ID   CDIP1_RAT               Reviewed;         208 AA.
AC   Q5U2U6;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Cell death-inducing p53-target protein 1;
DE   AltName: Full=LITAF-like protein;
GN   Name=Cdip1;
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 MRNA].
RC   TISSUE=Heart;
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: Acts as an important p53/TP53-apoptotic effector. Regulates
CC       TNF-alpha-mediated apoptosis in a p53/TP53-dependent manner.
CC       {ECO:0000250|UniProtKB:Q9H305}.
CC   -!- SUBCELLULAR LOCATION: Late endosome membrane
CC       {ECO:0000250|UniProtKB:Q9H305}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:Q9H305}; Cytoplasmic side
CC       {ECO:0000250|UniProtKB:Q9H305}. Lysosome membrane
CC       {ECO:0000250|UniProtKB:Q9H305}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:Q9H305}; Cytoplasmic side
CC       {ECO:0000250|UniProtKB:Q9H305}.
CC   -!- DOMAIN: The LITAF domain is stabilized by a bound zinc ion. The LITAF
CC       domain contains an amphipathic helix that mediates interaction with
CC       lipid membranes. {ECO:0000250|UniProtKB:Q99732}.
CC   -!- SIMILARITY: Belongs to the CDIP1/LITAF family. {ECO:0000305}.
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DR   EMBL; BC085860; AAH85860.1; -; mRNA.
DR   RefSeq; NP_001008361.1; NM_001008360.1.
DR   RefSeq; XP_006245873.1; XM_006245811.3.
DR   RefSeq; XP_006245874.1; XM_006245812.3.
DR   RefSeq; XP_006245875.1; XM_006245813.3.
DR   RefSeq; XP_006245876.1; XM_006245814.3.
DR   RefSeq; XP_006245877.1; XM_006245815.3.
DR   RefSeq; XP_006245878.1; XM_006245816.2.
DR   AlphaFoldDB; Q5U2U6; -.
DR   BioGRID; 261967; 1.
DR   STRING; 10116.ENSRNOP00000004999; -.
DR   PhosphoSitePlus; Q5U2U6; -.
DR   PaxDb; Q5U2U6; -.
DR   PRIDE; Q5U2U6; -.
DR   Ensembl; ENSRNOT00000004999; ENSRNOP00000004999; ENSRNOG00000003328.
DR   GeneID; 360480; -.
DR   KEGG; rno:360480; -.
DR   UCSC; RGD:1310686; rat.
DR   CTD; 29965; -.
DR   RGD; 1310686; Cdip1.
DR   eggNOG; ENOG502S2GM; Eukaryota.
DR   GeneTree; ENSGT00940000157696; -.
DR   HOGENOM; CLU_095549_0_0_1; -.
DR   InParanoid; Q5U2U6; -.
DR   OMA; THEIGLM; -.
DR   OrthoDB; 1564782at2759; -.
DR   PhylomeDB; Q5U2U6; -.
DR   TreeFam; TF313294; -.
DR   PRO; PR:Q5U2U6; -.
DR   Proteomes; UP000002494; Chromosome 10.
DR   Bgee; ENSRNOG00000003328; Expressed in Ammon's horn and 19 other tissues.
DR   Genevisible; Q5U2U6; RN.
DR   GO; GO:0098560; C:cytoplasmic side of late endosome membrane; ISS:UniProtKB.
DR   GO; GO:0098574; C:cytoplasmic side of lysosomal membrane; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISO:RGD.
DR   GO; GO:0008270; F:zinc ion binding; IBA:GO_Central.
DR   GO; GO:0006915; P:apoptotic process; ISO:RGD.
DR   GO; GO:0042771; P:intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator; ISO:RGD.
DR   GO; GO:0033209; P:tumor necrosis factor-mediated signaling pathway; ISO:RGD.
DR   InterPro; IPR006629; LITAF.
DR   InterPro; IPR037519; LITAF_fam.
DR   PANTHER; PTHR23292; PTHR23292; 1.
DR   Pfam; PF10601; zf-LITAF-like; 1.
DR   SMART; SM00714; LITAF; 1.
DR   PROSITE; PS51837; LITAF; 1.
PE   2: Evidence at transcript level;
KW   Apoptosis; Endosome; Lysosome; Membrane; Metal-binding; Reference proteome;
KW   Zinc.
FT   CHAIN           1..208
FT                   /note="Cell death-inducing p53-target protein 1"
FT                   /id="PRO_0000280338"
FT   DOMAIN          122..206
FT                   /note="LITAF"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01181"
FT   REGION          1..70
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          164..184
FT                   /note="Membrane-binding amphipathic helix"
FT                   /evidence="ECO:0000305"
FT   COMPBIAS        32..67
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         142
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:Q99732"
FT   BINDING         145
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:Q99732"
FT   BINDING         194
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:Q99732"
FT   BINDING         197
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:Q99732"
SQ   SEQUENCE   208 AA;  21858 MW;  7CA564534957DEDF CRC64;
     MSNEPPPPYP GGPTAPLLEE KSGAPHTPGR TSPAVMQPPP GMPLPSADIA PPPYEPPGHP
     VPQPGFVPPH MNADGTYMPA GFYPPPGPHP PMGYYPPGPY PPGSYPGPGG HTATVLVPSG
     AATTVTVLQG EIFEGAPVQT VCPHCQQAIT TKISYEIGLM NFVLGFFCCF MGCDLGCCLI
     PCLINDFKDV THTCPSCKAY ICTYKRLC