RPN1_PONAB
ID RPN1_PONAB Reviewed; 607 AA.
AC Q5RFB6;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 73.
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 Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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 -!- 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; CR857244; CAH89541.1; -; mRNA.
DR RefSeq; NP_001124670.1; NM_001131198.1.
DR AlphaFoldDB; Q5RFB6; -.
DR SMR; Q5RFB6; -.
DR STRING; 9601.ENSPPYP00000015025; -.
DR GeneID; 100171515; -.
DR KEGG; pon:100171515; -.
DR CTD; 6184; -.
DR eggNOG; KOG2291; Eukaryota.
DR InParanoid; Q5RFB6; -.
DR OrthoDB; 1294725at2759; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000001595; Unplaced.
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:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
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..23
FT /evidence="ECO:0000250"
FT CHAIN 24..607
FT /note="Dolichyl-diphosphooligosaccharide--protein
FT glycosyltransferase subunit 1"
FT /id="PRO_0000331255"
FT TOPO_DOM 24..434
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 435..455
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 456..607
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
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; 68688 MW; 9D6E48092A1825A0 CRC64;
MEAPAARLFL LLLLGTWAPA PGSASSEAPP LINEDVKRTV DLSSHLAKVT AEVVLAHLGG
GSTSRATSFL LALEPELEAR LAHLGVQVKG EDEEENNLEV RETKIKGKSG RFFTVRLPVA
LDPGAKISVI VETVYTHVLQ PYPTQITQSE KQFVVFEGNH YFYSPYPTKT QTMRVKLASR
NVESYTKLGN PTRSEDLLDY GPFRDVPAYS QDTFKVHYEN NSPFLTITSM TRVIEVSHWG
NIAVEENVDL KHTGAVLKGP FSRYDYQRQP DSGISSIRSF KTILPAAAQD VYYRDEIGNV
STSHLLILDD SVEMEIRPRF PLFGGWKTHY IVGYNLPSYE YLYNLGDQYA LKMRFVDHVF
DEQVIDSLTV KIILPEGAKN IEIDSPYEIS RAPDELHYTY LDTFGRPVIV AYKKNLVEQH
IQDIVVHYTF NKVLMLQEPL LVVAAFYILF FTVIIYVRLD FSITKDPAAE ARMKVACITE
QVLTLVNKRI GLYRHFDETV NRYKQSRDIS TLNSGKKSLE TEHKALTSEI ALLQSRLKTE
GSDLCDRVSE MQKLDAQVKE LVLKSAVEAE RLVAGKLKKD TYIENEKLIS GKRQELVTKI
DHILDAL
