RPN1_RAT
ID RPN1_RAT Reviewed; 605 AA.
AC P07153;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1988, sequence version 1.
DT 25-MAY-2022, entry version 132.
DE RecName: Full=Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 1 {ECO:0000305};
DE AltName: Full=Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 67 kDa subunit;
DE AltName: Full=Ribophorin I;
DE Short=RPN-I;
DE AltName: Full=Ribophorin-1;
DE Flags: Precursor;
GN Name=Rpn1 {ECO:0000312|RGD:3594};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=3031084; DOI=10.1083/jcb.104.4.855;
RA Harnik-Ort V., Prakash K., Marcantonio E., Colman D.R., Rosenfeld M.G.,
RA Adesnik M., Sabatini D.D., Kreibich G.;
RT "Isolation and characterization of cDNA clones for rat ribophorin I:
RT complete coding sequence and in vitro synthesis and insertion of the
RT encoded product into endoplasmic reticulum membranes.";
RL J. Cell Biol. 104:855-863(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-31.
RX PubMed=2335524; DOI=10.1016/s0021-9258(19)39065-9;
RA Behal A., Prakash K., D'Eustachio P., Adesnik M., Sabatini D.D.,
RA Kreibich G.;
RT "Structure and chromosomal location of the rat ribophorin I gene.";
RL J. Biol. Chem. 265:8252-8258(1990).
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:0000250|UniProtKB:E2RQ08}.
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 STT3A complex assembly occurs through the formation of 3 subcomplexes.
CC Subcomplex 1 contains RPN1 and TMEM258, subcomplex 2 contains the
CC STT3A-specific subunits STT3A, DC2/OSTC, and KCP2 as well as the core
CC subunit OST4, and subcomplex 3 contains RPN2, DAD1, and OST48. The
CC STT3A complex can form stable complexes with the Sec61 complex or with
CC both the Sec61 and TRAP complexes (By similarity). Interacts with
CC TMEM35A/NACHO (By similarity). {ECO:0000250|UniProtKB:E2RQ08,
CC ECO:0000250|UniProtKB:Q91YQ5}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000250|UniProtKB:E2RQ08, ECO:0000250|UniProtKB:Q9GMB0}.
CC Endoplasmic reticulum membrane; Single-pass type I membrane protein
CC {ECO:0000305}. Melanosome {ECO:0000250|UniProtKB:P04843}.
CC -!- TISSUE SPECIFICITY: Expressed in all tissues tested.
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; X05300; CAA28919.1; -; mRNA.
DR EMBL; M33508; AAA42043.1; -; Genomic_DNA.
DR PIR; A27274; A27274.
DR AlphaFoldDB; P07153; -.
DR SMR; P07153; -.
DR BioGRID; 247626; 7.
DR IntAct; P07153; 5.
DR MINT; P07153; -.
DR STRING; 10116.ENSRNOP00000066002; -.
DR GlyGen; P07153; 1 site.
DR iPTMnet; P07153; -.
DR PhosphoSitePlus; P07153; -.
DR SwissPalm; P07153; -.
DR jPOST; P07153; -.
DR PaxDb; P07153; -.
DR PeptideAtlas; P07153; -.
DR PRIDE; P07153; -.
DR RGD; 3594; Rpn1.
DR eggNOG; KOG2291; Eukaryota.
DR InParanoid; P07153; -.
DR UniPathway; UPA00378; -.
DR PRO; PR:P07153; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISO:RGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0008250; C:oligosaccharyltransferase complex; ISO:RGD.
DR GO; GO:0005791; C:rough endoplasmic reticulum; IDA:RGD.
DR GO; GO:0015833; P:peptide transport; NAS:RGD.
DR GO; GO:0006487; P:protein N-linked glycosylation; ISO:RGD.
DR GO; GO:0018279; P:protein N-linked glycosylation via asparagine; ISO:RGD.
DR InterPro; IPR007676; Ribophorin_I.
DR PANTHER; PTHR21049; PTHR21049; 1.
DR Pfam; PF04597; Ribophorin_I; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Endoplasmic reticulum; Glycoprotein; Isopeptide bond;
KW Membrane; Reference proteome; Signal; Transmembrane; Transmembrane helix;
KW Ubl conjugation.
FT SIGNAL 1..22
FT CHAIN 23..605
FT /note="Dolichyl-diphosphooligosaccharide--protein
FT glycosyltransferase subunit 1"
FT /id="PRO_0000022243"
FT TOPO_DOM 23..437
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 438..455
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 456..605
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOD_RES 185
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P04843"
FT MOD_RES 536
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q91YQ5"
FT CARBOHYD 297
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CROSSLNK 536
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P04843"
FT CONFLICT 16..31
FT /note="APTPGSASSEAPPLVN -> PDAWQRLFGGSAAGQR (in Ref. 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 605 AA; 68304 MW; 60F8ECAAF9C4806F CRC64;
MEAPIVLLLL LWLALAPTPG SASSEAPPLV NEDVKRTVDL SSHLAKVTAE VVLAHPGGGS
TARASSFVLA LEPELESRLA HLGVQVKGED EEDNNLEVRE TKMKGKSGRF FTVKLPVALD
PGSKISIVVE TVYTHVLHPY PTQITQSEKQ FVVFEGNHYF YSPYPTKTQT MRVRLASRNV
ESHTKLGNPS RSEDILDYGP FKDIPAYSQD TFKVHYENNS PFLTITSMTR VIEVSHWGNI
AVEENVDLKH TGAVLKGPFS RYDYQRQPDS GISSIRSFKT ILPAAAQDVY YRDEIGNVST
SHLLILDDSV EMEIRPRFGL FGGWKTHYIV GYNLPSYEYL YNLGDQYALK MRFVDHVFDE
QVIDSLTVKI ILPEGAKNIQ VDSPYDISRA PDELHYTYLD TFGRPVIVAY KKNLVEQHIQ
DIVVHYTFNK VLMLQEPLLV VAAFYILFFT VIIYVRLDFS ITKDPAAEAR MKVACITEQV
LTLVNKRLGL YRHFDETVNR YKQSRDISTL NSGKKSLETE HKAVTSEIAV LQSRLKTEGS
DLCDRVSEMQ KLDAQVKELV LKSAVEAERL VAGKLKKDTY IENEKLSSGK RQELVTKIDH
ILDAL
