OST3_SCHPO
ID OST3_SCHPO Reviewed; 309 AA.
AC Q8TFH3;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 3;
DE AltName: Full=Oligosaccharyl transferase 34 kDa subunit;
DE AltName: Full=Oligosaccharyl transferase subunit OST3;
DE AltName: Full=Oligosaccharyl transferase subunit gamma;
DE Flags: Precursor;
GN Name=ost3; ORFNames=SPAPB17E12.11;
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).
RN [2]
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:P48439}.
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBUNIT: Component of the oligosaccharyltransferase (OST) complex.
CC {ECO:0000250|UniProtKB:P48439}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:16823372}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the OST3/OST6 family. {ECO:0000305}.
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DR EMBL; CU329670; CAD27504.1; -; Genomic_DNA.
DR RefSeq; NP_001018226.1; NM_001018706.2.
DR AlphaFoldDB; Q8TFH3; -.
DR SMR; Q8TFH3; -.
DR BioGRID; 280472; 2.
DR STRING; 4896.SPAPB17E12.11.1; -.
DR MaxQB; Q8TFH3; -.
DR PaxDb; Q8TFH3; -.
DR EnsemblFungi; SPAPB17E12.11.1; SPAPB17E12.11.1:pep; SPAPB17E12.11.
DR GeneID; 3361396; -.
DR KEGG; spo:SPAPB17E12.11; -.
DR PomBase; SPAPB17E12.11; ost3.
DR VEuPathDB; FungiDB:SPAPB17E12.11; -.
DR eggNOG; KOG2603; Eukaryota.
DR HOGENOM; CLU_052855_1_2_1; -.
DR InParanoid; Q8TFH3; -.
DR OMA; NLWAAVS; -.
DR PhylomeDB; Q8TFH3; -.
DR Reactome; R-SPO-5223345; Miscellaneous transport and binding events.
DR Reactome; R-SPO-6798695; Neutrophil degranulation.
DR UniPathway; UPA00378; -.
DR PRO; PR:Q8TFH3; -.
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:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR InterPro; IPR021149; OligosaccharylTrfase_OST3/OST6.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR12692; PTHR12692; 1.
DR Pfam; PF04756; OST3_OST6; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
PE 3: Inferred from homology;
KW Disulfide bond; Endoplasmic reticulum; Membrane; Reference proteome;
KW Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..309
FT /note="Dolichyl-diphosphooligosaccharide--protein
FT glycosyltransferase subunit 3"
FT /id="PRO_0000372619"
FT TRANSMEM 165..185
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 193..213
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 246..266
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 276..296
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 29..150
FT /note="Thioredoxin"
FT DISULFID 65..68
FT /note="Redox-active"
FT /evidence="ECO:0000250"
SQ SEQUENCE 309 AA; 34983 MW; AC7D08DFA715BF25 CRC64;
MNFFKILSFF SLFVITCFAK LDLNSKTDAD GVIQITGRLF HRIVNGKQDF TTVALFSADS
STMNCDVCRL IEPEFKALAN SYKLKYGLDS GIRFTYADFG KNKNLFQDFS IESVPNFWIF
KPKSIQAIHV DLSHGVTASH LAAIVEKHTG KIADIVYKQD QAKRVGAFLS YIIVGAALFF
TRKIIVKIFT SRKVWAALTI ITVITLSSGY MFTRIRFSPY SQRGEHGENL WLAGSQQFQF
GAEVQVVSLL YTALTMSSIF LAIVAPKVEG AKRQTLFVII WLAFLWIGYS FLVDIFKRKV
SMYPFKLLI
