ID   DAP1_RAT                Reviewed;         102 AA.
AC   Q9QX67;
DT   07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=Death-associated protein 1;
DE            Short=DAP-1;
DE   AltName: Full=Rap7a;
GN   Name=Dap; Synonyms=Rap7a;
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 [MRNA].
RC   TISSUE=Liver;
RA   Hartmann E., Goerlich D., Prehn S.;
RL   Submitted (JAN-1994) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Pituitary;
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   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
CC   -!- FUNCTION: Negative regulator of autophagy. Involved in mediating
CC       interferon-gamma-induced cell death (By similarity). {ECO:0000250}.
CC   -!- PTM: Phosphorylated. Phosphorylation by MTOR inhibits the suppressive
CC       activity of DAP toward autophagy (By similarity). {ECO:0000250}.
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DR   EMBL; U05334; AAF21441.1; -; mRNA.
DR   EMBL; BC060569; AAH60569.1; -; mRNA.
DR   RefSeq; NP_071971.1; NM_022526.2.
DR   AlphaFoldDB; Q9QX67; -.
DR   STRING; 10116.ENSRNOP00000014439; -.
DR   iPTMnet; Q9QX67; -.
DR   PhosphoSitePlus; Q9QX67; -.
DR   PaxDb; Q9QX67; -.
DR   PRIDE; Q9QX67; -.
DR   GeneID; 64322; -.
DR   KEGG; rno:64322; -.
DR   UCSC; RGD:620641; rat.
DR   CTD; 1611; -.
DR   RGD; 620641; Dap.
DR   VEuPathDB; HostDB:ENSRNOG00000010747; -.
DR   eggNOG; ENOG502S4ST; Eukaryota.
DR   HOGENOM; CLU_150759_2_0_1; -.
DR   InParanoid; Q9QX67; -.
DR   OMA; PTHDARP; -.
DR   OrthoDB; 1620337at2759; -.
DR   PhylomeDB; Q9QX67; -.
DR   TreeFam; TF329716; -.
DR   PRO; PR:Q9QX67; -.
DR   Proteomes; UP000002494; Chromosome 2.
DR   Bgee; ENSRNOG00000010747; Expressed in pancreas and 19 other tissues.
DR   Genevisible; Q9QX67; RN.
DR   GO; GO:0070513; F:death domain binding; ISO:RGD.
DR   GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; ISO:RGD.
DR   GO; GO:0006915; P:apoptotic process; ISO:RGD.
DR   GO; GO:0097190; P:apoptotic signaling pathway; ISO:RGD.
DR   GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR   GO; GO:0034198; P:cellular response to amino acid starvation; ISO:RGD.
DR   GO; GO:0010507; P:negative regulation of autophagy; ISO:RGD.
DR   GO; GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; ISO:RGD.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:RGD.
DR   InterPro; IPR024130; DAP1/DAPL1.
DR   PANTHER; PTHR13177; PTHR13177; 1.
DR   Pfam; PF15228; DAP; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Apoptosis; Autophagy; Phosphoprotein; Reference proteome.
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_0000079784"
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:0000250|UniProtKB:Q91XC8"
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:22673903"
FT   MOD_RES         91
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P51397"
SQ   SEQUENCE   102 AA;  11166 MW;  F7DBC05D845DDC92 CRC64;
     MSSPPEGKLE TKAGHPPAVK VAGIRIVQKH PHTGDGKEKK DKDDQEWEST SPPKPTVYIS
     GVIARGDKDF PPAAAQVAHQ KPHASMDKHV SPRTQHIQQP RK