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Protein

Polypeptide N-acetylgalactosaminyltransferase 5

Gene

gly-5

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.

Cofactori

Mn2+By similarity

Pathway: protein glycosylation

This protein is involved in the pathway protein glycosylation, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein glycosylation and in Protein modification.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei215 – 2151SubstrateBy similarity
Binding sitei245 – 2451SubstrateBy similarity
Metal bindingi268 – 2681ManganeseBy similarity
Binding sitei269 – 2691SubstrateBy similarity
Metal bindingi270 – 2701ManganeseBy similarity
Binding sitei376 – 3761SubstrateBy similarity
Metal bindingi404 – 4041ManganeseBy similarity
Binding sitei407 – 4071SubstrateBy similarity
Binding sitei412 – 4121SubstrateBy similarity

GO - Molecular functioni

GO - Biological processi

  • 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 5 (EC:2.4.1.41)
Short name:
pp-GaNTase 5
Alternative name(s):
Protein-UDP acetylgalactosaminyltransferase 5
UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 5
Gene namesi
Name:gly-5
ORF Names:Y39E4B.12
OrganismiCaenorhabditis elegans
Taxonomic identifieri6239 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis
ProteomesiUP000001940 Componenti: Chromosome III

Organism-specific databases

WormBaseiY39E4B.12a; CE24240; WBGene00001630; gly-5.
Y39E4B.12b; CE28119; WBGene00001630; gly-5.
Y39E4B.12c; CE28120; WBGene00001630; gly-5.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1111CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei12 – 3120Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST
Topological domaini32 – 626595LumenalSequence AnalysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 626626Polypeptide N-acetylgalactosaminyltransferase 5PRO_0000059148Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi32 – 321N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi165 ↔ 399PROSITE-ProRule annotation
Glycosylationi338 – 3381N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi390 ↔ 466PROSITE-ProRule annotation
Disulfide bondi502 ↔ 521PROSITE-ProRule annotation
Disulfide bondi544 ↔ 557PROSITE-ProRule annotation
Disulfide bondi583 ↔ 598PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ95ZJ1.
PRIDEiQ95ZJ1.

Interactioni

Protein-protein interaction databases

BioGridi41908. 4 interactions.
DIPiDIP-26207N.
IntActiQ95ZJ1. 3 interactions.
MINTiMINT-1041440.
STRINGi6239.Y39E4B.12a.1.

Structurei

3D structure databases

ProteinModelPortaliQ95ZJ1.
SMRiQ95ZJ1. Positions 133-613.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini488 – 610123Ricin B-type lectinPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni174 – 284111Catalytic subdomain AAdd
BLAST
Regioni345 – 40763Catalytic 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.
InParanoidiQ95ZJ1.
KOiK00710.
OMAiRTCLDSP.
PhylomeDBiQ95ZJ1.

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]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform a (identifier: Q95ZJ1-1) [UniParc]FASTAAdd to basket

Also known as: GLY5b, GLY-5b

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MIIFKKKAIL KVLLLVPVFW ICSLIFFAAT SNDSSQIGSN NDLANKIAEA
60 70 80 90 100
NFHPKAAKQD VIQGFGPPIE PEPVVENNKV EEEEQPGGNL AKPKFMVDPN
110 120 130 140 150
DPIYKKGDAA QAGELGKAVV VDKTKLSTEE KAKYDKGMLN NAFNQYASDM
160 170 180 190 200
ISVHRTLPTN IDAECKTEKY NENLPRTSVI ICFHNEAWSV LLRTVHSVLE
210 220 230 240 250
RTPDHLLEEV VLVDDFSDMD HTKRPLEEYM SQFGGKVKIL RMEKREGLIR
260 270 280 290 300
ARLRGAAVAT GEVLTYLDSH CECMEGWMEP LLDRIKRDPT TVVCPVIDVI
310 320 330 340 350
DDNTFEYHHS KAYFTSVGGF DWGLQFNWHS IPERDRKNRT RPIDPVRSPT
360 370 380 390 400
MAGGLFSIDK KYFEKLGTYD PGFDIWGGEN LELSFKIWMC GGTLEIVPCS
410 420 430 440 450
HVGHVFRKRS PYKWRTGVNV LKRNSIRLAE VWLDDYKTYY YERINNQLGD
460 470 480 490 500
FGDISSRKKL REDLGCKSFK WYLDNIYPEL FVPGESVAKG EVRNSAVQPA
510 520 530 540 550
RCLDCMVGRH EKNRPVGTYQ CHGQGGNQYW MLSKDGEIRR DESCVDYAGS
560 570 580 590 600
DVMVFPCHGM KGNQEWRYNH DTGRLQHAVS QKCLGMTKDG AKLEMVACQY
610 620
DDPYQHWKFK EYNEAKAIEH GAKPPS
Length:626
Mass (Da):71,382
Last modified:August 16, 2004 - v2
Checksum:i561BD0576514B983
GO
Isoform b (identifier: Q95ZJ1-2) [UniParc]FASTAAdd to basket

Also known as: GLY5a, GLY-5a

The sequence of this isoform differs from the canonical sequence as follows:
     492-523: VRNSAVQPARCLDCMVGRHEKNRPVGTYQCHG → MRNAGGKNRQCIDYKPSGGKTVGMYQCHN

Show »
Length:623
Mass (Da):71,014
Checksum:i722AC7E93EF5FE4D
GO
Isoform c (identifier: Q95ZJ1-3) [UniParc]FASTAAdd to basket

Also known as: GLY5c, GLY-5c

The sequence of this isoform differs from the canonical sequence as follows:
     492-523: VRNSAVQPARCLDCMVGRHEKNRPVGTYQCHG → LRNAQTSQCLDSAVGEEVENKAITPYPCHE

Show »
Length:624
Mass (Da):71,103
Checksum:i4959436CAE9916D4
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti361 – 3611K → E in AAC13671 (PubMed:9525933).Curated
Sequence conflicti361 – 3611K → E in AAC13672 (PubMed:9525933).Curated
Sequence conflicti361 – 3611K → E in AAC13673 (PubMed:9525933).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei492 – 52332VRNSA…YQCHG → MRNAGGKNRQCIDYKPSGGK TVGMYQCHN in isoform b. 1 PublicationVSP_011238Add
BLAST
Alternative sequencei492 – 52332VRNSA…YQCHG → LRNAQTSQCLDSAVGEEVEN KAITPYPCHE in isoform c. 1 PublicationVSP_011239Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF031835 mRNA. Translation: AAC13671.1.
AF031836 mRNA. Translation: AAC13672.1.
AF031837 mRNA. Translation: AAC13673.1.
AL110487 Genomic DNA. Translation: CAB54435.1.
AL110487 Genomic DNA. Translation: CAC42369.1.
AL110487 Genomic DNA. Translation: CAC42368.1.
PIRiT42245.
T42246.
T42247.
RefSeqiNP_001022850.1. NM_001027679.4. [Q95ZJ1-1]
NP_001022851.1. NM_001027680.4. [Q95ZJ1-2]
NP_001022852.1. NM_001027681.5. [Q95ZJ1-3]
UniGeneiCel.19665.

Genome annotation databases

EnsemblMetazoaiY39E4B.12a.1; Y39E4B.12a.1; WBGene00001630. [Q95ZJ1-1]
Y39E4B.12a.2; Y39E4B.12a.2; WBGene00001630. [Q95ZJ1-1]
GeneIDi176736.
KEGGicel:CELE_Y39E4B.12.
UCSCiY39E4B.12c. c. elegans. [Q95ZJ1-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF031835 mRNA. Translation: AAC13671.1.
AF031836 mRNA. Translation: AAC13672.1.
AF031837 mRNA. Translation: AAC13673.1.
AL110487 Genomic DNA. Translation: CAB54435.1.
AL110487 Genomic DNA. Translation: CAC42369.1.
AL110487 Genomic DNA. Translation: CAC42368.1.
PIRiT42245.
T42246.
T42247.
RefSeqiNP_001022850.1. NM_001027679.4. [Q95ZJ1-1]
NP_001022851.1. NM_001027680.4. [Q95ZJ1-2]
NP_001022852.1. NM_001027681.5. [Q95ZJ1-3]
UniGeneiCel.19665.

3D structure databases

ProteinModelPortaliQ95ZJ1.
SMRiQ95ZJ1. Positions 133-613.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi41908. 4 interactions.
DIPiDIP-26207N.
IntActiQ95ZJ1. 3 interactions.
MINTiMINT-1041440.
STRINGi6239.Y39E4B.12a.1.

Protein family/group databases

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

Proteomic databases

PaxDbiQ95ZJ1.
PRIDEiQ95ZJ1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiY39E4B.12a.1; Y39E4B.12a.1; WBGene00001630. [Q95ZJ1-1]
Y39E4B.12a.2; Y39E4B.12a.2; WBGene00001630. [Q95ZJ1-1]
GeneIDi176736.
KEGGicel:CELE_Y39E4B.12.
UCSCiY39E4B.12c. c. elegans. [Q95ZJ1-1]

Organism-specific databases

CTDi176736.
WormBaseiY39E4B.12a; CE24240; WBGene00001630; gly-5.
Y39E4B.12b; CE28119; WBGene00001630; gly-5.
Y39E4B.12c; CE28120; WBGene00001630; gly-5.

Phylogenomic databases

eggNOGiNOG239675.
GeneTreeiENSGT00760000118828.
HOGENOMiHOG000038227.
InParanoidiQ95ZJ1.
KOiK00710.
OMAiRTCLDSP.
PhylomeDBiQ95ZJ1.

Enzyme and pathway databases

UniPathwayiUPA00378.

Miscellaneous databases

NextBioi893796.
PROiQ95ZJ1.

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] (ISOFORMS A; B AND C).
    Strain: Bristol N2.
  2. "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 nameiGALT5_CAEEL
AccessioniPrimary (citable) accession number: Q95ZJ1
Secondary accession number(s): O61391
, O61392, O61393, Q95ZJ2, Q9U2J8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: August 16, 2004
Last modified: April 29, 2015
This is version 114 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.