Q9U2C4 (GALT9_CAEEL) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Probable N-acetylgalactosaminyltransferase 9
EC=2.4.1.-

Alternative name(s):
Protein-UDP acetylgalactosaminyltransferase 9
UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 9
Short name=pp-GaNTase 9

Gene names

Name:	gly-9
ORF Names:	Y47D3A.23

Organism

Caenorhabditis elegans

Taxonomic identifier

6239 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	579 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Probable glycopeptide transferase involved in O-linked oligosaccharide biosynthesis. Glycopeptide transferases catalyze the transfer of an N-acetyl-D-galactosamine residue to an already glycosylated peptide 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. 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
Coding sequence diversity	Alternative splicing
Domain	Signal-anchor Transmembrane Transmembrane helix
Ligand	Calcium Lectin Manganese
Molecular function	Glycosyltransferase Transferase
PTM	Disulfide bond Glycoprotein
Technical term	Complete proteome Reference 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	sugar binding Inferred from electronic annotation. Source: UniProtKB-KW transferase activity, transferring glycosyl groups Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform a (identifier: Q9U2C4-1)

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.

Isoform b (identifier: Q9U2C4-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-254: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 579	579	Probable N-acetylgalactosaminyltransferase 9		PRO_0000059152
Regions
	Topological domain	1 – 12	12	Cytoplasmic Potential
	Transmembrane	13 – 30	18	Helical; Signal-anchor for type II membrane protein; Potential
	Topological domain	31 – 579	549	Lumenal Potential
	Domain	450 – 574	125	Ricin B-type lectin
	Region	133 – 243	111	Catalytic subdomain A
	Region	302 – 364	63	Catalytic subdomain B
Amino acid modifications
	Glycosylation	67	1	N-linked (GlcNAc...) Potential
	Glycosylation	370	1	N-linked (GlcNAc...) Potential
	Disulfide bond	464 ↔ 483		By similarity
	Disulfide bond	507 ↔ 520		By similarity
	Disulfide bond	545 ↔ 562		By similarity
Natural variations
	Alternative sequence	1 – 254	254	Missing in isoform b.		VSP_020151
Experimental info
	Sequence conflict	203	1	V → D in AAC13679. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform a [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 2F50B222CFB13597	FASTA	579	66,430
	10 20 30 40 50 60 MLRYIIPRKK GTFVIAAFLT VAFFCIVAYH RNDRRRTKFQ FPDIEKYAEE LVRLPETWNG 70 80 90 100 110 120 ELHQIPNYTA PREGPGEKGK PVVLTGKDAE LGQADMKKWF MNVHASDKIS LDRDVPDPRI 130 140 150 160 170 180 QACKDIKYDY AALPKTSVII IFTDEAWTPL LRTVHSVINR SPPELLQEVI LLDDNSKRQE 190 200 210 220 230 240 LQEPLDEHIK RFGGKVRLIR KHVRHGLIRA KLAGAREAVG DIIVFLDSHC EANHGWLEPI 250 260 270 280 290 300 VQRISDERTA IVCPMIDSIS DNTLAYHGDW SLSTGGFSWA LHFTWEGLSE EEQKRRTKPT 310 320 330 340 350 360 DYIRSPTMAG GLLAANREYF FEVGGYDEEM DIWGGENLEI SFRAWMCGGS IEFIPCSHVG 370 380 390 400 410 420 HIFRAGHPYN MTGRNNNKDV HGTNSKRLAE VWMDDYKRLY YMHREDLRTK DVGDLTARHE 430 440 450 460 470 480 LRKRLNCKPF KWFLDNIAKG KFIMDEDVVA YGALHTVVSG TRMCTDTLQR DEKMSQLLGV 490 500 510 520 530 540 FHCQGKGSSP QLMSLSKEGN LRRENTCASE ENGNIRMKTC SKKAQFNERW AYENKMIRNL 550 560 570 KSGKCMSTAN LKPGDNAIVV ECDEKDEHQK WNFIDPAKA
	Isoform b [UniParc]. Checksum: 10091A101BC8CB0A	FASTA	325	37,284
	10 20 30 40 50 60 MIDSISDNTL AYHGDWSLST GGFSWALHFT WEGLSEEEQK RRTKPTDYIR SPTMAGGLLA 70 80 90 100 110 120 ANREYFFEVG GYDEEMDIWG GENLEISFRA WMCGGSIEFI PCSHVGHIFR AGHPYNMTGR 130 140 150 160 170 180 NNNKDVHGTN SKRLAEVWMD DYKRLYYMHR EDLRTKDVGD LTARHELRKR LNCKPFKWFL 190 200 210 220 230 240 DNIAKGKFIM DEDVVAYGAL HTVVSGTRMC TDTLQRDEKM SQLLGVFHCQ GKGSSPQLMS 250 260 270 280 290 300 LSKEGNLRRE NTCASEENGN IRMKTCSKKA QFNERWAYEN KMIRNLKSGK CMSTANLKPG 310 320 DNAIVVECDE KDEHQKWNFI DPAKA

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] (ISOFORM A). 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: 9851916] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], ALTERNATIVE SPLICING. Strain: Bristol N2.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF031843 mRNA. Translation: AAC13679.1. AL117202 Genomic DNA. Translation: CAB57897.1. AL117202 Genomic DNA. Translation: CAI46621.1.
PIR	T31549.
RefSeq	NP_001022876.1. NM_001027705.1. NP_001022877.1. NM_001027706.1.
UniGene	Cel.19662.
3D structure databases
ProteinModelPortal	Q9U2C4.
SMR	Q9U2C4. Positions 452-576.
ModBase	Search...
Protein family/group databases
CAZy	CBM13. Carbohydrate-Binding Module Family 13. GT27. Glycosyltransferase Family 27.
Proteomic databases
PRIDE	Q9U2C4.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	Y47D3A.23a; Y47D3A.23a; Y47D3A.23.
GeneID	176557.
KEGG	cel:Y47D3A.23.
NMPDR	fig|6239.3.peg.11654.
UCSC	Y47D3A.23a. c. elegans.
Organism-specific databases
CTD	176557.
WormBase	Y47D3A.23a; CE24334; WBGene00012934; gly-9. Y47D3A.23b; CE37859; WBGene00012934; gly-9.
Phylogenomic databases
eggNOG	meNOG05548.
GeneTree	EMGT00050000004056.
HOGENOM	HBG715048.
InParanoid	Q9U2C4.
OMA	WFMNVHA.
PhylomeDB	Q9U2C4.
Gene expression databases
ArrayExpress	Q9U2C4.
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]
SUPFAM	SSF50370. RicinB_like. 1 hit.
PROSITE	PS50231. RICIN_B_LECTIN. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	893070.

Entry information

Entry name

GALT9_CAEEL

Accession

Primary (citable) accession number: Q9U2C4
Secondary accession number(s): O61398, Q5GMH7

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 16, 2004
Last sequence update:	May 1, 2000
Last modified:	September 21, 2011
This is version 73 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Caenorhabditis annotation project