Reviewed, UniProtKB/Swiss-Prot A8Y236 (GLT10_CAEBR)

Names and origin

Protein names

Recommended name:
    Putative polypeptide N-acetylgalactosaminyltransferase 10
      Short name=pp-GaNTase 10
    EC=2.4.1.41
Alternative name(s):
    Protein-UDP acetylgalactosaminyltransferase 10
    UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 10

Gene names

Name:	gly-10
ORF Names:	CBG22373

Organism

Caenorhabditis briggsae [Complete proteome]

Taxonomic identifier

6238 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	629 AA.
Sequence status	Complete.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	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. UniProtKB Q86SR1
Catalytic activity	UDP-N-acetyl-D-galactosamine + polypeptide = UDP + N-acetyl-D-galactosaminyl-polypeptide. UniProtKB Q86SR1
Cofactor	Manganese By similarity. UniProtKB Q10472 Calcium By similarity. UniProtKB Q10472
Pathway	Protein modification; protein glycosylation. UniProtKB Q86SR1
Subcellular location	Golgi apparatus membrane; Single-pass type II membrane protein By similarity UniProtKB Q10472.
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. UniProtKB O08912 The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity By similarity. UniProtKB Q10473
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 Metal-binding
Molecular function	Glycosyltransferase Transferase
PTM	Disulfide bond Glycoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Cellular component	Golgi apparatus Inferred from electronic annotation. Source: UniProtKB-KW integral to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
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 – 629	629	Putative polypeptide N-acetylgalactosaminyltransferase 10		PRO_0000328999
Regions
	Topological domain	1 – 12	12	Cytoplasmic Potential
	Transmembrane	13 – 33	21	Signal-anchor for type II membrane protein
	Topological domain	34 – 629	596	Lumenal Potential
	Domain	526 – 629	104	Ricin B-type lectin
	Region	163 – 275	113	Catalytic subdomain A
	Region	331 – 393	63	Catalytic subdomain B
	Region	393 – 406	14	Flexible loop By similarity
Sites
	Metal binding	259	1	Manganese By similarity
	Metal binding	261	1	Manganese By similarity
	Metal binding	390	1	Manganese By similarity
	Binding site	204	1	Substrate By similarity
	Binding site	259	1	Substrate By similarity
Amino acid modifications
	Glycosylation	143	1	N-linked (GlcNAc...) Potential
	Glycosylation	177	1	N-linked (GlcNAc...) Potential
	Disulfide bond	154 ↔ 385		By similarity
	Disulfide bond	376 ↔ 454		By similarity
	Disulfide bond	493 ↔ 510		By similarity
	Disulfide bond	539 ↔ 556		By similarity
	Disulfide bond	582 ↔ 598		By similarity

Sequences

	Sequence		Length	Mass (Da)
	A8Y236-1 [UniParc]. Last modified October 13, 2009. Version 2. Checksum: FCD8FD9F61829238	FASTA	629	73,008
	10 20 30 40 50 60 MGLSRYLSRR HHWVIQYCAL LLFLYFIYSY VAVSNDAPRL NEEIPVFREF SEDLPQGSRK 70 80 90 100 110 120 FPEQKPAAAL GDEALDPFEK YRGHEKIKWE DEVAYEKDKA REGPGEWGKP VKLPDDKETE 130 140 150 160 170 180 KEALSLYKAN GYNAYISDMI SLNRSIKDIR HKECKKMTYS AKLPTVSVIF PFHEEHNSTL 190 200 210 220 230 240 LRSVYSVINR SPPELLKEII LVDDFSEKPA LRQPLEDFLK KNKIDHIVKI LRTKKREGLI 250 260 270 280 290 300 RGRQLGAQEA TGEILIFLDA HSECNYNWLP PLLDPIADDY RTVVCPFVDV IDCETYEIRP 310 320 330 340 350 360 QDEGARGSFD WAFNYKRLPL TKKDRENPTK PFDSPVMAGG YFAISAKWFW ELGGYDEGLD 370 380 390 400 410 420 IWGGEQYELS FKVWQCHGKM VDAPCSRVAH IYRCKYAPFK NAGMGDFVSR NYKRVAEVWM 430 440 450 460 470 480 DEYKETLYKH RPGIGNADAG DLKLMKGIRE KLQCKSFDWF MKEIAFDQDK YYPAIEPKAS 490 500 510 520 530 540 AEGEIRHVAS NLCIDTQFKE QNQRFGLRKC ASEDKDGGGE QDLRLTRWHD IRPKGRKICF 550 560 570 580 590 600 DVSTSVDKAP IILFDCHSMK GNQLFKYRMP QKQIYHPVSG QCLTADENGK GFLHMKKCDS 610 620 SSKLQQWAWQ TIDQELLDQR QANEHKELE

References

[1]

"The genome sequence of Caenorhabditis briggsae: a platform for comparative genomics." Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N., Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P., Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W., Hillier L.W. , Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A., Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E., Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K., Durbin R.M., Waterston R.H. PLoS Biol. 1:166-192(2003) [PubMed: 14624247] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: AF16.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CAAC02000592 Genomic DNA. Translation: CAP38976.2.
3D structure databases
ModBase	Search...
Organism-specific databases
WormBase	WBGene00040946. Cbr-gly-10.
Phylogenomic databases
PhylomeDB	A8Y236.
Enzyme and pathway databases
BRENDA	2.4.1.41. 261794.
Family and domain databases
InterPro	IPR001173. Glyco_trans_2. IPR008997. Ricin_B-rel_lectin. 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...

Entry information

Entry name

GLT10_CAEBR

Accession

Primary (citable) accession number: A8Y236

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 8, 2008
Last sequence update:	October 13, 2009
Last modified:	January 19, 2010
This is version 19 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Caenorhabditis annotation project