Reviewed, UniProtKB/Swiss-Prot P04843 (RPN1_HUMAN)

Names 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-1
    Ribophorin I
      Short name=RPN-I

Gene names

Name:

RPN1

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	607 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein 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.
Subcellular location	Endoplasmic reticulum membrane; Single-pass type I membrane protein. Melanosome. Note: Identified by mass spectrometry in melanosome fractions from stage I to stage IV. Ref.4 Ref.7
Tissue specificity	Expressed in all tissues tested. Ref.5
Sequence similarities	Belongs to the OST1 family.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum Membrane
Domain	Signal Transmembrane
Molecular function	Transferase
PTM	Glycoprotein
Gene Ontology (GO)
Biological process	protein amino acid N-linked glycosylation via asparagine Ref.6 Traceable author statement. Source: HGNC
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW melanosome Inferred from electronic annotation. Source: UniProtKB-SubCell oligosaccharyltransferase complex Ref.6 Traceable author statement. Source: HGNC rough endoplasmic reticulum membrane Inferred from sequence or structural similarity. Source: HGNC
Molecular function	dolichyl-diphosphooligosaccharide-protein glycotransferase activity Ref.6 Inferred from electronic annotation. Source: EC protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
GSTK1	Q9Y2Q3	1	EBI-355963,EBI-1053767
STT3B	Q8TCJ2	1	EBI-355963,EBI-2256290

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 23	23
	Chain	24 – 607	584	Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 1		PRO_0000022241
Regions
	Topological domain	24 – 438	415	Lumenal Potential
	Transmembrane	439 – 457	19	Potential
	Topological domain	458 – 607	150	Cytoplasmic Potential
Amino acid modifications
	Glycosylation	299	1	N-linked (GlcNAc...)

Sequences

	Sequence		Length	Mass (Da)
	P04843-1 [UniParc]. Last modified August 13, 1987. Version 1. Checksum: A2351A9CFABAEB6C	FASTA	607	68,569
	10 20 30 40 50 60 MEAPAAGLFL LLLLGTWAPA PGSASSEAPP LINEDVKRTV DLSSHLAKVT AEVVLAHLGG 70 80 90 100 110 120 GSTSRATSFL LALEPELEAR LAHLGVQVKG EDEEENNLEV RETKIKGKSG RFFTVKLPVA 130 140 150 160 170 180 LDPGAKISVI VETVYTHVLH PYPTQITQSE KQFVVFEGNH YFYSPYPTKT QTMRVKLASR 190 200 210 220 230 240 NVESYTKLGN PTRSEDLLDY GPFRDVPAYS QDTFKVHYEN NSPFLTITSM TRVIEVSHWG 250 260 270 280 290 300 NIAVEENVDL KHTGAVLKGP FSRYDYQRQP DSGISSIRSF KTILPAAAQD VYYRDEIGNV 310 320 330 340 350 360 STSHLLILDD SVEMEIRPRF PLFGGWKTHY IVGYNLPSYE YLYNLGDQYA LKMRFVDHVF 370 380 390 400 410 420 DEQVIDSLTV KIILPEGAKN IEIDSPYEIS RAPDELHYTY LDTFGRPVIV AYKKNLVEQH 430 440 450 460 470 480 IQDIVVHYTF NKVLMLQEPL LVVAAFYILF FTVIIYVRLD FSITKDPAAE ARMKVACITE 490 500 510 520 530 540 QVLTLVNKRI GLYRHFDETV NRYKQSRDIS TLNSGKKSLE TEHKALTSEI ALLQSRLKTE 550 560 570 580 590 600 GSDLCDRVSE MQKLDAQVKE LVLKSAVEAE RLVAGKLKKD TYIENEKLIS GKRQELVTKI DHILDAL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Human ribophorins I and II: the primary structure and membrane topology of two highly conserved rough endoplasmic reticulum-specific glycoproteins." Crimaudo C., Hortsch M., Gausepohl H., Meyer D.I. EMBO J. 6:75-82(1987) [PubMed: 3034581] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Blocker H., Heubner D., Hoerlein A., Michel G., Wedler H., Kohrer K., Ottenwalder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed: 17974005] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Uterine endothelium.
[3]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Cervix.
[4]	"Proteomic analysis of early melanosomes: identification of novel melanosomal proteins." Basrur V., Yang F., Kushimoto T., Higashimoto Y., Yasumoto K., Valencia J., Muller J., Vieira W.D., Watabe H., Shabanowitz J., Hearing V.J., Hunt D.F., Appella E. J. Proteome Res. 2:69-79(2003) [PubMed: 12643545] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[5]	"Oligosaccharyltransferase isoforms that contain different catalytic STT3 subunits have distinct enzymatic properties." Kelleher D.J., Karaoglu D., Mandon E.C., Gilmore R. Mol. Cell 12:101-111(2003) [PubMed: 12887896] [Abstract] Cited for: COMPOSITION OF THE OLIGOSACCHARYLTRANSFERASE COMPLEX, TISSUE SPECIFICITY.
[6]	"Proteomic analysis of mammalian oligosaccharyltransferase reveals multiple subcomplexes that contain Sec61, TRAP, and two potential new subunits." Shibatani T., David L.L., McCormack A.L., Frueh K., Skach W.R. Biochemistry 44:5982-5992(2005) [PubMed: 15835887] [Abstract] Cited for: COMPOSITION OF THE OLIGOSACCHARYLTRANSFERASE COMPLEX.
[7]	"Proteomic and bioinformatic characterization of the biogenesis and function of melanosomes." Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H., Mangini N.J., Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R., Yamagishi S., Shabanowitz J., Hearing V.J., Wu C., Appella E., Hunt D.F. J. Proteome Res. 5:3135-3144(2006) [PubMed: 17081065] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[8]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[9]	"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry." Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H. J. Proteome Res. 8:651-661(2009) [PubMed: 19159218] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-299, MASS SPECTROMETRY. Tissue: Liver.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	Y00281 mRNA. Translation: CAA68392.1. CR749284 mRNA. Translation: CAH18139.1. BC010839 mRNA. Translation: AAH10839.1.
IPI	IPI00025874.
PIR	A26168.
RefSeq	NP_002941.1.
UniGene	Hs.518244 Hs.603636
3D structure databases
ModBase	Search...
Protein-protein interaction databases
IntAct	P04843. 15 interactions.
PTM databases
PhosphoSite	P04843.
Proteomic databases
PRIDE	P04843.
Genome annotation databases
Ensembl	ENSG00000163902. Homo sapiens. [Contig view]
GeneID	6184.
KEGG	hsa:6184.
Organism-specific databases
GeneCards	GC03M129821.
H-InvDB	HIX0003655.
HGNC	HGNC:10381. RPN1.
HPA	CAB009748.
MIM	180470. gene.
PharmGKB	PA34777.
GenAtlas	Search...
Phylogenomic databases
HOGENOM	P04843.
HOVERGEN	P04843.
OMA	P04843. ENNLEVR.
Enzyme and pathway databases
BRENDA	2.4.1.119. 247.
Gene expression databases
Bgee	P04843.
CleanEx	HS_RPN1.
GermOnline	ENSG00000163902. Homo sapiens.
Family and domain databases
InterPro	IPR007676. Ribophorin_I. [Graphical view]
PANTHER	PTHR21049. Ribophorin_I. 1 hit.
Pfam	PF04597. Ribophorin_I. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	24017.
SOURCE	Search...

Entry information

Entry name

RPN1_HUMAN

Accession

Primary (citable) accession number: P04843
Secondary accession number(s): Q68DT1

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 13, 1987
Last sequence update:	August 13, 1987
Last modified:	June 16, 2009
This is version 89 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)