RPN1_CANLF
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-AUG-2022, entry version 75.
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}.
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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 AlphaFoldDB; E2RQ08; -.
DR SMR; E2RQ08; -.
DR CORUM; E2RQ08; -.
DR STRING; 9612.ENSCAFP00000006175; -.
DR PaxDb; E2RQ08; -.
DR PRIDE; E2RQ08; -.
DR Ensembl; ENSCAFT00030025258; ENSCAFP00030022058; ENSCAFG00030013592.
DR Ensembl; ENSCAFT00845033627; ENSCAFP00845026327; ENSCAFG00845019047.
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; KTYMDTL; -.
DR OrthoDB; 1294725at2759; -.
DR TreeFam; TF312988; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000002254; Chromosome 20.
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; 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; PTHR21049; 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
