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Protein

Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 1

Gene

Rpn1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein 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.By similarity

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

GO - Molecular functioni

  1. dolichyl-diphosphooligosaccharide-protein glycotransferase activity Source: InterPro
  2. poly(A) RNA binding Source: MGI

GO - Biological processi

  1. protein N-linked glycosylation via asparagine Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Enzyme and pathway databases

ReactomeiREACT_196445. SRP-dependent cotranslational protein targeting to membrane.
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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 6

Organism-specific databases

MGIiMGI:98084. Rpn1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini26 – 440415LumenalSequence AnalysisAdd
BLAST
Transmembranei441 – 45818HelicalSequence AnalysisAdd
BLAST
Topological domaini459 – 608150CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. endoplasmic reticulum membrane Source: MGI
  2. integral component of membrane Source: UniProtKB-KW
  3. melanosome Source: UniProtKB-SubCell
  4. membrane Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2525By similarityAdd
BLAST
Chaini26 – 608583Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 1PRO_0000022242Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei188 – 1881N6-acetyllysineBy similarity
Glycosylationi300 – 3001N-linked (GlcNAc...)Sequence Analysis
Modified residuei539 – 5391N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation, Glycoprotein

Proteomic databases

MaxQBiQ91YQ5.
PaxDbiQ91YQ5.
PRIDEiQ91YQ5.

PTM databases

PhosphoSiteiQ91YQ5.

Expressioni

Gene expression databases

BgeeiQ91YQ5.
CleanExiMM_RPN1.
ExpressionAtlasiQ91YQ5. baseline and differential.
GenevestigatoriQ91YQ5.

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

BioGridi222240. 2 interactions.
IntActiQ91YQ5. 3 interactions.
MINTiMINT-1581523.

Structurei

3D structure databases

ProteinModelPortaliQ91YQ5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the OST1 family.Curated

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG292474.
GeneTreeiENSGT00390000009630.
HOGENOMiHOG000247000.
HOVERGENiHBG012864.
InParanoidiQ91YQ5.
KOiK12666.
OMAiTFKVHYE.
OrthoDBiEOG7GFB53.
PhylomeDBiQ91YQ5.
TreeFamiTF312988.

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.

Q91YQ5-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MESPVALLLL LLLCLGALAP TPGSASSEAP PLVNEDVKRT VDLSSHLAKV
60 70 80 90 100
TAEVVLVHPG GGSTSRASSF VLALEPELES RLAHLGVQIK GEDEEDNNLE
110 120 130 140 150
VRETKIKGKS GRFFTVKLPV ALDPGSKISV VVETVYTHVL HPYPTQITQS
160 170 180 190 200
EKQFVVFEGN HYFYSPYPTK TQTMRVKLAS RNVESYTKLG NPSRSEDVLD
210 220 230 240 250
YGPFKDIPAY SQDTFKVHYE NNSPFLTITS MTRVIEVSHW GNIAVEENVD
260 270 280 290 300
LKHTGAVLKG PFSRYDYQRQ PDSGISSIRS FKTILPAAAQ DVYYRDEIGN
310 320 330 340 350
VSTSHLLILD DSVEMEIRPR FPLFGGWKTH YIVGYNLPSY EYLYNLGDQY
360 370 380 390 400
ALKMRFVDHV FDEQVIDSLT VKIILPEGAK NIQVDSPYDI SRAPDELHYT
410 420 430 440 450
YLDTFGRPVI VAYKKNLVEQ HIQDIVVHYT FNKVLMLQEP LLVVAAFYIL
460 470 480 490 500
FFTVIIYVRL DFSITKDPAA EARMKVACIT EQVLTLVNKR LGLYRHFDET
510 520 530 540 550
VNRYKQSRDI STLNSGKKSL ETEHKAVTSE IAVLQSRLKT EGSDLCDRVS
560 570 580 590 600
EMQKLDAQVK ELVLKSAVEA ERLVAGKLKK DTYLENEKLS SGKRQELVTK

IDHILDAL
Length:608
Mass (Da):68,528
Last modified:December 1, 2001 - v1
Checksum:iCBDFA74C792A496E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK052130 mRNA. Translation: BAC34853.1.
AK132750 mRNA. Translation: BAE21332.1.
AK151899 mRNA. Translation: BAE30782.1.
AK153867 mRNA. Translation: BAE32221.1.
BC016080 mRNA. Translation: AAH16080.1.
CCDSiCCDS20332.1.
RefSeqiNP_598694.3. NM_133933.4.
UniGeneiMm.188544.

Genome annotation databases

EnsembliENSMUST00000032143; ENSMUSP00000032143; ENSMUSG00000030062.
GeneIDi103963.
KEGGimmu:103963.
UCSCiuc009cva.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK052130 mRNA. Translation: BAC34853.1.
AK132750 mRNA. Translation: BAE21332.1.
AK151899 mRNA. Translation: BAE30782.1.
AK153867 mRNA. Translation: BAE32221.1.
BC016080 mRNA. Translation: AAH16080.1.
CCDSiCCDS20332.1.
RefSeqiNP_598694.3. NM_133933.4.
UniGeneiMm.188544.

3D structure databases

ProteinModelPortaliQ91YQ5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi222240. 2 interactions.
IntActiQ91YQ5. 3 interactions.
MINTiMINT-1581523.

PTM databases

PhosphoSiteiQ91YQ5.

Proteomic databases

MaxQBiQ91YQ5.
PaxDbiQ91YQ5.
PRIDEiQ91YQ5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000032143; ENSMUSP00000032143; ENSMUSG00000030062.
GeneIDi103963.
KEGGimmu:103963.
UCSCiuc009cva.2. mouse.

Organism-specific databases

CTDi6184.
MGIiMGI:98084. Rpn1.

Phylogenomic databases

eggNOGiNOG292474.
GeneTreeiENSGT00390000009630.
HOGENOMiHOG000247000.
HOVERGENiHBG012864.
InParanoidiQ91YQ5.
KOiK12666.
OMAiTFKVHYE.
OrthoDBiEOG7GFB53.
PhylomeDBiQ91YQ5.
TreeFamiTF312988.

Enzyme and pathway databases

UniPathwayiUPA00378.
ReactomeiREACT_196445. SRP-dependent cotranslational protein targeting to membrane.

Miscellaneous databases

ChiTaRSiRpn1. mouse.
NextBioi356253.
PROiQ91YQ5.
SOURCEiSearch...

Gene expression databases

BgeeiQ91YQ5.
CleanExiMM_RPN1.
ExpressionAtlasiQ91YQ5. baseline and differential.
GenevestigatoriQ91YQ5.

Family and domain databases

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

Publicationsi

  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J and NOD.
    Tissue: Bone marrow, Eye, Testis and Thymus.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  3. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-539, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiRPN1_MOUSE
AccessioniPrimary (citable) accession number: Q91YQ5
Secondary accession number(s): Q3U985
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 29, 2004
Last sequence update: December 1, 2001
Last modified: February 4, 2015
This is version 102 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.