OST1_SCHPO
ID OST1_SCHPO Reviewed; 450 AA.
AC Q10176;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 25-MAY-2022, entry version 138.
DE RecName: Full=Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 1;
DE AltName: Full=Oligosaccharyl transferase subunit alpha;
DE Flags: Precursor;
GN Name=ost1; ORFNames=SPAC27F1.07;
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]
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).
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:P41543}.
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBUNIT: Component of the oligosaccharyltransferase (OST) complex.
CC {ECO:0000250|UniProtKB:P41543}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Single-pass type I membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the OST1 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CU329670; CAA93296.1; -; Genomic_DNA.
DR PIR; T38465; T38465.
DR RefSeq; NP_594536.1; NM_001019965.2.
DR AlphaFoldDB; Q10176; -.
DR SMR; Q10176; -.
DR BioGRID; 278132; 2.
DR STRING; 4896.SPAC27F1.07.1; -.
DR MaxQB; Q10176; -.
DR PaxDb; Q10176; -.
DR EnsemblFungi; SPAC27F1.07.1; SPAC27F1.07.1:pep; SPAC27F1.07.
DR GeneID; 2541636; -.
DR KEGG; spo:SPAC27F1.07; -.
DR PomBase; SPAC27F1.07; ost1.
DR VEuPathDB; FungiDB:SPAC27F1.07; -.
DR eggNOG; KOG2291; Eukaryota.
DR HOGENOM; CLU_031381_1_0_1; -.
DR InParanoid; Q10176; -.
DR OMA; KTYMDTL; -.
DR PhylomeDB; Q10176; -.
DR UniPathway; UPA00378; -.
DR PRO; PR:Q10176; -.
DR Proteomes; UP000002485; Chromosome I.
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; IPR007676; Ribophorin_I.
DR PANTHER; PTHR21049; PTHR21049; 1.
DR Pfam; PF04597; Ribophorin_I; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum; Glycoprotein; Membrane; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..450
FT /note="Dolichyl-diphosphooligosaccharide--protein
FT glycosyltransferase subunit 1"
FT /id="PRO_0000021959"
FT TOPO_DOM 19..424
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 425..444
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 445..450
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 290
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 383
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 405
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 422
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 450 AA; 51684 MW; 8C96E34C2EEE1F11 CRC64;
MLVLKLLLWS IISGLSLAEQ VWRNSNAIRT IDLRSTYTKT LTSLIIVNEG DEPQNTYRYF
QQTSPGESVL SLSVSIKEEE KKGTNPIKVN NNVYDIPLQP PVKPGESRTL LIQAGLDGGV
RPLPAAVDQD EEQYLVYLTT LYLDSPYTTD LQRTRLILPS AKIDTYTTYN IDGAELPNRV
GNTLVYESRE TITGEDNDLG EIYVRYEHTV PIPRGADLYV QIDMHEYRKM LEVSERVVFE
NHAAKLKSNF DRAKWYMGNF YNPVSTAINR VVYSLPRNSK DVYYTDEVGN ITTSHMRVEP
HQTWIELNPR YPVFGGWNYL FQLDWKMPYE EFRSSKNRRE YLDIPLAWSP GDMIYEKAVW
SYVFPEGATN IEIEMPVEIS NSNVTKIHKF LDTLGRQVFT YEALNVTDGV PSDIVHISYE
YNSSAFFLRI AIITTLLILL AAAAYMIWAP
