CDIP1_BOVIN
ID CDIP1_BOVIN Reviewed; 208 AA.
AC Q58D45; Q3T0R0;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Cell death-inducing p53-target protein 1;
DE AltName: Full=LITAF-like protein;
GN Name=CDIP1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q58D45-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q58D45-2; Sequence=VSP_023631;
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; BT021752; AAX46599.1; -; mRNA.
DR EMBL; BC102294; AAI02295.1; -; mRNA.
DR RefSeq; NP_001014892.1; NM_001014892.1. [Q58D45-1]
DR RefSeq; XP_005224477.1; XM_005224420.2. [Q58D45-1]
DR AlphaFoldDB; Q58D45; -.
DR STRING; 9913.ENSBTAP00000037343; -.
DR PaxDb; Q58D45; -.
DR Ensembl; ENSBTAT00000037513; ENSBTAP00000037343; ENSBTAG00000018938. [Q58D45-2]
DR Ensembl; ENSBTAT00000079049; ENSBTAP00000060751; ENSBTAG00000018938. [Q58D45-1]
DR GeneID; 510242; -.
DR KEGG; bta:510242; -.
DR CTD; 29965; -.
DR VEuPathDB; HostDB:ENSBTAG00000018938; -.
DR eggNOG; ENOG502S2GM; Eukaryota.
DR GeneTree; ENSGT00940000157696; -.
DR HOGENOM; CLU_095549_0_0_1; -.
DR InParanoid; Q58D45; -.
DR OMA; THEIGLM; -.
DR TreeFam; TF313294; -.
DR Proteomes; UP000009136; Chromosome 25.
DR Bgee; ENSBTAG00000018938; Expressed in temporal cortex and 104 other tissues.
DR ExpressionAtlas; Q58D45; baseline and differential.
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 Alternative splicing; Apoptosis; Endosome; Lysosome; Membrane;
KW Metal-binding; Reference proteome; Zinc.
FT CHAIN 1..208
FT /note="Cell death-inducing p53-target protein 1"
FT /id="PRO_0000280335"
FT DOMAIN 122..206
FT /note="LITAF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01181"
FT REGION 1..65
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 31..65
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"
FT VAR_SEQ 173..208
FT /note="CDLGCCLIPCLINDFKDVTHTCPSCKAYIYTYKRLC -> PPSLLMQV (in
FT isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_023631"
SQ SEQUENCE 208 AA; 21864 MW; 0DB9C951738B8B68 CRC64;
MSNDPPPPYP GGPTAPLLEE KSGAPPTPGR TSPAVMQPPP GMSLPPADIG PPPYEPPGHP
MPQPGFIPPH VNADGTYMPS GFYPPPGPHP PMGYYPPGPY PPGPYAGPGG HTATVLVPSG
AATTVTVLQG EIFEGAPVQT VCPHCQQAIT TKISYEIGLM NFVLGFFCCF MGCDLGCCLI
PCLINDFKDV THTCPSCKAY IYTYKRLC
