RPN2_CAEEL
ID RPN2_CAEEL Reviewed; 280 AA.
AC P91390;
DT 22-JUL-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 2 {ECO:0000250|UniProtKB:P04844};
DE AltName: Full=Oligosaccharyl transferase delta subunit {ECO:0000312|WormBase:M01A10.3};
DE AltName: Full=Ribophorin II {ECO:0000250|UniProtKB:P04844};
DE Short=RPN-II {ECO:0000250|UniProtKB:P04844};
DE AltName: Full=Ribophorin-2 {ECO:0000250|UniProtKB:P04844};
DE Flags: Precursor;
GN Name=ostd-1 {ECO:0000312|WormBase:M01A10.3};
GN ORFNames=M01A10.3 {ECO:0000312|WormBase:M01A10.3};
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 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).
RN [3] {ECO:0000305}
RP DISRUPTION PHENOTYPE.
RX PubMed=24130834; DOI=10.1371/journal.pone.0077051;
RA Bonner M.K., Han B.H., Skop A.;
RT "Profiling of the mammalian mitotic spindle proteome reveals an ER protein,
RT OSTD-1, as being necessary for cell division and ER morphology.";
RL PLoS ONE 8:E77051-E77051(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:F1PCT7}.
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000250|UniProtKB:P04844}.
CC -!- SUBUNIT: Component of the oligosaccharyltransferase (OST) complex.
CC {ECO:0000250|UniProtKB:F1PCT7}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Multi-pass membrane protein {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knock-down is mostly embryonic
CC lethal (PubMed:23691084, PubMed:24130834). Embryogenesis proceeds more
CC slowly and embryos are osmo-sensitive (PubMed:23691084). Twenty-five
CC percent of embryos exhibit cytokinesis defects (PubMed:24130834).
CC Sixty-five percent of embryos have incorrectly positioned cleavage
CC furrows (PubMed:24130834). Other phenotypes include delayed chromosome
CC alignment at metaphase and disrupted endoplasmic reticulum morphology
CC (PubMed:24130834). {ECO:0000269|PubMed:23691084,
CC ECO:0000269|PubMed:24130834}.
CC -!- SIMILARITY: Belongs to the SWP1 family. {ECO:0000305}.
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DR EMBL; FO081508; CCD72083.1; -; Genomic_DNA.
DR PIR; T25829; T25829.
DR RefSeq; NP_491624.1; NM_059223.6.
DR AlphaFoldDB; P91390; -.
DR SMR; P91390; -.
DR ComplexPortal; CPX-968; Oligosaccharyl transferase complex.
DR STRING; 6239.M01A10.3.1; -.
DR EPD; P91390; -.
DR PaxDb; P91390; -.
DR PeptideAtlas; P91390; -.
DR EnsemblMetazoa; M01A10.3.1; M01A10.3.1; WBGene00019693.
DR GeneID; 172208; -.
DR KEGG; cel:CELE_M01A10.3; -.
DR UCSC; M01A10.3.1; c. elegans.
DR CTD; 172208; -.
DR WormBase; M01A10.3; CE12232; WBGene00019693; ostd-1.
DR eggNOG; KOG2447; Eukaryota.
DR GeneTree; ENSGT00390000002635; -.
DR HOGENOM; CLU_086778_0_0_1; -.
DR InParanoid; P91390; -.
DR OMA; FFMYYTS; -.
DR OrthoDB; 1598552at2759; -.
DR PhylomeDB; P91390; -.
DR UniPathway; UPA00378; -.
DR PRO; PR:P91390; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00019693; 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:0007029; P:endoplasmic reticulum organization; IMP:WormBase.
DR GO; GO:0006487; P:protein N-linked glycosylation; IBA:GO_Central.
DR GO; GO:0051302; P:regulation of cell division; IMP:WormBase.
DR InterPro; IPR008814; Swp1.
DR PANTHER; PTHR12640; PTHR12640; 1.
DR Pfam; PF05817; Ribophorin_II; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum; Membrane; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT CHAIN 17..280
FT /note="Dolichyl-diphosphooligosaccharide--protein
FT glycosyltransferase subunit 2"
FT /id="PRO_0000433508"
FT TOPO_DOM 17..187
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 188..208
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 209..222
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 223..243
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 244
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 245..265
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 266..280
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
SQ SEQUENCE 280 AA; 31148 MW; 1AF9E7D091716C1B CRC64;
MKLLLVLLTI ASVALAAVDD VAVNNFKVGI LAKDQQPSDE NLKTVALFSK LPNELKADAS
QRLYVSFTVA KKSDNAKVKP HQVFLRFVAQ NGEDVVVVVN PDANGNYVYD NVLRTAAKSF
RNLSGQFKIS LLVGDVTIKN PINWQFANID AALPVAYEPT PKSQQVHFEP LNEISHIFRQ
PEKRPSALIS DLFTIICLSP LLILVVLWSQ VGINFQNAPA SPWVPIFHVG LIGIFGIYFM
FWVQFDMFVT LKYLAVLGFL TFVAGNRVLR AISESKQKSE
