RPN2_PONAB
ID RPN2_PONAB Reviewed; 631 AA.
AC Q5RBM1;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 66.
DE RecName: Full=Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 2 {ECO:0000250|UniProtKB:P04844};
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:0000250|UniProtKB:P04844};
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: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; CR858617; CAH90839.1; -; mRNA.
DR RefSeq; NP_001128788.1; NM_001135316.1.
DR AlphaFoldDB; Q5RBM1; -.
DR SMR; Q5RBM1; -.
DR STRING; 9601.ENSPPYP00000012266; -.
DR GeneID; 100189691; -.
DR KEGG; pon:100189691; -.
DR CTD; 6185; -.
DR eggNOG; KOG2447; Eukaryota.
DR InParanoid; Q5RBM1; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0008250; C:oligosaccharyltransferase complex; IEA:InterPro.
DR GO; GO:0006487; P:protein N-linked glycosylation; IEA:InterPro.
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 /evidence="ECO:0000255"
FT CHAIN 23..631
FT /note="Dolichyl-diphosphooligosaccharide--protein
FT glycosyltransferase subunit 2"
FT /id="PRO_0000328634"
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..576
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 577..597
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 598..604
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 605..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:0000255"
FT CROSSLNK 154
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P04844"
SQ SEQUENCE 631 AA; 69300 MW; 004B5DC786D5B03E CRC64;
MAPLGSSTVF LLALTIIAST RALTPTHYLT KHDVERLKAS LDRPFTNLES AFYSIVGLSS
LGAQVPDAKK ACTYIRSNLD PSNVDSLFYA AQASQALSGC EISISNETKD LLLAAVSEDS
SVTQIYHAVA ALSGFGLPLA SQEALSALTA RLSKEETVLA TVQALQTASH LSQQADLRSI
VEEIEDLVAR LDELGGVYLQ FEEGLETTAL FVAATYKLMD HVGTEPSIKE DQVIQLMNAI
FSKKNFESLS EAFSVASVAA VLSHNRYHVP VVVVPEGSAS DTHEQAILRL QVTNVLSQPL
TQATVKLEHA KSVASRATVL QKTSFTPVGD VFELNFMNVK FSSGYYDFLV KVEGDNRYIA
NTVELRVKIS TEVGITNVDL STVDKDQSIA PKTTRVTYPA KAKGTFIADS HQNFALFFQL
VDVNTGAELT PHQTFVRLHN QKTGQEVVFV AEPDSKNVYK FELDTSERKI EFDSASGTYT
LYLIIGDATL KNPILWNVAD VVIKFPEEEA PSTVLSQNLF TPKQEIQHLF REPEKRPPTV
VSNTFTALIL SPLLLLFALW IRIGANVSNF TFTPSTIIFH LGHAAMLGLM YVYWTQLNMF
QTLKYLAILG SVTFLAGNRM LAQQAVKRTA H
