CDIP1_XENTR
ID CDIP1_XENTR Reviewed; 207 AA.
AC Q5BJ83;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 56.
DE RecName: Full=Cell death-inducing p53-target protein 1;
DE AltName: Full=LITAF-like protein;
GN Name=cdip1;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (MAR-2005) 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; BC091584; AAH91584.1; -; mRNA.
DR RefSeq; NP_001025631.1; NM_001030460.2.
DR AlphaFoldDB; Q5BJ83; -.
DR DNASU; 595019; -.
DR GeneID; 595019; -.
DR KEGG; xtr:595019; -.
DR CTD; 29965; -.
DR Xenbase; XB-GENE-5752851; cdip1.
DR InParanoid; Q5BJ83; -.
DR OrthoDB; 1564782at2759; -.
DR Proteomes; UP000008143; Chromosome 9.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000037174; Expressed in skeletal muscle tissue and 17 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:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IBA:GO_Central.
DR GO; GO:0042771; P:intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator; IBA:GO_Central.
DR GO; GO:0033209; P:tumor necrosis factor-mediated signaling pathway; IBA:GO_Central.
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_0000280340"
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 36..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; 22105 MW; A14399DA9F96FA3E CRC64;
MASDPPPPYP GGPSAPLLEE KQGLPRMEEP RAAPYPQAMP FAPPDCGPPP YDANPGYIAP
NPGFYPPPGP YAPMGYYPPT PGQFQPPYPS QYPSPGAQGT AVIVPPGPSS TSAATTVTST
TTTVTVLQGE IFQGSPVQTV CTNCQQPITT KISHDIGLMN FLLCCFCCFV GCDLGCCLIP
CIINDLKDVT HSCPNCKYHI YTYRRMC