ID   CDIP1_DICDI             Reviewed;         181 AA.
AC   Q54HX8;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=Cell death-inducing p53-target protein 1 homolog;
DE   AltName: Full=Protein LITAF homolog;
GN   Name=litaf; ORFNames=DDB_G0289149;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
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; AAFI02000130; EAL62882.1; -; Genomic_DNA.
DR   RefSeq; XP_636385.1; XM_631293.1.
DR   AlphaFoldDB; Q54HX8; -.
DR   PaxDb; Q54HX8; -.
DR   EnsemblProtists; EAL62882; EAL62882; DDB_G0289149.
DR   GeneID; 8626986; -.
DR   KEGG; ddi:DDB_G0289149; -.
DR   dictyBase; DDB_G0289149; litaf.
DR   eggNOG; ENOG502RSPP; Eukaryota.
DR   HOGENOM; CLU_1386668_0_0_1; -.
DR   InParanoid; Q54HX8; -.
DR   OMA; FCVDSCM; -.
DR   PRO; PR:Q54HX8; -.
DR   Proteomes; UP000002195; Chromosome 5.
DR   GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008270; F:zinc ion binding; IBA:GO_Central.
DR   GO; GO:0009617; P:response to bacterium; HEP:dictyBase.
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   3: Inferred from homology;
KW   Endosome; Lysosome; Membrane; Metal-binding; Reference proteome; Zinc.
FT   CHAIN           1..181
FT                   /note="Cell death-inducing p53-target protein 1 homolog"
FT                   /id="PRO_0000328224"
FT   DOMAIN          90..177
FT                   /note="LITAF"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01181"
FT   REGION          1..82
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          131..151
FT                   /note="Membrane-binding amphipathic helix"
FT                   /evidence="ECO:0000305"
FT   COMPBIAS        1..33
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        34..80
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         113
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:Q99732"
FT   BINDING         116
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:Q99732"
FT   BINDING         165
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:Q99732"
FT   BINDING         168
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:Q99732"
SQ   SEQUENCE   181 AA;  20589 MW;  70CB105AE11811FE CRC64;
     MGQDNINLNK VDGQPSSPPQ EQQQQQQYPP QGYPQQQQYP PQQGYPPQQY PPQQGYPPQQ
     YPPQQGYPQQ QPPQQYPAPV GAPQQPYMAT QQVVVQQVYV QPTFGVVPVD CICQHCQTRM
     STKTSYKSGS MVWLVCVLLI IFGCWLGCCL IPFGIDSLKD VQHKCSHCKK VLYRFDRMSG
     K