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Protein

Derlin-2

Gene

Derl2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Functional component of endoplasmic reticulum-associated degradation (ERAD) for misfolded lumenal glycoproteins, but not that of misfolded nonglycoproteins. May act by forming a channel that allows the retrotranslocation of misfolded glycoproteins into the cytosol where they are ubiquitinated and degraded by the proteasome. May mediate the interaction between VCP and the degradation substrate (By similarity).By similarity

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Unfolded protein response

Enzyme and pathway databases

ReactomeiR-MMU-5358346. Hedgehog ligand biogenesis.
R-MMU-901032. ER Quality Control Compartment (ERQC).

Names & Taxonomyi

Protein namesi
Recommended name:
Derlin-2
Alternative name(s):
Degradation in endoplasmic reticulum protein 2
Der1-like protein 2
F-LANa
Gene namesi
Name:Derl2
Synonyms:Der2, Flana
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:2151483. Derl2.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 5757CytoplasmicSequence analysisAdd
BLAST
Transmembranei58 – 7821Helical; Name=1Sequence analysisAdd
BLAST
Topological domaini79 – 9618LumenalSequence analysisAdd
BLAST
Transmembranei97 – 11721Helical; Name=2Sequence analysisAdd
BLAST
Topological domaini118 – 15033CytoplasmicSequence analysisAdd
BLAST
Transmembranei151 – 17121Helical; Name=3Sequence analysisAdd
BLAST
Topological domaini172 – 1721LumenalSequence analysis
Transmembranei173 – 19321Helical; Name=4Sequence analysisAdd
BLAST
Topological domaini194 – 23946CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • early endosome Source: MGI
  • endoplasmic reticulum Source: MGI
  • integral component of endoplasmic reticulum membrane Source: UniProtKB
  • late endosome Source: MGI
  • membrane Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 239239Derlin-2PRO_0000219046Add
BLAST

Proteomic databases

EPDiQ8BNI4.
MaxQBiQ8BNI4.
PaxDbiQ8BNI4.
PeptideAtlasiQ8BNI4.
PRIDEiQ8BNI4.

PTM databases

iPTMnetiQ8BNI4.
PhosphoSiteiQ8BNI4.

Expressioni

Tissue specificityi

Widely expressed, with lowest levels in brain and heart.2 Publications

Inductioni

Up-regulated in response to endoplasmic reticulum stress via the ERN1-XBP1 pathway of the unfolded protein response (UPR).2 Publications

Gene expression databases

BgeeiQ8BNI4.
CleanExiMM_DERL2.
ExpressionAtlasiQ8BNI4. baseline and differential.
GenevisibleiQ8BNI4. MM.

Interactioni

Subunit structurei

Forms homo- and heterooligomers with DERL3 and, to a lesser extent, with DERL1. Interacts with SELK, VIMP, VCP and EDEM1. Mediates association between VCP and EDEM1, as well as that between VCP and the degradation substrate. Interacts with the SEL1L/SYVN1 and VCP/VIMP protein complexes. Interacts with OS9. Part of a complex which includes CANX, DERL1, DERL2, DDOST/OST48, RPN1, RPN2, SELK, VIMP, STT3A AND VCP.1 Publication

Protein-protein interaction databases

BioGridi228066. 2 interactions.
IntActiQ8BNI4. 1 interaction.
STRINGi10090.ENSMUSP00000117052.

Structurei

3D structure databases

ProteinModelPortaliQ8BNI4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the derlin family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG0858. Eukaryota.
COG5291. LUCA.
GeneTreeiENSGT00530000063156.
HOGENOMiHOG000200948.
HOVERGENiHBG051338.
InParanoidiQ8BNI4.
KOiK13989.
OMAiVSPFQLY.
OrthoDBiEOG73RBC2.
PhylomeDBiQ8BNI4.
TreeFamiTF314715.

Family and domain databases

InterProiIPR007599. DER1.
[Graphical view]
PANTHERiPTHR11009. PTHR11009. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q8BNI4-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAYQSLRLEY LQIPPVSRAY TTACVLTTAA VQLELITPFQ LYFNPELIFK
60 70 80 90 100
HFQIWRLITN FLFFGPVGFN FLFNMIFLYR YCRMLEEGSF RGRTADFVFM
110 120 130 140 150
FLFGGFLMTL FGLFVSLVFL GQAFTIMLVY VWSRRNPYVR MNFFGLLNFQ
160 170 180 190 200
APFLPWVLMG FSLLLGNSII VDLLGIAVGH IYFFLEDIFP NQPGGIRILK
210 220 230
TPSILRTIFD TPDEDPNYNP LPEERPGGFA WGEGQRLGG
Length:239
Mass (Da):27,640
Last modified:July 19, 2004 - v2
Checksum:iD702B14B47516A8C
GO
Isoform 2 (identifier: Q8BNI4-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     233-239: EGQRLGG → WNKTDLD

Note: No experimental confirmation available.
Show »
Length:239
Mass (Da):27,815
Checksum:iD5DDECCEF2BD42EC
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti228 – 2281G → A in AAL14868 (PubMed:11500051).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei233 – 2397EGQRLGG → WNKTDLD in isoform 2. 1 PublicationVSP_011085

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF208064 mRNA. Translation: AAL14868.1.
AK048627 mRNA. Translation: BAC33399.1.
AK077659 mRNA. Translation: BAC36934.1.
AK082564 mRNA. Translation: BAC38533.1.
AK083632 mRNA. Translation: BAC38974.1.
BC005682 mRNA. Translation: AAH05682.1.
CCDSiCCDS24972.1. [Q8BNI4-1]
RefSeqiNP_001278075.1. NM_001291146.1.
NP_001278076.1. NM_001291147.1.
NP_001278077.1. NM_001291148.1.
NP_291040.1. NM_033562.4. [Q8BNI4-1]
UniGeneiMm.28131.
Mm.446351.

Genome annotation databases

EnsembliENSMUST00000108523; ENSMUSP00000104163; ENSMUSG00000018442. [Q8BNI4-2]
ENSMUST00000143850; ENSMUSP00000117052; ENSMUSG00000018442. [Q8BNI4-1]
GeneIDi116891.
KEGGimmu:116891.
UCSCiuc007jxi.2. mouse. [Q8BNI4-2]
uc007jxj.2. mouse. [Q8BNI4-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF208064 mRNA. Translation: AAL14868.1.
AK048627 mRNA. Translation: BAC33399.1.
AK077659 mRNA. Translation: BAC36934.1.
AK082564 mRNA. Translation: BAC38533.1.
AK083632 mRNA. Translation: BAC38974.1.
BC005682 mRNA. Translation: AAH05682.1.
CCDSiCCDS24972.1. [Q8BNI4-1]
RefSeqiNP_001278075.1. NM_001291146.1.
NP_001278076.1. NM_001291147.1.
NP_001278077.1. NM_001291148.1.
NP_291040.1. NM_033562.4. [Q8BNI4-1]
UniGeneiMm.28131.
Mm.446351.

3D structure databases

ProteinModelPortaliQ8BNI4.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi228066. 2 interactions.
IntActiQ8BNI4. 1 interaction.
STRINGi10090.ENSMUSP00000117052.

PTM databases

iPTMnetiQ8BNI4.
PhosphoSiteiQ8BNI4.

Proteomic databases

EPDiQ8BNI4.
MaxQBiQ8BNI4.
PaxDbiQ8BNI4.
PeptideAtlasiQ8BNI4.
PRIDEiQ8BNI4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000108523; ENSMUSP00000104163; ENSMUSG00000018442. [Q8BNI4-2]
ENSMUST00000143850; ENSMUSP00000117052; ENSMUSG00000018442. [Q8BNI4-1]
GeneIDi116891.
KEGGimmu:116891.
UCSCiuc007jxi.2. mouse. [Q8BNI4-2]
uc007jxj.2. mouse. [Q8BNI4-1]

Organism-specific databases

CTDi51009.
MGIiMGI:2151483. Derl2.

Phylogenomic databases

eggNOGiKOG0858. Eukaryota.
COG5291. LUCA.
GeneTreeiENSGT00530000063156.
HOGENOMiHOG000200948.
HOVERGENiHBG051338.
InParanoidiQ8BNI4.
KOiK13989.
OMAiVSPFQLY.
OrthoDBiEOG73RBC2.
PhylomeDBiQ8BNI4.
TreeFamiTF314715.

Enzyme and pathway databases

ReactomeiR-MMU-5358346. Hedgehog ligand biogenesis.
R-MMU-901032. ER Quality Control Compartment (ERQC).

Miscellaneous databases

ChiTaRSiDerl2. mouse.
PROiQ8BNI4.
SOURCEiSearch...

Gene expression databases

BgeeiQ8BNI4.
CleanExiMM_DERL2.
ExpressionAtlasiQ8BNI4. baseline and differential.
GenevisibleiQ8BNI4. MM.

Family and domain databases

InterProiIPR007599. DER1.
[Graphical view]
PANTHERiPTHR11009. PTHR11009. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and characterization of F-LANa, upregulated in human liver cancer."
    Ying H., Yu Y., Xu Y.
    Biochem. Biophys. Res. Commun. 286:394-400(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
    Tissue: Liver.
  2. "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] (ISOFORMS 1 AND 2).
    Strain: C57BL/6J.
    Tissue: Cerebellum, Embryo and Head.
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Mammary tumor.
  4. "Multiprotein complexes that link dislocation, ubiquitination, and extraction of misfolded proteins from the endoplasmic reticulum membrane."
    Lilley B.N., Ploegh H.L.
    Proc. Natl. Acad. Sci. U.S.A. 102:14296-14301(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, INDUCTION.
  5. "Derlin-2 and Derlin-3 are regulated by the mammalian unfolded protein response and are required for ER-associated degradation."
    Oda Y., Okada T., Yoshida H., Kaufman R.J., Nagata K., Mori K.
    J. Cell Biol. 172:383-393(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  7. "Selenoprotein K binds multiprotein complexes and is involved in the regulation of endoplasmic reticulum homeostasis."
    Shchedrina V.A., Everley R.A., Zhang Y., Gygi S.P., Hatfield D.L., Gladyshev V.N.
    J. Biol. Chem. 286:42937-42948(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SELK AND VIMP.

Entry informationi

Entry nameiDERL2_MOUSE
AccessioniPrimary (citable) accession number: Q8BNI4
Secondary accession number(s): Q920I5, Q99J12
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: July 19, 2004
Last modified: July 6, 2016
This is version 105 of the entry and version 2 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. SIMILARITY comments
    Index of protein domains and families

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 one 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.