RPN1_CAEEL
ID RPN1_CAEEL Reviewed; 586 AA.
AC Q9GZH4;
DT 22-JUL-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 2.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 1 {ECO:0000255|RuleBase:RU361143};
DE AltName: Full=Ribophorin I {ECO:0000250|UniProtKB:P04843};
DE Short=RPN-I {ECO:0000250|UniProtKB:P04843};
DE Flags: Precursor;
GN Name=ribo-1 {ECO:0000312|WormBase:T22D1.4};
GN ORFNames=T22D1.4 {ECO:0000312|WormBase:T22D1.4};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2] {ECO:0000305}
RP SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=23691084; DOI=10.1371/journal.pone.0063687;
RA Stevens J., Spang A.;
RT "N-glycosylation is required for secretion and mitosis in C. elegans.";
RL PLoS ONE 8:E63687-E63687(2013).
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:E2RQ08}.
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000255|RuleBase:RU361143}.
CC -!- SUBUNIT: Component of the oligosaccharyltransferase (OST) complex.
CC {ECO:0000250|UniProtKB:E2RQ08}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000255|RuleBase:RU361143}; Single-pass type I membrane protein
CC {ECO:0000255|RuleBase:RU361143}. Cytoplasmic granule
CC {ECO:0000269|PubMed:23691084}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knock-down is mostly embryonic
CC lethal (PubMed:23691084). Embryos exhibit cytokinesis defects which
CC lead to arrest during development (PubMed:23691084). Embryogenesis
CC proceeds more slowly and embryos are osmo-sensitive (PubMed:23691084).
CC Defective localization of the yolk receptor rme-2 and impaired yolk
CC secretion (PubMed:23691084). May result in chromosome segregation
CC defects (PubMed:23691084). {ECO:0000269|PubMed:23691084}.
CC -!- SIMILARITY: Belongs to the OST1 family.
CC {ECO:0000255|RuleBase:RU361143}.
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DR EMBL; FO080211; CCD62020.1; -; Genomic_DNA.
DR PIR; T32708; T32708.
DR RefSeq; NP_501065.2; NM_068664.6.
DR AlphaFoldDB; Q9GZH4; -.
DR SMR; Q9GZH4; -.
DR ComplexPortal; CPX-968; Oligosaccharyl transferase complex.
DR STRING; 6239.T22D1.4; -.
DR EPD; Q9GZH4; -.
DR PaxDb; Q9GZH4; -.
DR PeptideAtlas; Q9GZH4; -.
DR EnsemblMetazoa; T22D1.4.1; T22D1.4.1; WBGene00020683.
DR GeneID; 177456; -.
DR KEGG; cel:CELE_T22D1.4; -.
DR UCSC; T22D1.4; c. elegans.
DR CTD; 177456; -.
DR WormBase; T22D1.4; CE33704; WBGene00020683; ribo-1.
DR eggNOG; KOG2291; Eukaryota.
DR GeneTree; ENSGT00390000009630; -.
DR HOGENOM; CLU_031381_2_0_1; -.
DR InParanoid; Q9GZH4; -.
DR OMA; KTYMDTL; -.
DR OrthoDB; 1294725at2759; -.
DR PhylomeDB; Q9GZH4; -.
DR UniPathway; UPA00378; -.
DR PRO; PR:Q9GZH4; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00020683; Expressed in embryo and 4 other tissues.
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; IC:ComplexPortal.
DR GO; GO:0018279; P:protein N-linked glycosylation via asparagine; IBA:GO_Central.
DR InterPro; IPR007676; Ribophorin_I.
DR PANTHER; PTHR21049; PTHR21049; 1.
DR Pfam; PF04597; Ribophorin_I; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum; Membrane; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..15
FT /evidence="ECO:0000255"
FT CHAIN 16..586
FT /note="Dolichyl-diphosphooligosaccharide--protein
FT glycosyltransferase subunit 1"
FT /id="PRO_0000433511"
FT TOPO_DOM 16..421
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 422..442
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 443..586
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
SQ SEQUENCE 586 AA; 65737 MW; F350CB78B61CC8C5 CRC64;
MRLLFAIALL GAVFAEDAWK AANVDRTIDA TSQIVKVSTL YSFENVGNGP QSKVLIALSK
EESATLSFIS AGIDGSKGKL KISEKPAEKD LAVYEVDLRT PVAKGAKVTI RINLRITQVL
EPLPSKIQQS DSQFVVLHTS AYVPSLYETV TQKTTIRTTQ GGKLLSATTV SPSKQETERV
IYGPYVNIPA FETKPVKVHY ENNSPFVIAT IVERFIEVSH WGNIAVEEYI ELVHKGAELD
GPFSRIDYQM DRRGRRQPAL QQFTTVLPAQ AKDIYYRDEI GNISTSAVRI RADSVDVEIR
PRFPLFGGWK TSYVIGYNLP SEEYLYSKGN QYALKTKLFD HVFNDIVVEK LRTKVLLPEH
VKRVKVATPY AVDRRPEELK PTYLDTTGRL VLVLEKENIV PDHSQFFTVT YEFEFVDMLR
EPLLASAFFF SLFFVIIVYS RFDFTISSDP AKDAEERSQI ILGNLAKSVD SKQSAYEDLI
EASQQYKSTK NDADLQEAKK TFIAARNQEN STLTDKIATL KTDSGASAAE KASELLKYDK
TVFDAVDNYL KAVEKSTTKT AGTEEQQFLN KVKDARNRAD SVLASI
