarity
Metal bindingi386 – 3861ManganeseBy similarity
Binding sitei389 – 3891SubstrateBy similarity
Binding sitei392 – 3921SubstrateBy similarity
Binding sitei394 – 3941SubstrateBy 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

BRENDAi2.4.1.41. 1994.
UniPathwayiUPA00378.

Protein family/group databases

CAZyiCBM13. Carbohydrate-Binding Module Family 13.
GT27. Glycosyltransferase Family 27.

Names & Taxonomyi

Protein namesi
Recommended name:
Polypeptide N-acetylgalactosaminyltransferase 1 (EC:2.4.1.41)
Short name:
pp-GaNTase 1
Alternative name(s):
Protein-UDP acetylgalactosaminyltransferase 1
UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 1
Gene namesi
Name:GalNAc-T1
Synonyms:pgant1
ORF Names:CG8182
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803: Chromosome 2R

Organism-specific databases

FlyBaseiFBgn0034025. GalNAc-T1.

Subcellular locationi

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 – 601601Polypeptide N-acetylgalactosaminyltransferase 1PRO_0000059155Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi127 – 1271N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi138 ↔ 381PROSITE-ProRule annotation
Disulfide bondi372 ↔ 450PROSITE-ProRule annotation
Disulfide bondi485 ↔ 504PROSITE-ProRule annotation
Disulfide bondi528 ↔ 546PROSITE-ProRule annotation
Disulfide bondi571 ↔ 588PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ6WV20.

Expressioni

Tissue specificityi

Expressed in developing oocytes and egg chambers. No expression observed during embryonic stages 9-11. During embryonic stages 12-13, specific expression is observed in the developing tracheal branches and brain. During embryonic stages 14-17, expression is restricted to the dorsal longitudinal trachea. In third instar larvae imaginal wing disk, expressed in clusters of cells in the presumptive pleura and notum. In eye-antennal imaginal disk, shows a very distinct band of expression at the morphogenetic furrow and weaker expression in the presumptive eye posterior to the furrow, no expression is detected in the presumptive antennal or head region anterior to the furrow. No expression observed in leg or haltere imaginal disks.2 Publications

Developmental stagei

Expressed both maternally and zygotically. Expressed throughout embryonic, larval, pupal and adult stages, with increasing levels during larval development.2 Publications

Gene expression databases

BgeeiQ6WV20.

Interactioni

Protein-protein interaction databases

BioGridi62452. 2 interactions.
MINTiMINT-977265.
STRINGi7227.FBpp0086464.

Structurei

3D structure databases

ProteinModelPortaliQ6WV20.
SMRiQ6WV20. Positions 111-597.
ModBaseiSearch...
MobiDBiSearch...

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 77CytoplasmicSequence Analysis
Topological domaini29 – 601573LumenalSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei8 – 2821Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini472 – 600129Ricin B-type lectinPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni148 – 260113Catalytic subdomain AAdd
BLAST
Regioni327 – 38963Catalytic 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

eggNOGiNOG302022.
GeneTreeiENSGT00760000118828.
InParanoidiQ6WV20.
KOiK00710.
OMAiREICPAY.
OrthoDBiEOG7J9VP2.
PhylomeDBiQ6WV20.

Family and domain databases

Gene3Di3.90.550.10. 1 hit.
InterProiIPR027791. Galactosyl_T_C.
IPR001173. Glyco_trans_2-like.
IPR029044. Nucleotide-diphossugar_trans.
IPR000772. Ricin_B_lectin.
[Graphical view]
PfamiPF02709. Glyco_transf_7C. 1 hit.
PF00535. 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.

Q6WV20 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MLPRFRSFYG KLIIFILVAL CFILYSKVQQ NGSPEEPPVA PLVRAAALRG
60 70 80 90 100
HGRERFEAYS DSENEIARPA TQSPYEQIIQ LDLQKQKVGL GEQGVAVHLS
110 120 130 140 150
GAAKERGDEI YKKIALNEEL SEQLTYNRSV GDHRNPLCAK QRFDSDSLPT
160 170 180 190 200
ASVVIIFFNE PYSVLLRTVH STLSTCNEKA LKEIILVDDG SDNVELGAKL
210 220 230 240 250
DYYVRTRIPS GKVTILRLKN RLGLIRARLA GARIATGDVL IFLDAHCEGN
260 270 280 290 300
IGWCEPLLQR IKESRTSVLV PIIDVIDAND FQYSTNGYKS FQVGGFQWNG
310 320 330 340 350
HFDWINLPER EKQRQRRECK QEREICPAYS PTMAGGLFAI DRRYFWEVGS
360 370 380 390 400
YDEQMDGWGG ENLEMSFRIW QCGGTIETIP CSRVGHIFRD FHPYKFPNDR
410 420 430 440 450
DTHGINTARM ALVWMDEYIN IFFLNRPDLK FHADIGDVTH RVMLRKKLRC
460 470 480 490 500
KSFEWYLKNI YPEKFVPTKD VQGWGKVHAV NSNICLDDLL QNNEKPYNAG
510 520 530 540 550
LYPCGKVLQK SQLFSFTNTN VLRNELSCAT VQHSESPPYR VVMVPCMEND
560 570 580 590 600
EFNEQWRYEH QHIIHSNTGM CLDHQGLKSL DDAQVAPCDP HSESQRWTIE

H
Length:601
Mass (Da):68,961
Last modified:August 16, 2004 - v2
Checksum:i81BAF81E04C35BC2
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti146 – 1461D → E in AAQ56699. (PubMed:12829714)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY268063 mRNA. Translation: AAQ56699.1.
AF218236 mRNA. Translation: AAG13184.1.
AE013599 Genomic DNA. Translation: AAM70974.1.
AY113411 mRNA. Translation: AAM29416.1.
RefSeqiNP_611043.1. NM_137199.3.
NP_725472.1. NM_166099.2.
UniGeneiDm.3404.

Genome annotation databases

EnsemblMetazoaiFBtr0087331; FBpp0086464; FBgn0034025.
FBtr0087332; FBpp0086465; FBgn0034025.
GeneIDi36717.
KEGGidme:Dmel_CG8182.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY268063 mRNA. Translation: AAQ56699.1 .
AF218236 mRNA. Translation: AAG13184.1 .
AE013599 Genomic DNA. Translation: AAM70974.1 .
AY113411 mRNA. Translation: AAM29416.1 .
RefSeqi NP_611043.1. NM_137199.3.
NP_725472.1. NM_166099.2.
UniGenei Dm.3404.

3D structure databases

ProteinModelPortali Q6WV20.
SMRi Q6WV20. Positions 111-597.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 62452. 2 interactions.
MINTi MINT-977265.
STRINGi 7227.FBpp0086464.

Protein family/group databases

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

Proteomic databases

PaxDbi Q6WV20.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblMetazoai FBtr0087331 ; FBpp0086464 ; FBgn0034025 .
FBtr0087332 ; FBpp0086465 ; FBgn0034025 .
GeneIDi 36717.
KEGGi dme:Dmel_CG8182.

Organism-specific databases

CTDi 36717.
FlyBasei FBgn0034025. GalNAc-T1.

Phylogenomic databases

eggNOGi NOG302022.
GeneTreei ENSGT00760000118828.
InParanoidi Q6WV20.
KOi K00710.
OMAi REICPAY.
OrthoDBi EOG7J9VP2.
PhylomeDBi Q6WV20.

Enzyme and pathway databases

UniPathwayi UPA00378 .
BRENDAi 2.4.1.41. 1994.

Miscellaneous databases

GenomeRNAii 36717.
NextBioi 800028.

Gene expression databases

Bgeei Q6WV20.

Family and domain databases

Gene3Di 3.90.550.10. 1 hit.
InterProi IPR027791. Galactosyl_T_C.
IPR001173. Glyco_trans_2-like.
IPR029044. Nucleotide-diphossugar_trans.
IPR000772. Ricin_B_lectin.
[Graphical view ]
Pfami PF02709. Glyco_transf_7C. 1 hit.
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 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: NUCLEOTIDE SEQUENCE [MRNA], ENZYME ACTIVITY, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
    Strain: Canton-S.
    Tissue: Embryo.
  2. "Cloning of Drosophila protein-UDP acetylgalactosaminyltransferase."
    Farkas R., Medvedova L., Mechler B.M.
    Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "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.
  4. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Embryo.
  6. "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 nameiGALT1_DROME
AccessioniPrimary (citable) accession number: Q6WV20
Secondary accession number(s): Q0E964, Q9V7C8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: August 16, 2004
Last modified: October 29, 2014
This is version 92 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