Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q8MVS5

- GLT35_DROME

UniProt

Q8MVS5 - GLT35_DROME

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Polypeptide N-acetylgalactosaminyltransferase 35A

Gene

Pgant35A

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

Mn2+By similarity

Kineticsi

  1. KM=8.5 µM for UDP-GalNAc1 Publication
  2. KM=0.35 mM for EA2 acceptor peptide1 Publication

Pathwayi

Sites

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

ReactomeiREACT_231871. O-linked glycosylation of mucins.
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 – 66CytoplasmicSequence Analysis
Transmembranei7 – 2923Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST
Topological domaini30 – 632603LumenalSequence 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

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 35APRO_0000059168Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi49 – 491N-linked (GlcNAc...)1 Publication
Glycosylationi69 – 691N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi136 ↔ 371PROSITE-ProRule annotation
Glycosylationi264 – 2641N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi362 ↔ 439PROSITE-ProRule annotation
Disulfide bondi493 ↔ 516PROSITE-ProRule annotation
Disulfide bondi539 ↔ 553PROSITE-ProRule annotation
Disulfide bondi580 ↔ 597PROSITE-ProRule annotation

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 109-607.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini526 – 632107Ricin B-type lectinPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni147 – 259113Catalytic subdomain AAdd
BLAST
Regioni317 – 37963Catalytic 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.
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

        10         20         30         40         50
MMQIKRLLCK SCGLGTLLVA VVWLLALLFY SHSLRSSIRS AGWRIDEGNA
60 70 80 90 100
TPRAELSYQA RVTVGCTPNA SITTGESPAA PKPPSDPEQL ELLGVVRNKQ
110 120 130 140 150
DKYIRDIGYK HHAFNALVSN NIGLFRAIPD TRHKVCDRQE TTEAENLPQA
160 170 180 190 200
SIVMCFYNEH KMTLMRSIKT VLERTPSYLL REIILVDDHS DLPELEFHLH
210 220 230 240 250
GDLRARLKYD NLRYIKNEQR EGLIRSRVIG AREAVGDVLV FLDSHIEVNQ
260 270 280 290 300
QWLEPLLRLI KSENATLAVP VIDLINADTF EYTPSPLVRG GFNWGLHFRW
310 320 330 340 350
ENLPEGTLKV PEDFRGPFRS PTMAGGLFAV NRKYFQHLGE YDMAMDIWGG
360 370 380 390 400
ENIEISFRAW QCGGAIKIVP CSRVGHIFRK RRPYTSPDGA NTMLKNSLRL
410 420 430 440 450
AHVWMDQYKD YYLKHEKVPK TYDYGDISDR LKLRERLQCR DFAWYLKNVY
460 470 480 490 500
PELHVPGEES KKSAAAPIFQ PWHSRKRNYV DTFQLRLTGT ELCAAVVAPK
510 520 530 540 550
VKGFWKKGSS LQLQTCRRTP NQLWYETEKA EIVLDKLLCL EASGDAQVTV
560 570 580 590 600
NKCHEMLGDQ QWRHTRNANS PVYNMAKGTC LRAAAPTTGA LISLDLCSKS
610 620 630
NGAGGSWDIV QLKKPTEAEG RAKEARNSDK AL
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.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti72 – 721I → T in AAM62405. (PubMed:11925446)Curated
Sequence conflicti628 – 6281S → T in AAL49213. (PubMed:12537569)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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 109-607.
ModBasei Search...
MobiDBi 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 ENSGT00760000118828.
InParanoidi Q8MVS5.
KOi K00710.
OMAi KCHEMGG.
OrthoDBi EOG7J9VP2.
PhylomeDBi Q8MVS5.

Enzyme and pathway databases

UniPathwayi UPA00378 .
Reactomei REACT_231871. O-linked glycosylation of mucins.
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: November 26, 2014
This is version 98 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