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 10-APR-2019, entry version 61.
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).
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
RT at the mammalian endoplasmic reticulum.";
RL Science 360:215-219(2018).
CC -!- FUNCTION: Subunit of the oligosaccharyl transferase (OST) complex
CC that catalyzes the initial transfer of a defined glycan
CC (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier
CC dolichol-pyrophosphate to an asparagine residue within an Asn-X-
CC Ser/Thr consensus motif in nascent polypeptide chains, the first
CC step in protein N-glycosylation. N-glycosylation occurs
CC cotranslationally and the complex associates with the Sec61
CC complex at the channel-forming translocon complex that mediates
CC protein translocation across the endoplasmic reticulum (ER). All
CC subunits are required for a maximal enzyme activity.
CC {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 (PubMed:12887896, PubMed:15835887, PubMed:25135935).
CC STT3A complex assembly occurs through the formation of 3
CC subcomplexes. Subcomplex 1 contains RPN1 and TMEM258, subcomplex 2
CC contains the STT3A-specific subunits STT3A, DC2/OSTC, and KCP2 as
CC well as the core subunit OST4, and subcomplex 3 contains RPN2,
CC DAD1, and OST48. The STT3A complex can form stable complexes with
CC the Sec61 complex or with both the Sec61 and TRAP complexes
CC (PubMed:29519914). {ECO:0000269|PubMed:12887896,
CC ECO:0000269|PubMed:15835887, ECO:0000269|PubMed:25135935,
CC ECO:0000269|PubMed:29519914}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000269|PubMed:12887896}. Endoplasmic reticulum membrane;
CC Single-pass type I membrane protein {ECO:0000269|PubMed:29519914}.
CC -!- SIMILARITY: Belongs to the OST1 family. {ECO:0000305}.
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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 CORUM; E2RQ08; -.
DR STRING; 9612.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; 1294725at2759; -.
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:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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|PubMed:29519914}.
FT TRANSMEM 435 455 Helical. {ECO:0000269|PubMed:29519914}.
FT TOPO_DOM 456 607 Cytoplasmic.
FT {ECO:0000305|PubMed:29519914}.
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
//