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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}.
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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
 
 
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