Reviewed, UniProtKB/Swiss-Prot Q5RBM1 (RPN2_PONAB)

Names and origin

Protein names

Recommended name:
    Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 2
    EC=2.4.1.119
Alternative name(s):
    Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 63 kDa subunit
    Ribophorin-2
    Ribophorin II
      Short name=RPN-II

Gene names

Name:

RPN2

Organism

Pongo abelii (Sumatran orangutan)

Taxonomic identifier

9601 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	631 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript 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 By similarity.
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.
Subcellular location	Endoplasmic reticulum membrane; Multi-pass membrane protein Potential.
Sequence similarities	Belongs to the SWP1 family.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum Membrane
Domain	Signal Transmembrane
Molecular function	Transferase
PTM	Glycoprotein Isopeptide bond Phosphoprotein Ubl conjugation
Gene Ontology (GO)
Biological process	protein amino acid N-linked glycosylation via asparagine Inferred from electronic annotation. Source: InterPro
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell oligosaccharyltransferase complex Inferred from electronic annotation. Source: InterPro
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 – 22	22	Potential
	Chain	23 – 631	609	Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 2		PRO_0000328634
Regions
	Topological domain	23 – 540	518	Lumenal Potential
	Transmembrane	541 – 561	21	Potential
	Transmembrane	577 – 597	21	Potential
	Transmembrane	605 – 617	13	Potential
	Topological domain	618 – 631	14	Cytoplasmic Potential
	Compositional bias	269 – 274	6	Poly-Val
Amino acid modifications
	Modified residue	282	1	Phosphothreonine By similarity
	Glycosylation	106	1	N-linked (GlcNAc...) Potential
	Cross-link	154		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q5RBM1-1 [UniParc]. Last modified December 21, 2004. Version 1. Checksum: 004B5DC786D5B03E	FASTA	631	69,300
	10 20 30 40 50 60 MAPLGSSTVF LLALTIIAST RALTPTHYLT KHDVERLKAS LDRPFTNLES AFYSIVGLSS 70 80 90 100 110 120 LGAQVPDAKK ACTYIRSNLD PSNVDSLFYA AQASQALSGC EISISNETKD LLLAAVSEDS 130 140 150 160 170 180 SVTQIYHAVA ALSGFGLPLA SQEALSALTA RLSKEETVLA TVQALQTASH LSQQADLRSI 190 200 210 220 230 240 VEEIEDLVAR LDELGGVYLQ FEEGLETTAL FVAATYKLMD HVGTEPSIKE DQVIQLMNAI 250 260 270 280 290 300 FSKKNFESLS EAFSVASVAA VLSHNRYHVP VVVVPEGSAS DTHEQAILRL QVTNVLSQPL 310 320 330 340 350 360 TQATVKLEHA KSVASRATVL QKTSFTPVGD VFELNFMNVK FSSGYYDFLV KVEGDNRYIA 370 380 390 400 410 420 NTVELRVKIS TEVGITNVDL STVDKDQSIA PKTTRVTYPA KAKGTFIADS HQNFALFFQL 430 440 450 460 470 480 VDVNTGAELT PHQTFVRLHN QKTGQEVVFV AEPDSKNVYK FELDTSERKI EFDSASGTYT 490 500 510 520 530 540 LYLIIGDATL KNPILWNVAD VVIKFPEEEA PSTVLSQNLF TPKQEIQHLF REPEKRPPTV 550 560 570 580 590 600 VSNTFTALIL SPLLLLFALW IRIGANVSNF TFTPSTIIFH LGHAAMLGLM YVYWTQLNMF 610 620 630 QTLKYLAILG SVTFLAGNRM LAQQAVKRTA H

References

[1]	The German cDNA consortium Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Kidney.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CR858617 mRNA. Translation: CAH90839.1.
RefSeq	NP_001128788.1.
UniGene	Pab.11929
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	100189691.
Phylogenomic databases
HOVERGEN	Q5RBM1.
Enzyme and pathway databases
BRENDA	2.4.1.119. 269192.
Family and domain databases
InterPro	IPR008814. Ribophorin_II. [Graphical view]
PANTHER	PTHR12640. Ribophorin_II. 1 hit.
ProtoNet	Search...

Entry information

Entry name

RPN2_PONAB

Accession

Primary (citable) accession number: Q5RBM1

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 8, 2008
Last sequence update:	December 21, 2004
Last modified:	February 9, 2010
This is version 19 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)