RPN2_PIG
ID RPN2_PIG Reviewed; 629 AA.
AC Q9GL01;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 90.
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 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].
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).
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; AJ293583; CAC10571.1; -; mRNA.
DR RefSeq; NP_999106.1; NM_213941.1.
DR AlphaFoldDB; Q9GL01; -.
DR SMR; Q9GL01; -.
DR STRING; 9823.ENSSSCP00000026694; -.
DR PaxDb; Q9GL01; -.
DR PeptideAtlas; Q9GL01; -.
DR PRIDE; Q9GL01; -.
DR GeneID; 100154432; -.
DR KEGG; ssc:100154432; -.
DR CTD; 6185; -.
DR eggNOG; KOG2447; Eukaryota.
DR InParanoid; Q9GL01; -.
DR OrthoDB; 1001599at2759; -.
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:0008250; C:oligosaccharyltransferase complex; IBA:GO_Central.
DR GO; GO:0006487; P:protein N-linked glycosylation; IBA:GO_Central.
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..629
FT /note="Dolichyl-diphosphooligosaccharide--protein
FT glycosyltransferase subunit 2"
FT /id="PRO_5000066372"
FT TOPO_DOM 23..541
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 542..562
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 563..570
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 571..591
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 592..594
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 595..615
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 616..629
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 629 AA; 69274 MW; 93F22E2D0426C98C CRC64;
MAPPGSRTVL LLALTIIART QALKPTHYLT KHDVERLKAS LDRPFTSLES AFYSIVGLSS
LGAQVPDEKK ACTFIKSNLD PSNVDSLFYP PQSSQALSGC EISISNETKD LLLAAVSEDS
SVTQIYHAVA ALSGFGLPLA SQEALGALTA RLSKEETVLA TVQALQTASY LSQQADLRSI
VEEIEDLVAR LDELGGVYLQ FEEGLLETTA LFVAATYKLM DHEGTEPSIK EDQVIQLMNT
IFSKKNFESL PEAFSVASAA AALSQNRYHV PVVVVPEGSP SDTQEQAFLR LQVTNVLSQP
LTQATVKLEH AKSVASRATV LQKTSFTPVG DVFELNFVNV KFSSGYYDFS VKVEGDNRYI
ANTVELRVKI STEVGITNVD LSTVDKDQSI APKTTRVTYP AKAKGPFIAD SPQNFALFFQ
LVDVNTGAEL TPHQTFVRLH NQKTGQEVVF VAEPDSKNVY RFELDTSERK IEFDSASGTY
TLYLIIGDAT LKNPIHWNVA DVVIRFPEED APSTVLSKNL FTAKQEIQHL FRDPEKRPPT
VVSNTFTGLI LSPLLLLFAL WIRIGAKISN FTFGLTIIFH LGHAMLAMYV YWTQLNMFQT
LKYLAILGSV TFLAGNRMLA QQAIKRTAH
