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Q8MVS5

- GLT35_DROME

UniProt

Q8MVS5 - GLT35_DROME

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Protein
Polypeptide N-acetylgalactosaminyltransferase 35A
Gene
Pgant35A, CG7480
Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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 activityi

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

Cofactori

Manganese By similarity.

Kineticsi

  1. KM=8.5 µM for UDP-GalNAc1 Publication
  2. KM=0.35 mM for EA2 acceptor peptide

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei188 – 1881Substrate By similarity
Binding sitei220 – 2201Substrate By similarity
Metal bindingi243 – 2431Manganese By similarity
Binding sitei244 – 2441Substrate By similarity
Metal bindingi245 – 2451Manganese By similarity
Binding sitei348 – 3481Substrate By similarity
Metal bindingi376 – 3761Manganese By similarity
Binding sitei379 – 3791Substrate By similarity
Binding sitei384 – 3841Substrate By similarity

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. polypeptide N-acetylgalactosaminyltransferase activity Source: UniProtKB
Complete GO annotation...

GO - Biological processi

  1. oligosaccharide biosynthetic process Source: UniProtKB
  2. open tracheal system development Source: FlyBase
  3. protein glycosylation Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Ligandi

Lectin, Manganese, Metal-binding

Enzyme and pathway databases

SABIO-RKQ8MVS5.
UniPathwayiUPA00378.

Protein family/group databases

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

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:Pgant35A
ORF Names:CG7480
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803: Chromosome 2L

Organism-specific databases

FlyBaseiFBgn0001970. Pgant35A.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 66Cytoplasmic Reviewed prediction
Transmembranei7 – 2923Helical; Signal-anchor for type II membrane protein; Reviewed prediction
Add
BLAST
Topological domaini30 – 632603Lumenal Reviewed prediction
Add
BLAST

GO - Cellular componenti

  1. Golgi membrane Source: UniProtKB-SubCell
  2. Golgi stack Source: UniProtKB
  3. integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi227 – 2271R → W in SF32; induces lethality. 2 Publications
Mutagenesisi243 – 2431D → N: Abolishes glycosyltransferase activity. Not able to rescue lethality caused by SF32 mutation. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 632632Polypeptide N-acetylgalactosaminyltransferase 35A
PRO_0000059168Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi49 – 491N-linked (GlcNAc...)1 Publication
Glycosylationi69 – 691N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi136 ↔ 371 By similarity
Glycosylationi264 – 2641N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi362 ↔ 439 By similarity
Disulfide bondi493 ↔ 516 By similarity
Disulfide bondi539 ↔ 553 By similarity
Disulfide bondi580 ↔ 597 By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ8MVS5.

Expressioni

Tissue specificityi

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.2 Publications

Developmental stagei

Expressed both maternally and zygotically. Expressed throughout embryonic, larval, pupal and adult stages, with increasing levels during larval development.3 Publications

Gene expression databases

BgeeiQ8MVS5.

Structurei

3D structure databases

ProteinModelPortaliQ8MVS5.
SMRiQ8MVS5. Positions 113-607.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini526 – 632107Ricin B-type lectin
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni147 – 259113Catalytic subdomain A
Add
BLAST
Regioni317 – 37963Catalytic subdomain B
Add
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

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG239675.
GeneTreeiENSGT00740000115054.
InParanoidiQ8MVS5.
KOiK00710.
OMAiKCHEMGG.
OrthoDBiEOG7J9VP2.
PhylomeDBiQ8MVS5.

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]

Sequencei

Sequence statusi: Complete.

Q8MVS5-1 [UniParc]FASTAAdd to Basket

« Hide

MMQIKRLLCK SCGLGTLLVA VVWLLALLFY SHSLRSSIRS AGWRIDEGNA    50
TPRAELSYQA RVTVGCTPNA SITTGESPAA PKPPSDPEQL ELLGVVRNKQ 100
DKYIRDIGYK HHAFNALVSN NIGLFRAIPD TRHKVCDRQE TTEAENLPQA 150
SIVMCFYNEH KMTLMRSIKT VLERTPSYLL REIILVDDHS DLPELEFHLH 200
GDLRARLKYD NLRYIKNEQR EGLIRSRVIG AREAVGDVLV FLDSHIEVNQ 250
QWLEPLLRLI KSENATLAVP VIDLINADTF EYTPSPLVRG GFNWGLHFRW 300
ENLPEGTLKV PEDFRGPFRS PTMAGGLFAV NRKYFQHLGE YDMAMDIWGG 350
ENIEISFRAW QCGGAIKIVP CSRVGHIFRK RRPYTSPDGA NTMLKNSLRL 400
AHVWMDQYKD YYLKHEKVPK TYDYGDISDR LKLRERLQCR DFAWYLKNVY 450
PELHVPGEES KKSAAAPIFQ PWHSRKRNYV DTFQLRLTGT ELCAAVVAPK 500
VKGFWKKGSS LQLQTCRRTP NQLWYETEKA EIVLDKLLCL EASGDAQVTV 550
NKCHEMLGDQ QWRHTRNANS PVYNMAKGTC LRAAAPTTGA LISLDLCSKS 600
NGAGGSWDIV QLKKPTEAEG RAKEARNSDK AL 632
Length:632
Mass (Da):71,828
Last modified:August 16, 2004 - v2
Checksum:iE726B9F32481E4E9
GO

Sequence cautioni

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti72 – 721I → T in AAM62405. 1 Publication
Sequence conflicti628 – 6281S → T in AAL49213. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
RefSeqiNP_652069.2. NM_143812.4.
UniGeneiDm.1528.

Genome annotation databases

EnsemblMetazoaiFBtr0080629; FBpp0080202; FBgn0001970.
GeneIDi48775.
KEGGidme:Dmel_CG7480.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
RefSeqi NP_652069.2. NM_143812.4.
UniGenei Dm.1528.

3D structure databases

ProteinModelPortali Q8MVS5.
SMRi Q8MVS5. Positions 113-607.
ModBasei Search...

Protein family/group databases

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

Proteomic databases

PaxDbi Q8MVS5.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblMetazoai FBtr0080629 ; FBpp0080202 ; FBgn0001970 .
GeneIDi 48775.
KEGGi dme:Dmel_CG7480.

Organism-specific databases

CTDi 48775.
FlyBasei FBgn0001970. Pgant35A.

Phylogenomic databases

eggNOGi NOG239675.
GeneTreei ENSGT00740000115054.
InParanoidi Q8MVS5.
KOi K00710.
OMAi KCHEMGG.
OrthoDBi EOG7J9VP2.
PhylomeDBi Q8MVS5.

Enzyme and pathway databases

UniPathwayi UPA00378 .
SABIO-RK Q8MVS5.

Miscellaneous databases

GenomeRNAii 48775.
NextBioi 839543.
PROi Q8MVS5.

Gene expression databases

Bgeei Q8MVS5.

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. "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.
    , 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.
    , 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. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  6. 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.

Entry informationi

Entry nameiGLT35_DROME
AccessioniPrimary (citable) accession number: Q8MVS5
Secondary accession number(s): Q8MVS2
, Q8MVS3, Q8MVS4, Q8SYF1, Q965E4, Q9V3C9
Entry historyi
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 statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Miscellaneous

The human ortholog GALNT11 (AC Q8NCW6) is not able to rescue lethality caused by the SF32 mutation (1 Publication).

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

Similar proteinsi