Reviewed, UniProtKB/Swiss-Prot Q9GMB0 (RPN1_PIG)

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

Sus scrofa (Pig)

Taxonomic identifier

9823 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Suina › Suidae › Sus

Protein attributes

Sequence length	608 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. Ref.2
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. Ref.2
Subcellular location	Endoplasmic reticulum membrane; Single-pass type I membrane protein. Melanosome By similarity Ref.2 Ref.1.
Tissue specificity	Detected in liver (at protein level). Ref.2
Sequence similarities	Belongs to the OST1 family.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum Membrane
Domain	Signal Transmembrane
Molecular function	Transferase
PTM	Acetylation Glycoprotein
Gene Ontology (GO)
Biological process	protein amino acid glycosylation Inferred from electronic annotation. Source: InterPro
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell melanosome Inferred from electronic annotation. Source: UniProtKB-SubCell
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 – 24	24	By similarity
	Chain	25 – 608	584	Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 1		PRO_0000331254
Regions
	Topological domain	25 – 435	411	Lumenal Potential
	Transmembrane	436 – 456	21	Potential
	Topological domain	457 – 607	151	Cytoplasmic By similarity
Amino acid modifications
	Modified residue	188	1	N6-acetyllysine By similarity
	Glycosylation	300	1	N-linked (GlcNAc...) Potential

Sequences

	Sequence		Length	Mass (Da)
	Q9GMB0-1 [UniParc]. Last modified March 1, 2001. Version 1. Checksum: D8928F5AF03F851C	FASTA	608	68,695
	10 20 30 40 50 60 MEAPAVCLLP LLLLLWAWAP APGRASPEAL PLVNEDVKRT VDLSSHLAKV TAEVVLAHAG 70 80 90 100 110 120 SSSSPRAASF LLALEPELEA RLAHLGVQVK GEDEEENNLE VRETKIKGKR GRFFTVTLPV 130 140 150 160 170 180 ALDPGAKISV TVETVYTHVL QPYPTQITQS EKQFVVFEGN HYFYSPYPTK SQSMRVKLAS 190 200 210 220 230 240 RNVESYTKLG NPTRSEDLLD YGPFRDVPPY SQDTFKVHSE 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 ALKMRLVDHV 370 380 390 400 410 420 FDEQVIDSLT VKIILPEGAK NIQVDSPYEI SRAPDELHYT YLDTFGRPVI VAHKKNLVEQ 430 440 450 460 470 480 HIQDIVVHYT FNKVLMLQEP LLVVAAFYIL FFTVIVYVRL DFSITKDPAA EARMKVACIT 490 500 510 520 530 540 EQVLTLVNKR IGLYRHFDET INRYKQSRDV STLNSGKKSL ELEHKALTSE VALLQSRLKT 550 560 570 580 590 600 EGSDLCDKVS EMQKLDAQVK ELVLKSAVEA ERLVAGKLKK DTYIENEKLI SGKRQELVTK IDHILDAL

References

[1]	"The oligosaccharyltransferase complex from pig liver: cDNA cloning, expression and functional characterisation." Hardt B., Aparicio R., Bause E. Glycoconj. J. 17:767-779(2000) [PubMed: 11443278] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION. Tissue: Muscle.
[2]	"Oligosaccharyl transferase is a constitutive component of an oligomeric protein complex from pig liver endoplasmic reticulum." Breuer W., Bause E. Eur. J. Biochem. 228:689-696(1995) [PubMed: 7737165] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, TISSUE SPECIFICITY.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AJ293582 mRNA. Translation: CAC04096.1.
RefSeq	NP_999498.1.
UniGene	Ssc.12528
3D structure databases
ModBase	Search...
Genome annotation databases
Ensembl	ENSSSCT00000012709; ENSSSCP00000012376; ENSSSCG00000011612; Sus scrofa. [Genome view]
GeneID	397606.
KEGG	ssc:397606.
Organism-specific databases
CTD	397606.
Phylogenomic databases
HOVERGEN	Q9GMB0.
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...

Entry information

Entry name

RPN1_PIG

Accession

Primary (citable) accession number: Q9GMB0

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 29, 2008
Last sequence update:	March 1, 2001
Last modified:	November 24, 2009
This is version 30 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)