P07153 (RPN1_RAT) Reviewed, UniProtKB/Swiss-Prot
Last modified
November 16, 2011.
Version 85.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 1 EC=2.4.1.119 Alternative name(s): Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 67 kDa subunit Ribophorin I Short name=RPN-I Ribophorin-1 | ||
| Gene names |
| ||
| Organism | Rattus norvegicus (Rat) | ||
| Taxonomic identifier | 10116 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus |
Protein attributes
| Sequence length | 605 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at transcript level |
General annotation (Comments)
| Function | Essential subunit of N-oligosaccharyl transferase enzyme which catalyzes the transfer of a high mannose oligosaccharide from a lipid-linked oligosaccharide donor to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains. |
| Catalytic activity | Dolichyl diphosphooligosaccharide + protein L-asparagine = dolichyl diphosphate + a glycoprotein with the oligosaccharide chain attached by N-glycosyl linkage to protein L-asparagine. |
| Subunit structure | Component of the oligosaccharyltransferase (OST) complex. OST seems to exist in different forms which contain at least RPN1, RPN2, OST48, DAD1, OSTC, KRTCAP2 and either STT3A or STT3B. OST can form stable complexes with the Sec61 complex or with both the Sec61 and TRAP complexes By similarity. |
| Subcellular location | Endoplasmic reticulum membrane; Single-pass type I membrane protein. Melanosome By similarity. |
| Tissue specificity | Expressed in all tissues tested. |
| Sequence similarities | Belongs to the OST1 family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Endoplasmic reticulum Membrane |
| Domain | Signal Transmembrane Transmembrane helix |
| Molecular function | Transferase |
| PTM | Acetylation Glycoprotein |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological process | peptide transport Non-traceable author statement Ref.1. Source: RGD protein glycosylationInferred from electronic annotation. Source: InterPro |
| Cellular component | endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membraneInferred from electronic annotation. Source: UniProtKB-KW melanosomeInferred from electronic annotation. Source: UniProtKB-SubCell rough microsomeInferred from direct assay. Source: RGD |
| Molecular function | dolichyl-diphosphooligosaccharide-protein glycotransferase activity Inferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 22 | 22 | |||||||
| Chain | 23 – 605 | 583 | Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 1 | PRO_0000022243 | |||||
Regions | |||||||||
| Topological domain | 23 – 437 | 415 | Lumenal Potential | ||||||
| Transmembrane | 438 – 455 | 18 | Helical; Potential | ||||||
| Topological domain | 456 – 605 | 150 | Cytoplasmic Potential | ||||||
Amino acid modifications | |||||||||
| Modified residue | 185 | 1 | N6-acetyllysine By similarity | ||||||
| Glycosylation | 297 | 1 | N-linked (GlcNAc...) Potential | ||||||
Experimental info | |||||||||
| Sequence conflict | 16 – 31 | 16 | APTPG…PPLVN → PDAWQRLFGGSAAGQR Ref.2 | ||||||
Sequences
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References
| [1] | "Isolation and characterization of cDNA clones for rat ribophorin I: complete coding sequence and in vitro synthesis and insertion of the encoded product into endoplasmic reticulum membranes." Harnik-Ort V., Prakash K., Marcantonio E., Colman D.R., Rosenfeld M.G., Adesnik M., Sabatini D.D., Kreibich G. J. Cell Biol. 104:855-863(1987) [PubMed: 3031084] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Brain. |
| [2] | "Structure and chromosomal location of the rat ribophorin I gene." Behal A., Prakash K., D'Eustachio P., Adesnik M., Sabatini D.D., Kreibich G. J. Biol. Chem. 265:8252-8258(1990) [PubMed: 2335524] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-31. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | X05300 mRNA. Translation: CAA28919.1. M33508 Genomic DNA. Translation: AAA42043.1. |
| IPI | IPI00204365. |
| PIR | A27274. |
| RefSeq | NP_037199.1. NM_013067.1. |
| UniGene | Rn.4224. |
3D structure databases | |
| ModBase | Search... |
Protein-protein interaction databases | |
| IntAct | P07153. 1 interaction. |
| MINT | MINT-4996362. |
PTM databases | |
| PhosphoSite | P07153. |
Proteomic databases | |
| PRIDE | P07153. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 25596. |
| KEGG | rno:25596. |
Organism-specific databases | |
| CTD | 6184. |
| RGD | 3594. Rpn1. |
Phylogenomic databases | |
| HOVERGEN | HBG012864. |
Gene expression databases | |
| Genevestigator | P07153. |
Family and domain databases | |
| InterPro | IPR007676. Ribophorin_I. [Graphical view] |
| KO | K12666. |
| PANTHER | PTHR21049. Ribophorin_I. 1 hit. |
| Pfam | PF04597. Ribophorin_I. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other | |
| NextBio | 607287. |
Entry information
| Entry name | RPN1_RAT | ||||||||
| Accession | Primary (citable) accession number: P07153 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

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