ID RPN2_HUMAN Reviewed; 631 AA. AC P04844; Q5JYR6; Q6IBA5; Q96E21; Q9BUQ3; Q9UBE1; DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2000, sequence version 3. DT 27-MAR-2024, entry version 217. DE RecName: Full=Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 2 {ECO:0000305}; DE AltName: Full=Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 63 kDa subunit; DE AltName: Full=RIBIIR; DE AltName: Full=Ribophorin II; DE Short=RPN-II; DE AltName: Full=Ribophorin-2; DE Flags: Precursor; GN Name=RPN2 {ECO:0000312|HGNC:HGNC:10382}; 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] (ISOFORM 1). 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 [GENOMIC DNA]. RA Iolascon A., Totaro A., Gasparini P.; RT "Genomic structure of human ribophorin II gene."; RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). 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 MRNA] (ISOFORM 1). RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=11780052; DOI=10.1038/414865a; RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.; RT "The DNA sequence and comparative analysis of human chromosome 20."; RL Nature 414:865-871(2001). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton 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 [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Muscle, Pancreas, and Placenta; 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 [8] RP PROTEIN SEQUENCE OF 23-36. RC TISSUE=Platelet; RX PubMed=12665801; DOI=10.1038/nbt810; RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., RA Vandekerckhove J.; RT "Exploring proteomes and analyzing protein processing by mass spectrometric RT identification of sorted N-terminal peptides."; RL Nat. Biotechnol. 21:566-569(2003). RN [9] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-106. 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 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 [11] 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 [12] 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 [13] 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 [14] 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 [15] RP INTERACTION WITH DDI2. RX PubMed=29290612; DOI=10.1016/j.molcel.2017.11.035; RA Kottemann M.C., Conti B.A., Lach F.P., Smogorzewska A.; RT "Removal of RTF2 from Stalled Replisomes Promotes Maintenance of Genome RT Integrity."; RL Mol. Cell 69:24-35.E5(2018). RN [16] {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. {ECO:0000250|UniProtKB:F1PCT7, CC 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 DDI2 CC (PubMed:29290612). Interacts with TMEM35A/NACHO (By similarity). CC {ECO:0000250|UniProtKB:F1PCT7, ECO:0000250|UniProtKB:Q9DBG6, CC ECO:0000269|PubMed:23606741, ECO:0000269|PubMed:25135935, CC ECO:0000269|PubMed:29290612, ECO:0000269|PubMed:31831667}. CC -!- INTERACTION: CC P04844; Q9H5K3: POMK; NbExp=2; IntAct=EBI-719731, EBI-11337900; CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum CC {ECO:0000250|UniProtKB:F1PCT7}. Endoplasmic reticulum membrane; Multi- CC pass membrane protein {ECO:0000305}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P04844-1; Sequence=Displayed; CC Name=2; CC IsoId=P04844-2; Sequence=VSP_043051, VSP_043052; CC -!- TISSUE SPECIFICITY: Expressed in all tissues tested. CC -!- SIMILARITY: Belongs to the SWP1 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; Y00282; CAA68393.1; -; mRNA. DR EMBL; AJ237734; CAB54801.1; -; Genomic_DNA. DR EMBL; AJ237735; CAB54801.1; JOINED; Genomic_DNA. DR EMBL; AJ237733; CAB54801.1; JOINED; Genomic_DNA. DR EMBL; AJ237736; CAB54801.1; JOINED; Genomic_DNA. DR EMBL; AJ237737; CAB54801.1; JOINED; Genomic_DNA. DR EMBL; AJ237738; CAB54801.1; JOINED; Genomic_DNA. DR EMBL; AJ237739; CAB54801.1; JOINED; Genomic_DNA. DR EMBL; AJ237740; CAB54801.1; JOINED; Genomic_DNA. DR EMBL; AJ237741; CAB54801.1; JOINED; Genomic_DNA. DR EMBL; AJ237742; CAB54801.1; JOINED; Genomic_DNA. DR EMBL; AJ237743; CAB54801.1; JOINED; Genomic_DNA. DR EMBL; AJ237744; CAB54801.1; JOINED; Genomic_DNA. DR EMBL; AJ237745; CAB54801.1; JOINED; Genomic_DNA. DR EMBL; AJ237746; CAB54801.1; JOINED; Genomic_DNA. DR EMBL; AJ237747; CAB54801.1; JOINED; Genomic_DNA. DR EMBL; AJ237748; CAB54801.1; JOINED; Genomic_DNA. DR EMBL; AJ237749; CAB54801.1; JOINED; Genomic_DNA. DR EMBL; AK096243; BAG53237.1; -; mRNA. DR EMBL; CR456899; CAG33180.1; -; mRNA. DR EMBL; AL031659; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471077; EAW76073.1; -; Genomic_DNA. DR EMBL; BC002380; AAH02380.2; -; mRNA. DR EMBL; BC003560; AAH03560.1; -; mRNA. DR EMBL; BC013028; AAH13028.2; -; mRNA. DR EMBL; BC020222; AAH20222.1; -; mRNA. DR CCDS; CCDS13291.1; -. [P04844-1] DR CCDS; CCDS46599.1; -. [P04844-2] DR PIR; B26168; B26168. DR RefSeq; NP_001129243.1; NM_001135771.2. [P04844-2] DR RefSeq; NP_001311228.1; NM_001324299.1. DR RefSeq; NP_001311230.1; NM_001324301.1. DR RefSeq; NP_001311231.1; NM_001324302.1. DR RefSeq; NP_001311232.1; NM_001324303.1. DR RefSeq; NP_001311233.1; NM_001324304.1. DR RefSeq; NP_001311234.1; NM_001324305.1. DR RefSeq; NP_001311235.1; NM_001324306.1. DR RefSeq; NP_002942.2; NM_002951.4. [P04844-1] DR PDB; 6S7O; EM; 3.50 A; F=1-631. DR PDB; 6S7T; EM; 3.50 A; F=1-631. DR PDB; 8B6L; EM; 7.60 A; P=1-631. DR PDBsum; 6S7O; -. DR PDBsum; 6S7T; -. DR PDBsum; 8B6L; -. DR AlphaFoldDB; P04844; -. DR EMDB; EMD-10110; -. DR EMDB; EMD-10112; -. DR EMDB; EMD-15870; -. DR SMR; P04844; -. DR BioGRID; 112100; 799. DR ComplexPortal; CPX-5621; Oligosaccharyltransferase complex A. DR ComplexPortal; CPX-5622; Oligosaccharyltransferase complex B. DR CORUM; P04844; -. DR IntAct; P04844; 122. DR MINT; P04844; -. DR STRING; 9606.ENSP00000237530; -. DR TCDB; 9.B.142.3.17; the integral membrane glycosyltransferase family 39 (gt39) family. DR GlyConnect; 1187; 16 N-Linked glycans (1 site). DR GlyCosmos; P04844; 2 sites, 17 glycans. DR GlyGen; P04844; 6 sites, 16 N-linked glycans (1 site), 2 O-linked glycans (5 sites). DR iPTMnet; P04844; -. DR MetOSite; P04844; -. DR PhosphoSitePlus; P04844; -. DR SwissPalm; P04844; -. DR BioMuta; RPN2; -. DR DMDM; 9297108; -. DR EPD; P04844; -. DR jPOST; P04844; -. DR MassIVE; P04844; -. DR MaxQB; P04844; -. DR PaxDb; 9606-ENSP00000237530; -. DR PeptideAtlas; P04844; -. DR PRIDE; P04844; -. DR ProteomicsDB; 51750; -. [P04844-1] DR ProteomicsDB; 51751; -. [P04844-2] DR Pumba; P04844; -. DR TopDownProteomics; P04844-1; -. [P04844-1] DR Antibodypedia; 1855; 217 antibodies from 26 providers. DR DNASU; 6185; -. DR Ensembl; ENST00000237530.11; ENSP00000237530.6; ENSG00000118705.18. [P04844-1] DR Ensembl; ENST00000373622.9; ENSP00000362724.5; ENSG00000118705.18. [P04844-2] DR Ensembl; ENST00000709409.1; ENSP00000517677.1; ENSG00000291973.1. [P04844-2] DR Ensembl; ENST00000709412.1; ENSP00000517679.1; ENSG00000291973.1. [P04844-1] DR GeneID; 6185; -. DR KEGG; hsa:6185; -. DR MANE-Select; ENST00000237530.11; ENSP00000237530.6; NM_002951.5; NP_002942.2. DR UCSC; uc002xgp.4; human. [P04844-1] DR AGR; HGNC:10382; -. DR CTD; 6185; -. DR DisGeNET; 6185; -. DR GeneCards; RPN2; -. DR HGNC; HGNC:10382; RPN2. DR HPA; ENSG00000118705; Low tissue specificity. DR MIM; 180490; gene. DR neXtProt; NX_P04844; -. DR OpenTargets; ENSG00000118705; -. DR PharmGKB; PA34778; -. DR VEuPathDB; HostDB:ENSG00000118705; -. DR eggNOG; KOG2447; Eukaryota. DR GeneTree; ENSGT00390000002635; -. DR HOGENOM; CLU_017104_0_0_1; -. DR InParanoid; P04844; -. DR OMA; DGVYKQK; -. DR OrthoDB; 2877438at2759; -. DR PhylomeDB; P04844; -. DR TreeFam; TF106146; -. DR BRENDA; 2.4.99.18; 2681. DR PathwayCommons; P04844; -. 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 SignaLink; P04844; -. DR SIGNOR; P04844; -. DR UniPathway; UPA00378; -. DR BioGRID-ORCS; 6185; 642 hits in 1169 CRISPR screens. DR ChiTaRS; RPN2; human. DR GeneWiki; RPN2; -. DR GenomeRNAi; 6185; -. DR Pharos; P04844; Tbio. DR PRO; PR:P04844; -. DR Proteomes; UP000005640; Chromosome 20. DR RNAct; P04844; Protein. DR Bgee; ENSG00000118705; Expressed in corpus epididymis and 222 other cell types or tissues. DR ExpressionAtlas; P04844; baseline and differential. DR GO; GO:0005783; C:endoplasmic reticulum; IDA:HPA. DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0016604; C:nuclear body; IDA:HPA. DR GO; GO:0008250; C:oligosaccharyltransferase complex; IDA:UniProtKB. DR GO; GO:0036211; P:protein modification process; TAS:ProtInc. DR GO; GO:0006487; P:protein N-linked glycosylation; IDA:UniProtKB. DR GO; GO:0018279; P:protein N-linked glycosylation via asparagine; NAS:HGNC-UCL. DR InterPro; IPR008814; Swp1. DR PANTHER; PTHR12640:SF0; DOLICHYL-DIPHOSPHOOLIGOSACCHARIDE--PROTEIN GLYCOSYLTRANSFERASE SUBUNIT 2; 1. DR PANTHER; PTHR12640; RIBOPHORIN II; 1. DR Pfam; PF05817; Ribophorin_II; 1. DR Genevisible; P04844; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Direct protein sequencing; KW Endoplasmic reticulum; Glycoprotein; Isopeptide bond; Membrane; KW Reference proteome; Signal; Transmembrane; Transmembrane helix; KW Ubl conjugation. FT SIGNAL 1..22 FT /evidence="ECO:0000269|PubMed:12665801" FT CHAIN 23..631 FT /note="Dolichyl-diphosphooligosaccharide--protein FT glycosyltransferase subunit 2" FT /id="PRO_0000022244" FT TOPO_DOM 23..540 FT /note="Lumenal" FT /evidence="ECO:0000255" FT TRANSMEM 541..561 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 562..571 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 572..592 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 593..596 FT /note="Lumenal" FT /evidence="ECO:0000255" FT TRANSMEM 597..617 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 618..631 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT CARBOHYD 106 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19159218" FT CROSSLNK 154 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin)" FT VAR_SEQ 70..101 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_043051" FT VAR_SEQ 627 FT /note="K -> KRIAAEQSSRLAKYRTL (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_043052" FT VARIANT 597 FT /note="L -> F (in dbSNP:rs34951322)" FT /id="VAR_054040" FT CONFLICT 197 FT /note="V -> L (in Ref. 1; CAA68393)" FT /evidence="ECO:0000305" FT CONFLICT 201 FT /note="F -> C (in Ref. 1; CAA68393)" FT /evidence="ECO:0000305" FT CONFLICT 260 FT /note="A -> S (in Ref. 1; CAA68393)" FT /evidence="ECO:0000305" FT CONFLICT 286 FT /note="A -> S (in Ref. 4; CAG33180)" FT /evidence="ECO:0000305" FT CONFLICT 423 FT /note="V -> M (in Ref. 1; CAA68393)" FT /evidence="ECO:0000305" FT CONFLICT 427 FT /note="A -> V (in Ref. 4; CAG33180)" FT /evidence="ECO:0000305" FT CONFLICT 571 FT /note="T -> I (in Ref. 7; AAH13028)" FT /evidence="ECO:0000305" FT STRAND 374..376 FT /evidence="ECO:0007829|PDB:6S7O" FT STRAND 392..395 FT /evidence="ECO:0007829|PDB:6S7T" FT STRAND 398..400 FT /evidence="ECO:0007829|PDB:6S7O" FT STRAND 403..407 FT /evidence="ECO:0007829|PDB:6S7O" FT STRAND 419..421 FT /evidence="ECO:0007829|PDB:6S7O" FT STRAND 423..425 FT /evidence="ECO:0007829|PDB:6S7O" FT STRAND 435..440 FT /evidence="ECO:0007829|PDB:6S7O" FT TURN 441..443 FT /evidence="ECO:0007829|PDB:6S7O" FT STRAND 446..450 FT /evidence="ECO:0007829|PDB:6S7O" FT STRAND 452..454 FT /evidence="ECO:0007829|PDB:6S7T" FT STRAND 455..458 FT /evidence="ECO:0007829|PDB:6S7O" FT STRAND 465..467 FT /evidence="ECO:0007829|PDB:6S7O" FT TURN 469..471 FT /evidence="ECO:0007829|PDB:6S7O" FT STRAND 472..474 FT /evidence="ECO:0007829|PDB:6S7O" FT STRAND 479..483 FT /evidence="ECO:0007829|PDB:6S7O" FT STRAND 488..491 FT /evidence="ECO:0007829|PDB:6S7O" FT STRAND 497..502 FT /evidence="ECO:0007829|PDB:6S7O" FT HELIX 539..563 FT /evidence="ECO:0007829|PDB:6S7O" FT HELIX 574..595 FT /evidence="ECO:0007829|PDB:6S7O" FT HELIX 599..628 FT /evidence="ECO:0007829|PDB:6S7O" SQ SEQUENCE 631 AA; 69284 MW; E24D7B3565141676 CRC64; MAPPGSSTVF LLALTIIAST WALTPTHYLT KHDVERLKAS LDRPFTNLES AFYSIVGLSS LGAQVPDAKK ACTYIRSNLD PSNVDSLFYA AQASQALSGC EISISNETKD LLLAAVSEDS SVTQIYHAVA ALSGFGLPLA SQEALSALTA RLSKEETVLA TVQALQTASH LSQQADLRSI VEEIEDLVAR LDELGGVYLQ FEEGLETTAL FVAATYKLMD HVGTEPSIKE DQVIQLMNAI FSKKNFESLS EAFSVASAAA VLSHNRYHVP VVVVPEGSAS DTHEQAILRL QVTNVLSQPL TQATVKLEHA KSVASRATVL QKTSFTPVGD VFELNFMNVK FSSGYYDFLV EVEGDNRYIA NTVELRVKIS TEVGITNVDL STVDKDQSIA PKTTRVTYPA KAKGTFIADS HQNFALFFQL VDVNTGAELT PHQTFVRLHN QKTGQEVVFV AEPDNKNVYK FELDTSERKI EFDSASGTYT LYLIIGDATL KNPILWNVAD VVIKFPEEEA PSTVLSQNLF TPKQEIQHLF REPEKRPPTV VSNTFTALIL SPLLLLFALW IRIGANVSNF TFAPSTIIFH LGHAAMLGLM YVYWTQLNMF QTLKYLAILG SVTFLAGNRM LAQQAVKRTA H //