OST48_HUMAN
ID OST48_HUMAN Reviewed; 456 AA.
AC P39656; B2RDQ4; B4DJE3; B4DLI2; O43244; Q5VWA5; Q8NI93; Q9BUI2;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 4.
DT 03-AUG-2022, entry version 207.
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|HGNC:HGNC:2728}; Synonyms=KIAA0115, OST48;
GN ORFNames=OK/SW-cl.45;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT GLY-8.
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 [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT GLY-8.
RC TISSUE=Bone marrow;
RX PubMed=7788527; DOI=10.1093/dnares/2.1.37;
RA Nagase T., Miyajima N., Tanaka A., Sazuka T., Seki N., Sato S., Tabata S.,
RA Ishikawa K., Kawarabayasi Y., Kotani H., Nomura N.;
RT "Prediction of the coding sequences of unidentified human genes. III. The
RT coding sequences of 40 new genes (KIAA0081-KIAA0120) deduced by analysis of
RT cDNA clones from human cell line KG-1.";
RL DNA Res. 2:37-43(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3), AND VARIANT
RP GLY-8.
RC TISSUE=Subthalamic nucleus, Synovium, and Umbilical cord blood;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT GLY-8.
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT GLY-8.
RC 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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 9-456 (ISOFORM 1).
RC TISSUE=Colon adenocarcinoma;
RA Shichijo S., Itoh K.;
RT "Identification of immuno-peptidmics that are recognized by tumor-reactive
RT CTL generated from TIL of colon cancer patients.";
RL Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [9]
RP FUNCTION.
RX PubMed=22467853; DOI=10.1242/jcs.103952;
RA Roboti P., High S.;
RT "The oligosaccharyltransferase subunits OST48, DAD1 and KCP2 function as
RT ubiquitous and selective modulators of mammalian N-glycosylation.";
RL J. Cell Sci. 125:3474-3484(2012).
RN [10]
RP IDENTIFICATION IN THE OLIGOSACCHARYLTRANSFERASE COMPLEX.
RX PubMed=25135935; DOI=10.1083/jcb.201404083;
RA Cherepanova N.A., Shrimal S., Gilmore R.;
RT "Oxidoreductase activity is necessary for N-glycosylation of cysteine-
RT proximal acceptor sites in glycoproteins.";
RL J. Cell Biol. 206:525-539(2014).
RN [11]
RP IDENTIFICATION IN THE OLIGOSACCHARYLTRANSFERASE COMPLEX.
RX PubMed=23606741; DOI=10.1242/jcs.115410;
RA Dumax-Vorzet A., Roboti P., High S.;
RT "OST4 is a subunit of the mammalian oligosaccharyltransferase required for
RT efficient N-glycosylation.";
RL J. Cell Sci. 126:2595-2606(2013).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [14]
RP INTERACTION WITH SMIM22.
RX PubMed=29765154; DOI=10.1038/s41388-018-0281-5;
RA Polycarpou-Schwarz M., Gross M., Mestdagh P., Schott J., Grund S.E.,
RA Hildenbrand C., Rom J., Aulmann S., Sinn H.P., Vandesompele J.,
RA Diederichs S.;
RT "The cancer-associated microprotein CASIMO1 controls cell proliferation and
RT interacts with squalene epoxidase modulating lipid droplet formation.";
RL Oncogene 37:4750-4768(2018).
RN [15] {ECO:0007744|PDB:6S7O, ECO:0007744|PDB:6S7T}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.50 ANGSTROMS), IDENTIFICATION OF THE
RP OLIGOSACCHARYLTRANSFERASE (OST) COMPLEX, FUNCTION, AND PATHWAY.
RX PubMed=31831667; DOI=10.1126/science.aaz3505;
RA Ramirez A.S., Kowal J., Locher K.P.;
RT "Cryo-electron microscopy structures of human oligosaccharyltransferase
RT complexes OST-A and OST-B.";
RL Science 366:1372-1375(2019).
RN [16]
RP VARIANT CDG1R ASP-217.
RX PubMed=22305527; DOI=10.1016/j.ajhg.2011.12.024;
RA Jones M.A., Ng B.G., Bhide S., Chin E., Rhodenizer D., He P., Losfeld M.E.,
RA He M., Raymond K., Berry G., Freeze H.H., Hegde M.R.;
RT "DDOST mutations identified by whole-exome sequencing are implicated in
RT congenital disorders of glycosylation.";
RL Am. J. Hum. Genet. 90:363-368(2012).
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 (PubMed:31831667). 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
CC (PubMed:22467853). {ECO:0000250|UniProtKB:Q05052,
CC ECO:0000269|PubMed:22467853, ECO:0000269|PubMed:31831667}.
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000269|PubMed:31831667}.
CC -!- SUBUNIT: Component of the oligosaccharyltransferase (OST) complex
CC (PubMed:31831667). OST exists in two different complex forms which
CC contain common core subunits RPN1, RPN2, OST48, OST4, DAD1 and TMEM258,
CC either STT3A or STT3B as catalytic subunits, and form-specific
CC accessory subunits (PubMed:23606741, PubMed:25135935, PubMed:31831667).
CC STT3A complex assembly occurs through the formation of 3 subcomplexes.
CC Subcomplex 1 contains RPN1 and TMEM258, subcomplex 2 contains the
CC STT3A-specific subunits STT3A, DC2/OSTC, and KCP2 as well as the core
CC subunit OST4, and subcomplex 3 contains RPN2, DAD1, and OST48. The
CC STT3A complex can form stable complexes with the Sec61 complex or with
CC both the Sec61 and TRAP complexes (By similarity). Interacts with
CC SMIM22 (PubMed:29765154). {ECO:0000250|UniProtKB:Q05052,
CC ECO:0000269|PubMed:23606741, ECO:0000269|PubMed:25135935,
CC ECO:0000269|PubMed:29765154, ECO:0000269|PubMed:31831667}.
CC -!- INTERACTION:
CC P39656; Q86WV6: STING1; NbExp=2; IntAct=EBI-358866, EBI-2800345;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q29381}; Single-pass type I membrane protein
CC {ECO:0000250|UniProtKB:Q29381}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=P39656-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P39656-2; Sequence=VSP_055498;
CC Name=3;
CC IsoId=P39656-3; Sequence=VSP_055499;
CC -!- DISEASE: Congenital disorder of glycosylation 1R (CDG1R) [MIM:614507]:
CC A form of congenital disorder of glycosylation, a multisystem disorder
CC caused by a defect in glycoprotein biosynthesis and characterized by
CC under-glycosylated serum glycoproteins. Congenital disorders of
CC glycosylation result in a wide variety of clinical features, such as
CC defects in the nervous system development, psychomotor retardation,
CC dysmorphic features, hypotonia, coagulation disorders, and
CC immunodeficiency. The broad spectrum of features reflects the critical
CC role of N-glycoproteins during embryonic development, differentiation,
CC and maintenance of cell functions. {ECO:0000269|PubMed:22305527}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
CC -!- SIMILARITY: Belongs to the DDOST 48 kDa subunit family. {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-18 is the initiator.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB93478.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; D89060; BAA23670.1; -; Genomic_DNA.
DR EMBL; D29643; BAA06126.1; -; mRNA.
DR EMBL; AK296041; BAG58805.1; -; mRNA.
DR EMBL; AK297009; BAG59544.1; -; mRNA.
DR EMBL; AK315633; BAG38001.1; -; mRNA.
DR EMBL; AL391357; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471134; EAW94938.1; -; Genomic_DNA.
DR EMBL; BC002594; AAH02594.1; -; mRNA.
DR EMBL; AB062391; BAB93478.1; ALT_INIT; mRNA.
DR PIR; S66254; A44654.
DR RefSeq; NP_005207.2; NM_005216.4.
DR PDB; 6S7O; EM; 3.50 A; G=1-456.
DR PDB; 6S7T; EM; 3.50 A; G=1-456.
DR PDBsum; 6S7O; -.
DR PDBsum; 6S7T; -.
DR AlphaFoldDB; P39656; -.
DR SMR; P39656; -.
DR BioGRID; 108017; 238.
DR ComplexPortal; CPX-5622; Oligosaccharyltransferase complex B.
DR CORUM; P39656; -.
DR IntAct; P39656; 86.
DR MINT; P39656; -.
DR STRING; 9606.ENSP00000399457; -.
DR BindingDB; P39656; -.
DR ChEMBL; CHEMBL4239; -.
DR TCDB; 9.B.142.3.17; the integral membrane glycosyltransferase family 39 (gt39) family.
DR iPTMnet; P39656; -.
DR PhosphoSitePlus; P39656; -.
DR SwissPalm; P39656; -.
DR BioMuta; DDOST; -.
DR DMDM; 239938926; -.
DR CPTAC; CPTAC-349; -.
DR CPTAC; CPTAC-350; -.
DR EPD; P39656; -.
DR jPOST; P39656; -.
DR MassIVE; P39656; -.
DR MaxQB; P39656; -.
DR PaxDb; P39656; -.
DR PeptideAtlas; P39656; -.
DR PRIDE; P39656; -.
DR ProteomicsDB; 55317; -. [P39656-1]
DR TopDownProteomics; P39656-1; -. [P39656-1]
DR Antibodypedia; 29811; 240 antibodies from 25 providers.
DR DNASU; 1650; -.
DR Ensembl; ENST00000415136.6; ENSP00000399457.3; ENSG00000244038.11. [P39656-1]
DR GeneID; 1650; -.
DR KEGG; hsa:1650; -.
DR UCSC; uc001bdo.1; human. [P39656-1]
DR CTD; 1650; -.
DR DisGeNET; 1650; -.
DR GeneCards; DDOST; -.
DR GeneReviews; DDOST; -.
DR HGNC; HGNC:2728; DDOST.
DR HPA; ENSG00000244038; Low tissue specificity.
DR MalaCards; DDOST; -.
DR MIM; 602202; gene.
DR MIM; 614507; phenotype.
DR neXtProt; NX_P39656; -.
DR OpenTargets; ENSG00000244038; -.
DR Orphanet; 300536; DDOST-CDG.
DR PharmGKB; PA27195; -.
DR VEuPathDB; HostDB:ENSG00000244038; -.
DR eggNOG; KOG2754; Eukaryota.
DR GeneTree; ENSGT00390000017294; -.
DR InParanoid; P39656; -.
DR OMA; YQFKVDY; -.
DR OrthoDB; 975158at2759; -.
DR PhylomeDB; P39656; -.
DR TreeFam; TF314821; -.
DR BRENDA; 2.4.99.18; 2681.
DR PathwayCommons; P39656; -.
DR Reactome; R-HSA-1799339; SRP-dependent cotranslational protein targeting to membrane.
DR Reactome; R-HSA-446203; Asparagine N-linked glycosylation.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR Reactome; R-HSA-879415; Advanced glycosylation endproduct receptor signaling.
DR Reactome; R-HSA-9694548; Maturation of spike protein.
DR SignaLink; P39656; -.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 1650; 727 hits in 1055 CRISPR screens.
DR ChiTaRS; DDOST; human.
DR GeneWiki; DDOST; -.
DR GenomeRNAi; 1650; -.
DR Pharos; P39656; Tchem.
DR PRO; PR:P39656; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; P39656; protein.
DR Bgee; ENSG00000244038; Expressed in corpus epididymis and 203 other tissues.
DR ExpressionAtlas; P39656; baseline and differential.
DR Genevisible; P39656; HS.
DR GO; GO:0035577; C:azurophil granule membrane; TAS:Reactome.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:HPA.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0008250; C:oligosaccharyltransferase complex; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0008047; F:enzyme activator activity; IMP:ARUK-UCL.
DR GO; GO:0006486; P:protein glycosylation; ISS:UniProtKB.
DR GO; GO:0006487; P:protein N-linked glycosylation; IDA:UniProtKB.
DR GO; GO:0018279; P:protein N-linked glycosylation via asparagine; IBA:GO_Central.
DR GO; GO:0031647; P:regulation of protein stability; IMP:ARUK-UCL.
DR GO; GO:0034097; P:response to cytokine; IDA:UniProtKB.
DR GO; GO:0042110; P:T cell activation; IDA:UniProtKB.
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 3D-structure; Alternative splicing; Congenital disorder of glycosylation;
KW Disease variant; Endoplasmic reticulum; Membrane; Reference proteome;
KW Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..42
FT /evidence="ECO:0000250"
FT CHAIN 43..456
FT /note="Dolichyl-diphosphooligosaccharide--protein
FT glycosyltransferase 48 kDa subunit"
FT /id="PRO_0000021957"
FT TOPO_DOM 43..427
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 428..447
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 448..456
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT VAR_SEQ 69..105
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055498"
FT VAR_SEQ 124..141
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055499"
FT VARIANT 8
FT /note="R -> G (in dbSNP:rs537816)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:7788527,
FT ECO:0000269|PubMed:9367678, ECO:0000269|Ref.5"
FT /id="VAR_047911"
FT VARIANT 217
FT /note="G -> D (in CDG1R; dbSNP:rs387906831)"
FT /evidence="ECO:0000269|PubMed:22305527"
FT /id="VAR_067544"
FT CONFLICT 229
FT /note="P -> R (in Ref. 3; BAG59544)"
FT /evidence="ECO:0000305"
FT CONFLICT 343
FT /note="G -> A (in Ref. 1; BAA23670)"
FT /evidence="ECO:0000305"
FT CONFLICT 434
FT /note="S -> P (in Ref. 1; BAA23670 and 2; BAA06126)"
FT /evidence="ECO:0000305"
FT STRAND 45..53
FT /evidence="ECO:0007829|PDB:6S7O"
FT HELIX 56..59
FT /evidence="ECO:0007829|PDB:6S7O"
FT HELIX 61..69
FT /evidence="ECO:0007829|PDB:6S7O"
FT STRAND 73..78
FT /evidence="ECO:0007829|PDB:6S7O"
FT STRAND 88..90
FT /evidence="ECO:0007829|PDB:6S7O"
FT STRAND 95..100
FT /evidence="ECO:0007829|PDB:6S7O"
FT STRAND 103..106
FT /evidence="ECO:0007829|PDB:6S7T"
FT HELIX 113..121
FT /evidence="ECO:0007829|PDB:6S7O"
FT STRAND 125..130
FT /evidence="ECO:0007829|PDB:6S7O"
FT HELIX 136..143
FT /evidence="ECO:0007829|PDB:6S7O"
FT TURN 144..146
FT /evidence="ECO:0007829|PDB:6S7O"
FT STRAND 155..157
FT /evidence="ECO:0007829|PDB:6S7T"
FT STRAND 158..163
FT /evidence="ECO:0007829|PDB:6S7O"
FT STRAND 168..170
FT /evidence="ECO:0007829|PDB:6S7O"
FT STRAND 173..175
FT /evidence="ECO:0007829|PDB:6S7O"
FT STRAND 177..180
FT /evidence="ECO:0007829|PDB:6S7O"
FT TURN 184..186
FT /evidence="ECO:0007829|PDB:6S7O"
FT STRAND 195..197
FT /evidence="ECO:0007829|PDB:6S7O"
FT STRAND 202..204
FT /evidence="ECO:0007829|PDB:6S7T"
FT STRAND 209..211
FT /evidence="ECO:0007829|PDB:6S7T"
FT STRAND 212..215
FT /evidence="ECO:0007829|PDB:6S7O"
FT STRAND 222..224
FT /evidence="ECO:0007829|PDB:6S7T"
FT STRAND 226..228
FT /evidence="ECO:0007829|PDB:6S7T"
FT STRAND 243..248
FT /evidence="ECO:0007829|PDB:6S7O"
FT STRAND 254..259
FT /evidence="ECO:0007829|PDB:6S7O"
FT HELIX 261..264
FT /evidence="ECO:0007829|PDB:6S7O"
FT HELIX 266..269
FT /evidence="ECO:0007829|PDB:6S7O"
FT TURN 276..279
FT /evidence="ECO:0007829|PDB:6S7O"
FT STRAND 283..285
FT /evidence="ECO:0007829|PDB:6S7O"
FT HELIX 288..299
FT /evidence="ECO:0007829|PDB:6S7O"
FT STRAND 302..304
FT /evidence="ECO:0007829|PDB:6S7O"
FT STRAND 306..308
FT /evidence="ECO:0007829|PDB:6S7T"
FT STRAND 312..315
FT /evidence="ECO:0007829|PDB:6S7O"
FT STRAND 323..328
FT /evidence="ECO:0007829|PDB:6S7O"
FT STRAND 330..334
FT /evidence="ECO:0007829|PDB:6S7O"
FT STRAND 337..341
FT /evidence="ECO:0007829|PDB:6S7T"
FT STRAND 344..347
FT /evidence="ECO:0007829|PDB:6S7T"
FT STRAND 354..367
FT /evidence="ECO:0007829|PDB:6S7O"
FT STRAND 369..371
FT /evidence="ECO:0007829|PDB:6S7T"
FT STRAND 377..380
FT /evidence="ECO:0007829|PDB:6S7O"
FT STRAND 386..394
FT /evidence="ECO:0007829|PDB:6S7O"
FT STRAND 397..399
FT /evidence="ECO:0007829|PDB:6S7T"
FT STRAND 402..411
FT /evidence="ECO:0007829|PDB:6S7O"
FT STRAND 415..418
FT /evidence="ECO:0007829|PDB:6S7T"
FT HELIX 423..425
FT /evidence="ECO:0007829|PDB:6S7O"
FT HELIX 426..445
FT /evidence="ECO:0007829|PDB:6S7O"
SQ SEQUENCE 456 AA; 50801 MW; 2707ABAC8FF158CB CRC64;
MGYFRCARAG SFGRRRKMEP STAARAWALF WLLLPLLGAV CASGPRTLVL LDNLNVRETH
SLFFRSLKDR GFELTFKTAD DPSLSLIKYG EFLYDNLIIF SPSVEDFGGN INVETISAFI
DGGGSVLVAA SSDIGDPLRE LGSECGIEFD EEKTAVIDHH NYDISDLGQH TLIVADTENL
LKAPTIVGKS SLNPILFRGV GMVADPDNPL VLDILTGSST SYSFFPDKPI TQYPHAVGKN
TLLIAGLQAR NNARVIFSGS LDFFSDSFFN SAVQKAAPGS QRYSQTGNYE LAVALSRWVF
KEEGVLRVGP VSHHRVGETA PPNAYTVTDL VEYSIVIQQL SNGKWVPFDG DDIQLEFVRI
DPFVRTFLKK KGGKYSVQFK LPDVYGVFQF KVDYNRLGYT HLYSSTQVSV RPLQHTQYER
FIPSAYPYYA SAFSMMLGLF IFSIVFLHMK EKEKSD
