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Q6WV17 (GALT5_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 93. 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:
Polypeptide N-acetylgalactosaminyltransferase 5

Short name=pp-GaNTase 5
EC=2.4.1.41
Alternative name(s):
Protein-UDP acetylgalactosaminyltransferase 5
UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 5
Gene names
Name:pgant5
ORF Names:CG31651
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length630 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 EA2 as substrate.

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 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. Ref.4 Ref.5

Developmental stage

Expressed throughout embryonic, larval, pupal and adult stages, with increasing levels during larval development. Transcripts are first detected during embryonic stages 9-11. 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 caution

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

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform A (identifier: Q6WV17-1)

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.
Isoform B (identifier: Q6WV17-2)

The sequence of this isoform differs from the canonical sequence as follows:
     398-457: IWQCGGILEI...WRDFYYSMST → VWMCGGVLEI...WKEFYYSFYP
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 630630Polypeptide N-acetylgalactosaminyltransferase 5
PRO_0000059159

Regions

Topological domain1 – 2020Cytoplasmic Potential
Transmembrane21 – 3818Helical; Signal-anchor for type II membrane protein; Potential
Topological domain39 – 630592Lumenal Potential
Domain500 – 622123Ricin B-type lectin
Region186 – 296111Catalytic subdomain A
Region356 – 41863Catalytic subdomain B

Sites

Metal binding2801Manganese By similarity
Metal binding2821Manganese By similarity
Metal binding4151Manganese By similarity
Binding site2271Substrate By similarity
Binding site2571Substrate By similarity
Binding site3871Substrate By similarity
Binding site4181Substrate By similarity
Binding site4231Substrate By similarity

Amino acid modifications

Glycosylation1661N-linked (GlcNAc...) Potential
Disulfide bond177 ↔ 410 By similarity
Disulfide bond401 ↔ 479 By similarity
Disulfide bond513 ↔ 530 By similarity
Disulfide bond553 ↔ 568 By similarity
Disulfide bond594 ↔ 611 By similarity

Natural variations

Alternative sequence398 – 45760IWQCG…YSMST → VWMCGGVLEIAPCSRVGHVF RKSTPYTFPGGTTEIVNHNN ARLVEVWLDDWKEFYYSFYP in isoform B.
VSP_034631

Experimental info

Sequence conflict5911T → S in AAQ56702. Ref.4

Sequences

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

Last modified August 16, 2004. Version 2.
Checksum: A822748C9EC96175

FASTA63072,097
        10         20         30         40         50         60 
MTFSTFTRKM RGRMRSNTCR IVLLTSLVWV IFDFVLIARY SDCIGKDGWR CKRSGEYDVE 

        70         80         90        100        110        120 
LPNAERLVDD NQLVDDNEIN TEKSLDGESG GALIMGQGFA SGGISMTYPS VVLKKWFLAP 

       130        140        150        160        170        180 
SVQEAKGKPG EMGKPVKIPA DMKDLMKEKF KENQFNLLAS DMISLNRSLT DVRHEGCRRK 

       190        200        210        220        230        240 
HYASKLPTTS IVIVFHNEAW TTLLRTVWSV INRSPRALLK EIILVDDASE RDFLGKQLEE 

       250        260        270        280        290        300 
YVAKLPVKTF VLRTEKRSGL IRARLLGAEH VSGEVITFLD AHCECTEGWL EPLLARIVQN 

       310        320        330        340        350        360 
RRTVVCPIID VISDETFEYI TASDSTWGGF NWKLNFRWYR VPSREMARRN NDRTAPLRTP 

       370        380        390        400        410        420 
TMAGGLFSID KDYFYEIGSY DEGMDIWGGE NLEMSFRIWQ CGGILEIIPC SHVGHVFRDK 

       430        440        450        460        470        480 
SPYTFPGGVA KIVLHNAARV AEVWLDEWRD FYYSMSTGAR KASAGDVSDR KALRDRLKCK 

       490        500        510        520        530        540 
SFRWYLENVY PESLMPLDYY YLGEIRNAET ETCLDTMGRK YNEKVGISYC HGLGGNQVFA 

       550        560        570        580        590        600 
YTKRQQIMSD DLCLDASSSN GPVNMVRCHN MGGNQEWVYD AEEKWIRHTN TGQCLQRATR 

       610        620        630 
DDANTPLLRP CSYGKGQQWL MESKFKWQAH 

« Hide

Isoform B [UniParc].

Checksum: 51E9F2F0F41525AE
Show »

FASTA63072,214

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: 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE014134 Genomic DNA. Translation: AAF52218.2.
AE014134 Genomic DNA. Translation: ABI31292.1.
AY060338 mRNA. Translation: AAL25377.1. Sequence problems.
AY268066 mRNA. Translation: AAQ56702.1.
RefSeqNP_001036338.1. NM_001042873.2. [Q6WV17-2]
NP_608906.2. NM_135062.4. [Q6WV17-1]
UniGeneDm.4033.

3D structure databases

ProteinModelPortalQ6WV17.
SMRQ6WV17. Positions 166-623.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

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

Proteomic databases

PaxDbQ6WV17.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0079026; FBpp0078663; FBgn0031681. [Q6WV17-1]
GeneID326151.
KEGGdme:Dmel_CG31651.

Organism-specific databases

CTD326151.
FlyBaseFBgn0031681. pgant5.

Phylogenomic databases

eggNOGNOG239675.
GeneTreeENSGT00750000117385.
InParanoidQ6WV17.
KOK00710.
OMAETFEYMA.
OrthoDBEOG7J9VP2.
PhylomeDBQ6WV17.

Enzyme and pathway databases

BRENDA2.4.1.41. 1994.
UniPathwayUPA00378.

Gene expression databases

BgeeQ6WV17.

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

ChiTaRSpgant5. drosophila.
GenomeRNAi326151.
NextBio847327.
PROQ6WV17.

Entry information

Entry nameGALT5_DROME
AccessionPrimary (citable) accession number: Q6WV17
Secondary accession number(s): Q0E8T2, Q95T43, Q9VMU3
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: August 16, 2004
Last modified: July 9, 2014
This is version 93 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