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Protein

Polypeptide N-acetylgalactosaminyltransferase 3

Gene

gly-3

Organism
Caenorhabditis elegans
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

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.

Catalytic activityi

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

Cofactori

Mn2+By similarity

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei210 – 2101SubstrateBy similarity
Binding sitei240 – 2401SubstrateBy similarity
Metal bindingi263 – 2631ManganeseBy similarity
Metal bindingi265 – 2651ManganeseBy similarity
Binding sitei370 – 3701SubstrateBy similarity
Metal bindingi398 – 3981ManganeseBy similarity
Binding sitei401 – 4011SubstrateBy similarity
Binding sitei406 – 4061SubstrateBy similarity

GO - Molecular functioni

  1. carbohydrate binding Source: UniProtKB-KW
  2. metal ion binding Source: UniProtKB-KW
  3. polypeptide N-acetylgalactosaminyltransferase activity Source: WormBase

GO - Biological processi

  1. protein O-linked glycosylation via threonine Source: WormBase
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Ligandi

Lectin, Manganese, Metal-binding

Enzyme and pathway databases

UniPathwayiUPA00378.

Protein family/group databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
Polypeptide N-acetylgalactosaminyltransferase 3 (EC:2.4.1.41)
Alternative name(s):
GalNAc-T1
Protein-UDP acetylgalactosaminyltransferase 3
UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 3
Short name:
pp-GaNTase 3
Gene namesi
Name:gly-3
ORF Names:ZK688.8
OrganismiCaenorhabditis elegans
Taxonomic identifieri6239 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis
ProteomesiUP000001940 Componenti: Chromosome III

Organism-specific databases

WormBaseiZK688.8; CE29649; WBGene00001628; gly-3.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1313CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei14 – 3421Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST
Topological domaini35 – 612578LumenalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. Golgi membrane Source: UniProtKB-SubCell
  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 – 612612Polypeptide N-acetylgalactosaminyltransferase 3PRO_0000059146Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi146 – 1461N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi157 ↔ 393PROSITE-ProRule annotation
Glycosylationi239 – 2391N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi384 ↔ 462PROSITE-ProRule annotation
Disulfide bondi496 ↔ 513PROSITE-ProRule annotation
Disulfide bondi536 ↔ 554PROSITE-ProRule annotation
Disulfide bondi582 ↔ 595PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiP34678.

Interactioni

Protein-protein interaction databases

STRINGi6239.ZK688.8.1.

Structurei

3D structure databases

ProteinModelPortaliP34678.
SMRiP34678. Positions 110-611.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini478 – 607130Ricin B-type lectinPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni169 – 279111Catalytic subdomain AAdd
BLAST
Regioni339 – 40163Catalytic 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.
HOGENOMiHOG000038227.
InParanoidiP34678.
KOiK00710.
OMAiFYDIGSY.
OrthoDBiEOG7J9VP2.
PhylomeDBiP34678.

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.

P34678-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLSVGGGRSA VCRAVIATSI VWLLIDVVIL FYYLDPSTSQ QQPFPEDNRI
60 70 80 90 100
LNRARRIEPL PPAAQHDSDP DAHPIQPEKQ EKQVYPVDKE TANQLRKLME
110 120 130 140 150
TQAFGPGYHG QGGTGVTVPE DKKTIKEKRF LENQFNVVAS EMISVNRTLP
160 170 180 190 200
DYRSDACRTS GNNLKTAGMP KTSIIIVFHN EAWTTLLRTL HSVINRSPRH
210 220 230 240 250
LLEEIILVDD KSDRDYLVKP LDSYIKMFPI PIHLVHLENR SGLIRARLTG
260 270 280 290 300
SEMAKGKILL FLDAHVEVTD GWLEPLVSRV AEDRKRVVAP IIDVISDDTF
310 320 330 340 350
EYVTASETTW GGFNWHLNFR WYAVPKRELN RRGSDRSMPI QTPTIAGGLF
360 370 380 390 400
AIDKQFFYDI GSYDEGMQVW GGENLEISFR VWMCGGSLEI HPCSRVGHVF
410 420 430 440 450
RKQTPYTFPG GTAKVIHHNA ARTAEVWMDE YKAFFYKMVP AARNVEAGDV
460 470 480 490 500
SERKKLRETL QCKSFKWYLE NIYPEAPLPA DFRSLGAIVN RFTEKCVDTN
510 520 530 540 550
GKKDGQAPGI QACHGAGGNQ AWSLTGKGEI RSDDLCLSSG HVYQIGSELK
560 570 580 590 600
LERCSVSKIN VKHVFVFDDQ AGTLLHKKTG KCVTGADQRV TLDECGLGRK
610
DQMWQLEGYQ SP
Length:612
Mass (Da):68,912
Last modified:May 27, 2002 - v2
Checksum:i3031C2FE933F9858
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF031833 mRNA. Translation: AAC13669.1.
FO080277 Genomic DNA. Translation: CCD62541.1.
PIRiA88515.
T42243.
RefSeqiNP_498722.1. NM_066321.5.
UniGeneiCel.17588.

Genome annotation databases

EnsemblMetazoaiZK688.8; ZK688.8; WBGene00001628.
GeneIDi176112.
KEGGicel:CELE_ZK688.8.
UCSCiZK688.8.1. c. elegans.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF031833 mRNA. Translation: AAC13669.1.
FO080277 Genomic DNA. Translation: CCD62541.1.
PIRiA88515.
T42243.
RefSeqiNP_498722.1. NM_066321.5.
UniGeneiCel.17588.

3D structure databases

ProteinModelPortaliP34678.
SMRiP34678. Positions 110-611.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi6239.ZK688.8.1.

Protein family/group databases

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

Proteomic databases

PaxDbiP34678.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiZK688.8; ZK688.8; WBGene00001628.
GeneIDi176112.
KEGGicel:CELE_ZK688.8.
UCSCiZK688.8.1. c. elegans.

Organism-specific databases

CTDi176112.
WormBaseiZK688.8; CE29649; WBGene00001628; gly-3.

Phylogenomic databases

eggNOGiNOG239675.
GeneTreeiENSGT00760000118828.
HOGENOMiHOG000038227.
InParanoidiP34678.
KOiK00710.
OMAiFYDIGSY.
OrthoDBiEOG7J9VP2.
PhylomeDBiP34678.

Enzyme and pathway databases

UniPathwayiUPA00378.

Miscellaneous databases

NextBioi891164.
PROiP34678.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "cDNA cloning and expression of a family of UDP-N-acetyl-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase sequence homologs from Caenorhabditis elegans."
    Hagen F.K., Nehrke K.
    J. Biol. Chem. 273:8268-8277(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], ENZYME ACTIVITY.
    Strain: Bristol N2.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Bristol N2.
  3. "Genome sequence of the nematode C. elegans: a platform for investigating biology."
    The C. elegans sequencing consortium
    Science 282:2012-2018(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Bristol N2.

Entry informationi

Entry nameiGALT3_CAEEL
AccessioniPrimary (citable) accession number: P34678
Secondary accession number(s): Q9U003
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: May 27, 2002
Last modified: January 7, 2015
This is version 124 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programCaenorhabditis annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Caenorhabditis elegans
    Caenorhabditis elegans: entries, gene names and cross-references to WormBase
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.