ID E2RQ08_CANLF Unreviewed; 607 AA. AC E2RQ08; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 07-SEP-2016, entry version 44. DE RecName: Full=Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 1 {ECO:0000256|RuleBase:RU361143}; DE EC=2.4.99.18 {ECO:0000256|RuleBase:RU361143}; GN Name=RPN1 {ECO:0000313|Ensembl:ENSCAFP00000006175}; 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 {ECO:0000313|Ensembl:ENSCAFP00000006175, ECO:0000313|Proteomes:UP000002254}; RN [1] {ECO:0000313|Ensembl:ENSCAFP00000006175, ECO:0000313|Proteomes:UP000002254} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Boxer {ECO:0000313|Ensembl:ENSCAFP00000006175, RC ECO:0000313|Proteomes:UP000002254}; RX PubMed=16341006; DOI=10.1038/nature04338; RG Broad Sequencing Platform; 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] {ECO:0000313|Ensembl:ENSCAFP00000006175} RP IDENTIFICATION. RC STRAIN=Boxer {ECO:0000313|Ensembl:ENSCAFP00000006175}; RG Ensembl; RL Submitted (JUL-2011) to UniProtKB. 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:0000256|RuleBase:RU361143}. CC -!- CATALYTIC ACTIVITY: Dolichyl diphosphooligosaccharide + [protein]- CC L-asparagine = dolichyl diphosphate + a glycoprotein with the CC oligosaccharide chain attached by N-beta-D-glycosyl linkage to a CC protein L-asparagine. {ECO:0000256|RuleBase:RU361143}. CC -!- PATHWAY: Protein modification; protein glycosylation. CC {ECO:0000256|RuleBase:RU361143}. CC -!- SUBUNIT: Component of the oligosaccharyltransferase (OST) complex. CC {ECO:0000256|RuleBase:RU361143}. CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane CC {ECO:0000256|RuleBase:RU361143}; Single-pass type I membrane CC protein {ECO:0000256|RuleBase:RU361143}. CC -!- SIMILARITY: Belongs to the OST1 family. CC {ECO:0000256|RuleBase:RU361143}. CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSCAFP00000006175}. 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 STRING; 9615.ENSCAFP00000006175; -. DR PaxDb; E2RQ08; -. DR Ensembl; ENSCAFT00000006670; ENSCAFP00000006175; ENSCAFG00000004148. DR GeneID; 476516; -. DR KEGG; cfa:476516; -. DR CTD; 6184; -. DR eggNOG; KOG2291; Eukaryota. DR eggNOG; ENOG410XQVZ; LUCA. DR GeneTree; ENSGT00390000009630; -. DR InParanoid; E2RQ08; -. DR KO; K12666; -. DR OMA; PYPTHIT; -. DR OrthoDB; EOG091G05K5; -. DR TreeFam; TF312988; -. DR UniPathway; UPA00378; -. DR Proteomes; UP000002254; Chromosome 20. 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:0044822; F:poly(A) RNA binding; IEA:Ensembl. 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 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000002254}; KW Endoplasmic reticulum {ECO:0000256|RuleBase:RU361143}; KW Glycosyltransferase {ECO:0000256|RuleBase:RU361143}; KW Membrane {ECO:0000256|RuleBase:RU361143}; KW Reference proteome {ECO:0000313|Proteomes:UP000002254}; KW Signal {ECO:0000256|RuleBase:RU361143}; KW Transferase {ECO:0000256|RuleBase:RU361143}; KW Transmembrane {ECO:0000256|RuleBase:RU361143}; KW Transmembrane helix {ECO:0000256|RuleBase:RU361143}. FT SIGNAL 1 24 {ECO:0000256|RuleBase:RU361143}. FT CHAIN 25 607 Dolichyl-diphosphooligosaccharide-- FT protein glycosyltransferase subunit 1. FT {ECO:0000256|RuleBase:RU361143}. FT /FTId=PRO_5005127751. FT TRANSMEM 440 459 Helical. {ECO:0000256|RuleBase:RU361143}. 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 //