Reviewed, UniProtKB/Swiss-Prot Q6IS24 (GLTL3_HUMAN)

Names and origin

Protein names

Recommended name:
    Putative polypeptide N-acetylgalactosaminyltransferase-like protein 3
    EC=2.4.1.41
Alternative name(s):
    Polypeptide GalNAc transferase-like protein 3
      Short name=pp-GaNTase-like protein 3
      Short name=GalNAc-T-like protein 3
    Protein-UDP acetylgalactosaminyltransferase-like protein 3
    UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase-like protein 3
    Williams-Beuren syndrome chromosomal region 17 protein

Gene names

Name:	WBSCR17
Synonyms:	GALNTL3

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	598 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript level.

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.
Catalytic activity	UDP-N-acetyl-D-galactosamine + polypeptide = UDP + N-acetyl-D-galactosaminyl-polypeptide.
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.
Tissue specificity	Highly expressed in brain and heart. Weakly expressed in kidney, liver, lung and spleen. Ref.1
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 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 – 598	598	Putative polypeptide N-acetylgalactosaminyltransferase-like protein 3		PRO_0000059139
Regions
	Topological domain	1 – 6	6	Cytoplasmic Potential
	Transmembrane	7 – 27	21	Signal-anchor for type II membrane protein Potential
	Topological domain	28 – 598	571	Lumenal Potential
	Domain	465 – 594	130	Ricin B-type lectin
	Region	151 – 262	112	Catalytic subdomain A
	Region	319 – 381	63	Catalytic subdomain B
Amino acid modifications
	Glycosylation	50	1	N-linked (GlcNAc...) Potential
	Glycosylation	461	1	N-linked (GlcNAc...) Potential
	Glycosylation	486	1	N-linked (GlcNAc...) Potential
	Disulfide bond	478 ↔ 494		By similarity
	Disulfide bond	526 ↔ 541		By similarity
	Disulfide bond	568 ↔ 586		By similarity
Experimental info
	Sequence conflict	596	1	S → P in AAH69997. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q6IS24-1 [UniParc]. Last modified August 16, 2004. Version 2. Checksum: 9E2D52DBFBD907B1	FASTA	598	67,751
	10 20 30 40 50 60 MASLRRVKVL LVLNLIAVAG FVLFLAKCRP IAVRSGDAFH EIRPRAEVAN LSAHSASPIQ 70 80 90 100 110 120 DAVLKRLSLL EDIVYRQLNG LSKSLGLIEG YGGRGKGGLP ATLSPAEEEK AKGPHEKYGY 130 140 150 160 170 180 NSYLSEKISL DRSIPDYRPT KCKELKYSKD LPQISIIFIF VNEALSVILR SVHSAVNHTP 190 200 210 220 230 240 THLLKEIILV DDNSDEEELK VPLEEYVHKR YPGLVKVVRN QKREGLIRAR IEGWKVATGQ 250 260 270 280 290 300 VTGFFDAHVE FTAGWAEPVL SRIQENRKRV ILPSIDNIKQ DNFEVQRYEN SAHGYSWELW 310 320 330 340 350 360 CMYISPPKDW WDAGDPSLPI RTPAMIGCSF VVNRKFFGEI GLLDPGMDVY GGENIELGIK 370 380 390 400 410 420 VWLCGGSMEV LPCSRVAHIE RKKKPYNSNI GFYTKRNALR VAEVWMDDYK SHVYIAWNLP 430 440 450 460 470 480 LENPGIDIGD VSERRALRKS LKCKNFQWYL DHVYPEMRRY NNTVAYGELR NNKAKDVCLD 490 500 510 520 530 540 QGPLENHTAI LYPCHGWGPQ LARYTKEGFL HLGALGTTTL LPDTRCLVDN SKSRLPQLLD 550 560 570 580 590 CDKVKSSLYK RWNFIQNGAI MNKGTGRCLE VENRGLAGID LILRSCTGQR WTIKNSIK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification of additional transcripts in the Williams-Beuren syndrome critical region." Merla G., Ucla C., Guipponi M., Reymond A. Hum. Genet. 110:429-438(2002) [PubMed: 12073013] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
[2]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed: 17974005] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 466-598. Tissue: Amygdala.
+	Additional computationally mapped references.

Web resources

GGDB

GlycoGene database

Functional Glycomics Gateway - GTase

Putative polypeptide N-acetylgalactosaminyltransferase-like protein 3

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF410457 mRNA. Translation: AAM62306.1. BC067524 mRNA. Translation: AAH67524.1. BC067525 mRNA. Translation: AAH67525.1. BC069624 mRNA. Translation: AAH69624.1. BC069628 mRNA. Translation: AAH69628.1. BC069636 mRNA. Translation: AAH69636.1. BC069645 mRNA. Translation: AAH69645.1. BC069997 mRNA. Translation: AAH69997.1. AL137431 mRNA. Translation: CAB70734.1.
IPI	IPI00168921.
PIR	T46260.
RefSeq	NP_071924.1.
UniGene	Hs.488591
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q6IS24.
Protein family/group databases
CAZy	CBM13. Carbohydrate-Binding Module Family 13. GT27. Glycosyltransferase Family 27.
Proteomic databases
PRIDE	Q6IS24.
Genome annotation databases
Ensembl	ENST00000333538; ENSP00000329654; ENSG00000185274; Homo sapiens. [Genome view] ENST00000447516; ENSP00000392019; ENSG00000185274; Homo sapiens. [Genome view]
GeneID	64409.
KEGG	hsa:64409.
UCSC	uc003tvy.1. human.
Organism-specific databases
CTD	64409.
GeneCards	GC07P070235.
HGNC	HGNC:16347. WBSCR17.
HPA	HPA013624.
PharmGKB	PA38124.
GenAtlas	Search...
Phylogenomic databases
HOGENOM	Q6IS24.
HOVERGEN	Q6IS24.
OMA	PLEEYVN.
Enzyme and pathway databases
BRENDA	2.4.1.41. 247.
Gene expression databases
ArrayExpress	Q6IS24.
Bgee	Q6IS24.
CleanEx	HS_WBSCR17.
Genevestigator	Q6IS24.
GermOnline	ENSG00000185274. Homo sapiens.
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	66366.

Entry information

Entry name

GLTL3_HUMAN

Accession

Primary (citable) accession number: Q6IS24
Secondary accession number(s): Q8NFV9, Q9NTA8

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 16, 2004
Last sequence update:	August 16, 2004
Last modified:	November 3, 2009
This is version 59 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.