RPN1_MOUSE
ID RPN1_MOUSE Reviewed; 608 AA.
AC Q91YQ5; Q3U985;
DT 29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 148.
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|MGI:MGI:98084};
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, and NOD; TISSUE=Bone marrow, Eye, Testis, and Thymus;
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 MRNA].
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 [3]
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 [4]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-539, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
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:E2RQ08}.
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000250|UniProtKB:P04843}.
CC -!- SUBUNIT: Component of the oligosaccharyltransferase (OST) complex. OST
CC exists in two different complex forms which contain common core
CC subunits RPN1, RPN2, OST48, OST4, DAD1 and TMEM258, either STT3A or
CC STT3B as catalytic subunits, and form-specific accessory subunits.
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 (PubMed:32783947). {ECO:0000250|UniProtKB:E2RQ08,
CC ECO:0000269|PubMed:32783947}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000250|UniProtKB:E2RQ08, ECO:0000250|UniProtKB:Q9GMB0}.
CC Endoplasmic reticulum membrane; Single-pass type I membrane protein
CC {ECO:0000305}. Melanosome {ECO:0000250|UniProtKB:P04843}.
CC -!- PTM: Ufmylated by UFL1 in response to endoplasmic reticulum stress,
CC promoting reticulophagy of endoplasmic reticulum sheets.
CC {ECO:0000250|UniProtKB:P04843}.
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; AK052130; BAC34853.1; -; mRNA.
DR EMBL; AK132750; BAE21332.1; -; mRNA.
DR EMBL; AK151899; BAE30782.1; -; mRNA.
DR EMBL; AK153867; BAE32221.1; -; mRNA.
DR EMBL; BC016080; AAH16080.1; -; mRNA.
DR CCDS; CCDS20332.1; -.
DR RefSeq; NP_598694.3; NM_133933.4.
DR AlphaFoldDB; Q91YQ5; -.
DR SMR; Q91YQ5; -.
DR BioGRID; 222240; 12.
DR ComplexPortal; CPX-5821; Oligosaccharyltransferase complex A.
DR ComplexPortal; CPX-5822; Oligosaccharyltransferase complex B.
DR IntAct; Q91YQ5; 7.
DR MINT; Q91YQ5; -.
DR STRING; 10090.ENSMUSP00000032143; -.
DR GlyConnect; 2262; 5 N-Linked glycans (1 site).
DR GlyGen; Q91YQ5; 1 site, 5 N-linked glycans (1 site).
DR iPTMnet; Q91YQ5; -.
DR PhosphoSitePlus; Q91YQ5; -.
DR SwissPalm; Q91YQ5; -.
DR EPD; Q91YQ5; -.
DR jPOST; Q91YQ5; -.
DR MaxQB; Q91YQ5; -.
DR PaxDb; Q91YQ5; -.
DR PeptideAtlas; Q91YQ5; -.
DR PRIDE; Q91YQ5; -.
DR ProteomicsDB; 300484; -.
DR Antibodypedia; 4058; 572 antibodies from 30 providers.
DR DNASU; 103963; -.
DR Ensembl; ENSMUST00000032143; ENSMUSP00000032143; ENSMUSG00000030062.
DR GeneID; 103963; -.
DR KEGG; mmu:103963; -.
DR UCSC; uc009cva.2; mouse.
DR CTD; 6184; -.
DR MGI; MGI:98084; Rpn1.
DR VEuPathDB; HostDB:ENSMUSG00000030062; -.
DR eggNOG; KOG2291; Eukaryota.
DR GeneTree; ENSGT00390000009630; -.
DR HOGENOM; CLU_031381_2_0_1; -.
DR InParanoid; Q91YQ5; -.
DR OMA; KTYMDTL; -.
DR OrthoDB; 1294725at2759; -.
DR PhylomeDB; Q91YQ5; -.
DR TreeFam; TF312988; -.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 103963; 20 hits in 72 CRISPR screens.
DR ChiTaRS; Rpn1; mouse.
DR PRO; PR:Q91YQ5; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q91YQ5; protein.
DR Bgee; ENSMUSG00000030062; Expressed in metanephric proximal tubule and 260 other tissues.
DR ExpressionAtlas; Q91YQ5; baseline and differential.
DR Genevisible; Q91YQ5; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0008250; C:oligosaccharyltransferase complex; ISO:MGI.
DR GO; GO:0005791; C:rough endoplasmic reticulum; IDA:MGI.
DR GO; GO:0006487; P:protein N-linked glycosylation; ISO:MGI.
DR GO; GO:0018279; P:protein N-linked glycosylation via asparagine; ISO:MGI.
DR InterPro; IPR007676; Ribophorin_I.
DR PANTHER; PTHR21049; PTHR21049; 1.
DR Pfam; PF04597; Ribophorin_I; 1.
PE 1: Evidence at protein level;
KW Acetylation; Endoplasmic reticulum; Glycoprotein; Isopeptide bond;
KW Membrane; Reference proteome; Signal; Transmembrane; Transmembrane helix;
KW Ubl conjugation.
FT SIGNAL 1..25
FT /evidence="ECO:0000250"
FT CHAIN 26..608
FT /note="Dolichyl-diphosphooligosaccharide--protein
FT glycosyltransferase subunit 1"
FT /id="PRO_0000022242"
FT TOPO_DOM 26..440
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 441..458
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 459..608
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOD_RES 188
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P04843"
FT MOD_RES 539
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT CARBOHYD 300
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CROSSLNK 539
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P04843"
SQ SEQUENCE 608 AA; 68528 MW; CBDFA74C792A496E CRC64;
MESPVALLLL LLLCLGALAP TPGSASSEAP PLVNEDVKRT VDLSSHLAKV TAEVVLVHPG
GGSTSRASSF VLALEPELES RLAHLGVQIK GEDEEDNNLE VRETKIKGKS GRFFTVKLPV
ALDPGSKISV VVETVYTHVL HPYPTQITQS EKQFVVFEGN HYFYSPYPTK TQTMRVKLAS
RNVESYTKLG NPSRSEDVLD YGPFKDIPAY SQDTFKVHYE NNSPFLTITS MTRVIEVSHW
GNIAVEENVD LKHTGAVLKG PFSRYDYQRQ PDSGISSIRS FKTILPAAAQ DVYYRDEIGN
VSTSHLLILD DSVEMEIRPR FPLFGGWKTH YIVGYNLPSY EYLYNLGDQY ALKMRFVDHV
FDEQVIDSLT VKIILPEGAK NIQVDSPYDI SRAPDELHYT YLDTFGRPVI VAYKKNLVEQ
HIQDIVVHYT FNKVLMLQEP LLVVAAFYIL FFTVIIYVRL DFSITKDPAA EARMKVACIT
EQVLTLVNKR LGLYRHFDET VNRYKQSRDI STLNSGKKSL ETEHKAVTSE IAVLQSRLKT
EGSDLCDRVS EMQKLDAQVK ELVLKSAVEA ERLVAGKLKK DTYLENEKLS SGKRQELVTK
IDHILDAL
