ID   DAP1_MOUSE              Reviewed;         102 AA.
AC   Q91XC8;
DT   07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   24-JAN-2024, entry version 131.
DE   RecName: Full=Death-associated protein 1;
DE            Short=DAP-1;
GN   Name=Dap;
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=129, FVB/N, and FVB/N-3; TISSUE=Colon, and Mammary tumor;
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).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of electron
RT   capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC   Pancreas, Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [5]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-29, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA   Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA   Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT   "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT   pathways.";
RL   Mol. Cell 50:919-930(2013).
CC   -!- FUNCTION: Ribosome-binding protein involved in ribosome hibernation, a
CC       process during which ribosomes are stabilized in an inactive state and
CC       preserved from proteasomal degradation. Acts via its association with
CC       eiF5a (EIF5A and EIF5A2) at the polypeptide exit tunnel of the
CC       ribosome, preventing mRNA translation. Involved in ribosome hibernation
CC       in the mature oocyte by preventing mRNA translation, leading to
CC       ribosome inactivation. Ribosomes, which are produced in large
CC       quantities during oogenesis, are stored and translationally repressed
CC       in the oocyte and early embryo (By similarity). Also acts as a negative
CC       regulator of autophagy. Involved in mediating interferon-gamma-induced
CC       cell death (By similarity). {ECO:0000250|UniProtKB:P51397,
CC       ECO:0000250|UniProtKB:Q9I9N1}.
CC   -!- SUBUNIT: Associates with ribosomes; inhibiting translation. Interacts
CC       with eiF5a (EIF5A and EIF5A2); inhibiting translation.
CC       {ECO:0000250|UniProtKB:Q9I9N1}.
CC   -!- PTM: Phosphorylated. Phosphorylation by MTOR inhibits the suppressive
CC       activity of DAP toward autophagy. {ECO:0000250|UniProtKB:P51397}.
CC   -!- SIMILARITY: Belongs to the DAP-DAPL1 family. {ECO:0000305}.
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DR   EMBL; BC010828; AAH10828.1; -; mRNA.
DR   EMBL; BC024876; AAH24876.1; -; mRNA.
DR   EMBL; BC057669; AAH57669.1; -; mRNA.
DR   CCDS; CCDS27406.1; -.
DR   RefSeq; NP_666169.1; NM_146057.3.
DR   AlphaFoldDB; Q91XC8; -.
DR   SMR; Q91XC8; -.
DR   BioGRID; 230149; 3.
DR   STRING; 10090.ENSMUSP00000047186; -.
DR   iPTMnet; Q91XC8; -.
DR   PhosphoSitePlus; Q91XC8; -.
DR   EPD; Q91XC8; -.
DR   jPOST; Q91XC8; -.
DR   MaxQB; Q91XC8; -.
DR   PaxDb; 10090-ENSMUSP00000047186; -.
DR   ProteomicsDB; 279275; -.
DR   Pumba; Q91XC8; -.
DR   DNASU; 223453; -.
DR   Ensembl; ENSMUST00000044524.16; ENSMUSP00000047186.10; ENSMUSG00000039168.16.
DR   GeneID; 223453; -.
DR   KEGG; mmu:223453; -.
DR   UCSC; uc007vkc.2; mouse.
DR   AGR; MGI:1918190; -.
DR   CTD; 1611; -.
DR   MGI; MGI:1918190; Dap.
DR   VEuPathDB; HostDB:ENSMUSG00000039168; -.
DR   eggNOG; ENOG502S4ST; Eukaryota.
DR   GeneTree; ENSGT00940000154574; -.
DR   HOGENOM; CLU_150759_2_0_1; -.
DR   InParanoid; Q91XC8; -.
DR   OMA; HINQPRK; -.
DR   OrthoDB; 5397743at2759; -.
DR   PhylomeDB; Q91XC8; -.
DR   TreeFam; TF329716; -.
DR   BioGRID-ORCS; 223453; 3 hits in 76 CRISPR screens.
DR   ChiTaRS; Dap; mouse.
DR   PRO; PR:Q91XC8; -.
DR   Proteomes; UP000000589; Chromosome 15.
DR   RNAct; Q91XC8; Protein.
DR   Bgee; ENSMUSG00000039168; Expressed in urinary bladder urothelium and 251 other cell types or tissues.
DR   ExpressionAtlas; Q91XC8; baseline and differential.
DR   GO; GO:0070513; F:death domain binding; ISO:MGI.
DR   GO; GO:0006915; P:apoptotic process; ISO:MGI.
DR   GO; GO:0097190; P:apoptotic signaling pathway; ISO:MGI.
DR   GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR   GO; GO:0034198; P:cellular response to amino acid starvation; ISO:MGI.
DR   GO; GO:0010507; P:negative regulation of autophagy; ISO:MGI.
DR   GO; GO:0045892; P:negative regulation of DNA-templated transcription; ISO:MGI.
DR   GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
DR   InterPro; IPR024130; DAP1/DAPL1.
DR   PANTHER; PTHR13177; DEATH-ASSOCIATED PROTEIN 1; 1.
DR   PANTHER; PTHR13177:SF3; DEATH-ASSOCIATED PROTEIN 1; 1.
DR   Pfam; PF15228; DAP; 1.
DR   Genevisible; Q91XC8; MM.
PE   1: Evidence at protein level;
KW   Acetylation; Apoptosis; Autophagy; Phosphoprotein; Reference proteome;
KW   Translation regulation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P51397"
FT   CHAIN           2..102
FT                   /note="Death-associated protein 1"
FT                   /id="PRO_0000079783"
FT   REGION          1..102
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        30..49
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000250|UniProtKB:P51397"
FT   MOD_RES         3
FT                   /note="Phosphoserine; by MTOR"
FT                   /evidence="ECO:0000250|UniProtKB:P51397"
FT   MOD_RES         29
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         49
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P51397"
FT   MOD_RES         51
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17242355,
FT                   ECO:0007744|PubMed:19131326, ECO:0007744|PubMed:21183079"
FT   MOD_RES         91
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P51397"
SQ   SEQUENCE   102 AA;  11155 MW;  E6ECD12BEA21A557 CRC64;
     MSSPPEGKLE TKAGHPPAVK AGGMRIVQKH PHTGDGKEER DKDDQEWEST SPPKPTVFIS
     GVIARGDKDF PPAAAQVAHQ KPHASMDKHV SPRTQHIQQP RK
//