LOCUS       NM_024295               3213 bp    mRNA    linear   PRI 07-MAY-2024
DEFINITION  Homo sapiens derlin 1 (DERL1), transcript variant 1, mRNA.
ACCESSION   NM_024295 NM_018630
VERSION     NM_024295.6
KEYWORDS    RefSeq; MANE Select.
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 3213)
  AUTHORS   Wang,T., Wang,D., Kuang,G., Gong,X., Zhang,L., Wan,J. and Li,K.
  TITLE     Derlin-1 promotes diet-induced non-alcoholic fatty liver disease
            via increasing RIPK3-mediated necroptosis
  JOURNAL   Free Radic Biol Med 217, 29-47 (2024)
   PUBMED   38522486
  REMARK    GeneRIF: Derlin-1 promotes diet-induced non-alcoholic fatty liver
            disease via increasing RIPK3-mediated necroptosis.
REFERENCE   2  (bases 1 to 3213)
  AUTHORS   You,H., Wen,X., Wang,X., Zhu,C., Chen,H., Bu,L., Zhang,J. and Qu,S.
  TITLE     Derlin-1 ameliorates nonalcoholic hepatic steatosis by promoting
            ubiquitylation and degradation of FABP1
  JOURNAL   Free Radic Biol Med 207, 260-271 (2023)
   PUBMED   37499886
  REMARK    GeneRIF: Derlin-1 ameliorates nonalcoholic hepatic steatosis by
            promoting ubiquitylation and degradation of FABP1.
REFERENCE   3  (bases 1 to 3213)
  AUTHORS   Miyano,K., Okamoto,S., Kajikawa,M., Kiyohara,T., Kawai,C.,
            Yamauchi,A. and Kuribayashi,F.
  TITLE     Regulation of Derlin-1-mediated degradation of NADPH oxidase
            partner p22phox by thiol modification
  JOURNAL   Redox Biol 56, 102479 (2022)
   PUBMED   36122532
  REMARK    GeneRIF: Regulation of Derlin-1-mediated degradation of NADPH
            oxidase partner p22(phox) by thiol modification.
REFERENCE   4  (bases 1 to 3213)
  AUTHORS   Chevalier,B., Baatallah,N., Najm,M., Castanier,S., Jung,V.,
            Pranke,I., Golec,A., Stoven,V., Marullo,S., Antigny,F.,
            Guerrera,I.C., Sermet-Gaudelus,I., Edelman,A. and Hinzpeter,A.
  TITLE     Differential CFTR-Interactome Proximity Labeling Procedures
            Identify Enrichment in Multiple SLC Transporters
  JOURNAL   Int J Mol Sci 23 (16), 8937 (2022)
   PUBMED   36012204
  REMARK    Publication Status: Online-Only
REFERENCE   5  (bases 1 to 3213)
  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 3213)
  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 3213)
  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 3213)
  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 3213)
  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 3213)
  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, AY358818.1,
            AK023846.1, AF131854.1 and AA976062.1.
            
            On Nov 23, 2018 this sequence version replaced NM_024295.5.
            
            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].
            
            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 :: SRR1803613.95145.1,
                                           SRR1660809.180544.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000259512.9/ ENSP00000259512.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
            COMPLETENESS: full length.
PRIMARY     REFSEQ_SPAN         PRIMARY_IDENTIFIER PRIMARY_SPAN        COMP
            1-1                 DA800358.1         122-122
            2-1242              AY358818.1         1-1241
            1243-2234           AK023846.1         4533-5524
            2235-2486           AY358818.1         2232-2483
            2487-2940           AF131854.1         1116-1569
            2941-3035           AY358818.1         2939-3033
            3036-3213           AA976062.1         11-188              c
FEATURES             Location/Qualifiers
     source          1..3213
                     /organism="Homo sapiens"
                     /mol_type="mRNA"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q24.13"
     gene            1..3213
                     /gene="DERL1"
                     /gene_synonym="DER-1; DER1; derlin-1"
                     /note="derlin 1"
                     /db_xref="GeneID:79139"
                     /db_xref="HGNC:HGNC:28454"
                     /db_xref="MIM:608813"
     exon            1..333
                     /gene="DERL1"
                     /gene_synonym="DER-1; DER1; derlin-1"
                     /inference="alignment:Splign:2.1.0"
     CDS             181..936
                     /gene="DERL1"
                     /gene_synonym="DER-1; DER1; derlin-1"
                     /note="isoform a is encoded by transcript variant 1;
                     DERtrin-1; degradation in endoplasmic reticulum protein 1;
                     Der1-like domain family, member 1"
                     /codon_start=1
                     /product="derlin-1 isoform a"
                     /protein_id="NP_077271.1"
                     /db_xref="CCDS:CCDS6337.1"
                     /db_xref="GeneID:79139"
                     /db_xref="HGNC:HGNC:28454"
                     /db_xref="MIM:608813"
                     /translation="MSDIGDWFRSIPAITRYWFAATVAVPLVGKLGLISPAYLFLWPE
                     AFLYRFQIWRPITATFYFPVGPGTGFLYLVNLYFLYQYSTRLETGAFDGRPADYLFML
                     LFNWICIVITGLAMDMQLLMIPLIMSVLYVWAQLNRDMIVSFWFGTRFKACYLPWVIL
                     GFNYIIGGSVINELIGNLVGHLYFFLMFRYPMDLGGRNFLSTPQFLYRWLPSRRGGVS
                     GFGVPPASMRRAADQNGGGGRHNWGQGFRLGDQ"
     exon            334..445
                     /gene="DERL1"
                     /gene_synonym="DER-1; DER1; derlin-1"
                     /inference="alignment:Splign:2.1.0"
     exon            446..510
                     /gene="DERL1"
                     /gene_synonym="DER-1; DER1; derlin-1"
                     /inference="alignment:Splign:2.1.0"
     exon            511..537
                     /gene="DERL1"
                     /gene_synonym="DER-1; DER1; derlin-1"
                     /inference="alignment:Splign:2.1.0"
     exon            538..633
                     /gene="DERL1"
                     /gene_synonym="DER-1; DER1; derlin-1"
                     /inference="alignment:Splign:2.1.0"
     exon            634..686
                     /gene="DERL1"
                     /gene_synonym="DER-1; DER1; derlin-1"
                     /inference="alignment:Splign:2.1.0"
     exon            687..797
                     /gene="DERL1"
                     /gene_synonym="DER-1; DER1; derlin-1"
                     /inference="alignment:Splign:2.1.0"
     exon            798..3213
                     /gene="DERL1"
                     /gene_synonym="DER-1; DER1; derlin-1"
                     /inference="alignment:Splign:2.1.0"
     regulatory      1146..1151
                     /regulatory_class="polyA_signal_sequence"
                     /gene="DERL1"
                     /gene_synonym="DER-1; DER1; derlin-1"
                     /note="hexamer: AACAAA"
     polyA_site      1178
                     /gene="DERL1"
                     /gene_synonym="DER-1; DER1; derlin-1"
                     /note="major polyA site"
     regulatory      2215..2220
                     /regulatory_class="polyA_signal_sequence"
                     /gene="DERL1"
                     /gene_synonym="DER-1; DER1; derlin-1"
                     /note="hexamer: AATAAA"
     polyA_site      2235
                     /gene="DERL1"
                     /gene_synonym="DER-1; DER1; derlin-1"
     regulatory      3018..3023
                     /regulatory_class="polyA_signal_sequence"
                     /gene="DERL1"
                     /gene_synonym="DER-1; DER1; derlin-1"
                     /note="hexamer: ATTAAA"
     polyA_site      3037
                     /gene="DERL1"
                     /gene_synonym="DER-1; DER1; derlin-1"
                     /note="major polyA site"
     regulatory      3192..3197
                     /regulatory_class="polyA_signal_sequence"
                     /gene="DERL1"
                     /gene_synonym="DER-1; DER1; derlin-1"
                     /note="hexamer: AATGAA"
     polyA_site      3213
                     /gene="DERL1"
                     /gene_synonym="DER-1; DER1; derlin-1"
ORIGIN      
        1 agaaggctgc ctcgctggtc cgaattcggt ggcgccacgt ccgcccgtct ccgccttctg
       61 catcgcggct tcggcggctt ccacctagac acctaacagt cgcggagccg gccgcgtcgt
      121 gagggggtcg gcacggggag tcgggcggtc ttgtgcatct tggctacctg tgggtcgaag
      181 atgtcggaca tcggagactg gttcaggagc atcccggcga tcacgcgcta ttggttcgcc
      241 gccaccgtcg ccgtgccctt ggtcggcaaa ctcggcctca tcagcccggc ctacctcttc
      301 ctctggcccg aagccttcct ttatcgcttt cagatttgga ggccaatcac tgccaccttt
      361 tatttccctg tgggtccagg aactggattt ctttatttgg tcaatttata tttcttatat
      421 cagtattcta cgcgacttga aacaggagct tttgatggga ggccagcaga ctatttattc
      481 atgctcctct ttaactggat ttgcatcgtg attactggct tagcaatgga tatgcagttg
      541 ctgatgattc ctctgatcat gtcagtactt tatgtctggg cccagctgaa cagagacatg
      601 attgtatcat tttggtttgg aacacgattt aaggcctgct atttaccctg ggttatcctt
      661 ggattcaact atatcatcgg aggctcggta atcaatgagc ttattggaaa tctggttgga
      721 catctttatt ttttcctaat gttcagatac ccaatggact tgggaggaag aaattttcta
      781 tccacacctc agtttttgta ccgctggctg cccagtagga gaggaggagt atcaggattt
      841 ggtgtgcccc ctgctagcat gaggcgagct gctgatcaga atggcggagg cgggagacac
      901 aactggggcc agggctttcg acttggagac cagtgaaggg gcggcctcgg gcagccgctc
      961 ctctcaagcc acatttcctc ccagtgctgg gtgcacttaa caactgcgtt ctggctaaca
     1021 ctgttggacc tgacccacac tgaatgtagt ctttcagtac gagacaaagt ttcttaaatc
     1081 ccgaagaaaa atataagtgt tccacaagtt tcacgattct cattcaagtc cttactgctg
     1141 tgaagaacaa ataccaactg tgcaaattgc aaaactgact acattttttg gtgtcttctc
     1201 ttctcccctt tccgtctgaa taatgggttt tagcgggtcc tagtctgctg gcattgagct
     1261 ggggctgggt caccaaaccc ttcccaaaag gacccttatc tctttcttgc acacatgcct
     1321 ctctcccact tttcccaacc cccacatttg caactagaag aggttgccca taaaattgct
     1381 ctgcccttga caggttctgt tatttattga cttttgccaa ggcttggtca caacaatcat
     1441 attcacgtaa ttttccccct ttggtggcag aactgtagca atagggggag aagacaagca
     1501 gcggatgaag cgttttctca gcttttggaa ttgcttcgac ctgacatccg ttgtaaccgt
     1561 ttgccacttc ttcagatatt tttataaaaa agtaccactg agtcagtgag ggccacagat
     1621 tggtattaat gagatacgag ggttgttgct gggtgtttgt ttcctgagct aagtgatcaa
     1681 gactgtagtg gagttgcagc taacatgggt taggtttaaa ccatggggga tgcaacccct
     1741 ttgcgtttca tatgtaggcc tactggcttt gtgtagctgg agtagttggg ttgctttgtg
     1801 ttaggaggat ccagatcatg ttggctacag ggagatgctc tctttgagag gctcctgggc
     1861 attgattcca tttcaatctc attctggata tgtgttcatt gagtaaagga ggagagaccc
     1921 tcatacgcta tttaaatgtc acttttttgc ctatcccccg ttttttggtc atgtttcaat
     1981 taattgtgag gaaggcgcag ctcctctctg cacgtagatc attttttaaa gctaatgtaa
     2041 gcacatctaa gggaataaca tgatttaagg ttgaaatggc tttagaatca tttgggtttg
     2101 agggtgtgtt attttgagtc atgaatgtac aagctctgtg aatcagacca gcttaaatac
     2161 ccacaccttt ttttcgtagg tgggcttttc ctatcagagc ttggctcata accaaataaa
     2221 gttttttgaa ggccatggct tttcacacag ttattttatt ttatgacgtt atctgaaagc
     2281 agactgttag gagcagtatt gagtggctgt cacactttga ggcaactaaa aaggcttcaa
     2341 acgttttgat cagtttcttt tcaggaaaca ttgtgctcta acagtatgac tattctttcc
     2401 cccactctta aacagtgtga tgtgtgttat cctaggaaat gagagttggc aaacaacttc
     2461 tcattttgaa tagagtttgt gtgtacctct ccatatttaa tttatatgat aaaataggtg
     2521 gggagagtct gaaccttaac tgtcatgttt tgttgttcat ctgtggccac aataaagttt
     2581 acttgtaaaa ttttagaggc cattactcca attatgttgc acgtacactc attgtacagg
     2641 cgtggagact cattgtatgt ataagaatat tctgacagtg agtgacccgg agtctctggt
     2701 gtaccctctt accagtcagc tgcctgcgag cagtcatttt ttcctaaagg tttacaagta
     2761 tttagaactc ttcagttcag ggcaaaatgt tcatgaagtt attcctctta aacatggtta
     2821 ggaagctgat gacgttattg attttgtctg gattatgttt ctggaataat tttaccaaaa
     2881 caagctattt gagttttgac ttgacaaggc aaaacatgac agtggattct ctttacaaat
     2941 ggaaaaaaaa aatccttatt ttgtataaag gacttccctt tttgtaaact aatccttttt
     3001 attggtaaaa attgtaaatt aaaatgtgca acttgaaggt tgtctgtgtt aagtttccat
     3061 gtccctgctc tgctgtctct tagatatcac ataatttgtg taaccaatta tctcttgaag
     3121 agcatttagg aagtacccag tattttttgc tggattaatt cctggatgca gaattcctgg
     3181 gttttcattt taatgaagga ggatgcttgc taa
//
