RPN2_HUMAN
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 03-AUG-2022, entry version 208.
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}.
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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 PDBsum; 6S7O; -.
DR PDBsum; 6S7T; -.
DR AlphaFoldDB; P04844; -.
DR SMR; P04844; -.
DR BioGRID; 112100; 502.
DR ComplexPortal; CPX-5621; Oligosaccharyltransferase complex A.
DR ComplexPortal; CPX-5622; Oligosaccharyltransferase complex B.
DR CORUM; P04844; -.
DR IntAct; P04844; 107.
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 GlyGen; P04844; 2 sites, 16 N-linked glycans (1 site), 1 O-linked glycan (1 site).
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; P04844; -.
DR PeptideAtlas; P04844; -.
DR PRIDE; P04844; -.
DR ProteomicsDB; 51750; -. [P04844-1]
DR ProteomicsDB; 51751; -. [P04844-2]
DR TopDownProteomics; P04844-1; -. [P04844-1]
DR Antibodypedia; 1855; 198 antibodies from 26 providers.
DR DNASU; 6185; -.
DR Ensembl; ENST00000237530.11; ENSP00000237530.6; ENSG00000118705.17. [P04844-1]
DR Ensembl; ENST00000373622.9; ENSP00000362724.5; ENSG00000118705.17. [P04844-2]
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 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; TTWSART; -.
DR OrthoDB; 1001599at2759; -.
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 UniPathway; UPA00378; -.
DR BioGRID-ORCS; 6185; 607 hits in 1088 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 220 other tissues.
DR ExpressionAtlas; P04844; baseline and differential.
DR Genevisible; P04844; HS.
DR GO; GO:0000421; C:autophagosome membrane; IEA:Ensembl.
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: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:0005791; C:rough endoplasmic reticulum; IEA:Ensembl.
DR GO; GO:0043022; F:ribosome binding; IEA:Ensembl.
DR GO; GO:0007568; P:aging; IEA:Ensembl.
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 GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
DR InterPro; IPR008814; Swp1.
DR PANTHER; PTHR12640; PTHR12640; 1.
DR Pfam; PF05817; Ribophorin_II; 1.
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
