Q8BHT6 (B3GLT_MOUSE) Reviewed, UniProtKB/Swiss-Prot

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:	Gm1057

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	489 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript 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 By similarity.
Pathway	Protein modification; protein glycosylation.
Subcellular location	Endoplasmic reticulum membrane; Single-pass type II membrane protein By similarity.
Sequence similarities	Belongs to the glycosyltransferase 31 family.

Ontologies

Keywords
Biological process	Carbohydrate metabolism Fucose metabolism
Cellular component	Endoplasmic reticulum Membrane
Coding sequence diversity	Alternative splicing
Domain	Signal-anchor Transmembrane Transmembrane helix
Molecular function	Glycosyltransferase Transferase
PTM	Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	fucose metabolic process Inferred from electronic annotation. Source: UniProtKB-KW protein glycosylation Inferred from electronic annotation. Source: UniProtKB-UniPathway
Cellular_component	endoplasmic reticulum 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...

Alternative products

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

Isoform 1 (identifier: Q8BHT6-1)

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 2 (identifier: Q8BHT6-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-386: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 489	489	Beta-1,3-glucosyltransferase		PRO_0000252400
Regions
	Topological domain	1	1	Cytoplasmic Potential
	Transmembrane	2 – 22	21	Helical; Signal-anchor for type II membrane protein; Potential
	Topological domain	23 – 489	467	Lumenal Potential
	Motif	486 – 489	4	Prevents secretion from ER Potential
Amino acid modifications
	Glycosylation	78	1	N-linked (GlcNAc...) Potential
Natural variations
	Alternative sequence	1 – 386	386	Missing in isoform 2.		VSP_020936
Experimental info
	Sequence conflict	128	1	L → I in BAF02833. Ref.1
	Sequence conflict	253	1	V → I in BAF02833. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified July 27, 2011. Version 3. Checksum: 3FAD6846B25DB080	FASTA	489	55,358
	10 20 30 40 50 60 MRPPALLALF SCSAAFALMS EEIKEKVTPS QDLRQSSLPG RHDIDLKEIV FVIQSQSNSF 70 80 90 100 110 120 HAKRAEQLKK NILKQAANLT QDLPRVLLLH QLAKQEGAWT ILPLLPHFSV TYSKNSAWIF 130 140 150 160 170 180 FCEEETRLQI PRLLDTLRRY DPSKEWFLGK ALYDEESTII HHYAFSENPT VFKYPDFAAG 190 200 210 220 230 240 WALSIPLVNK LAKRLKSEAL KSDFTIDLKH EIALYIWDKG GGPALTPVPE FCTEDVDPRC 250 260 270 280 290 300 VTTFHSFLPL CGVPVKKEEI FVAVKTCKKF HADRIPIVKK TWAAQASLIE YYSDYAETAI 310 320 330 340 350 360 PTVDLGIPNT DRGHCGKTFA ILEKFLNHSH NKISWLVIVD DDTLISISRL RHLLSCYDSS 370 380 390 400 410 420 DPVFLGERYG YGLGTGGYSY VTGGGGMVFS REAIRRLLVS SCRCYSNDAP DDMVLGMCFS 430 440 450 460 470 480 GLGVPVTHSP LFHQARPVDY PKDYLAHQIP VSFHKHWHID PVKVYLTWLA PSEEDQATQE TQKDPREEL
	Isoform 2 [UniParc]. Checksum: CB1B1F4685D61F40	FASTA	103	11,881
	10 20 30 40 50 60 MVFSREAIRR LLVSSCRCYS NDAPDDMVLG MCFSGLGVPV THSPLFHQAR PVDYPKDYLA 70 80 90 100 HQIPVSFHKH WHIDPVKVYL TWLAPSEEDQ ATQETQKDPR EEL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]	"Lineage-specific biology revealed by a finished genome assembly of the mouse." Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P. PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6J.
[3]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
[4]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-352 (ISOFORM 1). Strain: C57BL/6J.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB253762 mRNA. Translation: BAF02833.1. AC114342 Genomic DNA. No translation available. BC115781 mRNA. Translation: AAI15782.1. BC117522 mRNA. Translation: AAI17523.1. AK089440 mRNA. Translation: BAC40885.1.
IPI	IPI00761932. IPI00798502.
RefSeq	NP_001074673.1. NM_001081204.1.
UniGene	Mm.45060.
3D structure databases
ProteinModelPortal	Q8BHT6.
SMR	Q8BHT6. Positions 259-433.
ModBase	Search...
Protein family/group databases
CAZy	GT31. Glycosyltransferase Family 31.
PTM databases
PhosphoSite	Q8BHT6.
Proteomic databases
PaxDb	Q8BHT6.
PRIDE	Q8BHT6.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000100404; ENSMUSP00000097972; ENSMUSG00000051950.
GeneID	381694.
KEGG	mmu:381694.
UCSC	uc009aqc.1. mouse. uc009aqd.1. mouse.
Organism-specific databases
CTD	145173.
MGI	MGI:2685903. B3galtl.
Phylogenomic databases
eggNOG	NOG150034.
GeneTree	ENSGT00390000000060.
HOGENOM	HOG000007375.
HOVERGEN	HBG059386.
InParanoid	Q8BHT6.
KO	K13675.
OMA	GGYSYVT.
OrthoDB	EOG4Q2DFR.
Enzyme and pathway databases
UniPathway	UPA00378.
Gene expression databases
Bgee	Q8BHT6.
CleanEx	MM_B3GALTL.
Genevestigator	Q8BHT6.
Family and domain databases
InterPro	IPR003378. Fringe-like. [Graphical view]
Pfam	PF02434. Fringe. 2 hits. [Graphical view]
PROSITE	PS00014. ER_TARGET. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	402439.
SOURCE	Search...

Entry information

Entry name

B3GLT_MOUSE

Accession

Primary (citable) accession number: Q8BHT6
Secondary accession number(s): E9QMK8, Q0PCR7, Q149S5

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 17, 2006
Last sequence update:	July 27, 2011
Last modified:	May 1, 2013
This is version 74 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program