ID   CDIP1_XENLA             Reviewed;         207 AA.
AC   Q8AVW3;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 50.
DE   RecName: Full=Cell death-inducing p53-target protein 1;
DE   AltName: Full=LITAF-like protein;
GN   Name=cdip1;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: May act as a p53/TP53-apoptotic effector.
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; BC041237; AAH41237.1; -; mRNA.
DR   RefSeq; NP_001079379.1; NM_001085910.1.
DR   AlphaFoldDB; Q8AVW3; -.
DR   DNASU; 379066; -.
DR   GeneID; 379066; -.
DR   KEGG; xla:379066; -.
DR   CTD; 379066; -.
DR   Xenbase; XB-GENE-5752923; cdip1.L.
DR   OrthoDB; 1564782at2759; -.
DR   Proteomes; UP000186698; Chromosome 9_10L.
DR   Bgee; 379066; Expressed in muscle tissue and 19 other tissues.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
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..207
FT                   /note="Cell death-inducing p53-target protein 1"
FT                   /id="PRO_0000280339"
FT   DOMAIN          121..205
FT                   /note="LITAF"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01181"
FT   REGION          1..54
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          161..183
FT                   /note="Membrane-binding amphipathic helix"
FT                   /evidence="ECO:0000305"
FT   COMPBIAS        29..54
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         141
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:Q99732"
FT   BINDING         144
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:Q99732"
FT   BINDING         193
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:Q99732"
FT   BINDING         196
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:Q99732"
SQ   SEQUENCE   207 AA;  22106 MW;  55238D6D578AC84F CRC64;
     MASDPPPPYP GGPSAPLLED KHGAPRMEEP RPAPYPQAMA FAPPDCGPPP YDANPGYIAP
     NPGFYPPPGP YVPMGYYPPS PSQFQPPYPS QYSSPGAQGT AVILPPGPTS TSGTTTVTSN
     TTTVTVLHGE IFQGSPVQTV CQHCQQPITT KISHEIGLMN FLLCCFCCFV GCDLGCCLIP
     CIINDLKDVT HTCPNCKAVI YTYRRMC