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Q6WV17

- GALT5_DROME

UniProt

Q6WV17 - GALT5_DROME

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Protein

Polypeptide N-acetylgalactosaminyltransferase 5

Gene

pgant5

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 EA2 as substrate.

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 sitei227 – 2271SubstrateBy similarity
Binding sitei257 – 2571SubstrateBy similarity
Metal bindingi280 – 2801ManganeseBy similarity
Metal bindingi282 – 2821ManganeseBy similarity
Binding sitei387 – 3871SubstrateBy similarity
Metal bindingi415 – 4151ManganeseBy similarity
Binding sitei418 – 4181SubstrateBy similarity
Binding sitei423 – 4231SubstrateBy 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.
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 5 (EC:2.4.1.41)
Short name:
pp-GaNTase 5
Alternative name(s):
Protein-UDP acetylgalactosaminyltransferase 5
UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 5
Gene namesi
Name:pgant5
ORF Names:CG31651
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803: Chromosome 2L

Organism-specific databases

FlyBaseiFBgn0031681. pgant5.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 2020CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei21 – 3818Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST
Topological domaini39 – 630592LumenalSequence 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 – 630630Polypeptide N-acetylgalactosaminyltransferase 5PRO_0000059159Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi166 – 1661N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi177 ↔ 410PROSITE-ProRule annotation
Disulfide bondi401 ↔ 479PROSITE-ProRule annotation
Disulfide bondi513 ↔ 530PROSITE-ProRule annotation
Disulfide bondi553 ↔ 568PROSITE-ProRule annotation
Disulfide bondi594 ↔ 611PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ6WV17.

Expressioni

Tissue specificityi

Expressed during oogenesis, in the somatically derived follicle cells that surround the developing oocyte, which are involved in the maturation of the oocyte and construction of the egg shell, as well as playing a role in subsequent embryonic pattern formation. During embryonic stages 9-11, expressed in the primordium of the foregut, midgut and hindgut. Expressed in salivary glands from embryonic stage 12 onwards. During embryonic stages 12-13, expressed in the posterior midgut and hindgut. During embryonic stages 14-17, expressed in the hindgut and the posterior spiracles. Expression is also detected in the epidermis and antennomaxillary complex at embryonic stages 16-17. In third instar larvae, ubiquitously expressed in wing, eye-antennal, leg and haltere imaginal disks.2 Publications

Developmental stagei

Expressed throughout embryonic, larval, pupal and adult stages, with increasing levels during larval development. Transcripts are first detected during embryonic stages 9-11.2 Publications

Gene expression databases

BgeeiQ6WV17.

Structurei

3D structure databases

ProteinModelPortaliQ6WV17.
SMRiQ6WV17. Positions 166-623.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini500 – 622123Ricin B-type lectinPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni186 – 296111Catalytic subdomain AAdd
BLAST
Regioni356 – 41863Catalytic 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

eggNOGiNOG239675.
GeneTreeiENSGT00760000118828.
InParanoidiQ6WV17.
KOiK00710.
OMAiETFEYMA.
OrthoDBiEOG7J9VP2.
PhylomeDBiQ6WV17.

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 (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform A (identifier: Q6WV17-1) [UniParc]FASTAAdd to Basket

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
MTFSTFTRKM RGRMRSNTCR IVLLTSLVWV IFDFVLIARY SDCIGKDGWR
60 70 80 90 100
CKRSGEYDVE LPNAERLVDD NQLVDDNEIN TEKSLDGESG GALIMGQGFA
110 120 130 140 150
SGGISMTYPS VVLKKWFLAP SVQEAKGKPG EMGKPVKIPA DMKDLMKEKF
160 170 180 190 200
KENQFNLLAS DMISLNRSLT DVRHEGCRRK HYASKLPTTS IVIVFHNEAW
210 220 230 240 250
TTLLRTVWSV INRSPRALLK EIILVDDASE RDFLGKQLEE YVAKLPVKTF
260 270 280 290 300
VLRTEKRSGL IRARLLGAEH VSGEVITFLD AHCECTEGWL EPLLARIVQN
310 320 330 340 350
RRTVVCPIID VISDETFEYI TASDSTWGGF NWKLNFRWYR VPSREMARRN
360 370 380 390 400
NDRTAPLRTP TMAGGLFSID KDYFYEIGSY DEGMDIWGGE NLEMSFRIWQ
410 420 430 440 450
CGGILEIIPC SHVGHVFRDK SPYTFPGGVA KIVLHNAARV AEVWLDEWRD
460 470 480 490 500
FYYSMSTGAR KASAGDVSDR KALRDRLKCK SFRWYLENVY PESLMPLDYY
510 520 530 540 550
YLGEIRNAET ETCLDTMGRK YNEKVGISYC HGLGGNQVFA YTKRQQIMSD
560 570 580 590 600
DLCLDASSSN GPVNMVRCHN MGGNQEWVYD AEEKWIRHTN TGQCLQRATR
610 620 630
DDANTPLLRP CSYGKGQQWL MESKFKWQAH
Length:630
Mass (Da):72,097
Last modified:August 16, 2004 - v2
Checksum:iA822748C9EC96175
GO
Isoform B (identifier: Q6WV17-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     398-457: IWQCGGILEI...WRDFYYSMST → VWMCGGVLEI...WKEFYYSFYP

Note: No experimental confirmation available.

Show »
Length:630
Mass (Da):72,214
Checksum:i51E9F2F0F41525AE
GO

Sequence cautioni

The sequence AAL25377.1 differs from that shown. Reason: Erroneous termination at position 29. Translated as Trp.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti591 – 5911T → S in AAQ56702. (PubMed:12829714)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei398 – 45760IWQCG…YSMST → VWMCGGVLEIAPCSRVGHVF RKSTPYTFPGGTTEIVNHNN ARLVEVWLDDWKEFYYSFYP in isoform B. CuratedVSP_034631Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014134 Genomic DNA. Translation: AAF52218.2.
AE014134 Genomic DNA. Translation: ABI31292.1.
AY060338 mRNA. Translation: AAL25377.1. Sequence problems.
AY268066 mRNA. Translation: AAQ56702.1.
RefSeqiNP_001036338.1. NM_001042873.2. [Q6WV17-2]
NP_608906.2. NM_135062.4. [Q6WV17-1]
UniGeneiDm.4033.

Genome annotation databases

EnsemblMetazoaiFBtr0079026; FBpp0078663; FBgn0031681. [Q6WV17-1]
GeneIDi326151.
KEGGidme:Dmel_CG31651.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014134 Genomic DNA. Translation: AAF52218.2 .
AE014134 Genomic DNA. Translation: ABI31292.1 .
AY060338 mRNA. Translation: AAL25377.1 . Sequence problems.
AY268066 mRNA. Translation: AAQ56702.1 .
RefSeqi NP_001036338.1. NM_001042873.2. [Q6WV17-2 ]
NP_608906.2. NM_135062.4. [Q6WV17-1 ]
UniGenei Dm.4033.

3D structure databases

ProteinModelPortali Q6WV17.
SMRi Q6WV17. Positions 166-623.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

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

Proteomic databases

PaxDbi Q6WV17.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblMetazoai FBtr0079026 ; FBpp0078663 ; FBgn0031681 . [Q6WV17-1 ]
GeneIDi 326151.
KEGGi dme:Dmel_CG31651.

Organism-specific databases

CTDi 326151.
FlyBasei FBgn0031681. pgant5.

Phylogenomic databases

eggNOGi NOG239675.
GeneTreei ENSGT00760000118828.
InParanoidi Q6WV17.
KOi K00710.
OMAi ETFEYMA.
OrthoDBi EOG7J9VP2.
PhylomeDBi Q6WV17.

Enzyme and pathway databases

UniPathwayi UPA00378 .
BRENDAi 2.4.1.41. 1994.
Reactomei REACT_231871. O-linked glycosylation of mucins.

Miscellaneous databases

ChiTaRSi pgant5. fly.
GenomeRNAii 326151.
NextBioi 847327.
PROi Q6WV17.

Gene expression databases

Bgeei Q6WV17.

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: Head.
  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: NUCLEOTIDE SEQUENCE [MRNA] OF 14-630 (ISOFORM A), ENZYME ACTIVITY, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
    Strain: Canton-S.
    Tissue: Embryo.
  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 nameiGALT5_DROME
AccessioniPrimary (citable) accession number: Q6WV17
Secondary accession number(s): Q0E8T2, Q95T43, Q9VMU3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: August 16, 2004
Last modified: November 26, 2014
This is version 96 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