OST48_MOUSE
ID OST48_MOUSE Reviewed; 441 AA.
AC O54734; Q8C4P7;
DT 13-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 48 kDa subunit {ECO:0000305};
DE Short=DDOST 48 kDa subunit;
DE Short=Oligosaccharyl transferase 48 kDa subunit;
DE Flags: Precursor;
GN Name=Ddost {ECO:0000312|MGI:MGI:1194508};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9367678; DOI=10.1006/geno.1997.4966;
RA Yamagata T., Tsuru T., Momoi M.Y., Suwa K., Nozaki Y., Mukasa T.,
RA Ohashi H., Fukushima Y., Momoi T.;
RT "Genome organization of human 48-kDa oligosaccharyltransferase (DDOST).";
RL Genomics 45:535-540(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Tsuru T.;
RT "Mouse 48-kDa oligosaccharyltransferase (DDOST).";
RL Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Head;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP PROTEIN SEQUENCE OF 32-42; 175-183; 225-235 AND 366-376, AND IDENTIFICATION
RP BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 (By similarity). N-glycosylation occurs
CC cotranslationally and the complex associates with the Sec61 complex at
CC the channel-forming translocon complex that mediates protein
CC translocation across the endoplasmic reticulum (ER). All subunits are
CC required for a maximal enzyme activity (By similarity). Required for
CC the assembly of both SST3A- and SS3B-containing OST complexes (By
CC similarity). {ECO:0000250|UniProtKB:P39656,
CC ECO:0000250|UniProtKB:Q05052}.
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000250|UniProtKB:P39656}.
CC -!- SUBUNIT: Component of the oligosaccharyltransferase (OST) complex (By
CC similarity). OST exists in two different complex forms which contain
CC common core subunits RPN1, RPN2, OST48, OST4, DAD1 and TMEM258, either
CC STT3A or STT3B as catalytic subunits, and form-specific accessory
CC subunits (By similarity). STT3A complex assembly occurs through the
CC formation of 3 subcomplexes. Subcomplex 1 contains RPN1 and TMEM258,
CC subcomplex 2 contains the STT3A-specific subunits STT3A, DC2/OSTC, and
CC KCP2 as well as the core subunit OST4, and subcomplex 3 contains RPN2,
CC DAD1, and OST48. The STT3A complex can form stable complexes with the
CC Sec61 complex or with both the Sec61 and TRAP complexes. Interacts with
CC SMIM22 (By similarity). {ECO:0000250|UniProtKB:P39656,
CC ECO:0000250|UniProtKB:Q05052}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q29381}; Single-pass type I membrane protein
CC {ECO:0000250|UniProtKB:Q29381}.
CC -!- SIMILARITY: Belongs to the DDOST 48 kDa subunit family. {ECO:0000305}.
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DR EMBL; D89063; BAA23671.1; -; mRNA.
DR EMBL; AB012717; BAB82434.1; -; Genomic_DNA.
DR EMBL; AK081542; BAC38250.1; -; mRNA.
DR EMBL; AL807249; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC068132; AAH68132.1; -; mRNA.
DR CCDS; CCDS18824.1; -.
DR RefSeq; NP_031864.2; NM_007838.2.
DR AlphaFoldDB; O54734; -.
DR SMR; O54734; -.
DR BioGRID; 199080; 8.
DR ComplexPortal; CPX-5821; Oligosaccharyltransferase complex A.
DR ComplexPortal; CPX-5822; Oligosaccharyltransferase complex B.
DR IntAct; O54734; 3.
DR STRING; 10090.ENSMUSP00000030538; -.
DR iPTMnet; O54734; -.
DR PhosphoSitePlus; O54734; -.
DR SwissPalm; O54734; -.
DR EPD; O54734; -.
DR jPOST; O54734; -.
DR MaxQB; O54734; -.
DR PaxDb; O54734; -.
DR PeptideAtlas; O54734; -.
DR PRIDE; O54734; -.
DR ProteomicsDB; 295479; -.
DR TopDownProteomics; O54734; -.
DR Antibodypedia; 29811; 240 antibodies from 25 providers.
DR DNASU; 13200; -.
DR Ensembl; ENSMUST00000030538; ENSMUSP00000030538; ENSMUSG00000028757.
DR GeneID; 13200; -.
DR KEGG; mmu:13200; -.
DR UCSC; uc008vkt.1; mouse.
DR CTD; 1650; -.
DR MGI; MGI:1194508; Ddost.
DR VEuPathDB; HostDB:ENSMUSG00000028757; -.
DR eggNOG; KOG2754; Eukaryota.
DR GeneTree; ENSGT00390000017294; -.
DR HOGENOM; CLU_031804_0_0_1; -.
DR InParanoid; O54734; -.
DR OMA; YQFKVDY; -.
DR OrthoDB; 975158at2759; -.
DR PhylomeDB; O54734; -.
DR TreeFam; TF314821; -.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 13200; 28 hits in 79 CRISPR screens.
DR ChiTaRS; Ddost; mouse.
DR PRO; PR:O54734; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; O54734; protein.
DR Bgee; ENSMUSG00000028757; Expressed in parotid gland and 263 other tissues.
DR Genevisible; O54734; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IC:ComplexPortal.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0008250; C:oligosaccharyltransferase complex; ISS:UniProtKB.
DR GO; GO:0008047; F:enzyme activator activity; ISO:MGI.
DR GO; GO:0006486; P:protein glycosylation; ISS:UniProtKB.
DR GO; GO:0006487; P:protein N-linked glycosylation; ISO:MGI.
DR GO; GO:0018279; P:protein N-linked glycosylation via asparagine; IBA:GO_Central.
DR GO; GO:0031647; P:regulation of protein stability; ISO:MGI.
DR GO; GO:0034097; P:response to cytokine; ISO:MGI.
DR GO; GO:0042110; P:T cell activation; ISO:MGI.
DR InterPro; IPR005013; DDOST_48_kDa_subunit.
DR PANTHER; PTHR10830; PTHR10830; 1.
DR Pfam; PF03345; DDOST_48kD; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Endoplasmic reticulum; Membrane;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..28
FT /evidence="ECO:0000250"
FT CHAIN 29..441
FT /note="Dolichyl-diphosphooligosaccharide--protein
FT glycosyltransferase 48 kDa subunit"
FT /id="PRO_0000021958"
FT TOPO_DOM 29..412
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 413..432
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 433..441
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CONFLICT 321
FT /note="I -> V (in Ref. 1; BAA23671 and 2; BAB82434)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 441 AA; 49028 MW; C1B9A0B94D2A1CAC CRC64;
MKMDPRLAVR AWPLCGLLLA VLGCVCASGP RTLVLLDNLN VRDTHSLFFR SLKDRGFELT
FKTADDPSLS LIKYGEFLYD NLIIFSPSVE DFGGNINVET ISAFIDGGGS VLVAASSDIG
DPLRELGSEC GIEFDEEKTA VIDHHNYDVS DLGQHTLIVA DTENLLKAPT IVGKSSLNPI
LFRGVGMVAD PDNPLVLDIL TGSSTSYSFF PDKPITQYPH AVGRNTLLIA GLQARNNARV
IFSGSLDFFS DAFFNSAVQK ATPGAQRYSQ TGNYELAVAL SRWVFKEEGV LRVGPVSHHR
VGEMAPPNAY TVTDLVEYSI IIEQLSNGKW VPFDGDDIQL EFVRIDPFVR TFLKRKGGKY
SVQFKLPDVY GVFQFKVDYN RLGYTHLYSS TQVSVRPLQH TQYERFIPSA YPYYASAFSM
MAGLFIFSIV FLHMKEKEKS D
