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Protein

Derlin-1

Gene

Derl1

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 proteins. May act by forming a channel that allows the retrotranslocation of misfolded proteins 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 - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Protein transport, Transport, Unfolded protein response

Names & Taxonomyi

Protein namesi
Recommended name:
Derlin-1
Alternative name(s):
Degradation in endoplasmic reticulum protein 1
Der1-like protein 1
Gene namesi
Name:Derl1
Synonyms:Der1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 15

Organism-specific databases

MGIiMGI:1915069. Derl1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini2 – 2221CytoplasmicSequence analysisAdd
BLAST
Transmembranei23 – 4321Helical; Name=1Sequence analysisAdd
BLAST
Topological domaini44 – 5916LumenalSequence analysisAdd
BLAST
Transmembranei60 – 8021Helical; Name=2Sequence analysisAdd
BLAST
Topological domaini81 – 10525CytoplasmicSequence analysisAdd
BLAST
Transmembranei106 – 12621Helical; Name=3Sequence analysisAdd
BLAST
Topological domaini127 – 15428LumenalSequence analysisAdd
BLAST
Transmembranei155 – 17521Helical; Name=4Sequence analysisAdd
BLAST
Topological domaini176 – 25176CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 251250Derlin-1PRO_0000219043Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineBy similarity
Modified residuei201 – 2011PhosphoserineCombined sources
Modified residuei202 – 2021PhosphothreonineBy similarity
Modified residuei226 – 2261PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ99J56.
MaxQBiQ99J56.
PaxDbiQ99J56.
PRIDEiQ99J56.

PTM databases

iPTMnetiQ99J56.
PhosphoSiteiQ99J56.
SwissPalmiQ99J56.

Expressioni

Tissue specificityi

Widely expressed, with lowest levels in brain and heart.1 Publication

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

BgeeiQ99J56.
CleanExiMM_DERL1.
GenevisibleiQ99J56. MM.

Interactioni

Subunit structurei

Forms homo- and heterooligomers with DERL2 and DERL3; binding to DERL3 is poorer than that between DERL2 and DERL3. Interacts with AMFR, VIMP/SELS, SEL1L, SELKM, SYVN1 and VCP, as well as with SEL1L-SYVN1 and VCP-VIMP protein complexes; this interaction is weaker than that observed between DERL2 and these complexes. Interacts with NGLY1 and YOD1. Does not bind to EDEM1 (By similarity). Interacts with RNF103 (By similarity). Interacts with DNAJB9 (PubMed:22267725). Part of a complex which includes CANX, DERL1, DERL2, DDOST/OST48, RPN1, RPN2, SELK, VIMP, STT3A AND VCP. Interacts with HM13. Interacts with XBP1 (via luminal/ectodomain domain); the interaction obviates the need for ectodomain shedding prior HM13/SPP-mediated XBP1 cleavage (By similarity).By similarity1 Publication

GO - Molecular functioni

Protein-protein interaction databases

BioGridi212459. 1 interaction.
STRINGi10090.ENSMUSP00000022993.

Structurei

3D structure databases

ProteinModelPortaliQ99J56.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the derlin family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG0858. Eukaryota.
COG5291. LUCA.
GeneTreeiENSGT00530000063156.
HOGENOMiHOG000200949.
HOVERGENiHBG105143.
InParanoidiQ99J56.
KOiK11519.
OMAiWICIVTK.
OrthoDBiEOG7353XM.
PhylomeDBiQ99J56.
TreeFamiTF354297.

Family and domain databases

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

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q99J56-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSDIGDWFRS IPAITRYWFA ATVAVPLIGK LGIISPAYFF LWPEAFLYRF
60 70 80 90 100
QIWRPFTATF YFPVGPGTGF LYLVNLYFLY QYSTRLEAGA FDGRPADYLF
110 120 130 140 150
MLLFNWICIV ITGLAMDMQL LMIPLIMSVL YVWAQLNRDL IVSFWFGTRF
160 170 180 190 200
KACYLPWVIL GFNYIIGGSV INELIGNLVG HLYFFLMFRY PMDLGGRNFL
210 220 230 240 250
STPQFLYRWL PSRRGGVSGF GVPPASMRRA ADQNGGGGRH NWGQGFRLGD

Q
Length:251
Mass (Da):28,835
Last modified:June 1, 2001 - v1
Checksum:i2E1B79DEAFD3FDC8
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti13 – 131A → V in BAB25036 (PubMed:16141072).Curated
Sequence conflicti17 – 171Y → N in BAB25036 (PubMed:16141072).Curated
Sequence conflicti20 – 201A → V in BAB25036 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK007435 mRNA. Translation: BAB25036.1.
AK043420 mRNA. Translation: BAC31545.1.
AK075631 mRNA. Translation: BAC35868.1.
AK152197 mRNA. Translation: BAE31026.1.
AK152901 mRNA. Translation: BAE31582.1.
BC003454 mRNA. Translation: AAH03454.1.
BC085490 mRNA. Translation: AAH85490.1.
CCDSiCCDS27484.1.
RefSeqiNP_077169.1. NM_024207.4.
UniGeneiMm.289387.
Mm.444431.

Genome annotation databases

EnsembliENSMUST00000022993; ENSMUSP00000022993; ENSMUSG00000022365.
GeneIDi67819.
KEGGimmu:67819.
UCSCiuc007vsq.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK007435 mRNA. Translation: BAB25036.1.
AK043420 mRNA. Translation: BAC31545.1.
AK075631 mRNA. Translation: BAC35868.1.
AK152197 mRNA. Translation: BAE31026.1.
AK152901 mRNA. Translation: BAE31582.1.
BC003454 mRNA. Translation: AAH03454.1.
BC085490 mRNA. Translation: AAH85490.1.
CCDSiCCDS27484.1.
RefSeqiNP_077169.1. NM_024207.4.
UniGeneiMm.289387.
Mm.444431.

3D structure databases

ProteinModelPortaliQ99J56.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi212459. 1 interaction.
STRINGi10090.ENSMUSP00000022993.

PTM databases

iPTMnetiQ99J56.
PhosphoSiteiQ99J56.
SwissPalmiQ99J56.

Proteomic databases

EPDiQ99J56.
MaxQBiQ99J56.
PaxDbiQ99J56.
PRIDEiQ99J56.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000022993; ENSMUSP00000022993; ENSMUSG00000022365.
GeneIDi67819.
KEGGimmu:67819.
UCSCiuc007vsq.1. mouse.

Organism-specific databases

CTDi79139.
MGIiMGI:1915069. Derl1.

Phylogenomic databases

eggNOGiKOG0858. Eukaryota.
COG5291. LUCA.
GeneTreeiENSGT00530000063156.
HOGENOMiHOG000200949.
HOVERGENiHBG105143.
InParanoidiQ99J56.
KOiK11519.
OMAiWICIVTK.
OrthoDBiEOG7353XM.
PhylomeDBiQ99J56.
TreeFamiTF354297.

Miscellaneous databases

ChiTaRSiDerl1. mouse.
PROiQ99J56.
SOURCEiSearch...

Gene expression databases

BgeeiQ99J56.
CleanExiMM_DERL1.
GenevisibleiQ99J56. MM.

Family and domain databases

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

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.
    Tissue: Bone marrow, Cerebellum and Pancreas.
  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].
    Strain: C57BL/6J.
    Tissue: Mammary tumor.
  3. "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.
  4. "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.
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-201, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brown adipose tissue, Liver, Lung, Pancreas, Spleen and Testis.
  6. "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.
  7. "ERdj4 protein is a soluble endoplasmic reticulum (ER) DnaJ family protein that interacts with ER-associated degradation machinery."
    Lai C.W., Otero J.H., Hendershot L.M., Snapp E.
    J. Biol. Chem. 287:7969-7978(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DNAJB9.

Entry informationi

Entry nameiDERL1_MOUSE
AccessioniPrimary (citable) accession number: Q99J56
Secondary accession number(s): Q3U6Z2, Q9D918
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: June 1, 2001
Last modified: July 6, 2016
This is version 106 of the entry and version 1 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.