Reviewed, UniProtKB/Swiss-Prot O13933 (ALG1_SCHPO)

Names and origin

Protein names

Recommended name:
    Chitobiosyldiphosphodolichol beta-mannosyltransferase
    EC=2.4.1.142
Alternative name(s):
    GDP-mannose-dolichol diphosphochitobiose mannosyltransferase
    GDP-Man:GlcNAc2-PP-dolichol mannosyltransferase
    Beta-1,4-mannosyltransferase
    Asparagine-linked glycosylation protein 1

Gene names

Name:	alg1
ORF Names:	SPAC23C4.14

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

General annotation (Comments)

Function	Participates in the formation of the lipid-linked precursor oligosaccharide for N-glycosylation. Involved in assembling the dolichol-pyrophosphate-GlcNAc(2)-Man5 intermediate on the cytoplasmic surface of the ER By similarity.
Catalytic activity	GDP-mannose + chitobiosyldiphosphodolichol = GDP + beta-1,4-D-mannosylchitobiosyldiphosphodolichol.
Pathway	Protein modification; protein glycosylation.
Subcellular location	Endoplasmic reticulum membrane; Single-pass type II membrane protein By similarity.
Sequence similarities	Belongs to the glycosyltransferase 1 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)
Biological process	biosynthetic process Inferred from electronic annotation. Source: InterPro
Cellular component	endoplasmic reticulum Inferred from direct assay. Source: GeneDB_SPombe integral to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	chitobiosyldiphosphodolichol beta-mannosyltransferase 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 – 424	424	Chitobiosyldiphosphodolichol beta-mannosyltransferase		PRO_0000080257
Regions
	Transmembrane	1 – 24	24	Signal-anchor for type II membrane protein Potential
	Topological domain	25 – 424	400	Lumenal Potential
Amino acid modifications
	Glycosylation	374	1	N-linked (GlcNAc...) Potential

Sequences

	Sequence		Length	Mass (Da)
	O13933-1 [UniParc]. Last modified May 1, 2000. Version 2. Checksum: E652399C61A28579	FASTA	424	48,726
	10 20 30 40 50 60 MLVLKIVLFL SLVIWFNLKK RTDKKRIIVL VLGDIARSPR MQYHAVSFAK LGWKVDLLGY 70 80 90 100 110 120 QHPGSSVGLF ESHENIRFYP IPSLPAYLQP KNRLQFLFLG PLKVLHQFLA LNWALFVRKP 130 140 150 160 170 180 ASFLFIQNPP CIPVFFIAQC LHILRGTKFI IDWHNFGYSI LALKLGKQHT FVKLLKIYEK 190 200 210 220 230 240 YMARGAYAHL TVSKRMKDVL QTWGMNPCYV CYDRPPNHFT PIKNEQKKQM SIKKIPCEYN 250 260 270 280 290 300 PSSTKLLITS TSWTPDEDIY ILWEALNEYD KTLDTPKLLV LITGKGPMKE EFSQYIKKHP 310 320 330 340 350 360 LHKVRFCMPW LSIEDYPQVM ACADLGVCLH TSSSGLDLPM KVVDLFGCGV PVIALSYPTI 370 380 390 400 410 420 SELVHDGENG LIVNDSKALS KKMQYLLTHA NELNSLKLGA LKESEYRWDD EWNKVIPPIV QGSN

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.

Cross-references

Sequence databases
EMBLGenBankDDBJ	CU329670 Genomic DNA. Translation: CAB16885.2.
PIR	T38269.
RefSeq	NP_593186.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	O13933.
Protein family/group databases
CAZy	GT33. Glycosyltransferase Family 33.
Genome annotation databases
GeneID	2541937.
GenomeReviews	Gene locus alg1 in contig CU329670_GR.
KEGG	spo:SPAC23C4.14.
NMPDR	fig|4896.1.peg.3156.
Organism-specific databases
GeneDB_Spombe	SPAC23C4.14.
Phylogenomic databases
OMA	CVITGKG.
Enzyme and pathway databases
BRENDA	2.4.1.142. 653.
Gene expression databases
ArrayExpress	O13933.
Family and domain databases
InterPro	IPR001296. Glyco_trans_1. [Graphical view]
Pfam	PF00534. Glycos_transf_1. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ALG1_SCHPO

Accession

Primary (citable) accession number: O13933

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 13, 2005
Last sequence update:	May 1, 2000
Last modified:	November 3, 2009
This is version 51 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)