O45293 (GALT8_CAEEL) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Probable N-acetylgalactosaminyltransferase 8
EC=2.4.1.-

Alternative name(s):
Protein-UDP acetylgalactosaminyltransferase 8
UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 8
Short name=pp-GaNTase 8

Gene names

Name:	gly-8
ORF Names:	Y66A7A.6

Organism

Caenorhabditis elegans [Reference proteome]

Taxonomic identifier

6239 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Protostomia › Ecdysozoa › Nematoda › Chromadorea › Rhabditida › Rhabditoidea › Rhabditidae › Peloderinae › Caenorhabditis

Protein attributes

Sequence length	421 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Potential glycopeptide transferase involved in O-linked oligosaccharide biosynthesis By similarity. In contrast to other members of the family, it does not act as a peptide transferase that transfers GalNAc onto serine or threonine residue on peptides that have been tested. Some peptide transferase activity is however not excluded, considering that its appropriate peptide substrate may remain unidentified.
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.
Sequence similarities	Belongs to the glycosyltransferase 2 family. GalNAc-T subfamily.
Caution	In contrast to other members of the family, it lacks the C-terminal ricin B-type lectin domain, which usually contributes to the glycopeptide specificity. It instead contains a motif that may retain its secretion form the endoplasmic reticulum.

Ontologies

Keywords
Cellular component	Golgi apparatus Membrane
Domain	Signal-anchor Transmembrane Transmembrane helix
Ligand	Calcium Manganese
Molecular function	Glycosyltransferase Transferase
PTM	Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	protein glycosylation Inferred from electronic annotation. Source: UniProtKB-UniPathway
Cellular_component	Golgi membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	transferase activity, transferring glycosyl groups 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 – 421	421	Probable N-acetylgalactosaminyltransferase 8		PRO_0000059151
Regions
	Topological domain	1 – 3	3	Cytoplasmic Potential
	Transmembrane	4 – 24	21	Helical; Signal-anchor for type II membrane protein; Potential
	Topological domain	25 – 421	397	Lumenal Potential
	Region	106 – 219	114	Catalytic subdomain A
	Region	277 – 339	63	Catalytic subdomain B
	Motif	418 – 421	4	Prevents secretion from ER Potential
Amino acid modifications
	Glycosylation	52	1	N-linked (GlcNAc...) Ref.3
	Glycosylation	58	1	N-linked (GlcNAc...) Ref.3

Sequences

	Sequence		Length	Mass (Da)
	O45293 [UniParc]. Last modified June 1, 1998. Version 1. Checksum: 3FA38E18702D087D	FASTA	421	48,358
	10 20 30 40 50 60 MRRHVVLSIF VFAGIVFAAE EAEKLPKCEH VDPYENLEGW LDLKPLTERK CNHTLKENLT 70 80 90 100 110 120 EAESKKSEWG IKSFAFDALS SEKLGPNRNV GKQAHKLCEE EKYDASYSTS VVVIHHNEAL 130 140 150 160 170 180 STILRMINGI IEFTPKSLLK EIVLYEDASE EDHVLTKHLE KFAKIKGLED KLIIKRSEYR 190 200 210 220 230 240 QGLIRAKVHA SRLATGEVIV FMDSHCEVAE RWLEPLLQPI KEDPKSIVLP VVDLINPVSF 250 260 270 280 290 300 DYSPSMVAKS GFDWGFTFKW IYLPWEYFET PENNVKPFNS PAMPGGLLAM RKEYFVELGE 310 320 330 340 350 360 YDMGMEIWGS ENIELSLKAW LCGGRVVVAP CSRVGHVFRM RRPYTSKPGM DTALYNAVRV 370 380 390 400 410 420 AKTWLGEYES KFFAVKPRGA KMVFGDLTEP MQVKDRLKCK DMKWFIENVY PELEPKVHDE L

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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. 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.
[3]	"Proteomics reveals N-linked glycoprotein diversity in Caenorhabditis elegans and suggests an atypical translocation mechanism for integral membrane proteins." Kaji H., Kamiie J., Kawakami H., Kido K., Yamauchi Y., Shinkawa T., Taoka M., Takahashi N., Isobe T. Mol. Cell. Proteomics 6:2100-2109(2007) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-52 AND ASN-58, MASS SPECTROMETRY. Strain: Bristol N2.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF031842 mRNA. Translation: AAC13678.1. AL032622 Genomic DNA. Translation: CAA21500.1. AL590342 Genomic DNA. Translation: CAC35860.1.
PIR	T42252.
RefSeq	NP_499504.1. NM_067103.4.
UniGene	Cel.19663.
3D structure databases
ProteinModelPortal	O45293.
SMR	O45293. Positions 76-421.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-24790N.
MINT	MINT-1070872.
STRING	6239.Y66A7A.6.1.
Protein family/group databases
CAZy	GT27. Glycosyltransferase Family 27.
Proteomic databases
PaxDb	O45293.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	Y66A7A.6.1; Y66A7A.6.1; Y66A7A.6. Y66A7A.6.2; Y66A7A.6.2; Y66A7A.6. Y66A7A.6.3; Y66A7A.6.3; Y66A7A.6.
GeneID	176595.
KEGG	cel:CELE_Y66A7A.6.
UCSC	Y66A7A.6.1. c. elegans.
Organism-specific databases
CTD	176595.
WormBase	Y66A7A.6; CE15691; WBGene00001633; gly-8.
Phylogenomic databases
eggNOG	NOG295988.
GeneTree	ENSGT00670000097647.
HOGENOM	HOG000038227.
InParanoid	O45293.
OMA	PENNVKP.
Enzyme and pathway databases
UniPathway	UPA00378.
Family and domain databases
InterPro	IPR001173. Glyco_trans_2. [Graphical view]
Pfam	PF00535. Glycos_transf_2. 1 hit. [Graphical view]
PROSITE	PS00014. ER_TARGET. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	893222.

Entry information

Entry name

GALT8_CAEEL

Accession

Primary (citable) accession number: O45293

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 16, 2004
Last sequence update:	June 1, 1998
Last modified:	May 1, 2013
This is version 92 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Caenorhabditis annotation project