Reviewed, UniProtKB/Swiss-Prot O60061 (ALG5_SCHPO)

Names and origin

Protein names

Recommended name:
    Dolichyl-phosphate beta-glucosyltransferase
      Short name=DolP-glucosyltransferase
    EC=2.4.1.117
Alternative name(s):
    Asparagine-linked glycosylation protein 5

Gene names

Name:	alg5
ORF Names:	SPBC56F2.10c

Organism

Schizosaccharomyces pombe (Fission yeast) [Complete proteome]

Taxonomic identifier

4896 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

Protein attributes

Sequence length	322 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Catalytic activity	UDP-glucose + dolichyl phosphate = UDP + dolichyl beta-D-glucosyl phosphate.
Pathway	Protein modification; protein glycosylation.
Subcellular location	Endoplasmic reticulum membrane; Single-pass type II membrane protein. Note: Its interaction with the substrate UDP-glucose may occur at the cytoplasmic side of the ER, whereas the steps utilizing dolichyl beta-D-glucosyl phosphate take place in the lumen of the ER By similarity.
Sequence similarities	Belongs to the glycosyltransferase 2 family.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum Membrane
Domain	Signal-anchor Transmembrane
Molecular function	Glycosyltransferase Transferase
PTM	Glycoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Cellular component	endoplasmic reticulum Ref.2 Inferred from direct assay. Source: GeneDB_SPombe integral to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	dolichyl-phosphate beta-glucosyltransferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 322	322	Dolichyl-phosphate beta-glucosyltransferase		PRO_0000311759
Regions
	Topological domain	1	1	Cytoplasmic By similarity
	Transmembrane	2 – 22	21	Signal-anchor for type II membrane protein
	Topological domain	23 – 322	300	Lumenal By similarity
Amino acid modifications
	Glycosylation	72	1	N-linked (GlcNAc...) Potential
	Glycosylation	307	1	N-linked (GlcNAc...) Potential

Sequences

	Sequence		Length	Mass (Da)
	O60061-1 [UniParc]. Last modified August 1, 1998. Version 1. Checksum: B97B2EF2C8D872C0	FASTA	322	36,774
	10 20 30 40 50 60 MVVYIVLYTC LAGFILLFLV YYYLTHSHCP RKQLEGEETC VFIENGQKKS LTLEKWSTSD 70 80 90 100 110 120 NIQITVIVPA YNESKRIGNM LQETVDHLEK YYRSSSSAGQ RRWEILIVDD ESKDTTVNAV 130 140 150 160 170 180 LEFSNKLDLR DHLRVCSLKR NRGKGGAVTW GMLYARGQYA IFADADGASQ FSDLELLFKN 190 200 210 220 230 240 MPPGPRGGVV VGSRAHMVNT AAVVKRSFIR NFLMHCFHKL LQILGIREIG DTQCGFKLFS 250 260 270 280 290 300 REAYQSIFPR MHVEGWIFDI EVLTLARFFG LPIIEVPITW HEVGGSKMTL LKDSISMAID 310 320 LLVIRLNYTF GIWERPSAKR IT

References

[1]

"The genome sequence of Schizosaccharomyces pombe." Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P. Nature 415:871-880(2002) [PubMed: 11859360] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 38366 / 972.

[2]

"ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe." Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., Yoshida M. Nat. Biotechnol. 24:841-847(2006) [PubMed: 16823372] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CU329671 Genomic DNA. Translation: CAA18889.1.
PIR	T40534.
RefSeq	NP_596707.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	O60061.
Protein family/group databases
CAZy	GT2. Glycosyltransferase Family 2.
Genome annotation databases
GeneID	2541053.
GenomeReviews	Gene locus alg5 in contig CU329671_GR.
KEGG	spo:SPBC56F2.10c.
NMPDR	fig|4896.1.peg.2573.
Organism-specific databases
GeneDB_Spombe	SPBC56F2.10c.
Phylogenomic databases
HOGENOM	HBG752660.
OMA	PITWHEV.
OrthoDB	EOG98KST9.
Enzyme and pathway databases
BRENDA	2.4.1.117. 653.
Gene expression databases
ArrayExpress	O60061.
Family and domain databases
InterPro	IPR001173. Glyco_trans_2. [Graphical view]
Pfam	PF00535. Glycos_transf_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ALG5_SCHPO

Accession

Primary (citable) accession number: O60061

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 13, 2007
Last sequence update:	August 1, 1998
Last modified:	December 15, 2009
This is version 46 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)