CDIP1_MOUSE
ID CDIP1_MOUSE Reviewed; 208 AA.
AC Q9DB75; Q3UD73; Q9CYP1;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Cell death-inducing p53-target protein 1;
DE AltName: Full=LITAF-like protein;
GN Name=Cdip1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J;
RC TISSUE=Bone marrow, Cerebellum, Lung, Spinal ganglion, and Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=Czech II; TISSUE=Mammary tumor;
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).
CC -!- FUNCTION: Acts as an important p53/TP53-apoptotic effector. Regulates
CC TNF-alpha-mediated apoptosis in a p53/TP53-dependent manner (By
CC similarity). {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=Q9DB75-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9DB75-2; Sequence=VSP_023632;
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; AK005157; BAB23848.1; -; mRNA.
DR EMBL; AK017480; BAB30764.1; -; mRNA.
DR EMBL; AK031705; BAC27523.1; -; mRNA.
DR EMBL; AK051560; BAC34673.1; -; mRNA.
DR EMBL; AK149939; BAE29181.1; -; mRNA.
DR EMBL; AK150219; BAE29388.1; -; mRNA.
DR EMBL; AK166141; BAE38594.1; -; mRNA.
DR EMBL; BC004063; AAH04063.1; -; mRNA.
DR CCDS; CCDS27925.1; -. [Q9DB75-1]
DR CCDS; CCDS88867.1; -. [Q9DB75-2]
DR RefSeq; NP_079946.2; NM_025670.4. [Q9DB75-1]
DR RefSeq; XP_006522530.1; XM_006522467.1.
DR RefSeq; XP_006522531.1; XM_006522468.1. [Q9DB75-1]
DR RefSeq; XP_011244298.1; XM_011245996.2.
DR AlphaFoldDB; Q9DB75; -.
DR IntAct; Q9DB75; 1.
DR STRING; 10090.ENSMUSP00000004173; -.
DR iPTMnet; Q9DB75; -.
DR PhosphoSitePlus; Q9DB75; -.
DR MaxQB; Q9DB75; -.
DR PaxDb; Q9DB75; -.
DR PeptideAtlas; Q9DB75; -.
DR PRIDE; Q9DB75; -.
DR ProteomicsDB; 281284; -. [Q9DB75-1]
DR ProteomicsDB; 281285; -. [Q9DB75-2]
DR Antibodypedia; 24347; 78 antibodies from 21 providers.
DR DNASU; 66626; -.
DR Ensembl; ENSMUST00000004173; ENSMUSP00000004173; ENSMUSG00000004071. [Q9DB75-1]
DR Ensembl; ENSMUST00000117713; ENSMUSP00000113618; ENSMUSG00000004071. [Q9DB75-2]
DR Ensembl; ENSMUST00000118703; ENSMUSP00000113889; ENSMUSG00000004071. [Q9DB75-1]
DR GeneID; 66626; -.
DR KEGG; mmu:66626; -.
DR UCSC; uc007yaj.1; mouse. [Q9DB75-1]
DR UCSC; uc012aau.1; mouse. [Q9DB75-2]
DR CTD; 29965; -.
DR MGI; MGI:1913876; Cdip1.
DR VEuPathDB; HostDB:ENSMUSG00000004071; -.
DR eggNOG; ENOG502S2GM; Eukaryota.
DR GeneTree; ENSGT00940000157696; -.
DR HOGENOM; CLU_095549_0_0_1; -.
DR InParanoid; Q9DB75; -.
DR OMA; THEIGLM; -.
DR OrthoDB; 1564782at2759; -.
DR PhylomeDB; Q9DB75; -.
DR TreeFam; TF313294; -.
DR BioGRID-ORCS; 66626; 2 hits in 71 CRISPR screens.
DR ChiTaRS; Cdip1; mouse.
DR PRO; PR:Q9DB75; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q9DB75; protein.
DR Bgee; ENSMUSG00000004071; Expressed in dentate gyrus of hippocampal formation granule cell and 261 other tissues.
DR ExpressionAtlas; Q9DB75; baseline and differential.
DR Genevisible; Q9DB75; MM.
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; ISO:MGI.
DR GO; GO:0008270; F:zinc ion binding; IBA:GO_Central.
DR GO; GO:0006915; P:apoptotic process; ISO:MGI.
DR GO; GO:0042771; P:intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator; ISO:MGI.
DR GO; GO:0033209; P:tumor necrosis factor-mediated signaling pathway; ISO:MGI.
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_0000280337"
FT DOMAIN 122..206
FT /note="LITAF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01181"
FT REGION 1..70
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 32..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 81..97
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_023632"
FT CONFLICT 70
FT /note="H -> R (in Ref. 1; BAE29388)"
FT /evidence="ECO:0000305"
FT CONFLICT 180
FT /note="I -> V (in Ref. 1; BAB30764)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 208 AA; 21835 MW; DC1A9A7C17EC0B90 CRC64;
MSNEPPPPYP GGPTAPLLEE KSGAPLTPGR TSPAVMQPPP GMPLPSADIA PPPYEPPGQP
VPQPGFVPPH MNADGTYMPA GFYPPPGPHP PMGYYPPGPY PPGPYPGPGG HTATVLVPSG
AATTVTVLQG EIFEGAPVQT VCPHCQQAIT TKISYEIGLM NFVLGFFCCF MGCDLGCCLI
PCLINDFKDV THTCPSCKAY ICTYKRLC
