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Q91YQ5 (RPN1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 93. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:Rpn1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length608 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 activity

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.

Pathway

Protein modification; protein glycosylation.

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. 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.

Subcellular location

Endoplasmic reticulum membrane; Single-pass type I membrane protein. Melanosome By similarity.

Sequence similarities

Belongs to the OST1 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2525 By similarity
Chain26 – 608583Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 1
PRO_0000022242

Regions

Topological domain26 – 440415Lumenal Potential
Transmembrane441 – 45818Helical; Potential
Topological domain459 – 608150Cytoplasmic Potential

Amino acid modifications

Modified residue1881N6-acetyllysine By similarity
Modified residue5391N6-acetyllysine Ref.3
Glycosylation3001N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
Q91YQ5 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: CBDFA74C792A496E

FASTA60868,528
        10         20         30         40         50         60 
MESPVALLLL LLLCLGALAP TPGSASSEAP PLVNEDVKRT VDLSSHLAKV TAEVVLVHPG 

        70         80         90        100        110        120 
GGSTSRASSF VLALEPELES RLAHLGVQIK GEDEEDNNLE VRETKIKGKS GRFFTVKLPV 

       130        140        150        160        170        180 
ALDPGSKISV VVETVYTHVL HPYPTQITQS EKQFVVFEGN HYFYSPYPTK TQTMRVKLAS 

       190        200        210        220        230        240 
RNVESYTKLG NPSRSEDVLD YGPFKDIPAY SQDTFKVHYE NNSPFLTITS MTRVIEVSHW 

       250        260        270        280        290        300 
GNIAVEENVD LKHTGAVLKG PFSRYDYQRQ PDSGISSIRS FKTILPAAAQ DVYYRDEIGN 

       310        320        330        340        350        360 
VSTSHLLILD DSVEMEIRPR FPLFGGWKTH YIVGYNLPSY EYLYNLGDQY ALKMRFVDHV 

       370        380        390        400        410        420 
FDEQVIDSLT VKIILPEGAK NIQVDSPYDI SRAPDELHYT YLDTFGRPVI VAYKKNLVEQ 

       430        440        450        460        470        480 
HIQDIVVHYT FNKVLMLQEP LLVVAAFYIL FFTVIIYVRL DFSITKDPAA EARMKVACIT 

       490        500        510        520        530        540 
EQVLTLVNKR LGLYRHFDET VNRYKQSRDI STLNSGKKSL ETEHKAVTSE IAVLQSRLKT 

       550        560        570        580        590        600 
EGSDLCDRVS EMQKLDAQVK ELVLKSAVEA ERLVAGKLKK DTYLENEKLS SGKRQELVTK 


IDHILDAL 

« Hide

References

[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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_598694.3. NM_133933.4.
UniGeneMm.188544.

3D structure databases

ProteinModelPortalQ91YQ5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid222240. 1 interaction.
IntActQ91YQ5. 3 interactions.
MINTMINT-1581523.

PTM databases

PhosphoSiteQ91YQ5.

Proteomic databases

PaxDbQ91YQ5.
PRIDEQ91YQ5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000032143; ENSMUSP00000032143; ENSMUSG00000030062.
GeneID103963.
KEGGmmu:103963.
UCSCuc009cva.2. mouse.

Organism-specific databases

CTD6184.
MGIMGI:98084. Rpn1.

Phylogenomic databases

eggNOGNOG292474.
GeneTreeENSGT00390000009630.
HOGENOMHOG000247000.
HOVERGENHBG012864.
InParanoidQ91YQ5.
KOK12666.
OMATFKVHYE.
OrthoDBEOG7GFB53.
PhylomeDBQ91YQ5.
TreeFamTF312988.

Enzyme and pathway databases

UniPathwayUPA00378.

Gene expression databases

ArrayExpressQ91YQ5.
BgeeQ91YQ5.
CleanExMM_RPN1.
GenevestigatorQ91YQ5.

Family and domain databases

InterProIPR007676. Ribophorin_I.
[Graphical view]
PANTHERPTHR21049. PTHR21049. 1 hit.
PfamPF04597. Ribophorin_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSRPN1. mouse.
NextBio356253.
PROQ91YQ5.
SOURCESearch...

Entry information

Entry nameRPN1_MOUSE
AccessionPrimary (citable) accession number: Q91YQ5
Secondary accession number(s): Q3U985
Entry history
Integrated into UniProtKB/Swiss-Prot: March 29, 2004
Last sequence update: December 1, 2001
Last modified: April 16, 2014
This is version 93 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot