ID   RPN2_BOVIN              Reviewed;         631 AA.
AC   Q3SZI6;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   03-AUG-2022, entry version 98.
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   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA   Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA   Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT   "Characterization of 954 bovine full-CDS cDNA sequences.";
RL   BMC Genomics 6:166-166(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2005) 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; BT030513; ABQ12953.1; -; mRNA.
DR   EMBL; BC102838; AAI02839.1; -; mRNA.
DR   RefSeq; NP_001029776.1; NM_001034604.2.
DR   AlphaFoldDB; Q3SZI6; -.
DR   SMR; Q3SZI6; -.
DR   STRING; 9913.ENSBTAP00000051209; -.
DR   PaxDb; Q3SZI6; -.
DR   PeptideAtlas; Q3SZI6; -.
DR   PRIDE; Q3SZI6; -.
DR   GeneID; 534231; -.
DR   KEGG; bta:534231; -.
DR   CTD; 6185; -.
DR   eggNOG; KOG2447; Eukaryota.
DR   HOGENOM; CLU_017104_0_0_1; -.
DR   InParanoid; Q3SZI6; -.
DR   OrthoDB; 1001599at2759; -.
DR   TreeFam; TF106146; -.
DR   UniPathway; UPA00378; -.
DR   Proteomes; UP000009136; 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..631
FT                   /note="Dolichyl-diphosphooligosaccharide--protein
FT                   glycosyltransferase subunit 2"
FT                   /id="PRO_0000328635"
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: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;  69214 MW;  006BFB6A50A246F1 CRC64;
     MALPGSSTVF LLALTIIAST QALTPTHYLT KHDVERLKAS LDRPFTSLES AFYSIVGLSS
     LGAQVPDVKK ACTFIKSNLD PSNVDSLFYA AQSSQALSGC EISISNETKD LLLAAVSEDS
     SVAQIYHAVA ALSGFGLPLA SQEALGALTA RLSKEETVLA TVQALQTASY LSQQADLRSI
     VEEIEDLVAR LDELGGVYLQ FEEGLETTAL FVAATYKLMD HVGTEPSIKE DQVIQLMNAI
     FSKKNFESLS EAFSVASAAA ALSENRYHVP VVVVPEGSPS YTQEQAILRL QVTNVLSQPL
     TQATVKLEHA KSVASRATVL QKTSFTLIGD VFELNFMNVK FSSGYYDFSV KVEGDNRYIA
     NTVELRVKIS TEVGITNVDL STVDKDQSIA PKTTRVTYPA KAKGTFIADS HQNFALFFQL
     VDVNTGAELT PHQTFVRLHN QKTGQEVVFV AEPDSKNVYK FELDTSERKL EFDSASGTYT
     LYLIIGDATL KNPILWNVAD VVIRFPEDDV PSTVLSKNIF TPKQEIQHLF REPEKRPPTV
     VSNTFTALIL SPLLLLFALW IRIGANVSNF TFAPSTIVFH LGHAAMLGLM YVYWTQLNMF
     QTLKYLAILG SVTFLAGNRM LAQQAIKRTA H