RPN1_PIG
ID RPN1_PIG Reviewed; 608 AA.
AC Q9GMB0;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 76.
DE RecName: Full=Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 1 {ECO:0000250|UniProtKB:P04843};
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:0000250|UniProtKB:P04843};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND SUBCELLULAR LOCATION.
RC TISSUE=Muscle;
RX PubMed=11443278; DOI=10.1023/a:1010980524785;
RA Hardt B., Aparicio R., Bause E.;
RT "The oligosaccharyltransferase complex from pig liver: cDNA cloning,
RT expression and functional characterisation.";
RL Glycoconj. J. 17:767-779(2000).
RN [2]
RP FUNCTION OF THE OLIGOSACCHARYLTRANSFERASE COMPLEX, SUBCELLULAR LOCATION,
RP SUBUNIT, AND TISSUE SPECIFICITY.
RX PubMed=7737165; DOI=10.1111/j.1432-1033.1995.tb20311.x;
RA Breuer W., Bause E.;
RT "Oligosaccharyl transferase is a constitutive component of an oligomeric
RT protein complex from pig liver endoplasmic reticulum.";
RL Eur. J. Biochem. 228:689-696(1995).
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 (Probable). N-glycosylation occurs
CC cotranslationally and the complex associates with the Sec61 complex at
CC the channel-forming translocon complex that mediates protein
CC translocation across the endoplasmic reticulum (ER). All subunits are
CC required for a maximal enzyme activity (By similarity).
CC {ECO:0000250|UniProtKB:E2RQ08, ECO:0000305|PubMed:7737165}.
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:7737165). STT3A complex assembly occurs through the formation
CC of 3 subcomplexes. Subcomplex 1 contains RPN1 and TMEM258, subcomplex 2
CC contains the STT3A-specific subunits STT3A, DC2/OSTC, and KCP2 as well
CC as the core subunit OST4, and subcomplex 3 contains RPN2, DAD1, and
CC OST48. The STT3A complex can form stable complexes with the Sec61
CC complex or with both the Sec61 and TRAP complexes (By similarity).
CC Interacts with TMEM35A/NACHO (By similarity).
CC {ECO:0000250|UniProtKB:E2RQ08, ECO:0000250|UniProtKB:Q91YQ5,
CC ECO:0000269|PubMed:7737165}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000269|PubMed:7737165}. Endoplasmic reticulum membrane; Single-
CC pass type I membrane protein {ECO:0000305}. Melanosome
CC {ECO:0000250|UniProtKB:P04843}.
CC -!- TISSUE SPECIFICITY: Detected in liver (at protein level).
CC {ECO:0000269|PubMed:7737165}.
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; AJ293582; CAC04096.1; -; mRNA.
DR RefSeq; NP_999498.1; NM_214333.1.
DR AlphaFoldDB; Q9GMB0; -.
DR SMR; Q9GMB0; -.
DR STRING; 9823.ENSSSCP00000012376; -.
DR PaxDb; Q9GMB0; -.
DR PeptideAtlas; Q9GMB0; -.
DR PRIDE; Q9GMB0; -.
DR GeneID; 397606; -.
DR KEGG; ssc:397606; -.
DR CTD; 6184; -.
DR eggNOG; KOG2291; Eukaryota.
DR InParanoid; Q9GMB0; -.
DR OrthoDB; 1294725at2759; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
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; 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 Acetylation; Endoplasmic reticulum; Glycoprotein; Isopeptide bond;
KW Membrane; Reference proteome; Signal; Transmembrane; Transmembrane helix;
KW Ubl conjugation.
FT SIGNAL 1..24
FT /evidence="ECO:0000250"
FT CHAIN 25..608
FT /note="Dolichyl-diphosphooligosaccharide--protein
FT glycosyltransferase subunit 1"
FT /id="PRO_0000331254"
FT TOPO_DOM 25..435
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 436..456
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 457..607
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT MOD_RES 188
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P04843"
FT MOD_RES 539
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q91YQ5"
FT CARBOHYD 300
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CROSSLNK 539
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P04843"
SQ SEQUENCE 608 AA; 68695 MW; D8928F5AF03F851C CRC64;
MEAPAVCLLP LLLLLWAWAP APGRASPEAL PLVNEDVKRT VDLSSHLAKV TAEVVLAHAG
SSSSPRAASF LLALEPELEA RLAHLGVQVK GEDEEENNLE VRETKIKGKR GRFFTVTLPV
ALDPGAKISV TVETVYTHVL QPYPTQITQS EKQFVVFEGN HYFYSPYPTK SQSMRVKLAS
RNVESYTKLG NPTRSEDLLD YGPFRDVPPY SQDTFKVHSE NNSPFLTITS MTRVIEVSHW
GNIAVEENVD LKHTGAVLKG PFSRYDYQRQ PDSGISSIRS FKTILPAAAQ DVYYRDEIGN
VSTSHLLILD DSVEMEIRPR FPLFGGWKTH YIVGYNLPSY EYLYNLGDQY ALKMRLVDHV
FDEQVIDSLT VKIILPEGAK NIQVDSPYEI SRAPDELHYT YLDTFGRPVI VAHKKNLVEQ
HIQDIVVHYT FNKVLMLQEP LLVVAAFYIL FFTVIVYVRL DFSITKDPAA EARMKVACIT
EQVLTLVNKR IGLYRHFDET INRYKQSRDV STLNSGKKSL ELEHKALTSE VALLQSRLKT
EGSDLCDKVS EMQKLDAQVK ELVLKSAVEA ERLVAGKLKK DTYIENEKLI SGKRQELVTK
IDHILDAL
