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2025-05-09 18:41:13, GGRNA : RefSeq release 60 (20130726)
LOCUS NM_001134671 3284 bp mRNA linear PRI 20-APR-2013
DEFINITION Homo sapiens derlin 1 (DERL1), transcript variant 2, mRNA.
ACCESSION NM_001134671
VERSION NM_001134671.2 GI:402232740
KEYWORDS RefSeq.
SOURCE Homo sapiens (human)
ORGANISM Homo sapiens
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
REFERENCE 1 (bases 1 to 3284)
AUTHORS Honjo,Y., Ito,H., Horibe,T., Shimada,H., Nakanishi,A., Mori,H.,
Takahashi,R. and Kawakami,K.
TITLE Derlin-1-immunopositive inclusions in patients with Alzheimer's
disease
JOURNAL Neuroreport 23 (10), 611-615 (2012)
PUBMED 22627700
REMARK GeneRIF: Upregulation of derlin-1 may be associated with
endoplasmic reticulum stress in neuronal cells in Alzheimer's
disease.
REFERENCE 2 (bases 1 to 3284)
AUTHORS Wang,F., Olson,E.M. and Shyng,S.L.
TITLE Role of Derlin-1 protein in proteostasis regulation of
ATP-sensitive potassium channels
JOURNAL J. Biol. Chem. 287 (13), 10482-10493 (2012)
PUBMED 22311976
REMARK GeneRIF: Derlin-1 expression levels may affect glucose-stimulated
insulin secretion by altering surface expression of K(ATP)
channels.
REFERENCE 3 (bases 1 to 3284)
AUTHORS Suzuki,M., Otsuka,T., Ohsaki,Y., Cheng,J., Taniguchi,T.,
Hashimoto,H., Taniguchi,H. and Fujimoto,T.
TITLE Derlin-1 and UBXD8 are engaged in dislocation and degradation of
lipidated ApoB-100 at lipid droplets
JOURNAL Mol. Biol. Cell 23 (5), 800-810 (2012)
PUBMED 22238364
REMARK GeneRIF: These results indicate that ApoB after lipidation is
dislocated from the ER lumen to the LD surface for proteasomal
degradation and that Derlin-1 and UBXD8 are engaged in the
predislocation and postdislocation steps, respectively.
REFERENCE 4 (bases 1 to 3284)
AUTHORS Greenblatt,E.J., Olzmann,J.A. and Kopito,R.R.
TITLE Derlin-1 is a rhomboid pseudoprotease required for the dislocation
of mutant alpha-1 antitrypsin from the endoplasmic reticulum
JOURNAL Nat. Struct. Mol. Biol. 18 (10), 1147-1152 (2011)
PUBMED 21909096
REMARK Publication Status: Online-Only
REFERENCE 5 (bases 1 to 3284)
AUTHORS Schulze,A., Standera,S., Buerger,E., Kikkert,M., van Voorden,S.,
Wiertz,E., Koning,F., Kloetzel,P.M. and Seeger,M.
TITLE The ubiquitin-domain protein HERP forms a complex with components
of the endoplasmic reticulum associated degradation pathway
JOURNAL J. Mol. Biol. 354 (5), 1021-1027 (2005)
PUBMED 16289116
REFERENCE 6 (bases 1 to 3284)
AUTHORS Ye,Y., Shibata,Y., Kikkert,M., van Voorden,S., Wiertz,E. and
Rapoport,T.A.
TITLE Recruitment of the p97 ATPase and ubiquitin ligases to the site of
retrotranslocation at the endoplasmic reticulum membrane
JOURNAL Proc. Natl. Acad. Sci. U.S.A. 102 (40), 14132-14138 (2005)
PUBMED 16186510
REMARK GeneRIF: Derlin-1 is part of a retrotranslocation channel that is
associated with both the polyubiquitination and p97-ATPase
machineries at the endoplasmic reticulum membrane.
REFERENCE 7 (bases 1 to 3284)
AUTHORS Lilley,B.N. and Ploegh,H.L.
TITLE Multiprotein complexes that link dislocation, ubiquitination, and
extraction of misfolded proteins from the endoplasmic reticulum
membrane
JOURNAL Proc. Natl. Acad. Sci. U.S.A. 102 (40), 14296-14301 (2005)
PUBMED 16186509
REFERENCE 8 (bases 1 to 3284)
AUTHORS Katiyar,S., Joshi,S. and Lennarz,W.J.
TITLE The retrotranslocation protein Derlin-1 binds peptide:N-glycanase
to the endoplasmic reticulum
JOURNAL Mol. Biol. Cell 16 (10), 4584-4594 (2005)
PUBMED 16055502
REMARK GeneRIF: Derlin-1 interacts with the N-terminal domain of PNGase
via its cytosolic C-terminus. PNGase distributed in two
populations; ER-associated and free in the cytosol, which suggests
the deglycosylation process can proceed at either site
REFERENCE 9 (bases 1 to 3284)
AUTHORS Ye,Y., Shibata,Y., Yun,C., Ron,D. and Rapoport,T.A.
TITLE A membrane protein complex mediates retro-translocation from the ER
lumen into the cytosol
JOURNAL Nature 429 (6994), 841-847 (2004)
PUBMED 15215856
REMARK GeneRIF: Derlin-1 interacts with US11, a virally encoded ER protein
that specifically targets MHC class I heavy chains for export from
the ER, as well as with VIMP, a novel membrane protein that
recruits the p97 ATPase and its cofactor
REFERENCE 10 (bases 1 to 3284)
AUTHORS Lilley,B.N. and Ploegh,H.L.
TITLE A membrane protein required for dislocation of misfolded proteins
from the ER
JOURNAL Nature 429 (6994), 834-840 (2004)
PUBMED 15215855
REMARK GeneRIF: Derlin-1 is an important factor for the extraction of
certain aberrantly folded proteins from the mammalian ER
COMMENT REVIEWED REFSEQ: This record has been curated by NCBI staff. The
reference sequence was derived from DA800358.1, DA906855.1,
AK124086.1, AY358818.1, AK023846.1, AF131854.1 and AA976062.1.
On Aug 24, 2012 this sequence version replaced gi:197927277.
Summary: The protein encoded by this gene is a member of the derlin
family. Members of this family participate in the ER-associated
degradation response and retrotranslocate misfolded or unfolded
proteins from the ER lumen to the cytosol for proteasomal
degradation. This protein recognizes substrate in the ER and works
in a complex to retrotranslocate it across the ER membrane into the
cytosol. This protein may select cystic fibrosis transmembrane
conductance regulator protein (CFTR) for degradation as well as
unfolded proteins in Alzheimer's disease. Alternative splicing
results in multiple transcript variants that encode different
protein isoforms. [provided by RefSeq, Aug 2012].
Transcript Variant: This variant (2) uses an alternate in-frame
splice site in the coding region compared to variant 1. It encodes
isoform 2 which is shorter than isoform 1.
Publication Note: This RefSeq record includes a subset of the
publications that are available for this gene. Please see the Gene
record to access additional publications.
##Evidence-Data-START##
Transcript exon combination :: AK124086.1, DB013661.1 [ECO:0000332]
RNAseq introns :: single sample supports all introns
ERS025088 [ECO:0000348]
##Evidence-Data-END##
COMPLETENESS: complete on the 3' end.
PRIMARY REFSEQ_SPAN PRIMARY_IDENTIFIER PRIMARY_SPAN COMP
1-438 DA800358.1 1-438
439-439 DA906855.1 425-425
440-1055 AK124086.1 1-616
1056-1303 AY358818.1 994-1241
1304-2295 AK023846.1 4533-5524
2296-2547 AY358818.1 2232-2483
2548-3001 AF131854.1 1116-1569
3002-3096 AY358818.1 2939-3033
3097-3284 AA976062.1 1-188 c
FEATURES Location/Qualifiers
source 1..3284
/organism="Homo sapiens"
/mol_type="mRNA"
/db_xref="taxon:9606"
/chromosome="8"
/map="8q24.13"
gene 1..3284
/gene="DERL1"
/gene_synonym="DER-1; DER1"
/note="derlin 1"
/db_xref="GeneID:79139"
/db_xref="HGNC:28454"
/db_xref="MIM:608813"
exon 1..454
/gene="DERL1"
/gene_synonym="DER-1; DER1"
/inference="alignment:Splign:1.39.8"
misc_feature 215..217
/gene="DERL1"
/gene_synonym="DER-1; DER1"
/note="upstream in-frame stop codon"
CDS 302..997
/gene="DERL1"
/gene_synonym="DER-1; DER1"
/note="isoform b is encoded by transcript variant 2;
derlin-1; DERtrin-1; degradation in endoplasmic reticulum
protein 1; Der1-like domain family, member 1"
/codon_start=1
/product="derlin-1 isoform b"
/protein_id="NP_001128143.1"
/db_xref="GI:197927278"
/db_xref="CCDS:CCDS47915.1"
/db_xref="GeneID:79139"
/db_xref="HGNC:28454"
/db_xref="MIM:608813"
/translation="
MSDIGDWFRSIPAITRYWFAATVAVPLVGKLGLISPAYLFLWPEAFLYRFQIWRPITATFYFPVGPGTGFLYLVNLYFLYQYSTRLETGAFDGRPADYLFMLLFNWICIVITGLAMDMQLLMIPLIMSVLYVWAQLNRDMIVSFWFGTRFKACYLPWVILGFNYIIGGSYPMDLGGRNFLSTPQFLYRWLPSRRGGVSGFGVPPASMRRAADQNGGGGRHNWGQGFRLGDQ
"
misc_feature 332..853
/gene="DERL1"
/gene_synonym="DER-1; DER1"
/note="Der1-like family; Region: DER1; pfam04511"
/db_xref="CDD:203034"
variation 416
/gene="DERL1"
/gene_synonym="DER-1; DER1"
/replace="a"
/replace="c"
/db_xref="dbSNP:11551730"
exon 455..566
/gene="DERL1"
/gene_synonym="DER-1; DER1"
/inference="alignment:Splign:1.39.8"
exon 567..631
/gene="DERL1"
/gene_synonym="DER-1; DER1"
/inference="alignment:Splign:1.39.8"
exon 632..658
/gene="DERL1"
/gene_synonym="DER-1; DER1"
/inference="alignment:Splign:1.39.8"
exon 659..754
/gene="DERL1"
/gene_synonym="DER-1; DER1"
/inference="alignment:Splign:1.39.8"
exon 755..807
/gene="DERL1"
/gene_synonym="DER-1; DER1"
/inference="alignment:Splign:1.39.8"
exon 808..858
/gene="DERL1"
/gene_synonym="DER-1; DER1"
/inference="alignment:Splign:1.39.8"
exon 859..3280
/gene="DERL1"
/gene_synonym="DER-1; DER1"
/inference="alignment:Splign:1.39.8"
variation 1056
/gene="DERL1"
/gene_synonym="DER-1; DER1"
/replace="a"
/replace="g"
/db_xref="dbSNP:7159"
variation 1122
/gene="DERL1"
/gene_synonym="DER-1; DER1"
/replace="a"
/replace="g"
/db_xref="dbSNP:7812"
variation 1176
/gene="DERL1"
/gene_synonym="DER-1; DER1"
/replace="a"
/replace="g"
/db_xref="dbSNP:11691"
STS 1689..1845
/gene="DERL1"
/gene_synonym="DER-1; DER1"
/standard_name="D8S1422E"
/db_xref="UniSTS:151210"
variation 1784
/gene="DERL1"
/gene_synonym="DER-1; DER1"
/replace="a"
/replace="g"
/db_xref="dbSNP:1059588"
variation 1937
/gene="DERL1"
/gene_synonym="DER-1; DER1"
/replace="a"
/replace="g"
/db_xref="dbSNP:3739292"
STS 2101..2269
/gene="DERL1"
/gene_synonym="DER-1; DER1"
/standard_name="STS-F13780"
/db_xref="UniSTS:70380"
polyA_signal 2276..2281
/gene="DERL1"
/gene_synonym="DER-1; DER1"
STS 2330..3178
/gene="DERL1"
/gene_synonym="DER-1; DER1"
/standard_name="MGC3067__7703"
/db_xref="UniSTS:466327"
STS 2365..2517
/gene="DERL1"
/gene_synonym="DER-1; DER1"
/standard_name="SHGC-64153"
/db_xref="UniSTS:80876"
STS 2378..2610
/gene="DERL1"
/gene_synonym="DER-1; DER1"
/standard_name="RH68084"
/db_xref="UniSTS:2791"
polyA_signal 2632..2637
/gene="DERL1"
/gene_synonym="DER-1; DER1"
STS 2833..3059
/gene="DERL1"
/gene_synonym="DER-1; DER1"
/standard_name="RH81010"
/db_xref="UniSTS:83749"
variation 3002
/gene="DERL1"
/gene_synonym="DER-1; DER1"
/replace="g"
/replace="t"
/db_xref="dbSNP:7160"
polyA_signal 3079..3084
/gene="DERL1"
/gene_synonym="DER-1; DER1"
polyA_site 3098
/gene="DERL1"
/gene_synonym="DER-1; DER1"
/note="The 3' most polyA site has not been determined.
This is an internal site."
ORIGIN
acctggctccgccccccaggacgccgagcctcggccgggcggtaaaatcggcgcttaccctttaagcggcgggacttctggtcacgtcgtccgcggtcgccggaaggggaagtttcgcctcagaaggctgcctcgctggtccgaattcggtggcgccacgtccgcccgtctccgccttctgcatcgcggcttcggcggcttccacctagacacctaacagtcgcggagccggccgcgtcgtgagggggtcggcacggggagtcgggcggtcttgtgcatcttggctacctgtgggtcgaagatgtcggacatcggagactggttcaggagcatcccggcgatcacgcgctattggttcgccgccaccgtcgccgtgcccttggtcggcaaactcggcctcatcagcccggcctacctcttcctctggcccgaagccttcctttatcgctttcagatttggaggccaatcactgccaccttttatttccctgtgggtccaggaactggatttctttatttggtcaatttatatttcttatatcagtattctacgcgacttgaaacaggagcttttgatgggaggccagcagactatttattcatgctcctctttaactggatttgcatcgtgattactggcttagcaatggatatgcagttgctgatgattcctctgatcatgtcagtactttatgtctgggcccagctgaacagagacatgattgtatcattttggtttggaacacgatttaaggcctgctatttaccctgggttatccttggattcaactatatcatcggaggctcatacccaatggacttgggaggaagaaattttctatccacacctcagtttttgtaccgctggctgcccagtaggagaggaggagtatcaggatttggtgtgccccctgctagcatgaggcgagctgctgatcagaatggcggaggcgggagacacaactggggccagggctttcgacttggagaccagtgaaggggcggcctcgggcagccgctcctctcaagccacatttcctcccagtgctgggtgcacttaacaactgcgttctggctaacactgttggacctgacccacactgaatgtagtctttcagtacgagacaaagtttcttaaatcccgaagaaaaatataagtgttccacaagtttcacgattctcattcaagtccttactgctgtgaagaacaaataccaactgtgcaaattgcaaaactgactacattttttggtgtcttctcttctcccctttccgtctgaataatgggttttagcgggtcctagtctgctggcattgagctggggctgggtcaccaaacccttcccaaaaggacccttatctctttcttgcacacatgcctctctcccacttttcccaacccccacatttgcaactagaagaggttgcccataaaattgctctgcccttgacaggttctgttatttattgacttttgccaaggcttggtcacaacaatcatattcacgtaattttccccctttggtggcagaactgtagcaatagggggagaagacaagcagcggatgaagcgttttctcagcttttggaattgcttcgacctgacatccgttgtaaccgtttgccacttcttcagatatttttataaaaaagtaccactgagtcagtgagggccacagattggtattaatgagatacgagggttgttgctgggtgtttgtttcctgagctaagtgatcaagactgtagtggagttgcagctaacatgggttaggtttaaaccatgggggatgcaacccctttgcgtttcatatgtaggcctactggctttgtgtagctggagtagttgggttgctttgtgttaggaggatccagatcatgttggctacagggagatgctctctttgagaggctcctgggcattgattccatttcaatctcattctggatatgtgttcattgagtaaaggaggagagaccctcatacgctatttaaatgtcacttttttgcctatcccccgttttttggtcatgtttcaattaattgtgaggaaggcgcagctcctctctgcacgtagatcattttttaaagctaatgtaagcacatctaagggaataacatgatttaaggttgaaatggctttagaatcatttgggtttgagggtgtgttattttgagtcatgaatgtacaagctctgtgaatcagaccagcttaaatacccacacctttttttcgtaggtgggcttttcctatcagagcttggctcataaccaaataaagttttttgaaggccatggcttttcacacagttattttattttatgacgttatctgaaagcagactgttaggagcagtattgagtggctgtcacactttgaggcaactaaaaaggcttcaaacgttttgatcagtttcttttcaggaaacattgtgctctaacagtatgactattctttcccccactcttaaacagtgtgatgtgtgttatcctaggaaatgagagttggcaaacaacttctcattttgaatagagtttgtgtgtacctctccatatttaatttatatgataaaataggtggggagagtctgaaccttaactgtcatgttttgttgttcatctgtggccacaataaagtttacttgtaaaattttagaggccattactccaattatgttgcacgtacactcattgtacaggcgtggagactcattgtatgtataagaatattctgacagtgagtgacccggagtctctggtgtaccctcttaccagtcagctgcctgcgagcagtcattttttcctaaaggtttacaagtatttagaactcttcagttcagggcaaaatgttcatgaagttattcctcttaaacatggttaggaagctgatgacgttattgattttgtctggattatgtttctggaataattttaccaaaacaagctatttgagttttgacttgacaaggcaaaacatgacagtggattctctttacaaatggaaaaaaaaaatccttattttgtataaaggacttccctttttgtaaactaatcctttttattggtaaaaattgtaaattaaaatgtgcaacttgaaggttgtctgtgttaagtttccatgtccctgctctgctgtctcttagatatcacataatttgtgtaaccaattatctcttgaagagcatttaggaagtacccagtattttttgctggattaattcctggatgcagaattcctgggttttcattttaatgaaggaggatgcttgctaactttgaaaaa
//
ANNOTATIONS from NCBI Entrez Gene (20130726):
GeneID:79139 -> Molecular function: GO:0004872 [receptor activity] evidence: NAS
GeneID:79139 -> Molecular function: GO:0005515 [protein binding] evidence: IPI
GeneID:79139 -> Molecular function: GO:0042288 [MHC class I protein binding] evidence: IDA
GeneID:79139 -> Biological process: GO:0006986 [response to unfolded protein] evidence: IMP
GeneID:79139 -> Biological process: GO:0019060 [intracellular transport of viral proteins in host cell] evidence: TAS
GeneID:79139 -> Biological process: GO:0030433 [ER-associated protein catabolic process] evidence: IDA
GeneID:79139 -> Biological process: GO:0030968 [endoplasmic reticulum unfolded protein response] evidence: IDA
GeneID:79139 -> Biological process: GO:0030970 [retrograde protein transport, ER to cytosol] evidence: IDA
GeneID:79139 -> Biological process: GO:0030970 [retrograde protein transport, ER to cytosol] evidence: IMP
GeneID:79139 -> Biological process: GO:0045184 [establishment of protein localization] evidence: TAS
GeneID:79139 -> Cellular component: GO:0005769 [early endosome] evidence: IEA
GeneID:79139 -> Cellular component: GO:0005770 [late endosome] evidence: IEA
GeneID:79139 -> Cellular component: GO:0005783 [endoplasmic reticulum] evidence: IDA
GeneID:79139 -> Cellular component: GO:0005783 [endoplasmic reticulum] evidence: IMP
GeneID:79139 -> Cellular component: GO:0016021 [integral to membrane] evidence: IDA
GeneID:79139 -> Cellular component: GO:0030176 [integral to endoplasmic reticulum membrane] evidence: IDA
by
@meso_cacase at
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