RPN2_MOUSE
ID RPN2_MOUSE Reviewed; 631 AA.
AC Q9DBG6; A2ACG6; Q3TKY0; Q91XH0;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 2 {ECO:0000305};
DE AltName: Full=Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 63 kDa subunit;
DE AltName: Full=Ribophorin II;
DE Short=RPN-II;
DE AltName: Full=Ribophorin-2;
DE Flags: Precursor;
GN Name=Rpn2 {ECO:0000312|MGI:MGI:98085};
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Liver;
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 [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, and Colon;
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 [4]
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).
RN [5]
RP INTERACTION WITH TMEM35A/NACHO.
RX PubMed=32783947; DOI=10.1016/j.celrep.2020.108025;
RA Kweon H.J., Gu S., Witham E., Dhara M., Yu H., Mandon E.D., Jawhari A.,
RA Bredt D.S.;
RT "NACHO Engages N-Glycosylation ER Chaperone Pathways for alpha7 Nicotinic
RT Receptor Assembly.";
RL Cell Rep. 32:108025-108025(2020).
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. N-glycosylation occurs cotranslationally and
CC the complex associates with the Sec61 complex at the channel-forming
CC translocon complex that mediates protein translocation across the
CC endoplasmic reticulum (ER). All subunits are required for a maximal
CC enzyme activity. {ECO:0000250|UniProtKB:F1PCT7}.
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000250|UniProtKB:P04844}.
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 DDI2 (By similarity). Interacts with TMEM35A/NACHO (PubMed:32783947).
CC {ECO:0000250|UniProtKB:F1PCT7, ECO:0000250|UniProtKB:P04844,
CC ECO:0000269|PubMed:32783947}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000250|UniProtKB:F1PCT7}. Endoplasmic reticulum membrane; Multi-
CC pass membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the SWP1 family. {ECO:0000305}.
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DR EMBL; AK004968; BAB23707.1; -; mRNA.
DR EMBL; AK161624; BAE36498.1; -; mRNA.
DR EMBL; AK166778; BAE39013.1; -; mRNA.
DR EMBL; AL669828; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC010509; AAH10509.1; -; mRNA.
DR EMBL; BC046806; AAH46806.1; -; mRNA.
DR CCDS; CCDS16975.1; -.
DR RefSeq; NP_062616.2; NM_019642.4.
DR PDB; 5J6G; X-ray; 3.30 A; E/F=373-380.
DR PDB; 5J6H; X-ray; 2.30 A; F=373-380.
DR PDBsum; 5J6G; -.
DR PDBsum; 5J6H; -.
DR AlphaFoldDB; Q9DBG6; -.
DR SMR; Q9DBG6; -.
DR BioGRID; 202990; 9.
DR ComplexPortal; CPX-5821; Oligosaccharyltransferase complex A.
DR ComplexPortal; CPX-5822; Oligosaccharyltransferase complex B.
DR IntAct; Q9DBG6; 8.
DR MINT; Q9DBG6; -.
DR STRING; 10090.ENSMUSP00000112081; -.
DR GlyConnect; 2263; 3 N-Linked glycans (1 site).
DR GlyGen; Q9DBG6; 1 site, 3 N-linked glycans (1 site).
DR iPTMnet; Q9DBG6; -.
DR PhosphoSitePlus; Q9DBG6; -.
DR SwissPalm; Q9DBG6; -.
DR EPD; Q9DBG6; -.
DR jPOST; Q9DBG6; -.
DR MaxQB; Q9DBG6; -.
DR PaxDb; Q9DBG6; -.
DR PeptideAtlas; Q9DBG6; -.
DR PRIDE; Q9DBG6; -.
DR ProteomicsDB; 260935; -.
DR TopDownProteomics; Q9DBG6; -.
DR Antibodypedia; 1855; 198 antibodies from 26 providers.
DR DNASU; 20014; -.
DR Ensembl; ENSMUST00000116380; ENSMUSP00000112081; ENSMUSG00000027642.
DR GeneID; 20014; -.
DR KEGG; mmu:20014; -.
DR UCSC; uc008now.1; mouse.
DR CTD; 6185; -.
DR MGI; MGI:98085; Rpn2.
DR VEuPathDB; HostDB:ENSMUSG00000027642; -.
DR eggNOG; KOG2447; Eukaryota.
DR GeneTree; ENSGT00390000002635; -.
DR InParanoid; Q9DBG6; -.
DR OMA; TTWSART; -.
DR OrthoDB; 1001599at2759; -.
DR PhylomeDB; Q9DBG6; -.
DR TreeFam; TF106146; -.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 20014; 19 hits in 78 CRISPR screens.
DR ChiTaRS; Rpn2; mouse.
DR PRO; PR:Q9DBG6; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q9DBG6; protein.
DR Bgee; ENSMUSG00000027642; Expressed in ileal epithelium and 267 other tissues.
DR ExpressionAtlas; Q9DBG6; baseline and differential.
DR Genevisible; Q9DBG6; MM.
DR GO; GO:0000421; C:autophagosome membrane; ISO:MGI.
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:0016604; C:nuclear body; ISO:MGI.
DR GO; GO:0008250; C:oligosaccharyltransferase complex; ISO:MGI.
DR GO; GO:0005791; C:rough endoplasmic reticulum; ISO:MGI.
DR GO; GO:0043022; F:ribosome binding; ISO:MGI.
DR GO; GO:0007568; P:aging; IEA:Ensembl.
DR GO; GO:0006487; P:protein N-linked glycosylation; IMP:MGI.
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; Endoplasmic reticulum; Glycoprotein; Isopeptide bond;
KW Membrane; Reference proteome; Signal; Transmembrane; Transmembrane helix;
KW Ubl conjugation.
FT SIGNAL 1..22
FT /evidence="ECO:0000250"
FT CHAIN 23..631
FT /note="Dolichyl-diphosphooligosaccharide--protein
FT glycosyltransferase subunit 2"
FT /id="PRO_0000022248"
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:0000255"
FT CROSSLNK 154
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P04844"
SQ SEQUENCE 631 AA; 69063 MW; D20745D10D5486F9 CRC64;
MAPPGSSAVF LLALTITASV QALTPTHYLT KQDVERLKAS LDRPFTDLES AFYSIVGLSS
LGVQVPDVKK ACTFIKSNLD PSNVDSLFYA AQSSQVLSGC EISVSNETKE LLLAAVSEDS
PIAQIYHAVA ALSGFGLPLA SNEALGALTA RLGKEETVLA TVQALQTASH LSQQADLRNI
VEEIEDLVAR LDELGGVYLQ FEEGLELTAL FVAATYKLMD HVGTEPSMKE DQVIQLMNTI
FSKKNFESLS EAFSVASAAA ALSQNRYHVP VVVVPEGSTS DTQEQAILRL QVSNVLSQPL
AQAAVKLEHA KSAATRATVL QKTPFSLVGN VFELNFKNVK LSSGYYDFSV RVEGDSRYIA
NTVELRVKIS TEVGITNVDL STVDKDQSIA PKTTRVTYPA KAKGTFIADS HQNFALFFQL
VDVNTGAELT PHQTFVRLHN QKTGQEVVFV AEPDNKNVYK FELDTSERKI EFDSASGTYT
LYLIIGDATL KNPILWNVAD VVIKFPEEEA PSTVLSQSLF TPKQEIQHLF REPEKRPPTV
VSNTFTALIL SPLLLLFALW IRIGANVSNF TFAPSTVIFH LGHAAMLGLM YIYWTQLNMF
QTLKYLAVLG TVTFLAGNRM LAQHAVKRTA H
