ID CDIP1_HUMAN Reviewed; 208 AA. AC Q9H305; A8K7M1; B4DFU1; B4DY75; D3DUD6; Q96ID8; Q9H0Q4; Q9P112; DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2001, sequence version 1. DT 24-JAN-2024, entry version 155. DE RecName: Full=Cell death-inducing p53-target protein 1; DE AltName: Full=Cell death involved p53-target; DE AltName: Full=Cell death-inducing protein; DE AltName: Full=LITAF-like protein; DE AltName: Full=Lipopolysaccharide-induced tumor necrosis factor-alpha-like protein; DE AltName: Full=Transmembrane protein I1; GN Name=CDIP1; Synonyms=C16orf5, CDIP, LITAFL; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY. RC TISSUE=Brain; RX PubMed=10570909; DOI=10.1007/s100380050183; RA Bhalla K., Eyre H.J., Whitmore S.A., Sutherland G.R., Callen D.F.; RT "C16orf5, a novel proline-rich gene at 16p13.3, is highly expressed in the RT brain."; RL J. Hum. Genet. 44:383-387(1999). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RA Zhou Y., Du G., Wang J., Yuan J., Qiang B.; RT "Cloning a novel human cDNA encoding a novel transmembrane protein."; RL Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INDUCTION, AND FUNCTION. RX PubMed=17599062; DOI=10.1038/sj.emboj.7601779; RA Brown L., Ongusaha P.P., Kim H.G., Nuti S., Mandinova A., Lee J.W., RA Khosravi-Far R., Aaronson S.A., Lee S.W.; RT "CDIP, a novel pro-apoptotic gene, regulates TNFalpha-mediated apoptosis in RT a p53-dependent manner."; RL EMBO J. 26:3410-3422(2007). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Brain; RX PubMed=11230166; DOI=10.1101/gr.gr1547r; RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B., RA Klein M., Poustka A.; RT "Towards a catalog of human genes and proteins: sequencing and analysis of RT 500 novel complete protein coding human cDNAs."; RL Genome Res. 11:422-435(2001). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3). RC TISSUE=Amygdala, Spleen, and Testis; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15616553; DOI=10.1038/nature03187; RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M., RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., RA Myers R.M., Rubin E.M., Pennacchio L.A.; RT "The sequence and analysis of duplication-rich human chromosome 16."; RL Nature 432:988-994(2004). RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Amygdala; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [10] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Eye, and Lung; 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). RN [11] RP SUBCELLULAR LOCATION, AND TOPOLOGY. RX PubMed=27582497; DOI=10.1042/bcj20160657; RA Qin W., Wunderley L., Barrett A.L., High S., Woodman P.G.; RT "The Charcot Marie Tooth disease protein LITAF is a zinc-binding monotopic RT membrane protein."; RL Biochem. J. 473:3965-3978(2016). CC -!- FUNCTION: Acts as an important p53/TP53-apoptotic effector. Regulates CC TNF-alpha-mediated apoptosis in a p53/TP53-dependent manner. CC {ECO:0000269|PubMed:17599062}. CC -!- INTERACTION: CC Q9H305; Q96GG9: DCUN1D1; NbExp=3; IntAct=EBI-2876678, EBI-740086; CC Q9H305; Q6ICB0: DESI1; NbExp=4; IntAct=EBI-2876678, EBI-2806959; CC Q9H305; O95208-2: EPN2; NbExp=3; IntAct=EBI-2876678, EBI-12135243; CC Q9H305; O43561-2: LAT; NbExp=3; IntAct=EBI-2876678, EBI-8070286; CC Q9H305; Q96DC9: OTUB2; NbExp=3; IntAct=EBI-2876678, EBI-746259; CC Q9H305; Q6GQQ9: OTUD7B; NbExp=3; IntAct=EBI-2876678, EBI-527784; CC Q9H305; Q15025: TNIP1; NbExp=4; IntAct=EBI-2876678, EBI-357849; CC Q9H305; Q9H0E2: TOLLIP; NbExp=3; IntAct=EBI-2876678, EBI-74615; CC Q9H305; P0CG47: UBB; NbExp=3; IntAct=EBI-2876678, EBI-413034; CC Q9H305; P0CG48: UBC; NbExp=3; IntAct=EBI-2876678, EBI-3390054; CC Q9H305; Q9UMX0: UBQLN1; NbExp=3; IntAct=EBI-2876678, EBI-741480; CC Q9H305; Q9UHD9: UBQLN2; NbExp=3; IntAct=EBI-2876678, EBI-947187; CC -!- SUBCELLULAR LOCATION: Late endosome membrane CC {ECO:0000269|PubMed:27582497}; Peripheral membrane protein CC {ECO:0000269|PubMed:27582497}; Cytoplasmic side CC {ECO:0000269|PubMed:27582497}. Lysosome membrane CC {ECO:0000269|PubMed:27582497}; Peripheral membrane protein CC {ECO:0000269|PubMed:27582497}; Cytoplasmic side CC {ECO:0000269|PubMed:27582497}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q9H305-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9H305-2; Sequence=VSP_046929; CC Name=3; CC IsoId=Q9H305-3; Sequence=VSP_046928; CC -!- TISSUE SPECIFICITY: Highly expressed in brain. Expressed at lower level CC in heart, skeletal muscle, kidney, pancreas and liver. Weakly or not CC expressed in placenta and lung. {ECO:0000269|PubMed:10570909}. CC -!- INDUCTION: Up-regulated by p53/TP53. {ECO:0000269|PubMed:17599062}. 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 -!- MISCELLANEOUS: [Isoform 2]: May be due to competing acceptor splice CC site. {ECO:0000305}. CC -!- SIMILARITY: Belongs to the CDIP1/LITAF family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAF26619.1; Type=Frameshift; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF131218; AAF26619.1; ALT_FRAME; mRNA. DR EMBL; AF195661; AAG35583.1; -; mRNA. DR EMBL; DQ167023; AAZ94626.1; -; mRNA. DR EMBL; AL136698; CAB66633.1; -; mRNA. DR EMBL; CR533446; CAG38477.1; -; mRNA. DR EMBL; AK292036; BAF84725.1; -; mRNA. DR EMBL; AK294257; BAG57552.1; -; mRNA. DR EMBL; AK302297; BAG63637.1; -; mRNA. DR EMBL; AL833853; CAD38712.1; -; mRNA. DR EMBL; AC007606; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC023830; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471112; EAW85291.1; -; Genomic_DNA. DR EMBL; CH471112; EAW85292.1; -; Genomic_DNA. DR EMBL; CH471112; EAW85293.1; -; Genomic_DNA. DR EMBL; CH471112; EAW85294.1; -; Genomic_DNA. DR EMBL; CH471112; EAW85296.1; -; Genomic_DNA. DR EMBL; BC002882; AAH02882.1; -; mRNA. DR EMBL; BC007604; AAH07604.1; -; mRNA. DR CCDS; CCDS42114.1; -. [Q9H305-1] DR CCDS; CCDS58419.1; -. [Q9H305-2] DR CCDS; CCDS58420.1; -. [Q9H305-3] DR RefSeq; NP_001185983.1; NM_001199054.1. [Q9H305-1] DR RefSeq; NP_001185984.1; NM_001199055.1. [Q9H305-2] DR RefSeq; NP_001185985.1; NM_001199056.1. [Q9H305-3] DR RefSeq; NP_037531.2; NM_013399.2. [Q9H305-1] DR AlphaFoldDB; Q9H305; -. DR BioGRID; 118998; 18. DR IntAct; Q9H305; 18. DR MINT; Q9H305; -. DR STRING; 9606.ENSP00000382508; -. DR iPTMnet; Q9H305; -. DR PhosphoSitePlus; Q9H305; -. DR SwissPalm; Q9H305; -. DR BioMuta; CDIP1; -. DR DMDM; 74733567; -. DR jPOST; Q9H305; -. DR MassIVE; Q9H305; -. DR MaxQB; Q9H305; -. DR PaxDb; 9606-ENSP00000382508; -. DR PeptideAtlas; Q9H305; -. DR ProteomicsDB; 4079; -. DR ProteomicsDB; 5503; -. DR ProteomicsDB; 80639; -. [Q9H305-1] DR Pumba; Q9H305; -. DR Antibodypedia; 24347; 94 antibodies from 21 providers. DR DNASU; 29965; -. DR Ensembl; ENST00000399599.7; ENSP00000382508.2; ENSG00000089486.17. [Q9H305-1] DR Ensembl; ENST00000562334.5; ENSP00000455050.1; ENSG00000089486.17. [Q9H305-3] DR Ensembl; ENST00000563332.6; ENSP00000454994.1; ENSG00000089486.17. [Q9H305-1] DR Ensembl; ENST00000563507.5; ENSP00000455462.1; ENSG00000089486.17. [Q9H305-2] DR Ensembl; ENST00000567695.6; ENSP00000457877.1; ENSG00000089486.17. [Q9H305-1] DR Ensembl; ENST00000611166.2; ENSP00000480842.1; ENSG00000274336.2. [Q9H305-1] DR Ensembl; ENST00000631859.1; ENSP00000488843.1; ENSG00000274336.2. [Q9H305-3] DR Ensembl; ENST00000632680.1; ENSP00000488474.1; ENSG00000274336.2. [Q9H305-1] DR Ensembl; ENST00000632937.1; ENSP00000488066.1; ENSG00000274336.2. [Q9H305-1] DR Ensembl; ENST00000633324.1; ENSP00000487657.1; ENSG00000274336.2. [Q9H305-2] DR GeneID; 29965; -. DR KEGG; hsa:29965; -. DR MANE-Select; ENST00000567695.6; ENSP00000457877.1; NM_013399.3; NP_037531.2. DR UCSC; uc002cwu.4; human. [Q9H305-1] DR AGR; HGNC:13234; -. DR CTD; 29965; -. DR DisGeNET; 29965; -. DR GeneCards; CDIP1; -. DR HGNC; HGNC:13234; CDIP1. DR HPA; ENSG00000089486; Tissue enhanced (brain). DR MIM; 610503; gene. DR neXtProt; NX_Q9H305; -. DR OpenTargets; ENSG00000089486; -. DR PharmGKB; PA134879441; -. DR VEuPathDB; HostDB:ENSG00000089486; -. DR eggNOG; ENOG502S2GM; Eukaryota. DR GeneTree; ENSGT00940000157696; -. DR HOGENOM; CLU_095549_0_0_1; -. DR InParanoid; Q9H305; -. DR OMA; PHAPMGY; -. DR OrthoDB; 1383925at2759; -. DR PhylomeDB; Q9H305; -. DR TreeFam; TF313294; -. DR PathwayCommons; Q9H305; -. DR SignaLink; Q9H305; -. DR BioGRID-ORCS; 29965; 11 hits in 1168 CRISPR screens. DR ChiTaRS; CDIP1; human. DR GenomeRNAi; 29965; -. DR Pharos; Q9H305; Tbio. DR PRO; PR:Q9H305; -. DR Proteomes; UP000005640; Chromosome 16. DR RNAct; Q9H305; Protein. DR Bgee; ENSG00000089486; Expressed in prefrontal cortex and 99 other cell types or tissues. DR ExpressionAtlas; Q9H305; baseline and differential. DR GO; GO:0098560; C:cytoplasmic side of late endosome membrane; IDA:UniProtKB. DR GO; GO:0098574; C:cytoplasmic side of lysosomal membrane; IDA:UniProtKB. DR GO; GO:0005634; C:nucleus; IDA:MGI. 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; IMP:MGI. DR InterPro; IPR006629; LITAF. DR InterPro; IPR037519; LITAF_fam. DR PANTHER; PTHR23292:SF7; CELL DEATH-INDUCING P53-TARGET PROTEIN 1; 1. DR PANTHER; PTHR23292; LIPOPOLYSACCHARIDE-INDUCED TUMOR NECROSIS FACTOR-ALPHA FACTOR; 1. DR Pfam; PF10601; zf-LITAF-like; 1. DR SMART; SM00714; LITAF; 1. DR PROSITE; PS51837; LITAF; 1. DR Genevisible; Q9H305; HS. PE 1: Evidence at protein 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_0000280336" FT DOMAIN 122..206 FT /note="LITAF" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01181" FT REGION 1..71 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..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" FT VAR_SEQ 42..120 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_046928" FT VAR_SEQ 82..120 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_046929" FT CONFLICT 150 FT /note="T -> A (in Ref. 4; CAB66633 and 5; CAG38477)" FT /evidence="ECO:0000305" SQ SEQUENCE 208 AA; 21892 MW; 6C7334668A3C15A7 CRC64; MSSEPPPPYP GGPTAPLLEE KSGAPPTPGR SSPAVMQPPP GMPLPPADIG PPPYEPPGHP MPQPGFIPPH MSADGTYMPP GFYPPPGPHP PMGYYPPGPY TPGPYPGPGG HTATVLVPSG AATTVTVLQG EIFEGAPVQT VCPHCQQAIT TKISYEIGLM NFVLGFFCCF MGCDLGCCLI PCLINDFKDV THTCPSCKAY IYTYKRLC //