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Q8IA44

- GLT12_DROME

UniProt

Q8IA44 - GLT12_DROME

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Protein

Putative polypeptide N-acetylgalactosaminyltransferase 12

Gene

pgant12

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli

Functioni

May catalyze 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.By similarity

Catalytic activityi

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

Cofactori

Mn2+By similarity

Pathwayi

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. multicellular organism reproduction Source: FlyBase
  2. oligosaccharide biosynthetic process Source: UniProtKB
  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.
UniPathwayiUPA00378.

Protein family/group databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
Putative polypeptide N-acetylgalactosaminyltransferase 12 (EC:2.4.1.41)
Short name:
pp-GaNTase 12
Alternative name(s):
Protein-UDP acetylgalactosaminyltransferase 12
UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 12
Gene namesi
Name:pgant12
ORF Names:CG7304
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803: Chromosome 3L

Organism-specific databases

FlyBaseiFBgn0036527. CG7304.

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 – 563534LumenalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. Golgi apparatus Source: UniProtKB-KW
  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 – 563563Putative polypeptide N-acetylgalactosaminyltransferase 12PRO_0000059166Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi50 – 501N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi97 ↔ 334PROSITE-ProRule annotation
Glycosylationi389 – 3891N-linked (GlcNAc...)Sequence Analysis
Glycosylationi428 – 4281N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi446 ↔ 461PROSITE-ProRule annotation
Glycosylationi464 – 4641N-linked (GlcNAc...)Sequence Analysis
Glycosylationi469 – 4691N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi485 ↔ 499PROSITE-ProRule annotation
Disulfide bondi523 ↔ 537PROSITE-ProRule annotation
Glycosylationi552 – 5521N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PRIDEiQ8IA44.

Expressioni

Gene expression databases

BgeeiQ8IA44.

Interactioni

Protein-protein interaction databases

STRINGi7227.FBpp0075329.

Structurei

3D structure databases

ProteinModelPortaliQ8IA44.
SMRiQ8IA44. Positions 46-560.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini433 – 549117Ricin B-type lectinPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni109 – 225117Catalytic subdomain AAdd
BLAST
Regioni280 – 34263Catalytic 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

eggNOGiNOG252016.
GeneTreeiENSGT00670000097647.
InParanoidiQ8IA44.
KOiK00710.
OMAiQVPCSRV.
OrthoDBiEOG79CXZ1.
PhylomeDBiQ8IA44.

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.

Q8IA44-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MEVFASVLNC CFKYIVLPVW IFIVLLLLHR DLSSWDGLMG PLSHPGLGEN
60 70 80 90 100
GSASYLSVPS WEIDEYTQGW RYYLYNSWLA ERIPLRRSLP DLRDHRCQKL
110 120 130 140 150
EYDEDSDEMK PASIIMIFRN EQLVVLLRTL HSLVERTPKY LYIELILVND
160 170 180 190 200
HSDTDFWNDK LSLIFFDNYV HRYIHPKARI LHLPEQVGLI KARNLAASEA
210 220 230 240 250
KAENLVFVDA QVEFTNGWLS PLLDTIAEQS YTLATPILDN LDEQTLAYQR
260 270 280 290 300
SIERRGMYDW SLTRREVPLS RARRSHLPWP YEVAAVRTSV FAIPAVWFQD
310 320 330 340 350
ISNFDNNLRG FGAAELELSF KVWCTGGRIV QVPCSRVGHL QPKDEDYLKR
360 370 380 390 400
YGDLHKMGEQ KSRNLKRIIE VWTGDLKSAI YKYQPHLLNI SEGDLNEPRK
410 420 430 440 450
LYKQNECQSF KEFINDITPG LNHVAALNRT DYASGHVKTL EFPKKCLTIN
460 470 480 490 500
AKSQNLFLER CSTNNTLQNW TLTYVKDLRV AGNICAEVRP NLRLGYSFCH
510 520 530 540 550
SLGGRQSWHY DSVSNQLMSN TKCLEFTDEL NIFLAICDAA NGKQRWILDN
560
INLSVMQSAN ILV
Length:563
Mass (Da):65,108
Last modified:March 1, 2003 - v1
Checksum:iF56D71430BD88B36
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF324750 mRNA. Translation: AAN75749.1.
AE014296 Genomic DNA. Translation: AAS64999.1.
RefSeqiNP_996098.1. NM_206376.1.
UniGeneiDm.14885.

Genome annotation databases

EnsemblMetazoaiFBtr0075577; FBpp0075330; FBgn0036527.
GeneIDi39713.
KEGGidme:Dmel_CG7304.
UCSCiCG7304-RA. d. melanogaster.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF324750 mRNA. Translation: AAN75749.1 .
AE014296 Genomic DNA. Translation: AAS64999.1 .
RefSeqi NP_996098.1. NM_206376.1.
UniGenei Dm.14885.

3D structure databases

ProteinModelPortali Q8IA44.
SMRi Q8IA44. Positions 46-560.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 7227.FBpp0075329.

Protein family/group databases

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

Proteomic databases

PRIDEi Q8IA44.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblMetazoai FBtr0075577 ; FBpp0075330 ; FBgn0036527 .
GeneIDi 39713.
KEGGi dme:Dmel_CG7304.
UCSCi CG7304-RA. d. melanogaster.

Organism-specific databases

FlyBasei FBgn0036527. CG7304.

Phylogenomic databases

eggNOGi NOG252016.
GeneTreei ENSGT00670000097647.
InParanoidi Q8IA44.
KOi K00710.
OMAi QVPCSRV.
OrthoDBi EOG79CXZ1.
PhylomeDBi Q8IA44.

Enzyme and pathway databases

UniPathwayi UPA00378 .
Reactomei REACT_231871. O-linked glycosylation of mucins.

Miscellaneous databases

GenomeRNAii 39713.
NextBioi 815001.

Gene expression databases

Bgeei Q8IA44.

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. "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].
  2. "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.
  3. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.

Entry informationi

Entry nameiGLT12_DROME
AccessioniPrimary (citable) accession number: Q8IA44
Secondary accession number(s): Q9VUT4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: March 1, 2003
Last modified: November 26, 2014
This is version 88 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Caution

Although strongly related to polypeptide N-acetylgalactosaminyltransferase proteins, it lacks the conserved Asp-Xaa-His motif in positions 209-211 and the conserved His residue in position 211. This suggests that it may have lost its activity.Curated

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