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 07-NOV-2018, entry version 57. DE RecName: Full=Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 1; DE AltName: Full=Ribophorin I; DE Short=RPN-I; DE AltName: Full=Ribophorin-1; DE Flags: Precursor; GN Name=RPN1; OS Canis lupus familiaris (Dog) (Canis familiaris). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; OC 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., RA Mauceli E., Xie X., Breen M., Wayne R.K., Ostrander E.A., RA Ponting C.P., Galibert F., Smith D.R., deJong P.J., Kirkness E.F., RA Alvarez P., Biagi T., Brockman W., Butler J., Chin C.-W., Cook A., RA Cuff J., Daly M.J., DeCaprio D., Gnerre S., Grabherr M., Kellis M., RA Kleber M., Bardeleben C., Goodstadt L., Heger A., Hitte C., Kim L., RA Koepfli K.-P., Parker H.G., Pollinger J.P., Searle S.M.J., RA 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., RA Bachantsang P., Barry A., Bayul T., Benamara M., Berlin A., RA Bessette D., Blitshteyn B., Bloom T., Blye J., Boguslavskiy L., RA Bonnet C., Boukhgalter B., Brown A., Cahill P., Calixte N., RA Camarata J., Cheshatsang Y., Chu J., Citroen M., Collymore A., RA Cooke P., Dawoe T., Daza R., Decktor K., DeGray S., Dhargay N., RA Dooley K., Dooley K., Dorje P., Dorjee K., Dorris L., Duffey N., RA Dupes A., Egbiremolen O., Elong R., Falk J., Farina A., Faro S., RA Ferguson D., Ferreira P., Fisher S., FitzGerald M., Foley K., RA Foley C., Franke A., Friedrich D., Gage D., Garber M., Gearin G., RA Giannoukos G., Goode T., Goyette A., Graham J., Grandbois E., RA Gyaltsen K., Hafez N., Hagopian D., Hagos B., Hall J., Healy C., RA Hegarty R., Honan T., Horn A., Houde N., Hughes L., Hunnicutt L., RA Husby M., Jester B., Jones C., Kamat A., Kanga B., Kells C., RA Khazanovich D., Kieu A.C., Kisner P., Kumar M., Lance K., Landers T., RA Lara M., Lee W., Leger J.-P., Lennon N., Leuper L., LeVine S., Liu J., RA Liu X., Lokyitsang Y., Lokyitsang T., Lui A., Macdonald J., Major J., RA Marabella R., Maru K., Matthews C., McDonough S., Mehta T., RA Meldrim J., Melnikov A., Meneus L., Mihalev A., Mihova T., Miller K., RA Mittelman R., Mlenga V., Mulrain L., Munson G., Navidi A., Naylor J., RA 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., RA Osman S., Oyono L., Patti C., Perrin D., Phunkhang P., Pierre F., RA Priest M., Rachupka A., Raghuraman S., Rameau R., Ray V., Raymond C., RA Rege F., Rise C., Rogers J., Rogov P., Sahalie J., Settipalli S., RA Sharpe T., Shea T., Sheehan M., Sherpa N., Shi J., Shih D., Sloan J., RA Smith C., Sparrow T., Stalker J., Stange-Thomann N., Stavropoulos S., RA Stone C., Stone S., Sykes S., Tchuinga P., Tenzing P., Tesfaye S., RA Thoulutsang D., Thoulutsang Y., Topham K., Topping I., Tsamla T., RA Vassiliev H., Venkataraman V., Vo A., Wangchuk T., Wangdi T., RA Weiand M., Wilkinson J., Wilson A., Yadav S., Yang S., Yang X., RA Young G., Yu Q., Zainoun J., 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, RP FUNCTION OF THE OLIGOSACCHARYLTRANSFERASE (OST) COMPLEX, AND RP 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 RT STT3 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 RT multiple subcomplexes that contain Sec61, TRAP, and two potential new RT 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). CC -!- FUNCTION: Essential subunit of the N-oligosaccharyl transferase CC (OST) complex which catalyzes the transfer of a high mannose CC oligosaccharide from a lipid-linked oligosaccharide donor to an CC asparagine residue within an Asn-X-Ser/Thr consensus motif in CC nascent polypeptide chains. {ECO:0000269|PubMed:12887896}. CC -!- PATHWAY: Protein modification; protein glycosylation. CC -!- SUBUNIT: Component of the oligosaccharyltransferase (OST) complex. CC OST exists in two different complex forms which contain common CC core subunits RPN1, RPN2, OST48, OST4, DAD1 and TMEM258, either CC STT3A or STT3B as catalytic subunits, and form-specific accessory CC subunits. OST can form stable complexes with the Sec61 complex or CC with both the Sec61 and TRAP complexes. CC {ECO:0000269|PubMed:12887896, ECO:0000269|PubMed:15835887, CC ECO:0000269|PubMed:25135935, ECO:0000305}. CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum CC {ECO:0000269|PubMed:12887896}. Endoplasmic reticulum membrane; CC Single-pass type I membrane protein {ECO:0000305}. 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 SMR; E2RQ08; -. DR STRING; 9615.ENSCAFP00000006175; -. DR PaxDb; E2RQ08; -. DR PRIDE; E2RQ08; -. DR Ensembl; ENSCAFT00000006670; ENSCAFP00000006175; ENSCAFG00000004148. DR GeneID; 476516; -. DR KEGG; cfa:476516; -. DR CTD; 6184; -. DR VGNC; VGNC:45721; RPN1. DR eggNOG; KOG2291; Eukaryota. DR eggNOG; ENOG410XQVZ; LUCA. DR GeneTree; ENSGT00390000009630; -. DR InParanoid; E2RQ08; -. DR KO; K12666; -. DR OMA; DFAITKD; -. DR OrthoDB; EOG091G05K5; -. DR TreeFam; TF312988; -. DR UniPathway; UPA00378; -. DR Proteomes; UP000002254; Chromosome 20. DR Bgee; ENSCAFG00000004148; Expressed in 3 organ(s), highest expression level in adult mammalian kidney. DR GO; GO:0005829; C:cytosol; IEA:Ensembl. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0008250; C:oligosaccharyltransferase complex; IBA:GO_Central. DR GO; GO:0005791; C:rough endoplasmic reticulum; IEA:Ensembl. DR GO; GO:0004579; F:dolichyl-diphosphooligosaccharide-protein glycotransferase activity; IBA:GO_Central. DR GO; GO:0018279; P:protein N-linked glycosylation via asparagine; IBA:GO_Central. DR InterPro; IPR007676; Ribophorin_I. DR PANTHER; PTHR21049; PTHR21049; 1. DR Pfam; PF04597; Ribophorin_I; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Complete proteome; Endoplasmic reticulum; KW Glycoprotein; Isopeptide bond; Membrane; Reference proteome; Signal; KW Transmembrane; Transmembrane helix; Ubl conjugation. FT SIGNAL 1 24 {ECO:0000255}. FT CHAIN 25 607 Dolichyl-diphosphooligosaccharide-- FT protein glycosyltransferase subunit 1. FT /FTId=PRO_5005127751. FT TOPO_DOM 25 434 Lumenal. {ECO:0000305}. FT TRANSMEM 435 455 Helical. {ECO:0000255}. FT TOPO_DOM 456 607 Cytoplasmic. {ECO:0000305}. FT MOD_RES 187 187 N6-acetyllysine. FT {ECO:0000250|UniProtKB:P04843}. FT MOD_RES 538 538 N6-acetyllysine; alternate. FT {ECO:0000250|UniProtKB:Q91YQ5}. FT CARBOHYD 299 299 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CROSSLNK 538 538 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in SUMO2); FT alternate. FT {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 //