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Q8MVS5 (GLT35_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 95. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Polypeptide N-acetylgalactosaminyltransferase 35A

EC=2.4.1.41
Alternative name(s):
Protein l(2)35Aa
Protein-UDP acetylgalactosaminyltransferase 35A
UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 35A
Short name=pp-GaNTase 35A
dGalNAc-T1
Gene names
Name:Pgant35A
ORF Names:CG7480
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length632 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Essential glycotransferase, which 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.

Catalytic activity

UDP-N-acetyl-alpha-D-galactosamine + polypeptide = UDP + N-acetyl-alpha-D-galactosaminyl-polypeptide. Ref.1 Ref.2

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 at high level in ovaries. Expressed at low level in testis. Expressed at higher level in adult females than males. During oogenesis, it is detected in germ cells and follicle epithelia of all developmental stages. Initially expressed during early stages of oogenesis in region I and reaches high levels in regions IIa and IIb of the germarium. Highly expressed in stage 2 egg chambers. Remains highly expressed during later stages of oogenesis. 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 14-15, expression continues in the hindgut. During embryonic stages 16-17, expressed in the dorsal longitudinal trachea and posterior spiracles. In third instar larvae, ubiquitously expressed in wing, eye-antennal, leg and haltere imaginal disks. Ref.2 Ref.7

Developmental stage

Expressed both maternally and zygotically. Expressed throughout embryonic, larval, pupal and adult stages, with increasing levels during larval development. Ref.1 Ref.2 Ref.7

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.

Miscellaneous

The human ortholog GALNT11 (AC Q8NCW6) is not able to rescue lethality caused by the SF32 mutation (Ref.9).

Sequence similarities

Belongs to the glycosyltransferase 2 family. GalNAc-T subfamily.

Contains 1 ricin B-type lectin domain.

Biophysicochemical properties

Kinetic parameters:

KM=8.5 µM for UDP-GalNAc Ref.1

KM=0.35 mM for EA2 acceptor peptide

Sequence caution

The sequence AAK66862.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 632632Polypeptide N-acetylgalactosaminyltransferase 35A
PRO_0000059168

Regions

Topological domain1 – 66Cytoplasmic Potential
Transmembrane7 – 2923Helical; Signal-anchor for type II membrane protein; Potential
Topological domain30 – 632603Lumenal Potential
Domain526 – 632107Ricin B-type lectin
Region147 – 259113Catalytic subdomain A
Region317 – 37963Catalytic subdomain B

Sites

Metal binding2431Manganese By similarity
Metal binding2451Manganese By similarity
Metal binding3761Manganese By similarity
Binding site1881Substrate By similarity
Binding site2201Substrate By similarity
Binding site2441Substrate By similarity
Binding site3481Substrate By similarity
Binding site3791Substrate By similarity
Binding site3841Substrate By similarity

Amino acid modifications

Glycosylation491N-linked (GlcNAc...) Ref.8
Glycosylation691N-linked (GlcNAc...) Potential
Glycosylation2641N-linked (GlcNAc...) Potential
Disulfide bond136 ↔ 371 By similarity
Disulfide bond362 ↔ 439 By similarity
Disulfide bond493 ↔ 516 By similarity
Disulfide bond539 ↔ 553 By similarity
Disulfide bond580 ↔ 597 By similarity

Experimental info

Mutagenesis2271R → W in SF32; induces lethality. Ref.1 Ref.2
Mutagenesis2431D → N: Abolishes glycosyltransferase activity. Not able to rescue lethality caused by SF32 mutation. Ref.9
Sequence conflict721I → T in AAM62405. Ref.1
Sequence conflict6281S → T in AAL49213. Ref.6

Sequences

Sequence LengthMass (Da)Tools
Q8MVS5 [UniParc].

Last modified August 16, 2004. Version 2.
Checksum: E726B9F32481E4E9

FASTA63271,828
        10         20         30         40         50         60 
MMQIKRLLCK SCGLGTLLVA VVWLLALLFY SHSLRSSIRS AGWRIDEGNA TPRAELSYQA 

        70         80         90        100        110        120 
RVTVGCTPNA SITTGESPAA PKPPSDPEQL ELLGVVRNKQ DKYIRDIGYK HHAFNALVSN 

       130        140        150        160        170        180 
NIGLFRAIPD TRHKVCDRQE TTEAENLPQA SIVMCFYNEH KMTLMRSIKT VLERTPSYLL 

       190        200        210        220        230        240 
REIILVDDHS DLPELEFHLH GDLRARLKYD NLRYIKNEQR EGLIRSRVIG AREAVGDVLV 

       250        260        270        280        290        300 
FLDSHIEVNQ QWLEPLLRLI KSENATLAVP VIDLINADTF EYTPSPLVRG GFNWGLHFRW 

       310        320        330        340        350        360 
ENLPEGTLKV PEDFRGPFRS PTMAGGLFAV NRKYFQHLGE YDMAMDIWGG ENIEISFRAW 

       370        380        390        400        410        420 
QCGGAIKIVP CSRVGHIFRK RRPYTSPDGA NTMLKNSLRL AHVWMDQYKD YYLKHEKVPK 

       430        440        450        460        470        480 
TYDYGDISDR LKLRERLQCR DFAWYLKNVY PELHVPGEES KKSAAAPIFQ PWHSRKRNYV 

       490        500        510        520        530        540 
DTFQLRLTGT ELCAAVVAPK VKGFWKKGSS LQLQTCRRTP NQLWYETEKA EIVLDKLLCL 

       550        560        570        580        590        600 
EASGDAQVTV NKCHEMLGDQ QWRHTRNANS PVYNMAKGTC LRAAAPTTGA LISLDLCSKS 

       610        620        630 
NGAGGSWDIV QLKKPTEAEG RAKEARNSDK AL 

« Hide

References

« Hide 'large scale' references
[1]"A UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase is essential for viability in Drosophila melanogaster."
Ten Hagen K.G., Tran D.T.
J. Biol. Chem. 277:22616-22622(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], ENZYME ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, DEVELOPMENTAL STAGE, MUTAGENESIS OF ARG-227.
Strain: Canton-S.
Tissue: Embryo.
[2]"Functional conservation of subfamilies of putative UDP-N-acetylgalactosamine:polypeptide N-acetylgalactosaminyltransferases in Drosophila, Caenorhabditis elegans, and mammals. One subfamily composed of l(2)35Aa is essential in Drosophila."
Schwientek T., Bennett E.P., Flores C., Thacker J., Hollmann M., Reis C.A., Behrens J., Mandel U., Keck B., Schaefer M.A., Haselmann K., Zubarev R., Roepstorff P., Burchell J.M., Taylor-Papadimitriou J., Hollingsworth M.A., Clausen H.
J. Biol. Chem. 277:22623-22638(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], ENZYME ACTIVITY, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, MUTAGENESIS OF ARG-227.
[3]"An exploration of the sequence of a 2.9-Mb region of the genome of Drosophila melanogaster: the Adh region."
Ashburner M., Misra S., Roote J., Lewis S.E., Blazej R.G., Davis T., Doyle C., Galle R.F., George R.A., Harris N.L., Hartzell G., Harvey D.A., Hong L., Houston K.A., Hoskins R.A., Johnson G., Martin C., Moshrefi A.R. expand/collapse author list , Palazzolo M., Reese M.G., Spradling A.C., Tsang G., Wan K.H., Whitelaw K., Celniker S.E., Rubin G.M.
Genetics 153:179-219(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Berkeley.
[4]"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.
[5]"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.
Strain: Berkeley.
[6]"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].
Strain: Berkeley.
Tissue: Embryo.
[7]"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.
[8]"Identification of N-glycosylated proteins from the central nervous system of Drosophila melanogaster."
Koles K., Lim J.-M., Aoki K., Porterfield M., Tiemeyer M., Wells L., Panin V.
Glycobiology 17:1388-1403(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-49, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: Oregon-R.
Tissue: Head.
[9]"Rescue of Drosophila Melanogaster l(2)35Aa lethality is only mediated by polypeptide GalNAc-transferase pgant35A, but not by the evolutionary conserved human ortholog GalNAc-transferase-T11."
Bennett E.P., Chen Y.W., Schwientek T., Mandel U., Schjoldager K.T., Cohen S.M., Clausen H.
Glycoconj. J. 27:435-444(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF ASP-243.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF478697 mRNA. Translation: AAM62405.1.
AF478698 Genomic DNA. Translation: AAM62406.1.
AF478699 Genomic DNA. Translation: AAM62407.1.
AF478700 Genomic DNA. Translation: AAM62408.1.
AF158747 mRNA. Translation: AAK66862.1. Different initiation.
AE014134 Genomic DNA. Translation: AAF53391.1.
AY071591 mRNA. Translation: AAL49213.1.
RefSeqNP_652069.2. NM_143812.4.
UniGeneDm.1528.

3D structure databases

ProteinModelPortalQ8MVS5.
SMRQ8MVS5. Positions 113-607.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

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

Proteomic databases

PaxDbQ8MVS5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0080629; FBpp0080202; FBgn0001970.
GeneID48775.
KEGGdme:Dmel_CG7480.

Organism-specific databases

CTD48775.
FlyBaseFBgn0001970. Pgant35A.

Phylogenomic databases

eggNOGNOG239675.
GeneTreeENSGT00740000115054.
InParanoidQ8MVS5.
KOK00710.
OMAKCHEMGG.
OrthoDBEOG7J9VP2.
PhylomeDBQ8MVS5.

Enzyme and pathway databases

SABIO-RKQ8MVS5.
UniPathwayUPA00378.

Gene expression databases

BgeeQ8MVS5.

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

GenomeRNAi48775.
NextBio839543.
PROQ8MVS5.

Entry information

Entry nameGLT35_DROME
AccessionPrimary (citable) accession number: Q8MVS5
Secondary accession number(s): Q8MVS2 expand/collapse secondary AC list , Q8MVS3, Q8MVS4, Q8SYF1, Q965E4, Q9V3C9
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: August 16, 2004
Last modified: July 9, 2014
This is version 95 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