ID RPN1_CANLF Reviewed; 607 AA. AC E2RQ08; DT 12-APR-2017, integrated into UniProtKB/Swiss-Prot. DT 30-NOV-2010, sequence version 1. DT 03-MAY-2023, entry version 78. DE RecName: Full=Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 1 {ECO:0000250|UniProtKB:P04843}; DE AltName: Full=Ribophorin I; DE Short=RPN-I; DE AltName: Full=Ribophorin-1; DE Flags: Precursor; GN Name=RPN1 {ECO:0000250|UniProtKB:P04843}; OS Canis lupus familiaris (Dog) (Canis familiaris). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis. OX NCBI_TaxID=9615; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Boxer; RX PubMed=16341006; DOI=10.1038/nature04338; RA Lindblad-Toh K., Wade C.M., Mikkelsen T.S., Karlsson E.K., Jaffe D.B., RA Kamal M., Clamp M., Chang J.L., Kulbokas E.J. III, Zody M.C., Mauceli E., RA Xie X., Breen M., Wayne R.K., Ostrander E.A., Ponting C.P., Galibert F., RA Smith D.R., deJong P.J., Kirkness E.F., Alvarez P., Biagi T., Brockman W., RA Butler J., Chin C.-W., Cook A., Cuff J., Daly M.J., DeCaprio D., Gnerre S., RA Grabherr M., Kellis M., Kleber M., Bardeleben C., Goodstadt L., Heger A., RA Hitte C., Kim L., Koepfli K.-P., Parker H.G., Pollinger J.P., RA Searle S.M.J., Sutter N.B., Thomas R., Webber C., Baldwin J., Abebe A., RA Abouelleil A., Aftuck L., Ait-Zahra M., Aldredge T., Allen N., An P., RA Anderson S., Antoine C., Arachchi H., Aslam A., Ayotte L., Bachantsang P., RA Barry A., Bayul T., Benamara M., Berlin A., Bessette D., Blitshteyn B., RA Bloom T., Blye J., Boguslavskiy L., Bonnet C., Boukhgalter B., Brown A., RA Cahill P., Calixte N., Camarata J., Cheshatsang Y., Chu J., Citroen M., RA Collymore A., Cooke P., Dawoe T., Daza R., Decktor K., DeGray S., RA Dhargay N., Dooley K., Dooley K., Dorje P., Dorjee K., Dorris L., RA Duffey N., Dupes A., Egbiremolen O., Elong R., Falk J., Farina A., Faro S., RA Ferguson D., Ferreira P., Fisher S., FitzGerald M., Foley K., Foley C., RA Franke A., Friedrich D., Gage D., Garber M., Gearin G., Giannoukos G., RA Goode T., Goyette A., Graham J., Grandbois E., Gyaltsen K., Hafez N., RA Hagopian D., Hagos B., Hall J., Healy C., Hegarty R., Honan T., Horn A., RA Houde N., Hughes L., Hunnicutt L., Husby M., Jester B., Jones C., Kamat A., RA Kanga B., Kells C., Khazanovich D., Kieu A.C., Kisner P., Kumar M., RA Lance K., Landers T., Lara M., Lee W., Leger J.-P., Lennon N., Leuper L., RA LeVine S., Liu J., Liu X., Lokyitsang Y., Lokyitsang T., Lui A., RA Macdonald J., Major J., Marabella R., Maru K., Matthews C., McDonough S., RA Mehta T., Meldrim J., Melnikov A., Meneus L., Mihalev A., Mihova T., RA Miller K., Mittelman R., Mlenga V., Mulrain L., Munson G., Navidi A., RA Naylor J., Nguyen T., Nguyen N., Nguyen C., Nguyen T., Nicol R., Norbu N., RA Norbu C., Novod N., Nyima T., Olandt P., O'Neill B., O'Neill K., Osman S., RA Oyono L., Patti C., Perrin D., Phunkhang P., Pierre F., Priest M., RA Rachupka A., Raghuraman S., Rameau R., Ray V., Raymond C., Rege F., RA Rise C., Rogers J., Rogov P., Sahalie J., Settipalli S., Sharpe T., RA Shea T., Sheehan M., Sherpa N., Shi J., Shih D., Sloan J., Smith C., RA Sparrow T., Stalker J., Stange-Thomann N., Stavropoulos S., Stone C., RA Stone S., Sykes S., Tchuinga P., Tenzing P., Tesfaye S., Thoulutsang D., RA Thoulutsang Y., Topham K., Topping I., Tsamla T., Vassiliev H., RA Venkataraman V., Vo A., Wangchuk T., Wangdi T., Weiand M., Wilkinson J., RA Wilson A., Yadav S., Yang S., Yang X., Young G., Yu Q., Zainoun J., RA Zembek L., Zimmer A., Lander E.S.; RT "Genome sequence, comparative analysis and haplotype structure of the RT domestic dog."; RL Nature 438:803-819(2005). RN [2] RP IDENTIFICATION IN THE OLIGOSACCHARYLTRANSFERASE (OST) COMPLEX, FUNCTION OF RP THE OLIGOSACCHARYLTRANSFERASE (OST) COMPLEX, AND SUBCELLULAR LOCATION. 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 [3] RP IDENTIFICATION IN THE OLIGOSACCHARYLTRANSFERASE (OST) COMPLEX. RX PubMed=15835887; DOI=10.1021/bi047328f; RA Shibatani T., David L.L., McCormack A.L., Frueh K., Skach W.R.; RT "Proteomic analysis of mammalian oligosaccharyltransferase reveals multiple RT subcomplexes that contain Sec61, TRAP, and two potential new subunits."; RL Biochemistry 44:5982-5992(2005). RN [4] RP IDENTIFICATION IN THE OLIGOSACCHARYLTRANSFERASE (OST) 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 [5] RP STRUCTURE BY ELECTRON MICROSCOPY (4.20 ANGSTROMS) OF 438-573. RX PubMed=29519914; DOI=10.1126/science.aar7899; RA Braunger K., Pfeffer S., Shrimal S., Gilmore R., Berninghausen O., RA Mandon E.C., Becker T., Foerster F., Beckmann R.; RT "Structural basis for coupling protein transport and N-glycosylation at the RT mammalian endoplasmic reticulum."; RL Science 360:215-219(2018). 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:0000269|PubMed:12887896}. 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 (PubMed:12887896, PubMed:15835887, PubMed:25135935). STT3A complex CC assembly occurs through the formation of 3 subcomplexes. Subcomplex 1 CC contains RPN1 and TMEM258, subcomplex 2 contains the STT3A-specific CC subunits STT3A, DC2/OSTC, and KCP2 as well as the core subunit OST4, CC and subcomplex 3 contains RPN2, DAD1, and OST48. The STT3A complex can CC form stable complexes with the Sec61 complex or with both the Sec61 and CC TRAP complexes (PubMed:29519914). Interacts with TMEM35A/NACHO (By CC similarity). {ECO:0000250|UniProtKB:Q91YQ5, CC ECO:0000269|PubMed:12887896, ECO:0000269|PubMed:15835887, CC ECO:0000269|PubMed:25135935, ECO:0000269|PubMed:29519914}. CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum CC {ECO:0000269|PubMed:12887896}. Endoplasmic reticulum membrane; Single- CC pass type I membrane protein {ECO:0000269|PubMed:29519914}. 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; AAEX03012018; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; XP_848830.1; XM_843737.4. DR PDB; 6FTG; EM; 9.10 A; 1=438-459. DR PDB; 6FTI; EM; 4.20 A; 1=438-476. DR PDB; 6FTJ; EM; 4.70 A; 1=438-573. DR PDBsum; 6FTG; -. DR PDBsum; 6FTI; -. DR PDBsum; 6FTJ; -. DR AlphaFoldDB; E2RQ08; -. DR SMR; E2RQ08; -. DR CORUM; E2RQ08; -. DR STRING; 9612.ENSCAFP00000006175; -. DR GlyCosmos; E2RQ08; 1 site, No reported glycans. DR PaxDb; E2RQ08; -. DR Ensembl; ENSCAFT00030025258.1; ENSCAFP00030022058.1; ENSCAFG00030013592.1. DR Ensembl; ENSCAFT00805023577; ENSCAFP00805018540; ENSCAFG00805012924. DR Ensembl; ENSCAFT00845033627.1; ENSCAFP00845026327.1; ENSCAFG00845019047.1. DR GeneID; 476516; -. DR KEGG; cfa:476516; -. DR CTD; 6184; -. DR VEuPathDB; HostDB:ENSCAFG00845019047; -. DR eggNOG; KOG2291; Eukaryota. DR GeneTree; ENSGT00390000009630; -. DR HOGENOM; CLU_031381_2_0_1; -. DR InParanoid; E2RQ08; -. DR OMA; TSHTRIK; -. DR OrthoDB; 5265755at2759; -. DR TreeFam; TF312988; -. DR UniPathway; UPA00378; -. DR Proteomes; UP000002254; Chromosome 20. DR GO; GO:0005829; C:cytosol; IEA:Ensembl. DR GO; GO:0008250; C:oligosaccharyltransferase complex; IDA:UniProtKB. DR GO; GO:0005791; C:rough endoplasmic reticulum; IEA:Ensembl. DR GO; GO:0006486; P:protein glycosylation; IDA:UniProtKB. DR GO; GO:0018279; P:protein N-linked glycosylation via asparagine; IBA:GO_Central. 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. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Endoplasmic reticulum; Glycoprotein; KW Isopeptide bond; Membrane; Reference proteome; Signal; Transmembrane; KW Transmembrane helix; Ubl conjugation. FT SIGNAL 1..24 FT /evidence="ECO:0000255" FT CHAIN 25..607 FT /note="Dolichyl-diphosphooligosaccharide--protein FT glycosyltransferase subunit 1" FT /id="PRO_5005127751" FT TOPO_DOM 25..434 FT /note="Lumenal" FT /evidence="ECO:0000305|PubMed:29519914" FT TRANSMEM 435..455 FT /note="Helical" FT /evidence="ECO:0000269|PubMed:29519914" FT TOPO_DOM 456..607 FT /note="Cytoplasmic" FT /evidence="ECO:0000305|PubMed:29519914" FT MOD_RES 187 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P04843" 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:0000255" FT CROSSLNK 538 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0000250|UniProtKB:P04843" SQ SEQUENCE 607 AA; 68577 MW; 5A5BBA92F3202F60 CRC64; MEVPTARLLL LLLLGAWAPA PESASPEAPL LVNEDVKRTV DLSSHLAKVT AEVVLAHPGG GSTARAASFL LALEPELEAR LAHLGVQVKG EDEEENNLEV RETKIKGKSG RFFTVKLPVA LDPGAKVSVV VETVYTHVLQ PYPTQITQSE KQFVVFEGNH YFYSPYPTKT QTMRVKLASR NVESYTKLGN PTRSEDLLDY GPFRDIPAYS QDTFKVHYEN NSPFLTITSM TRVIEVSHWG NIAVEENVDL KHTGAVLKGP FSRYDYQRQP DSGIASIRSF KTILPAAAQD VYYRDEIGNV STSHLLILDD SVEMEIRPRF PLFGGWKTHY IVGYNLPSYE YLYNLGDQYA LKMRFVDHVF DEQVIDSLTV KIILPEGAKN IQVDSPYEIS RAPDELHYTY LDTFGRPVIV AYKKNLVEQH IQDIVVHYTF NKVLMLQEPL LVVAAFYILF FTVIIYVRLD FSITKDPAAE ARMKVACITE QVLTLVNKRI GLYRHFDETI NRYKQSRDVS TLNSGKKSLE TEHKALTSEI ASLQSRLKTE GSDLCDKVSE MQKLDAQVKE LVLKSAVEAE RLVAGKLKKD TYIENEKLIS GKRQELVTKI DHILDAL //