Reviewed, UniProtKB/Swiss-Prot P34678 (GALT3_CAEEL)

Names and origin

Protein names

Recommended name:
    Polypeptide N-acetylgalactosaminyltransferase 3
    EC=2.4.1.41
Alternative name(s):
    Protein-UDP acetylgalactosaminyltransferase 3
    UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 3
      Short name=pp-GaNTase 3
    GalNAc-T1

Gene names

Name:	gly-3
ORF Names:	ZK688.8

Organism

Caenorhabditis elegans [Complete proteome]

Taxonomic identifier

6239 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Nematoda › Chromadorea › Rhabditida › Rhabditoidea › Rhabditidae › Peloderinae › Caenorhabditis

Protein attributes

Sequence length	612 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	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 activity	UDP-N-acetyl-D-galactosamine + polypeptide = UDP + N-acetyl-D-galactosaminyl-polypeptide. Ref.1
Cofactor	Manganese By similarity. Calcium By similarity.
Pathway	Protein modification; protein glycosylation.
Subcellular location	Golgi apparatus membrane; Single-pass type II membrane protein By similarity.
Domain	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 similarities	Belongs to the glycosyltransferase 2 family. GalNAc-T subfamily. Contains 1 ricin B-type lectin domain.

Ontologies

Keywords
Cellular component	Golgi apparatus Membrane
Domain	Signal-anchor Transmembrane
Ligand	Calcium Lectin Manganese
Molecular function	Glycosyltransferase Transferase
PTM	Disulfide bond Glycoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Cellular component	Golgi membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	calcium ion binding Inferred from electronic annotation. Source: UniProtKB-KW manganese ion binding Inferred from electronic annotation. Source: UniProtKB-KW polypeptide N-acetylgalactosaminyltransferase activity Inferred from electronic annotation. Source: EC sugar binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 612	612	Polypeptide N-acetylgalactosaminyltransferase 3		PRO_0000059146
Regions
	Topological domain	1 – 13	13	Cytoplasmic Potential
	Transmembrane	14 – 34	21	Signal-anchor for type II membrane protein Potential
	Topological domain	35 – 612	578	Lumenal Potential
	Domain	478 – 607	130	Ricin B-type lectin
	Region	169 – 279	111	Catalytic subdomain A
	Region	339 – 401	63	Catalytic subdomain B
Amino acid modifications
	Glycosylation	146	1	N-linked (GlcNAc...) Potential
	Glycosylation	239	1	N-linked (GlcNAc...) Potential
	Disulfide bond	496 ↔ 513		By similarity
	Disulfide bond	536 ↔ 554		By similarity
	Disulfide bond	582 ↔ 595		By similarity

Sequences

	Sequence		Length	Mass (Da)
	P34678-1 [UniParc]. Last modified May 27, 2002. Version 2. Checksum: 3031C2FE933F9858	FASTA	612	68,912
	10 20 30 40 50 60 MLSVGGGRSA VCRAVIATSI VWLLIDVVIL FYYLDPSTSQ QQPFPEDNRI LNRARRIEPL 70 80 90 100 110 120 PPAAQHDSDP DAHPIQPEKQ EKQVYPVDKE TANQLRKLME TQAFGPGYHG QGGTGVTVPE 130 140 150 160 170 180 DKKTIKEKRF LENQFNVVAS EMISVNRTLP DYRSDACRTS GNNLKTAGMP KTSIIIVFHN 190 200 210 220 230 240 EAWTTLLRTL HSVINRSPRH LLEEIILVDD KSDRDYLVKP LDSYIKMFPI PIHLVHLENR 250 260 270 280 290 300 SGLIRARLTG SEMAKGKILL FLDAHVEVTD GWLEPLVSRV AEDRKRVVAP IIDVISDDTF 310 320 330 340 350 360 EYVTASETTW GGFNWHLNFR WYAVPKRELN RRGSDRSMPI QTPTIAGGLF AIDKQFFYDI 370 380 390 400 410 420 GSYDEGMQVW GGENLEISFR VWMCGGSLEI HPCSRVGHVF RKQTPYTFPG GTAKVIHHNA 430 440 450 460 470 480 ARTAEVWMDE YKAFFYKMVP AARNVEAGDV SERKKLRETL QCKSFKWYLE NIYPEAPLPA 490 500 510 520 530 540 DFRSLGAIVN RFTEKCVDTN GKKDGQAPGI QACHGAGGNQ AWSLTGKGEI RSDDLCLSSG 550 560 570 580 590 600 HVYQIGSELK LERCSVSKIN VKHVFVFDDQ AGTLLHKKTG KCVTGADQRV TLDECGLGRK 610 DQMWQLEGYQ SP

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 9525933] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], ENZYME ACTIVITY. Strain: Bristol N2.
[2]	"2.2 Mb of contiguous nucleotide sequence from chromosome III of C. elegans." Wilson R., Ainscough R., Anderson K., Baynes C., Berks M., Bonfield J., Burton J., Connell M., Copsey T., Cooper J., Coulson A., Craxton M., Dear S., Du Z., Durbin R., Favello A., Fraser A., Fulton L. , Gardner A., Green P., Hawkins T., Hillier L., Jier M., Johnston L., Jones M., Kershaw J., Kirsten J., Laisster N., Latreille P., Lightning J., Lloyd C., Mortimore B., O'Callaghan M., Parsons J., Percy C., Rifken L., Roopra A., Saunders D., Shownkeen R., Sims M., Smaldon N., Smith A., Smith M., Sonnhammer E., Staden R., Sulston J., Thierry-Mieg J., Thomas K., Vaudin M., Vaughan K., Waterston R., Watson A., Weinstock L., Wilkinson-Sproat J., Wohldman P. Nature 368:32-38(1994) [PubMed: 7906398] [Abstract] 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: 9851916] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Bristol N2.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF031833 mRNA. Translation: AAC13669.1. L16621 Genomic DNA. Translation: AAA28224.3.
PIR	A88515. T42243.
RefSeq	NP_498722.1.
UniGene	Cel.17588
3D structure databases
ModBase	Search...
Protein family/group databases
CAZy	CBM13. Carbohydrate-Binding Module Family 13. GT27. Glycosyltransferase Family 27.
Genome annotation databases
Ensembl	ZK688.8. Caenorhabditis elegans. [Contig view]
GeneID	176112.
KEGG	cel:ZK688.8.
Organism-specific databases
WormBase	WBGene00001628. gly-3.
WormPep	ZK688.8. CE29649. [WorfDB]
Phylogenomic databases
OMA	P34678. CRAVIAT.
Enzyme and pathway databases
BRENDA	2.4.1.41. 672.
Gene expression databases
ArrayExpress	P34678.
Family and domain databases
InterPro	IPR001173. Glyco_trans_2. IPR000772. Ricin_B_lectin. [Graphical view]
Pfam	PF00535. Glycos_transf_2. 1 hit. PF00652. Ricin_B_lectin. 1 hit. [Graphical view]
SMART	SM00458. RICIN. 1 hit. [Graphical view]
PROSITE	PS50231. RICIN_B_LECTIN. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	891164.

Entry information

Entry name

GALT3_CAEEL

Accession

Primary (citable) accession number: P34678
Secondary accession number(s): Q9U003

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1994
Last sequence update:	May 27, 2002
Last modified:	May 5, 2009
This is version 74 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Caenorhabditis annotation project