Reviewed, UniProtKB/Swiss-Prot Q6Y288 (B3GLT_HUMAN)

Names and origin

Protein names

Recommended name:
    Beta-1,3-glucosyltransferase
      Short name=Beta3Glc-T
    EC=2.4.1.-
Alternative name(s):
    Beta-3-glycosyltransferase-like

Gene names

Name:	B3GALTL
Synonyms:	B3GTL

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	498 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	O-fucosyltransferase that transfers glucose toward fucose with a beta-1,3 linkage. Specifically glucosylates O-linked fucosylglycan on TSP type-1 domains of proteins, thereby contributing to elongation of O-fucosylglycan. Ref.2
Pathway	Protein modification; protein glycosylation.
Subcellular location	Endoplasmic reticulum membrane; Single-pass type II membrane protein.
Tissue specificity	Widely expressed, with highest levels in testis and uterus. Ref.2 Ref.1
Involvement in disease	Defects in B3GALTL are the cause of Peters-plus syndrome (PPS) [MIM:261540]. PPS is an autosomal recessive disorder characterized by anterior eye-chamber abnormalities, disproportionate short stature, developmental delay, characteristic craniofacial features, cleft lip and/or palate. Ref.7
Sequence similarities	Belongs to the glycosyltransferase 31 family.

Ontologies

Keywords
Biological process	Carbohydrate metabolism Fucose metabolism
Cellular component	Endoplasmic reticulum Membrane
Coding sequence diversity	Polymorphism
Disease	Congenital disorder of glycosylation
Domain	Signal-anchor Transmembrane
Molecular function	Glycosyltransferase Transferase
PTM	Glycoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	fucose metabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	endoplasmic reticulum Inferred from electronic annotation. Source: UniProtKB-KW integral to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
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 – 498	498	Beta-1,3-glucosyltransferase		PRO_0000252399
Regions
	Topological domain	1 – 6	6	Cytoplasmic Potential
	Transmembrane	7 – 27	21	Signal-anchor for type II membrane protein Potential
	Topological domain	28 – 498	471	Lumenal Potential
	Motif	495 – 498	4	Prevents secretion from ER
Amino acid modifications
	Glycosylation	336	1	N-linked (GlcNAc...) Potential
Natural variations
	Natural variant	370	1	E → K: dbSNP rs1041073. Ref.2 Ref.1 Ref.3 Ref.5		VAR_027849
Experimental info
	Mutagenesis	495 – 498	4	Missing: Abolishes endoplasmic reticulum localization. Ref.2
	Sequence conflict	284	1	I → M in AAH68595. Ref.6

Sequences

	Sequence		Length	Mass (Da)
	Q6Y288-1 [UniParc]. Last modified October 17, 2006. Version 2. Checksum: CDC6A479A1564D48	FASTA	498	56,564
	10 20 30 40 50 60 MRPPACWWLL APPALLALLT CSLAFGLASE DTKKEVKQSQ DLEKSGISRK NDIDLKGIVF 70 80 90 100 110 120 VIQSQSNSFH AKRAEQLKKS ILKQAADLTQ ELPSVLLLHQ LAKQEGAWTI LPLLPHFSVT 130 140 150 160 170 180 YSRNSSWIFF CEEETRIQIP KLLETLRRYD PSKEWFLGKA LHDEEATIIH HYAFSENPTV 190 200 210 220 230 240 FKYPDFAAGW ALSIPLVNKL TKRLKSESLK SDFTIDLKHE IALYIWDKGG GPPLTPVPEF 250 260 270 280 290 300 CTNDVDFYCA TTFHSFLPLC RKPVKKKDIF VAVKTCKKFH GDRIPIVKQT WESQASLIEY 310 320 330 340 350 360 YSDYTENSIP TVDLGIPNTD RGHCGKTFAI LERFLNRSQD KTAWLVIVDD DTLISISRLQ 370 380 390 400 410 420 HLLSCYDSGE PVFLGERYGY GLGTGGYSYI TGGGGMVFSR EAVRRLLASK CRCYSNDAPD 430 440 450 460 470 480 DMVLGMCFSG LGIPVTHSPL FHQARPVDYP KDYLSHQVPI SFHKHWNIDP VKVYFTWLAP 490 SDEDKARQET QKGFREEL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A novel human glycosyltransferase: primary structure and characterization of the gene and transcripts." Heinonen T.Y.K., Pasternack L., Lindfors K., Breton C., Gastinel L.N., Maeki M., Kainulainen H. Biochem. Biophys. Res. Commun. 309:166-174(2003) [PubMed: 12943678] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, VARIANT LYS-370.
[2]	"Molecular cloning and characterization of a novel human beta1,3-glucosyltransferase, which is localized at the endoplasmic reticulum and glucosylates O-linked fucosylglycan on thrombospondin type 1 repeat domain." Sato T., Sato M., Kiyohara K., Sogabe M., Shikanai T., Kikuchi N., Togayachi A., Ishida H., Ito H., Kameyama A., Gotoh M., Narimatsu H. Glycobiology 16:1194-1206(2006) [PubMed: 16899492] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, ENZYME ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MUTAGENESIS OF 495-ARG--LEU-498, VARIANT LYS-370.
[3]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT LYS-370.
[4]	"The DNA sequence and analysis of human chromosome 13." Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T. , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L., Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T. Nature 428:522-528(2004) [PubMed: 15057823] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT LYS-370.
[6]	"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]. Tissue: Testis.
[7]	"Peters plus syndrome is caused by mutations in B3GALTL, a putative glycosyltransferase." Lesnik Oberstein S.A., Kriek M., White S.J., Kalf M.E., Szuhai K., den Dunnen J.T., Breuning M.H., Hennekam R.C.M. Am. J. Hum. Genet. 79:562-566(2006) [PubMed: 16909395] [Abstract] Cited for: INVOLVEMENT IN PPS.
+	Additional computationally mapped references.

Web resources

GGDB

GlycoGene database

GeneReviews

Cross-references

Sequence databases
EMBLGenBankDDBJ	AY190526 mRNA. Translation: AAO37647.1. AB101481 mRNA. Translation: BAD13528.1. AK291273 mRNA. Translation: BAF83962.1. AL137142, AL138965 Genomic DNA. Translation: CAI12432.2. AL138965, AL137142 Genomic DNA. Translation: CAH73049.2. CH471075 Genomic DNA. Translation: EAX08483.1. BC068595 mRNA. Translation: AAH68595.1.
IPI	IPI00375600.
RefSeq	NP_919299.3.
UniGene	Hs.13205
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q6Y288.
Protein family/group databases
CAZy	GT31. Glycosyltransferase Family 31.
Proteomic databases
PRIDE	Q6Y288.
Genome annotation databases
Ensembl	ENST00000343307; ENSP00000343002; ENSG00000187676; Homo sapiens. [Genome view]
GeneID	145173.
KEGG	hsa:145173.
NMPDR	fig|9606.3.peg.8696.
UCSC	uc010aaz.1. human.
Organism-specific databases
CTD	145173.
GeneCards	GC13P030674.
HGNC	HGNC:20207. B3GALTL.
HPA	HPA017664.
MIM	261540. phenotype. 610308. gene.
Orphanet	709. Peters-plus syndrome.
GenAtlas	Search...
Phylogenomic databases
HOVERGEN	Q6Y288.
OMA	GYSYVTG
OrthoDB	EOG9WHC52
Gene expression databases
ArrayExpress	Q6Y288.
Bgee	Q6Y288.
CleanEx	HS_B3GALTL.
Genevestigator	Q6Y288.
GermOnline	ENSG00000187676. Homo sapiens.
Family and domain databases
InterPro	IPR003378. Fringe-like. [Graphical view]
Pfam	PF02434. Fringe. 1 hit. [Graphical view]
PROSITE	PS00014. ER_TARGET. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	85032.
SOURCE	Search...

Entry information

Entry name

B3GLT_HUMAN

Accession

Primary (citable) accession number: Q6Y288
Secondary accession number(s): A8K5F8, Q5W0H2, Q6NUI3

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 17, 2006
Last sequence update:	October 17, 2006
Last modified:	November 24, 2009
This is version 46 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.