Reviewed, UniProtKB/Swiss-Prot O59866 (OSTB_SCHPO)

Names and origin

Protein names

Recommended name:
    Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 48 kDa subunit
      Short name=Oligosaccharyl transferase 48 kDa subunit
    EC=2.4.1.119
Alternative name(s):
    Oligosaccharyl transferase subunit beta

Gene names

ORF Names:

SPCC338.15

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	437 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	Essential subunit of N-oligosaccharyl transferase enzyme which catalyzes the transfer of a high mannose oligosaccharide to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER) By similarity. UniProtKB P33767
Catalytic activity	Dolichyl diphosphooligosaccharide + protein L-asparagine = dolichyl diphosphate + a glycoprotein with the oligosaccharide chain attached by N-glycosyl linkage to protein L-asparagine. UniProtKB P33767
Pathway	Protein modification; protein glycosylation. UniProtKB P33767
Subunit structure	Component of the oligosaccharyl transferase (OST) complex By similarity. UniProtKB P33767
Subcellular location	Endoplasmic reticulum. Membrane; Single-pass type I membrane protein By similarity. UniProtKB P33767 Ref.3
Domain	The cytoplasmic C-terminal domain contains a functional dilysine-retrieval motif, which is involved in the retrograde Golgi-to-ER transport of the protein By similarity. UniProtKB P33767
Sequence similarities	Belongs to the DDOST 48 kDa subunit family.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum Membrane
Domain	Signal Transmembrane
Molecular function	Transferase
PTM	Glycoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	protein amino acid N-linked glycosylation via asparagine Inferred from electronic annotation. Source: InterPro
Cellular component	endoplasmic reticulum membrane Inferred from electronic annotation. Source: InterPro integral to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	dolichyl-diphosphooligosaccharide-protein glycotransferase 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
	Signal peptide	1 – 19	19	Potential
	Chain	20 – 437	418	Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 48 kDa subunit		PRO_0000315923
Regions
	Topological domain	20 – 401	382	Lumenal Potential UniProtKB P33767
	Transmembrane	402 – 422	21	Potential
	Topological domain	423 – 437	15	Cytoplasmic Potential UniProtKB P33767
Amino acid modifications
	Glycosylation	275	1	N-linked (GlcNAc...) Potential
	Glycosylation	289	1	N-linked (GlcNAc...) Potential

Sequences

	Sequence		Length	Mass (Da)
	O59866-1 [UniParc]. Last modified August 1, 1999. Version 2. Checksum: E90CEDD0D0C4FC55	FASTA	437	48,899
	10 20 30 40 50 60 MKSALCIALA LTWSLLVQAA RQTVLAVADH DIGGYSTFLQ SLTDRDFDVK TSYIKDESAK 70 80 90 100 110 120 LFEYGERLYD NLILLSSQSK SLGPVFSPKS LLEFVQSGGN LFVVAGSQLP EGIRELGRQL 130 140 150 160 170 180 DMFLAERQSV VVDHFNHAEG SDDIILLDGI SENPYIISDE TRAAGPILYK GIGHYLGPNP 190 200 210 220 230 240 QTQPILRGNP TSYIYNTKTE AEVSKNPWAA GTQLFLVSVL QSSTGERVGL SGSIDMLKDE 250 260 270 280 290 300 YLSPQSPSFS KSNFLFARDL TNWVFQRKGV LQATNMTYGK VAEPLESRNA SCYRIKDEMI 310 320 330 340 350 360 FSIDISLLED GQQTPYVADD VQLELIMLDP YYRVNLVPVP SDSQTSQHYE AVLVAPDHYG 370 380 390 400 410 420 DFTFKIEYKR PGLTPIEEKS TFTLRQFFHN EFPRFLPHAY PYYASCFSVL GAFLLFCGIW 430 LLQKPAKPVV PSAKKQN

References

	« Hide 'large scale' referencesShow 'large scale' 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]	"S. pombe oligosaccharyltransferase homolog." Kawamukai M. Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 304-437.
[3]	"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	CU329672 Genomic DNA. Translation: CAA19346.1. AB015170 mRNA. Translation: BAA28753.1.
PIR	T41728. T43367.
RefSeq	NP_588153.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	O59866.
Genome annotation databases
GeneID	2539520.
KEGG	spo:SPCC338.15.
NMPDR	fig|4896.1.peg.491.
Organism-specific databases
GeneDB_Spombe	SPCC338.15.
Phylogenomic databases
OMA	VQLEFVR.
Enzyme and pathway databases
BRENDA	2.4.1.119. 653.
Gene expression databases
ArrayExpress	O59866.
Family and domain databases
InterPro	IPR005013. DDOST_48kDa. [Graphical view]
PANTHER	PTHR10830. DDOST_48kDa. 1 hit.
Pfam	PF03345. DDOST_48kD. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

OSTB_SCHPO

Accession

Primary (citable) accession number: O59866
Secondary accession number(s): Q7LWC1

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	August 1, 1999
Last modified:	November 3, 2009
This is version 44 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)