DELE1_RAT
ID DELE1_RAT Reviewed; 509 AA.
AC P60924; G3V8I7;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 17-JUN-2020, sequence version 2.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=DAP3-binding cell death enhancer 1 {ECO:0000312|RGD:735029};
DE AltName: Full=DAP3-binding cell death enhancer 1, long form {ECO:0000250|UniProtKB:Q14154};
DE Short=DELE1(L) {ECO:0000250|UniProtKB:Q14154};
DE AltName: Full=Death ligand signal enhancer {ECO:0000250|UniProtKB:Q14154};
DE Contains:
DE RecName: Full=DAP3-binding cell death enhancer 1 short form {ECO:0000250|UniProtKB:Q14154};
DE Short=DELE1(S) {ECO:0000250|UniProtKB:Q14154};
DE Short=S-DELE1 {ECO:0000250|UniProtKB:Q14154};
DE Flags: Precursor;
GN Name=Dele1 {ECO:0000312|RGD:735029};
GN Synonyms=Dele {ECO:0000250|UniProtKB:Q14154};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: [DAP3-binding cell death enhancer 1]: Key activator of the
CC integrated stress response (ISR) following mitochondrial stress. In
CC response to mitochondrial stress, cleaved by the protease OMA1,
CC generating the DAP3-binding cell death enhancer 1 short form (DELE1(S)
CC or S-DELE1), which translocates to the cytosol and activates
CC EIF2AK1/HRI to trigger the ISR. Essential for the induction of death
CC receptor-mediated apoptosis through the regulation of caspase
CC activation. {ECO:0000250|UniProtKB:Q14154}.
CC -!- FUNCTION: [DAP3-binding cell death enhancer 1 short form]: Protein
CC kinase activator generated by protein cleavage in response to
CC mitochondrial stress, which accumulates in the cytosol and specifically
CC binds to and activates the protein kinase activity of EIF2AK1/HRI. It
CC thereby activates the integrated stress response (ISR): EIF2AK1/HRI
CC activation promotes eIF-2-alpha (EIF2S1) phosphorylation, leading to a
CC decrease in global protein synthesis and the induction of selected
CC genes, including the transcription factor ATF4, the master
CC transcriptional regulator of the ISR. {ECO:0000250|UniProtKB:Q14154}.
CC -!- SUBUNIT: Interacts with DAP3. {ECO:0000250|UniProtKB:Q14154}.
CC -!- SUBUNIT: [DAP3-binding cell death enhancer 1 short form]: Interacts
CC (via TPR repeats) with EIF2AK1/HRI; activating the protein kinase
CC activity of EIF2AK1/HRI, thereby promoting the integrated stress
CC response (ISR). {ECO:0000250|UniProtKB:Q14154}.
CC -!- SUBCELLULAR LOCATION: [DAP3-binding cell death enhancer 1]:
CC Mitochondrion {ECO:0000250|UniProtKB:Q14154}. Mitochondrion inner
CC membrane {ECO:0000250|UniProtKB:Q14154}. Note=Associates with the
CC mitochondrion inner membrane in response to mitochondrial stress,
CC leading to its proteolytic processing by OMA1, and generation of the
CC AP3-binding cell death enhancer 1 short form (DELE1(S) or S-DELE1).
CC {ECO:0000250|UniProtKB:Q14154}.
CC -!- SUBCELLULAR LOCATION: [DAP3-binding cell death enhancer 1 short form]:
CC Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q14154}. Note=This short form
CC is generated by proteolytic processing by OMA1 in response to
CC mitochondrial stress, leading to translocation to the cytosol.
CC {ECO:0000250|UniProtKB:Q14154}.
CC -!- DOMAIN: [DAP3-binding cell death enhancer 1 short form]: The TPR
CC repeats bind to and activate EIF2AK1/HRI.
CC {ECO:0000250|UniProtKB:Q14154}.
CC -!- PTM: [DAP3-binding cell death enhancer 1]: Cleaved by OMA1 in response
CC to mitochondrial stress, generating the DAP3-binding cell death
CC enhancer 1 short form (DELE1(S) or S-DELE1) that accumulates in the
CC cytosol and activates the protein kinase activity of EIF2AK1/HRI.
CC Protein cleavage by OMA1 can take place at different positions, and
CC apparently does not require a specific sequence motif.
CC {ECO:0000250|UniProtKB:Q14154}.
CC -!- SIMILARITY: Belongs to the DELE1 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AABR07031745; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH473974; EDL76436.1; -; Genomic_DNA.
DR EMBL; BC064660; AAH64660.1; -; mRNA.
DR RefSeq; NP_955787.1; NM_199493.1.
DR AlphaFoldDB; P60924; -.
DR SMR; P60924; -.
DR STRING; 10116.ENSRNOP00000026273; -.
DR iPTMnet; P60924; -.
DR PhosphoSitePlus; P60924; -.
DR PaxDb; P60924; -.
DR Ensembl; ENSRNOT00000026273; ENSRNOP00000026273; ENSRNOG00000019276.
DR GeneID; 307480; -.
DR KEGG; rno:307480; -.
DR UCSC; RGD:735029; rat.
DR CTD; 9812; -.
DR RGD; 735029; Dele1.
DR eggNOG; KOG1550; Eukaryota.
DR GeneTree; ENSGT00390000002137; -.
DR HOGENOM; CLU_039734_0_0_1; -.
DR InParanoid; P60924; -.
DR OMA; HAWSTGN; -.
DR OrthoDB; 1039341at2759; -.
DR PhylomeDB; P60924; -.
DR TreeFam; TF329996; -.
DR PRO; PR:P60924; -.
DR Proteomes; UP000002494; Chromosome 18.
DR Proteomes; UP000234681; Chromosome 18.
DR Bgee; ENSRNOG00000019276; Expressed in heart and 18 other tissues.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005743; C:mitochondrial inner membrane; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0043539; F:protein serine/threonine kinase activator activity; ISS:UniProtKB.
DR GO; GO:0008625; P:extrinsic apoptotic signaling pathway via death domain receptors; ISS:UniProtKB.
DR GO; GO:0140468; P:HRI-mediated signaling; ISS:UniProtKB.
DR GO; GO:0140467; P:integrated stress response signaling; ISS:UniProtKB.
DR GO; GO:0043281; P:regulation of cysteine-type endopeptidase activity involved in apoptotic process; ISS:UniProtKB.
DR Gene3D; 1.25.40.10; -; 1.
DR InterPro; IPR006597; Sel1-like.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR Pfam; PF08238; Sel1; 5.
DR SMART; SM00671; SEL1; 5.
PE 2: Evidence at transcript level;
KW Apoptosis; Cytoplasm; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Reference proteome; Repeat; TPR repeat;
KW Transit peptide.
FT TRANSIT 1..101
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 102..509
FT /note="DAP3-binding cell death enhancer 1"
FT /id="PRO_0000050723"
FT CHAIN ?143..509
FT /note="DAP3-binding cell death enhancer 1 short form"
FT /evidence="ECO:0000250|UniProtKB:Q14154"
FT /id="PRO_0000450310"
FT REPEAT 213..245
FT /note="TPR 1"
FT /evidence="ECO:0000255"
FT REPEAT 246..278
FT /note="TPR 2"
FT /evidence="ECO:0000255"
FT REPEAT 279..313
FT /note="TPR 3"
FT /evidence="ECO:0000255"
FT REPEAT 314..351
FT /note="TPR 4"
FT /evidence="ECO:0000255"
FT REPEAT 352..385
FT /note="TPR 5"
FT /evidence="ECO:0000255"
FT REPEAT 386..423
FT /note="TPR 6"
FT /evidence="ECO:0000255"
FT REPEAT 470..498
FT /note="TPR 7"
FT /evidence="ECO:0000255"
FT REGION 19..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 143..185
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..45
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 142..143
FT /note="Cleavage; by OMA1"
FT /evidence="ECO:0000250|UniProtKB:Q14154"
FT CONFLICT 41
FT /note="P -> L (in Ref. 3; AAH64660)"
FT CONFLICT 142
FT /note="H -> Y (in Ref. 3; AAH64660)"
SQ SEQUENCE 509 AA; 55208 MW; 29A8A7A972828E56 CRC64;
MWRLTGILGR ALPRLLGPGF RGITPKPTSS DGPQTTSTTL PLPRVNFDRS GSHGSKRNRD
PKCCGWKEAF HWMSAHVSPN TLRDAVSWGT LAVLALHLAR QIHFHAPLVA GPQSAERCSW
HSPLYRFLSS SWWHPHSSLR RHVLPSPDCP APRNTGLREP RLGQEEPAAR SQGLPSDSSL
KPGLLNLPEE EPSDFGFLNA SRDFTSQAKA AEAGPPGGKN EQDKPKALPL EEAVTSIQQL
FQLSVAIAFN FLGTENIKTG DYTAAFSYFQ KAADRGYSKA QYNVGLCLEH GRGTPRDLSK
AVLFYHLAAV QGHSLAQYRY ARCLLQSPGS MSDPERQRAV SLLKQAADSG LTEAQAFLGV
LFTKEPHLDE QKAVKYFWLA ASNGDSQSRF HLGICYEKGL GVQRNLGEAV KCYQKSAAMG
NEPAQERLRT LFNVEAAGPS HLAIGLKSFS SPSLCSLNTF LAGASGLPHA SSTGNLGLLC
RSGHLGTSHG APSRAMPSLE RSLVRLGFG
