ID RPN1_HUMAN Reviewed; 607 AA. AC P04843; B2R5Z0; D3DNB6; Q68DT1; DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot. DT 13-AUG-1987, sequence version 1. DT 02-SEP-2026, entry version 226. DE RecName: Full=Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 1 {ECO:0000305}; DE AltName: Full=Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 67 kDa subunit; DE AltName: Full=Ribophorin I; DE Short=RPN-I; DE AltName: Full=Ribophorin-1; DE Flags: Precursor; GN Name=RPN1 {ECO:0000312|HGNC:HGNC:10381}; 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 [MRNA]. RX PubMed=3034581; DOI=10.1002/j.1460-2075.1987.tb04721.x; RA Crimaudo C., Hortsch M., Gausepohl H., Meyer D.I.; RT "Human ribophorins I and II: the primary structure and membrane topology of RT two highly conserved rough endoplasmic reticulum-specific glycoproteins."; RL EMBO J. 6:75-82(1987). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Amygdala; 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Uterine endothelium; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. 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 (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Cervix; 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 SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]. RC TISSUE=Melanoma; RX PubMed=12643545; DOI=10.1021/pr025562r; RA Basrur V., Yang F., Kushimoto T., Higashimoto Y., Yasumoto K., Valencia J., RA Muller J., Vieira W.D., Watabe H., Shabanowitz J., Hearing V.J., Hunt D.F., RA Appella E.; RT "Proteomic analysis of early melanosomes: identification of novel RT melanosomal proteins."; RL J. Proteome Res. 2:69-79(2003). RN [7] RP TISSUE SPECIFICITY. RX PubMed=12887896; DOI=10.1016/s1097-2765(03)00243-0; RA Kelleher D.J., Karaoglu D., Mandon E.C., Gilmore R.; RT "Oligosaccharyltransferase isoforms that contain different catalytic STT3 RT subunits have distinct enzymatic properties."; RL Mol. Cell 12:101-111(2003). RN [8] RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]. RC TISSUE=Melanoma; RX PubMed=17081065; DOI=10.1021/pr060363j; RA Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H., Mangini N.J., RA Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R., Yamagishi S., RA Shabanowitz J., Hearing V.J., Wu C., Appella E., Hunt D.F.; RT "Proteomic and bioinformatic characterization of the biogenesis and RT function of melanosomes."; RL J. Proteome Res. 5:3135-3144(2006). RN [9] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-299. RC TISSUE=Liver; RX PubMed=19159218; DOI=10.1021/pr8008012; RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.; RT "Glycoproteomics analysis of human liver tissue by combination of multiple RT enzyme digestion and hydrazide chemistry."; RL J. Proteome Res. 8:651-661(2009). RN [10] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-187, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., RA Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [11] 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 [12] 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 [13] 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 [14] RP UBIQUITINATION. RX PubMed=24337577; DOI=10.1074/jbc.m113.534602; RA Andresen C.A., Smedegaard S., Sylvestersen K.B., Svensson C., RA Iglesias-Gato D., Cazzamali G., Nielsen T.K., Nielsen M.L., RA Flores-Morales A.; RT "Protein interaction screening for the ankyrin repeats and suppressor of RT cytokine signaling (SOCS) box (ASB) family identify Asb11 as a novel RT endoplasmic reticulum resident ubiquitin ligase."; RL J. Biol. Chem. 289:2043-2054(2014). RN [15] 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 [16] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-538, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25114211; DOI=10.1073/pnas.1413825111; RA Impens F., Radoshevich L., Cossart P., Ribet D.; RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by RT external stimuli."; RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014). RN [17] 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 [18] RP UFMYLATION. RX PubMed=32160526; DOI=10.1016/j.cell.2020.02.017; RA Liang J.R., Lingeman E., Luong T., Ahmed S., Muhar M., Nguyen T., RA Olzmann J.A., Corn J.E.; RT "A genome-wide ER-phagy screen highlights key roles of mitochondrial RT metabolism and ER-Resident UFMylation."; RL Cell 180:1160-1177(2020). RN [19] RP FUNCTION, AND UBIQUITINATION. RX PubMed=39567208; DOI=10.5483/bmbrep.2024-0142; RA Cho E.B., Vu V.A., Park S.H., Trinh L.T., Yoon J.B., Kim S.; RT "Transmembrane E3 ligase RNF128 regulates N-glycosylation by promoting RT ribophorin I ubiquitination and degradation."; RL BMB Rep. 0:0-0(2024). RN [20] {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). 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). CC {ECO:0000250|UniProtKB:E2RQ08, ECO:0000269|PubMed:31831667, CC ECO:0000269|PubMed:39567208}. 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 TMEM35A/NACHO (By similarity). {ECO:0000250|UniProtKB:E2RQ08, CC ECO:0000250|UniProtKB:Q91YQ5, ECO:0000269|PubMed:23606741, CC ECO:0000269|PubMed:25135935, ECO:0000269|PubMed:31831667}. CC -!- INTERACTION: CC P04843; P49069: CAMLG; NbExp=3; IntAct=EBI-355963, EBI-1748958; CC P04843; Q8IUG1: KRTAP1-3; NbExp=3; IntAct=EBI-355963, EBI-11749135; CC P04843; Q14165: MLEC; NbExp=3; IntAct=EBI-355963, EBI-1046466; CC P04843; Q9H5K3: POMK; NbExp=2; IntAct=EBI-355963, EBI-11337900; CC P04843; O43765: SGTA; NbExp=7; IntAct=EBI-355963, EBI-347996; CC P04843; P46977: STT3A; NbExp=3; IntAct=EBI-355963, EBI-719212; CC P04843; Q8TCJ2: STT3B; NbExp=4; IntAct=EBI-355963, EBI-2256290; CC P04843; Q9UMX0: UBQLN1; NbExp=4; IntAct=EBI-355963, EBI-741480; CC P04843; Q9UMX0-2: UBQLN1; NbExp=3; IntAct=EBI-355963, EBI-10173939; CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane CC {ECO:0000250|UniProtKB:E2RQ08}; Single-pass type I membrane protein CC {ECO:0000250|UniProtKB:E2RQ08}. Melanosome CC {ECO:0000269|PubMed:12643545, ECO:0000269|PubMed:17081065}. CC Note=Identified by mass spectrometry in melanosome fractions from stage CC I to stage IV. {ECO:0000269|PubMed:12643545, CC ECO:0000269|PubMed:17081065}. CC -!- TISSUE SPECIFICITY: Expressed in all tissues tested. CC {ECO:0000269|PubMed:12887896}. CC -!- PTM: Ubiquitinated by the ECS(ASB11) complex. Ubiquitinated by RNF128, CC leading to degradation in a proteasome/lysosome-dependent manner CC (PubMed:39567208). {ECO:0000269|PubMed:24337577, CC ECO:0000269|PubMed:39567208}. CC -!- PTM: Ufmylated by UFL1 in response to endoplasmic reticulum stress, CC promoting reticulophagy of endoplasmic reticulum sheets. CC {ECO:0000269|PubMed:32160526}. 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; Y00281; CAA68392.1; -; mRNA. DR EMBL; AK312369; BAG35287.1; -; mRNA. DR EMBL; CR749284; CAH18139.1; -; mRNA. DR EMBL; CH471052; EAW79306.1; -; Genomic_DNA. DR EMBL; CH471052; EAW79307.1; -; Genomic_DNA. DR EMBL; CH471052; EAW79308.1; -; Genomic_DNA. DR EMBL; BC010839; AAH10839.1; -; mRNA. DR CCDS; CCDS3051.1; -. DR PIR; A26168; A26168. DR RefSeq; NP_002941.1; NM_002950.4. DR PDB; 6S7O; EM; 3.50 A; E=1-607. DR PDB; 6S7T; EM; 3.50 A; E=1-607. DR PDB; 8B6L; EM; 7.60 A; O=1-607. DR PDB; 8PN9; EM; 3.61 A; E=1-607. DR PDB; 9N9J; EM; 3.20 A; O2=1-607. DR PDB; 9YGY; EM; 4.10 A; O2=1-607. DR AlphaFoldDB; P04843; -. DR EMDB; EMD-10110; -. DR EMDB; EMD-10112; -. DR EMDB; EMD-15870; -. DR EMDB; EMD-17779; -. DR EMDB; EMD-49171; -. DR EMDB; EMD-72945; -. DR SMR; P04843; -. DR BioGRID; 112099; 890. DR ComplexPortal; CPX-5621; Oligosaccharyltransferase complex A. DR ComplexPortal; CPX-5622; Oligosaccharyltransferase complex B, MAGT1 variant. DR ComplexPortal; CPX-8738; Oligosaccharyltransferase complex B, TUCS3 variant. DR CORUM; P04843; -. DR DIP; DIP-38152N; -. DR FunCoup; P04843; 3302. DR IntAct; P04843; 254. DR MINT; P04843; -. DR NDEx; IQUERY-CP-RPN1; 2 NDEx IQuery Curated Pathways. DR STRING; 9606.ENSP00000296255; -. DR BindingDB; P04843; -. DR ChEMBL; CHEMBL4295697; -. DR TCDB; 9.B.142.3.17; the integral membrane glycosyltransferase family 39 (gt39) family. DR GlyConnect; P04843; 5 N-Linked glycans (1 site). DR GlyCosmos; P04843; 2 sites, 7 glycans. DR GlyGen; P04843; 15 sites, 20 N-linked glycans (2 sites), 3 O-linked glycans (13 sites). DR iPTMnet; P04843; -. DR PhosphoSitePlus; P04843; -. DR SwissPalm; P04843; -. DR BioMuta; RPN1; -. DR DMDM; 132559; -. DR CPTAC; CPTAC-125; -. DR CPTAC; CPTAC-126; -. DR jPOST; P04843; -. DR MassIVE; P04843; -. DR PaxDb; 9606-ENSP00000296255; -. DR PeptideAtlas; P04843; -. DR ProteomicsDB; 51749; -. DR Pumba; P04843; -. DR TopDownProteomics; P04843; -. DR Antibodypedia; 4058; 590 antibodies from 33 providers. DR DNASU; 6184; -. DR Ensembl; ENST00000296255.8; ENSP00000296255.3; ENSG00000163902.13. DR GeneID; 6184; -. DR KEGG; hsa:6184; -. DR MANE-Select; ENST00000296255.8; ENSP00000296255.3; NM_002950.4; NP_002941.1. DR UCSC; uc003ekr.2; human. DR AGR; HGNC:10381; -. DR ClinPGx; PA34777; -. DR CTD; 6184; -. DR DisGeNET; 6184; -. DR GeneCards; RPN1; -. DR HGNC; HGNC:10381; RPN1. DR HPA; ENSG00000163902; Low tissue specificity. DR MalaCards; RPN1; -. DR MIM; 180470; gene. DR OpenTargets; ENSG00000163902; -. DR Orphanet; 402020; Acute myeloid leukemia with inv(3)(q21q26.2) or t(3;3)(q21;q26.2). DR VEuPathDB; HostDB:ENSG00000163902; -. DR eggNOG; KOG2291; Eukaryota. DR GeneTree; ENSGT00390000009630; -. DR InParanoid; P04843; -. DR OMA; RYEYARE; -. DR OrthoDB; 310030at2759; -. DR PAN-GO; P04843; 2 GO annotations based on evolutionary models. DR PhylomeDB; P04843; -. DR BRENDA; 2.4.99.18; 2681. DR PathwayCommons; P04843; -. 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-9694548; Maturation of spike protein. DR Reactome; R-HSA-9768727; Regulation of CDH1 posttranslational processing and trafficking to plasma membrane. DR Reactome; R-HSA-9918432; Maturation of DENV proteins. DR Reactome; R-HSA-9931295; PD-L1(CD274) glycosylation and translocation to plasma membrane. DR SignaLink; P04843; -. DR SIGNOR; P04843; -. DR UniPathway; UPA00378; -. DR Agora; ENSG00000163902; -. DR BioGRID-ORCS; 6184; 643 hits in 1163 CRISPR screens. DR CD-CODE; FB4E32DD; Presynaptic clusters and postsynaptic densities. DR ChiTaRS; RPN1; human. DR GeneWiki; RPN1; -. DR GenomeRNAi; 6184; -. DR Pharos; P04843; Tbio. DR PRO; PR:P04843; -. DR Proteomes; UP000005640; Chromosome 3. DR RNAct; P04843; protein. DR Bgee; ENSG00000163902; Expressed in stromal cell of endometrium and 206 other cell types or tissues. DR ExpressionAtlas; P04843; baseline and differential. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0005783; C:endoplasmic reticulum; IDA:HPA. DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB. DR GO; GO:0042470; C:melanosome; EXP:UniProtKB. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0008250; C:oligosaccharyltransferase complex; IDA:UniProtKB. DR GO; GO:0160226; C:oligosaccharyltransferase complex A; IDA:UniProtKB. DR GO; GO:0160227; C:oligosaccharyltransferase complex B; IDA:UniProtKB. DR GO; GO:0005791; C:rough endoplasmic reticulum; IEA:Ensembl. DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB. DR GO; GO:0006487; P:protein N-linked glycosylation; IDA:UniProtKB. DR InterPro; IPR007676; Ribophorin_I. DR PANTHER; PTHR21049:SF0; DOLICHYL-DIPHOSPHOOLIGOSACCHARIDE--PROTEIN GLYCOSYLTRANSFERASE SUBUNIT 1; 1. DR PANTHER; PTHR21049; RIBOPHORIN I; 1. DR Pfam; PF04597; Ribophorin_I; 1. DR PDBsum; 6S7O; -. DR PDBsum; 6S7T; -. DR PDBsum; 8B6L; -. DR PDBsum; 8PN9; -. DR PDBsum; 9N9J; -. DR PDBsum; 9YGY; -. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Endoplasmic reticulum; Glycoprotein; KW Isopeptide bond; Membrane; Proteomics identification; Reference proteome; KW Signal; Transmembrane; Transmembrane helix; Ubl conjugation. FT SIGNAL 1..23 FT CHAIN 24..607 FT /note="Dolichyl-diphosphooligosaccharide--protein FT glycosyltransferase subunit 1" FT /id="PRO_0000022241" FT TOPO_DOM 24..438 FT /note="Lumenal" FT /evidence="ECO:0000255" FT TRANSMEM 439..457 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 458..607 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT MOD_RES 187 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 538 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q91YQ5" FT CARBOHYD 299 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19159218" FT CROSSLNK 538 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0007744|PubMed:25114211" FT STRAND 31..33 FT /evidence="ECO:0007829|PDB:6S7O" FT STRAND 35..41 FT /evidence="ECO:0007829|PDB:6S7O" FT STRAND 43..57 FT /evidence="ECO:0007829|PDB:6S7O" FT STRAND 66..71 FT /evidence="ECO:0007829|PDB:6S7O" FT STRAND 77..80 FT /evidence="ECO:0007829|PDB:6S7O" FT STRAND 83..91 FT /evidence="ECO:0007829|PDB:6S7O" FT STRAND 95..98 FT /evidence="ECO:0007829|PDB:6S7O" FT STRAND 113..121 FT /evidence="ECO:0007829|PDB:6S7O" FT STRAND 126..137 FT /evidence="ECO:0007829|PDB:6S7O" FT STRAND 140..143 FT /evidence="ECO:0007829|PDB:6S7O" FT STRAND 153..158 FT /evidence="ECO:0007829|PDB:6S7O" FT STRAND 169..176 FT /evidence="ECO:0007829|PDB:6S7O" FT STRAND 178..180 FT /evidence="ECO:0007829|PDB:6S7O" FT STRAND 182..185 FT /evidence="ECO:0007829|PDB:6S7T" FT STRAND 195..199 FT /evidence="ECO:0007829|PDB:6S7O" FT STRAND 214..219 FT /evidence="ECO:0007829|PDB:6S7O" FT STRAND 226..235 FT /evidence="ECO:0007829|PDB:6S7O" FT STRAND 238..240 FT /evidence="ECO:0007829|PDB:6S7O" FT STRAND 242..251 FT /evidence="ECO:0007829|PDB:6S7O" FT STRAND 254..257 FT /evidence="ECO:0007829|PDB:6S7O" FT HELIX 263..267 FT /evidence="ECO:0007829|PDB:6S7O" FT STRAND 270..272 FT /evidence="ECO:0007829|PDB:6S7O" FT STRAND 280..284 FT /evidence="ECO:0007829|PDB:6S7O" FT STRAND 292..294 FT /evidence="ECO:0007829|PDB:6S7T" FT STRAND 296..299 FT /evidence="ECO:0007829|PDB:6S7O" FT STRAND 303..307 FT /evidence="ECO:0007829|PDB:6S7O" FT STRAND 312..316 FT /evidence="ECO:0007829|PDB:6S7O" FT STRAND 328..336 FT /evidence="ECO:0007829|PDB:6S7O" FT HELIX 339..341 FT /evidence="ECO:0007829|PDB:6S7O" FT STRAND 342..345 FT /evidence="ECO:0007829|PDB:6S7O" FT STRAND 348..356 FT /evidence="ECO:0007829|PDB:6S7O" FT STRAND 364..366 FT /evidence="ECO:0007829|PDB:6S7O" FT STRAND 368..373 FT /evidence="ECO:0007829|PDB:6S7O" FT STRAND 382..384 FT /evidence="ECO:0007829|PDB:6S7O" FT HELIX 392..394 FT /evidence="ECO:0007829|PDB:6S7O" FT STRAND 395..397 FT /evidence="ECO:0007829|PDB:6S7O" FT STRAND 406..413 FT /evidence="ECO:0007829|PDB:6S7O" FT STRAND 415..417 FT /evidence="ECO:0007829|PDB:6S7O" FT HELIX 418..420 FT /evidence="ECO:0007829|PDB:6S7O" FT STRAND 423..429 FT /evidence="ECO:0007829|PDB:6S7O" FT HELIX 433..436 FT /evidence="ECO:0007829|PDB:6S7O" FT HELIX 437..456 FT /evidence="ECO:0007829|PDB:6S7O" FT HELIX 467..500 FT /evidence="ECO:0007829|PDB:6S7O" FT TURN 506..508 FT /evidence="ECO:0007829|PDB:6S7O" FT HELIX 509..533 FT /evidence="ECO:0007829|PDB:6S7O" FT STRAND 535..537 FT /evidence="ECO:0007829|PDB:6S7O" FT HELIX 541..564 FT /evidence="ECO:0007829|PDB:6S7O" FT STRAND 567..569 FT /evidence="ECO:0007829|PDB:6S7O" FT HELIX 573..592 FT /evidence="ECO:0007829|PDB:6S7O" SQ SEQUENCE 607 AA; 68569 MW; A2351A9CFABAEB6C CRC64; MEAPAAGLFL LLLLGTWAPA PGSASSEAPP LINEDVKRTV DLSSHLAKVT AEVVLAHLGG GSTSRATSFL LALEPELEAR LAHLGVQVKG EDEEENNLEV RETKIKGKSG RFFTVKLPVA LDPGAKISVI VETVYTHVLH PYPTQITQSE KQFVVFEGNH YFYSPYPTKT QTMRVKLASR NVESYTKLGN PTRSEDLLDY GPFRDVPAYS QDTFKVHYEN NSPFLTITSM TRVIEVSHWG NIAVEENVDL KHTGAVLKGP FSRYDYQRQP DSGISSIRSF KTILPAAAQD VYYRDEIGNV STSHLLILDD SVEMEIRPRF PLFGGWKTHY IVGYNLPSYE YLYNLGDQYA LKMRFVDHVF DEQVIDSLTV KIILPEGAKN IEIDSPYEIS RAPDELHYTY LDTFGRPVIV AYKKNLVEQH IQDIVVHYTF NKVLMLQEPL LVVAAFYILF FTVIIYVRLD FSITKDPAAE ARMKVACITE QVLTLVNKRI GLYRHFDETV NRYKQSRDIS TLNSGKKSLE TEHKALTSEI ALLQSRLKTE GSDLCDRVSE MQKLDAQVKE LVLKSAVEAE RLVAGKLKKD TYIENEKLIS GKRQELVTKI DHILDAL //