OSTB_SCHPO
ID OSTB_SCHPO Reviewed; 437 AA.
AC O59866; Q7LWC1;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1999, sequence version 2.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit wbp1;
DE Short=Oligosaccharyl transferase 48 kDa subunit;
DE AltName: Full=Oligosaccharyl transferase subunit beta;
DE Flags: Precursor;
GN Name=wbp1; ORFNames=SPCC338.15;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1] {ECO:0000312|EMBL:CAA19346.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2] {ECO:0000305, ECO:0000312|EMBL:BAA28753.1}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 304-437.
RA Kawamukai M.;
RT "S. pombe oligosaccharyltransferase homolog.";
RL Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000305}
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
CC -!- FUNCTION: Subunit of the oligosaccharyl transferase (OST) complex that
CC catalyzes the initial transfer of a defined glycan
CC (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-
CC pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr
CC consensus motif in nascent polypeptide chains, the first step in
CC protein N-glycosylation. N-glycosylation occurs cotranslationally and
CC the complex associates with the Sec61 complex at the channel-forming
CC translocon complex that mediates protein translocation across the
CC endoplasmic reticulum (ER). All subunits are required for a maximal
CC enzyme activity. {ECO:0000250|UniProtKB:P33767}.
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000250|UniProtKB:P33767}.
CC -!- SUBUNIT: Component of the oligosaccharyltransferase (OST) complex.
CC {ECO:0000250|UniProtKB:P33767}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000269|PubMed:16823372}. Membrane {ECO:0000250|UniProtKB:P33767};
CC Single-pass type I membrane protein {ECO:0000250|UniProtKB:P33767}.
CC -!- DOMAIN: The cytoplasmic C-terminal domain contains a functional
CC dilysine-retrieval motif, which is involved in the retrograde Golgi-to-
CC ER transport of the protein. {ECO:0000250|UniProtKB:P33767}.
CC -!- SIMILARITY: Belongs to the DDOST 48 kDa subunit family. {ECO:0000255}.
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DR EMBL; CU329672; CAA19346.1; -; Genomic_DNA.
DR EMBL; AB015170; BAA28753.1; -; mRNA.
DR PIR; T41728; T41728.
DR PIR; T43367; T43367.
DR RefSeq; NP_588153.1; NM_001023142.2.
DR AlphaFoldDB; O59866; -.
DR SMR; O59866; -.
DR BioGRID; 276082; 2.
DR STRING; 4896.SPCC338.15.1; -.
DR iPTMnet; O59866; -.
DR MaxQB; O59866; -.
DR PaxDb; O59866; -.
DR PRIDE; O59866; -.
DR EnsemblFungi; SPCC338.15.1; SPCC338.15.1:pep; SPCC338.15.
DR GeneID; 2539520; -.
DR KEGG; spo:SPCC338.15; -.
DR PomBase; SPCC338.15; wbp1.
DR VEuPathDB; FungiDB:SPCC338.15; -.
DR eggNOG; KOG2754; Eukaryota.
DR HOGENOM; CLU_031804_0_0_1; -.
DR InParanoid; O59866; -.
DR OMA; YQFKVDY; -.
DR PhylomeDB; O59866; -.
DR Reactome; R-SPO-6798695; Neutrophil degranulation.
DR UniPathway; UPA00378; -.
DR PRO; PR:O59866; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:PomBase.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0008250; C:oligosaccharyltransferase complex; ISO:PomBase.
DR GO; GO:0018279; P:protein N-linked glycosylation via asparagine; IBA:GO_Central.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR005013; DDOST_48_kDa_subunit.
DR PANTHER; PTHR10830; PTHR10830; 1.
DR Pfam; PF03345; DDOST_48kD; 1.
DR SUPFAM; SSF52317; SSF52317; 1.
PE 2: Evidence at transcript level;
KW Endoplasmic reticulum; Glycoprotein; Membrane; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..437
FT /note="Dolichyl-diphosphooligosaccharide--protein
FT glycosyltransferase subunit wbp1"
FT /id="PRO_0000315923"
FT TOPO_DOM 20..401
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:P33767, ECO:0000255"
FT TRANSMEM 402..422
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 423..437
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P33767, ECO:0000255"
FT CARBOHYD 275
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 289
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 437 AA; 48899 MW; E90CEDD0D0C4FC55 CRC64;
MKSALCIALA LTWSLLVQAA RQTVLAVADH DIGGYSTFLQ SLTDRDFDVK TSYIKDESAK
LFEYGERLYD NLILLSSQSK SLGPVFSPKS LLEFVQSGGN LFVVAGSQLP EGIRELGRQL
DMFLAERQSV VVDHFNHAEG SDDIILLDGI SENPYIISDE TRAAGPILYK GIGHYLGPNP
QTQPILRGNP TSYIYNTKTE AEVSKNPWAA GTQLFLVSVL QSSTGERVGL SGSIDMLKDE
YLSPQSPSFS KSNFLFARDL TNWVFQRKGV LQATNMTYGK VAEPLESRNA SCYRIKDEMI
FSIDISLLED GQQTPYVADD VQLELIMLDP YYRVNLVPVP SDSQTSQHYE AVLVAPDHYG
DFTFKIEYKR PGLTPIEEKS TFTLRQFFHN EFPRFLPHAY PYYASCFSVL GAFLLFCGIW
LLQKPAKPVV PSAKKQN
