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Protein

Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 1

Gene

Rpn1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Essential subunit of the N-oligosaccharyl transferase (OST) complex 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 activityi

Dolichyl diphosphooligosaccharide + [protein]-L-asparagine = dolichyl diphosphate + a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to a protein L-asparagine.

Pathwayi: protein glycosylation

This protein is involved in the pathway protein glycosylation, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein glycosylation and in Protein modification.

GO - Molecular functioni

GO - Biological processi

  • peptide transport Source: RGD
  • protein glycosylation Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Enzyme and pathway databases

UniPathwayiUPA00378.

Names & Taxonomyi

Protein namesi
Recommended name:
Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 1 (EC:2.4.99.18)
Alternative name(s):
Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 67 kDa subunit
Ribophorin I
Short name:
RPN-I
Ribophorin-1
Gene namesi
Name:Rpn1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi3594. Rpn1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini23 – 437415LumenalSequence analysisAdd
BLAST
Transmembranei438 – 45518HelicalSequence analysisAdd
BLAST
Topological domaini456 – 605150CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2222Add
BLAST
Chaini23 – 605583Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 1PRO_0000022243Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei185 – 1851N6-acetyllysineBy similarity
Glycosylationi297 – 2971N-linked (GlcNAc...)Sequence analysis
Modified residuei536 – 5361N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation, Glycoprotein

Proteomic databases

PaxDbiP07153.
PRIDEiP07153.

PTM databases

iPTMnetiP07153.
PhosphoSiteiP07153.
SwissPalmiP07153.

Expressioni

Tissue specificityi

Expressed in all tissues tested.

Interactioni

Subunit structurei

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. Also identified as part of a complex which includes CANX, DERL1, DERL2, DDOST/OST48, RPN1, RPN2, SELK, VIMP, STT3A AND VCP. This contains known members of the OST complex and may be a form of this complex (By similarity).By similarity

Protein-protein interaction databases

BioGridi247626. 4 interactions.
IntActiP07153. 2 interactions.
MINTiMINT-4996362.
STRINGi10116.ENSRNOP00000066002.

Family & Domainsi

Sequence similaritiesi

Belongs to the OST1 family.Curated

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG2291. Eukaryota.
ENOG410XQVZ. LUCA.
HOVERGENiHBG012864.
InParanoidiP07153.

Family and domain databases

InterProiIPR007676. Ribophorin_I.
[Graphical view]
PANTHERiPTHR21049. PTHR21049. 1 hit.
PfamiPF04597. Ribophorin_I. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P07153-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEAPIVLLLL LWLALAPTPG SASSEAPPLV NEDVKRTVDL SSHLAKVTAE
60 70 80 90 100
VVLAHPGGGS TARASSFVLA LEPELESRLA HLGVQVKGED EEDNNLEVRE
110 120 130 140 150
TKMKGKSGRF FTVKLPVALD PGSKISIVVE TVYTHVLHPY PTQITQSEKQ
160 170 180 190 200
FVVFEGNHYF YSPYPTKTQT MRVRLASRNV ESHTKLGNPS RSEDILDYGP
210 220 230 240 250
FKDIPAYSQD TFKVHYENNS PFLTITSMTR VIEVSHWGNI AVEENVDLKH
260 270 280 290 300
TGAVLKGPFS RYDYQRQPDS GISSIRSFKT ILPAAAQDVY YRDEIGNVST
310 320 330 340 350
SHLLILDDSV EMEIRPRFGL FGGWKTHYIV GYNLPSYEYL YNLGDQYALK
360 370 380 390 400
MRFVDHVFDE QVIDSLTVKI ILPEGAKNIQ VDSPYDISRA PDELHYTYLD
410 420 430 440 450
TFGRPVIVAY KKNLVEQHIQ DIVVHYTFNK VLMLQEPLLV VAAFYILFFT
460 470 480 490 500
VIIYVRLDFS ITKDPAAEAR MKVACITEQV LTLVNKRLGL YRHFDETVNR
510 520 530 540 550
YKQSRDISTL NSGKKSLETE HKAVTSEIAV LQSRLKTEGS DLCDRVSEMQ
560 570 580 590 600
KLDAQVKELV LKSAVEAERL VAGKLKKDTY IENEKLSSGK RQELVTKIDH

ILDAL
Length:605
Mass (Da):68,304
Last modified:April 1, 1988 - v1
Checksum:i60F8ECAAF9C4806F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti16 – 3116APTPG…PPLVN → PDAWQRLFGGSAAGQR (PubMed:2335524).CuratedAdd
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X05300 mRNA. Translation: CAA28919.1.
M33508 Genomic DNA. Translation: AAA42043.1.
PIRiA27274.
UniGeneiRn.233900.
Rn.4224.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X05300 mRNA. Translation: CAA28919.1.
M33508 Genomic DNA. Translation: AAA42043.1.
PIRiA27274.
UniGeneiRn.233900.
Rn.4224.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi247626. 4 interactions.
IntActiP07153. 2 interactions.
MINTiMINT-4996362.
STRINGi10116.ENSRNOP00000066002.

PTM databases

iPTMnetiP07153.
PhosphoSiteiP07153.
SwissPalmiP07153.

Proteomic databases

PaxDbiP07153.
PRIDEiP07153.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

RGDi3594. Rpn1.

Phylogenomic databases

eggNOGiKOG2291. Eukaryota.
ENOG410XQVZ. LUCA.
HOVERGENiHBG012864.
InParanoidiP07153.

Enzyme and pathway databases

UniPathwayiUPA00378.

Miscellaneous databases

PROiP07153.

Family and domain databases

InterProiIPR007676. Ribophorin_I.
[Graphical view]
PANTHERiPTHR21049. PTHR21049. 1 hit.
PfamiPF04597. Ribophorin_I. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-31.

Entry informationi

Entry nameiRPN1_RAT
AccessioniPrimary (citable) accession number: P07153
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: April 1, 1988
Last modified: June 8, 2016
This is version 109 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.