RPN2_ORYSJ
ID RPN2_ORYSJ Reviewed; 698 AA.
AC Q5N7W3; A0A0P0VBZ6;
DT 09-JAN-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 2;
DE AltName: Full=Ribophorin II;
DE Short=RPN-II;
DE AltName: Full=Ribophorin-2;
DE Flags: Precursor;
GN Name=RPN2; OrderedLocusNames=Os01g0911200, LOC_Os01g68324;
GN ORFNames=P0470A12.10;
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12447438; DOI=10.1038/nature01184;
RA Sasaki T., Matsumoto T., Yamamoto K., Sakata K., Baba T., Katayose Y.,
RA Wu J., Niimura Y., Cheng Z., Nagamura Y., Antonio B.A., Kanamori H.,
RA Hosokawa S., Masukawa M., Arikawa K., Chiden Y., Hayashi M., Okamoto M.,
RA Ando T., Aoki H., Arita K., Hamada M., Harada C., Hijishita S., Honda M.,
RA Ichikawa Y., Idonuma A., Iijima M., Ikeda M., Ikeno M., Ito S., Ito T.,
RA Ito Y., Ito Y., Iwabuchi A., Kamiya K., Karasawa W., Katagiri S.,
RA Kikuta A., Kobayashi N., Kono I., Machita K., Maehara T., Mizuno H.,
RA Mizubayashi T., Mukai Y., Nagasaki H., Nakashima M., Nakama Y.,
RA Nakamichi Y., Nakamura M., Namiki N., Negishi M., Ohta I., Ono N., Saji S.,
RA Sakai K., Shibata M., Shimokawa T., Shomura A., Song J., Takazaki Y.,
RA Terasawa K., Tsuji K., Waki K., Yamagata H., Yamane H., Yoshiki S.,
RA Yoshihara R., Yukawa K., Zhong H., Iwama H., Endo T., Ito H., Hahn J.H.,
RA Kim H.-I., Eun M.-Y., Yano M., Jiang J., Gojobori T.;
RT "The genome sequence and structure of rice chromosome 1.";
RL Nature 420:312-316(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
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:Q02795}.
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBUNIT: Component of the oligosaccharyltransferase (OST) complex.
CC {ECO:0000250|UniProtKB:Q02795}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Multi-pass membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the SWP1 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AP003436; BAD82429.1; -; Genomic_DNA.
DR EMBL; AP008207; BAF07073.1; -; Genomic_DNA.
DR EMBL; AP014957; BAS75839.1; -; Genomic_DNA.
DR EMBL; AK101333; BAG95014.1; -; mRNA.
DR RefSeq; XP_015613641.1; XM_015758155.1.
DR AlphaFoldDB; Q5N7W3; -.
DR STRING; 4530.OS01T0911200-01; -.
DR PaxDb; Q5N7W3; -.
DR PRIDE; Q5N7W3; -.
DR EnsemblPlants; Os01t0911200-01; Os01t0911200-01; Os01g0911200.
DR GeneID; 4324876; -.
DR Gramene; Os01t0911200-01; Os01t0911200-01; Os01g0911200.
DR KEGG; osa:4324876; -.
DR eggNOG; KOG2447; Eukaryota.
DR HOGENOM; CLU_017104_1_0_1; -.
DR InParanoid; Q5N7W3; -.
DR OMA; TTWSART; -.
DR OrthoDB; 1001599at2759; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000000763; Chromosome 1.
DR Proteomes; UP000059680; Chromosome 1.
DR Genevisible; Q5N7W3; OS.
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 GO; GO:0009409; P:response to cold; IEA:EnsemblPlants.
DR InterPro; IPR008814; Swp1.
DR PANTHER; PTHR12640; PTHR12640; 1.
DR Pfam; PF05817; Ribophorin_II; 1.
PE 2: Evidence at transcript level;
KW Endoplasmic reticulum; Membrane; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..29
FT /evidence="ECO:0000255"
FT CHAIN 30..698
FT /note="Dolichyl-diphosphooligosaccharide--protein
FT glycosyltransferase subunit 2"
FT /id="PRO_0000420812"
FT TOPO_DOM 30..600
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 601..621
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 622..638
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 639..659
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 660
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 661..681
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 682..698
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
SQ SEQUENCE 698 AA; 75207 MW; E6BE11301560C82C CRC64;
MAAAGGLPAS ATLLLLVIAA VAVAPLASAV RPVSDAHRSA AAELFAASPD GSFGDLETTY
EAVRTFQILG VEKDKGLIGK ACKFAAEKLA SSSSSPAKDL FHAARISGVL KCSVDSGVYD
DVATRLKAVI KDTNSLLELY YSVGGLLSIK EQGHNVVLPD ADNTFHAIKA LSQSDGRWRY
DTNSAESSTF AAGIALEALS AVISLADSEV DSSMIAVVKN DIVKLFDTIK SYDDGTFYFD
EKHVDAAEYK GPITTSASVV RGVTSFAAVA SGKLNIPGEK ILGLAKFFLG IGLPGSAKDC
FNQIESLSFL ENNRVFVPLV LSLPSKVFSL TSKDQLKVEV TTVFGSAAPP LRVNLVQVLG
SDSKVITTET KELQFDLDNN VHYLDIAPLK IDVGKYSLVF EISLQEQEHE TIYATGGTNT
EAIFVTGLIK VDKAEIGISD NDAGTVESVQ KIDLQKDTSV SLSANHLQKL RLSFQLSTPL
GKTFKPHQVF LKLKHDESKV EHLFVVPGSA RQFKIVLDFL GLVEKFYYLS GRYDLELAVG
DAAMENSFLR ALGHIELDLP EAPEKAPKPP AQAVDPFSKF GPKKEISHIF RSPEKRPPKE
LSFAFTGLTL LPIVGFLIGL MRLGVNLKNF PSLPAPAAFA SLFHAGIGAV LLLYVLFWIK
LDLFTTLKYL SFLGVFLVFV GHRALSYLSS TSAKQKTA