DELE1_MOUSE
ID DELE1_MOUSE Reviewed; 510 AA.
AC Q9DCV6; Q6A0B8;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=DAP3-binding cell death enhancer 1 {ECO:0000312|MGI:MGI:1914089};
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|MGI:MGI:1914089};
GN Synonyms=Dele {ECO:0000250|UniProtKB:Q14154},
GN Kiaa0141 {ECO:0000250|UniProtKB:Q14154};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Kidney;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryonic intestine;
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 11:205-218(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 -!- SEQUENCE CAUTION:
CC Sequence=BAD32178.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK002437; BAB22100.1; -; mRNA.
DR EMBL; AK172900; BAD32178.1; ALT_INIT; mRNA.
DR CCDS; CCDS50260.1; -.
DR RefSeq; NP_077141.2; NM_024179.5.
DR AlphaFoldDB; Q9DCV6; -.
DR SMR; Q9DCV6; -.
DR STRING; 10090.ENSMUSP00000025314; -.
DR PhosphoSitePlus; Q9DCV6; -.
DR PaxDb; Q9DCV6; -.
DR PRIDE; Q9DCV6; -.
DR ProteomicsDB; 279366; -.
DR Antibodypedia; 27388; 66 antibodies from 25 providers.
DR DNASU; 66839; -.
DR Ensembl; ENSMUST00000025314; ENSMUSP00000025314; ENSMUSG00000024442.
DR Ensembl; ENSMUST00000235904; ENSMUSP00000157678; ENSMUSG00000024442.
DR GeneID; 66839; -.
DR KEGG; mmu:66839; -.
DR UCSC; uc008erz.2; mouse.
DR CTD; 9812; -.
DR MGI; MGI:1914089; Dele1.
DR VEuPathDB; HostDB:ENSMUSG00000024442; -.
DR eggNOG; KOG1550; Eukaryota.
DR GeneTree; ENSGT00390000002137; -.
DR HOGENOM; CLU_039734_0_0_1; -.
DR InParanoid; Q9DCV6; -.
DR OMA; HAWSTGN; -.
DR OrthoDB; 1039341at2759; -.
DR PhylomeDB; Q9DCV6; -.
DR TreeFam; TF329996; -.
DR BioGRID-ORCS; 66839; 5 hits in 72 CRISPR screens.
DR ChiTaRS; Dele1; mouse.
DR PRO; PR:Q9DCV6; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; Q9DCV6; protein.
DR Bgee; ENSMUSG00000024442; Expressed in hindlimb stylopod muscle and 232 other tissues.
DR ExpressionAtlas; Q9DCV6; baseline and differential.
DR Genevisible; Q9DCV6; MM.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005743; C:mitochondrial inner membrane; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
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..510
FT /note="DAP3-binding cell death enhancer 1"
FT /id="PRO_0000050722"
FT CHAIN ?142..510
FT /note="DAP3-binding cell death enhancer 1 short form"
FT /evidence="ECO:0000250|UniProtKB:Q14154"
FT /id="PRO_0000450309"
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 471..499
FT /note="TPR 7"
FT /evidence="ECO:0000255"
FT REGION 19..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 142..185
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 26..49
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 165..183
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 141..142
FT /note="Cleavage; by OMA1"
FT /evidence="ECO:0000250|UniProtKB:Q14154"
SQ SEQUENCE 510 AA; 55430 MW; 54B911DF9F23ADFE CRC64;
MWRLTGILGR ALPRLLGPGF RGITPKPTSS DGSQTTSPTL PLTRLSFDRS GSHGSKRSRD
PKCCGWKDAF HWMSAHVSPN TLRDAISWGT LAVLALHLAR QIHFHAPLVA GPQPAERSWH
SPLYRFLSSS WWHPHSSLRR HVLPRSDCPA PRNTGLREPR QGQEDHPSAP SQCLPSDSSL
RSGLLNLPEE EPSDFDFLHA SRDFASQAKA AEAHPPGGKN EQDKAKALPL EEAVTSIQQL
FQLSVAITFN FLGTENIKTG DYTAAFSYFQ KAADRGYSKA QYNVGLCLEH GRGTPRDLSK
AILFYHLAAV QGHSLAQYRY ARCLLQSPGS LSDPERERAV SLLKQAADSG LTEAQAFLGV
LFTKEPHLDE QRAVKYLWLA ASNGDSQSRF HLGICYEKGL GAQRNLGEAV KCYQQAAAMG
NEPARERLRT LFNVEAAGPS HLATTGLKSF SSPSLCSLNT LLAGASGLPH ASSTGNLGLL
CRSGHLGASH GAPSRTIPSL ERSLVRLGFG
