RPN2_RAT
ID RPN2_RAT Reviewed; 631 AA.
AC P25235; Q6P9X0;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2005, sequence version 2.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 2 {ECO:0000305};
DE AltName: Full=Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 63 kDa subunit;
DE AltName: Full=Ribophorin II;
DE Short=RPN-II;
DE AltName: Full=Ribophorin-2;
DE Flags: Precursor;
GN Name=Rpn2 {ECO:0000312|RGD:62075};
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].
RX PubMed=1710116; DOI=10.1016/0006-291x(91)90454-f;
RA Pirozzi G., Zhou Z., D'Eustachio P., Sabatini D.D., Kreibich G.;
RT "Rat ribophorin II: molecular cloning and chromosomal localization of a
RT highly conserved transmembrane glycoprotein of the rough endoplasmic
RT reticulum.";
RL Biochem. Biophys. Res. Commun. 176:1482-1486(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pituitary;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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:F1PCT7}.
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000250|UniProtKB:P04844}.
CC -!- SUBUNIT: Component of the oligosaccharyltransferase (OST) complex (By
CC similarity). OST exists in two different complex forms which contain
CC common core subunits RPN1, RPN2, OST48, OST4, DAD1 and TMEM258, either
CC STT3A or STT3B as catalytic subunits, and form-specific accessory
CC subunits (By similarity). STT3A complex assembly occurs through the
CC formation of 3 subcomplexes. Subcomplex 1 contains RPN1 and TMEM258,
CC subcomplex 2 contains the STT3A-specific subunits STT3A, DC2/OSTC, and
CC KCP2 as well as the core subunit OST4, and subcomplex 3 contains RPN2,
CC DAD1, and OST48. The STT3A complex can form stable complexes with the
CC Sec61 complex or with both the Sec61 and TRAP complexes. Interacts with
CC DDI2 (By similarity). Interacts with TMEM35A/NACHO (By similarity).
CC {ECO:0000250|UniProtKB:F1PCT7, ECO:0000250|UniProtKB:P04844,
CC ECO:0000250|UniProtKB:Q9DBG6}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000250|UniProtKB:F1PCT7}. Endoplasmic reticulum membrane; Multi-
CC pass membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the SWP1 family. {ECO:0000305}.
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DR EMBL; X55298; CAB56805.1; -; mRNA.
DR EMBL; BC060556; AAH60556.1; -; mRNA.
DR PIR; JN0065; JN0065.
DR RefSeq; NP_113886.1; NM_031698.1.
DR AlphaFoldDB; P25235; -.
DR SMR; P25235; -.
DR BioGRID; 249196; 3.
DR IntAct; P25235; 4.
DR MINT; P25235; -.
DR STRING; 10116.ENSRNOP00000063207; -.
DR GlyGen; P25235; 1 site.
DR iPTMnet; P25235; -.
DR PhosphoSitePlus; P25235; -.
DR SwissPalm; P25235; -.
DR jPOST; P25235; -.
DR PaxDb; P25235; -.
DR PRIDE; P25235; -.
DR Ensembl; ENSRNOT00000118622; ENSRNOP00000076455; ENSRNOG00000007492.
DR GeneID; 64701; -.
DR KEGG; rno:64701; -.
DR UCSC; RGD:62075; rat.
DR CTD; 6185; -.
DR RGD; 62075; Rpn2.
DR eggNOG; KOG2447; Eukaryota.
DR GeneTree; ENSGT00390000002635; -.
DR HOGENOM; CLU_017104_0_0_1; -.
DR InParanoid; P25235; -.
DR OMA; TTWSART; -.
DR OrthoDB; 1001599at2759; -.
DR PhylomeDB; P25235; -.
DR UniPathway; UPA00378; -.
DR PRO; PR:P25235; -.
DR Proteomes; UP000002494; Chromosome 3.
DR Bgee; ENSRNOG00000007492; Expressed in pancreas and 20 other tissues.
DR ExpressionAtlas; P25235; baseline and differential.
DR Genevisible; P25235; RN.
DR GO; GO:0000421; C:autophagosome membrane; IDA:RGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016604; C:nuclear body; IEA:Ensembl.
DR GO; GO:0008250; C:oligosaccharyltransferase complex; ISO:RGD.
DR GO; GO:0005791; C:rough endoplasmic reticulum; IDA:RGD.
DR GO; GO:0043022; F:ribosome binding; IDA:RGD.
DR GO; GO:0007568; P:aging; IEP:RGD.
DR GO; GO:0006487; P:protein N-linked glycosylation; ISO:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
DR InterPro; IPR008814; Swp1.
DR PANTHER; PTHR12640; PTHR12640; 1.
DR Pfam; PF05817; Ribophorin_II; 1.
PE 2: Evidence at transcript level;
KW Endoplasmic reticulum; Glycoprotein; Isopeptide bond; Membrane;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix;
KW Ubl conjugation.
FT SIGNAL 1..22
FT CHAIN 23..631
FT /note="Dolichyl-diphosphooligosaccharide--protein
FT glycosyltransferase subunit 2"
FT /id="PRO_0000022245"
FT TOPO_DOM 23..540
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 541..561
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 562..571
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 572..592
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 593..596
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 597..617
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 618..631
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 106
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT CROSSLNK 154
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P04844"
FT CONFLICT 298..299
FT /note="QP -> HA (in Ref. 1; CAB56805)"
FT /evidence="ECO:0000305"
FT CONFLICT 378
FT /note="V -> A (in Ref. 1; CAB56805)"
FT /evidence="ECO:0000305"
FT CONFLICT 390
FT /note="A -> P (in Ref. 1; CAB56805)"
FT /evidence="ECO:0000305"
FT CONFLICT 459
FT /note="Y -> H (in Ref. 1; CAB56805)"
FT /evidence="ECO:0000305"
FT CONFLICT 575..577
FT /note="STV -> TTI (in Ref. 1; CAB56805)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 631 AA; 69078 MW; 9BC0486C9C8469CD CRC64;
MAPPGSSAVF LLALTITAST QALTPTHYLT KHDVERLKAS LDRPFTSLES AFYSIVGLNS
LGAQVPDVKK ACAFIKSNLD PSNVDSLFYA AQSSQVLSGC EISVSNETRD LLLAAVSEDS
SVAQIYHAVA ALSGFGLPLA SHEALGALTA RLSKEETVLA TVQALHTASH LSQQADLRNI
VEEIEDLVAR LDELGGVYLQ FEEGLELTAL FVAATYKLMD HVGTEPSIKE DQVIQLMNTI
FSKKNFESLS EAFSVASAAA ALSQNRYHVP VVVVPEGSAS DTQEQAILRL QVSSVLSQPL
AQAAVKLEHA KSVASRATVL QKMPFSLVGD VFELNFKNVK LPSGYYDFSV RVEGDNRYIA
NTVELRVKIS TEVGITNVDL STVDKDQSIA PKTTRVTYPA KAKGTFIADS HQNFALFFQL
VDVNTGAELT PHQTFVRLHN QKTGQEVVFV AEPDNKNVYK FELDTSERKI EFDSASGTYT
LYLIIGDATL KNPILWNVAD VVIKFPEEEA PSTVLSQNLF TPKQEIQHLF REPEKRPPTV
VSNTFTALIL SPLLLLFALW IRIGANVSNF TFAPSTVIFH LGHAAMLGLM YVYWTQLNMF
QTLKYLAVLG TVTFLAGNRM LAQQAVKRTA H
