ID CIDEB_HUMAN Reviewed; 219 AA. AC Q9UHD4; D3DS73; Q546V8; Q9NNW9; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 27-MAR-2002, sequence version 2. DT 24-JAN-2024, entry version 180. DE RecName: Full=Lipid transferase CIDEB {ECO:0000305}; DE AltName: Full=Cell death activator CIDE-B {ECO:0000303|PubMed:10619428}; DE AltName: Full=Cell death-inducing DFFA-like effector B {ECO:0000303|PubMed:10619428}; GN Name=CIDEB {ECO:0000303|PubMed:35939579, ECO:0000312|HGNC:HGNC:1977}; 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], STRUCTURE BY NMR OF 1-116, FUNCTION, AND RP INTERACTION WITH DFFA AND DFFB. RX PubMed=10619428; DOI=10.1016/s0092-8674(00)81672-4; RA Lugovskoy A.A., Zhou P., Chou J.J., McCarty J.S., Li P., Wagner G.; RT "Solution structure of the CIDE-N domain of CIDE-B and a model for CIDE- RT N/CIDE-N interactions in the DNA fragmentation pathway of apoptosis."; RL Cell 99:747-755(1999). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=9564035; DOI=10.1093/emboj/17.9.2526; RA Inohara N., Koseki T., Chen S., Wu X., Nunez G.; RT "CIDE, a novel family of cell death activators with homology to the 45 kDa RT subunit of the DNA fragmentation factor."; RL EMBO J. 17:2526-2533(1998). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Liver; RA Liang L., Zhao M., Li T.; RL Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Ileal mucosa; 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 [5] 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 [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Liver; 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 [7] RP TISSUE SPECIFICITY. RX PubMed=12429024; DOI=10.1042/bj20020656; RA Liang L., Zhao M., Xu Z., Yokoyama K.K., Li T.; RT "Molecular cloning and characterization of CIDE-3, a novel member of the RT cell-death-inducing DNA-fragmentation-factor (DFF45)-like effector RT family."; RL Biochem. J. 370:195-203(2003). RN [8] RP INTERACTION WITH HCV NON-STRUCTURAL PROTEIN 5A (MICROBIAL INFECTION), AND RP FUNCTION (MICROBIAL INFECTION). RX PubMed=27282740; DOI=10.1038/srep27778; RA Cai H., Yao W., Li L., Li X., Hu L., Mai R., Peng T.; RT "Cell-death-inducing DFFA-like Effector B Contributes to the Assembly of RT Hepatitis C Virus (HCV) Particles and Interacts with HCV NS5A."; RL Sci. Rep. 6:27778-27778(2016). RN [9] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=35939579; DOI=10.1056/nejmoa2117872; RA Verweij N., Haas M.E., Nielsen J.B., Sosina O.A., Kim M., Akbari P., De T., RA Hindy G., Bovijn J., Persaud T., Miloscio L., Germino M., Panagis L., RA Watanabe K., Mbatchou J., Jones M., LeBlanc M., Balasubramanian S., RA Lammert C., Enhoerning S., Melander O., Carey D.J., Still C.D., RA Mirshahi T., Rader D.J., Parasoglou P., Walls J.R., Overton J.D., RA Reid J.G., Economides A., Cantor M.N., Zambrowicz B., Murphy A.J., RA Abecasis G.R., Ferreira M.A.R., Smagris E., Gusarova V., Sleeman M., RA Yancopoulos G.D., Marchini J., Kang H.M., Karalis K., Shuldiner A.R., RA Della Gatta G., Locke A.E., Baras A., Lotta L.A.; RT "Germline Mutations in CIDEB and Protection against Liver Disease."; RL N. Engl. J. Med. 387:332-344(2022). CC -!- FUNCTION: Lipid transferase specifically expressed in hepatocytes, CC which promotes unilocular lipid droplet formation by mediating lipid CC droplet fusion (PubMed:35939579). Lipid droplet fusion promotes their CC enlargement, restricting lipolysis and favoring lipid storage CC (PubMed:35939579). Localizes on the lipid droplet surface, at focal CC contact sites between lipid droplets, and mediates atypical lipid CC droplet fusion by promoting directional net neutral lipid transfer from CC the smaller to larger lipid droplets (By similarity). The transfer CC direction may be driven by the internal pressure difference between the CC contacting lipid droplet pair (By similarity). Promotes lipid exchange CC and lipid droplet fusion in both small and large lipid droplet- CC containing hepatocytes (By similarity). In addition to its role in CC lipid droplet fusion, also involved in cytoplasmic vesicle biogenesis CC and transport (By similarity). Required for very-low-density CC lipoprotein (VLDL) lipidation and maturation (By similarity). Probably CC involved in the biogenesis of VLDL transport vesicles by forming a CC COPII vesicle coat and facilitating the formation of endoplasmic CC reticulum-derived large vesicles (By similarity). Also involved in CC sterol-regulated export of the SCAP-SREBP complex, composed of SCAP, CC SREBF1/SREBP1 and SREBF2/SREBP2, by promoting loading of SCAP-SREBP CC into COPII vesicles (By similarity). May also activate apoptosis CC (PubMed:10619428). {ECO:0000250|UniProtKB:O70303, CC ECO:0000250|UniProtKB:P56198, ECO:0000269|PubMed:10619428, CC ECO:0000269|PubMed:35939579}. CC -!- FUNCTION: (Microbial infection) Involved in Hepatatis C virus (HCV) CC assembly and required for HCV entry into hepatocytes. CC {ECO:0000269|PubMed:27282740}. CC -!- SUBUNIT: Interacts with DFFA (PubMed:10619428). Interacts with DFFB; CC inhibited by DFFB (PubMed:10619428). Interacts with APOB. Interacts CC with PREB/SEC12; facilitating loading of SCAP-SREBP into COPII vesicles CC (By similarity). {ECO:0000250|UniProtKB:O70303, CC ECO:0000269|PubMed:10619428}. CC -!- SUBUNIT: (Microbial infection) Interacts (via N-terminus) with HCV non- CC structural protein 5A (via N-terminus); this interaction seems to CC regulate the association of HCV particles with ApoE. CC {ECO:0000269|PubMed:27282740}. CC -!- INTERACTION: CC Q9UHD4; O95870: ABHD16A; NbExp=3; IntAct=EBI-7062247, EBI-348517; CC Q9UHD4; Q8WV93: AFG1L; NbExp=3; IntAct=EBI-7062247, EBI-2865743; CC Q9UHD4; P02654: APOC1; NbExp=3; IntAct=EBI-7062247, EBI-1220105; CC Q9UHD4; Q9NVJ2: ARL8B; NbExp=3; IntAct=EBI-7062247, EBI-718376; CC Q9UHD4; P56385: ATP5ME; NbExp=3; IntAct=EBI-7062247, EBI-2270000; CC Q9UHD4; P56378-2: ATP5MPL; NbExp=3; IntAct=EBI-7062247, EBI-17870477; CC Q9UHD4; Q92843: BCL2L2; NbExp=3; IntAct=EBI-7062247, EBI-707714; CC Q9UHD4; O75155: CAND2; NbExp=3; IntAct=EBI-7062247, EBI-5656182; CC Q9UHD4; Q9UHD4: CIDEB; NbExp=7; IntAct=EBI-7062247, EBI-7062247; CC Q9UHD4; P35523: CLCN1; NbExp=3; IntAct=EBI-7062247, EBI-10206780; CC Q9UHD4; P30085-3: CMPK1; NbExp=3; IntAct=EBI-7062247, EBI-23373346; CC Q9UHD4; Q03692: COL10A1; NbExp=3; IntAct=EBI-7062247, EBI-2528309; CC Q9UHD4; P27658: COL8A1; NbExp=3; IntAct=EBI-7062247, EBI-747133; CC Q9UHD4; P15954: COX7C; NbExp=3; IntAct=EBI-7062247, EBI-2606678; CC Q9UHD4; Q8N5I4: DHRSX; NbExp=3; IntAct=EBI-7062247, EBI-3923585; CC Q9UHD4; Q96EY1: DNAJA3; NbExp=3; IntAct=EBI-7062247, EBI-356767; CC Q9UHD4; Q96MZ4: FAM218A; NbExp=3; IntAct=EBI-7062247, EBI-10291578; CC Q9UHD4; Q14318: FKBP8; NbExp=3; IntAct=EBI-7062247, EBI-724839; CC Q9UHD4; Q6VB84: FOXD4L3; NbExp=3; IntAct=EBI-7062247, EBI-11961494; CC Q9UHD4; Q9BWH2: FUNDC2; NbExp=3; IntAct=EBI-7062247, EBI-714482; CC Q9UHD4; P23434: GCSH; NbExp=3; IntAct=EBI-7062247, EBI-715444; CC Q9UHD4; P16520-2: GNB3; NbExp=3; IntAct=EBI-7062247, EBI-17871073; CC Q9UHD4; Q9HCL2: GPAM; NbExp=3; IntAct=EBI-7062247, EBI-7600236; CC Q9UHD4; Q99525: H4C7; NbExp=3; IntAct=EBI-7062247, EBI-10294329; CC Q9UHD4; Q9GZV7: HAPLN2; NbExp=3; IntAct=EBI-7062247, EBI-11956675; CC Q9UHD4; P53701: HCCS; NbExp=3; IntAct=EBI-7062247, EBI-10763431; CC Q9UHD4; A8MV81: HIGD1C; NbExp=3; IntAct=EBI-7062247, EBI-12809676; CC Q9UHD4; P42858: HTT; NbExp=3; IntAct=EBI-7062247, EBI-466029; CC Q9UHD4; Q86SI9: IRX2-DT; NbExp=3; IntAct=EBI-7062247, EBI-17872065; CC Q9UHD4; P13473-2: LAMP2; NbExp=3; IntAct=EBI-7062247, EBI-21591415; CC Q9UHD4; Q5EB52: MEST; NbExp=3; IntAct=EBI-7062247, EBI-1050204; CC Q9UHD4; Q5TGZ0: MICOS10; NbExp=3; IntAct=EBI-7062247, EBI-12886442; CC Q9UHD4; O95563: MPC2; NbExp=3; IntAct=EBI-7062247, EBI-719403; CC Q9UHD4; Q9P0J6: MRPL36; NbExp=3; IntAct=EBI-7062247, EBI-2115401; CC Q9UHD4; Q9BQC6: MRPL57; NbExp=3; IntAct=EBI-7062247, EBI-1055359; CC Q9UHD4; Q7Z6M4: MTERF4; NbExp=3; IntAct=EBI-7062247, EBI-948435; CC Q9UHD4; Q9Y3Q0: NAALAD2; NbExp=3; IntAct=EBI-7062247, EBI-2863682; CC Q9UHD4; Q9ULP0-2: NDRG4; NbExp=3; IntAct=EBI-7062247, EBI-11978907; CC Q9UHD4; Q9UMS0: NFU1; NbExp=3; IntAct=EBI-7062247, EBI-725252; CC Q9UHD4; O00746: NME4; NbExp=3; IntAct=EBI-7062247, EBI-744871; CC Q9UHD4; Q96AL5: PBX3; NbExp=3; IntAct=EBI-7062247, EBI-741171; CC Q9UHD4; O00330: PDHX; NbExp=3; IntAct=EBI-7062247, EBI-751566; CC Q9UHD4; Q96LB9: PGLYRP3; NbExp=3; IntAct=EBI-7062247, EBI-12339509; CC Q9UHD4; Q9UG56-2: PISD; NbExp=3; IntAct=EBI-7062247, EBI-17870882; CC Q9UHD4; P30405: PPIF; NbExp=3; IntAct=EBI-7062247, EBI-5544229; CC Q9UHD4; O60895: RAMP2; NbExp=3; IntAct=EBI-7062247, EBI-9009040; CC Q9UHD4; Q6NTF9-3: RHBDD2; NbExp=3; IntAct=EBI-7062247, EBI-17589229; CC Q9UHD4; P60602: ROMO1; NbExp=3; IntAct=EBI-7062247, EBI-11909831; CC Q9UHD4; Q14D33: RTP5; NbExp=3; IntAct=EBI-7062247, EBI-10217913; CC Q9UHD4; P0DJI9: SAA2; NbExp=3; IntAct=EBI-7062247, EBI-6677144; CC Q9UHD4; P35542: SAA4; NbExp=3; IntAct=EBI-7062247, EBI-750242; CC Q9UHD4; Q9Y6B6: SAR1B; NbExp=3; IntAct=EBI-7062247, EBI-4290665; CC Q9UHD4; O75880: SCO1; NbExp=3; IntAct=EBI-7062247, EBI-6656171; CC Q9UHD4; O43819: SCO2; NbExp=3; IntAct=EBI-7062247, EBI-357012; CC Q9UHD4; A6NFY7: SDHAF1; NbExp=3; IntAct=EBI-7062247, EBI-12011488; CC Q9UHD4; Q9H9B4: SFXN1; NbExp=3; IntAct=EBI-7062247, EBI-355861; CC Q9UHD4; Q9Y371: SH3GLB1; NbExp=3; IntAct=EBI-7062247, EBI-2623095; CC Q9UHD4; Q92922: SMARCC1; NbExp=3; IntAct=EBI-7062247, EBI-355653; CC Q9UHD4; Q9NZD8: SPG21; NbExp=3; IntAct=EBI-7062247, EBI-742688; CC Q9UHD4; Q9UL54: TAOK2; NbExp=3; IntAct=EBI-7062247, EBI-352832; CC Q9UHD4; Q13207: TBX2; NbExp=3; IntAct=EBI-7062247, EBI-2853051; CC Q9UHD4; Q53QW1: TEX44; NbExp=5; IntAct=EBI-7062247, EBI-10278496; CC Q9UHD4; P07204: THBD; NbExp=3; IntAct=EBI-7062247, EBI-941422; CC Q9UHD4; O60830: TIMM17B; NbExp=5; IntAct=EBI-7062247, EBI-2372529; CC Q9UHD4; Q9NUH8: TMEM14B; NbExp=3; IntAct=EBI-7062247, EBI-8638294; CC Q9UHD4; Q6ZUI0: TPRG1; NbExp=3; IntAct=EBI-7062247, EBI-17249488; CC Q9UHD4; Q2NL82: TSR1; NbExp=3; IntAct=EBI-7062247, EBI-358058; CC Q9UHD4; Q6NVU6: UFSP1; NbExp=3; IntAct=EBI-7062247, EBI-12068150; CC Q9UHD4; PRO_0000037572 [P27958]; Xeno; NbExp=6; IntAct=EBI-7062247, EBI-6919131; CC -!- SUBCELLULAR LOCATION: Lipid droplet {ECO:0000269|PubMed:35939579}. CC Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:O70303}; CC Peripheral membrane protein {ECO:0000250|UniProtKB:O70303}; Cytoplasmic CC side {ECO:0000250|UniProtKB:O70303}. Golgi apparatus CC {ECO:0000250|UniProtKB:O70303}. Cytoplasmic vesicle, COPI-coated CC vesicle {ECO:0000250|UniProtKB:O70303}. Note=Enriched at lipid droplet CC contact sites. {ECO:0000250|UniProtKB:O70303}. CC -!- TISSUE SPECIFICITY: Highly expressed in liver and small intestine and, CC at lower levels, in colon, kidney and spleen. CC {ECO:0000269|PubMed:12429024}. CC -!- SIMILARITY: Belongs to the CIDE family. {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; AF190901; AAF23324.1; -; mRNA. DR EMBL; AF218586; AAF27658.1; -; mRNA. DR EMBL; AF544398; AAN37907.1; -; mRNA. DR EMBL; AK000387; BAA91132.1; -; mRNA. DR EMBL; CH471078; EAW66031.1; -; Genomic_DNA. DR EMBL; CH471078; EAW66032.1; -; Genomic_DNA. DR EMBL; CH471078; EAW66033.1; -; Genomic_DNA. DR EMBL; BC035970; AAH35970.1; -; mRNA. DR CCDS; CCDS32056.1; -. DR RefSeq; NP_001305736.1; NM_001318807.1. DR RefSeq; NP_055245.2; NM_014430.2. DR RefSeq; XP_011534961.1; XM_011536659.2. DR RefSeq; XP_016876710.1; XM_017021221.1. DR PDB; 1D4B; NMR; -; A=1-116. DR PDBsum; 1D4B; -. DR AlphaFoldDB; Q9UHD4; -. DR BMRB; Q9UHD4; -. DR SMR; Q9UHD4; -. DR BioGRID; 118027; 78. DR IntAct; Q9UHD4; 69. DR STRING; 9606.ENSP00000337731; -. DR iPTMnet; Q9UHD4; -. DR PhosphoSitePlus; Q9UHD4; -. DR BioMuta; CIDEB; -. DR DMDM; 20141283; -. DR MassIVE; Q9UHD4; -. DR PaxDb; 9606-ENSP00000337731; -. DR PeptideAtlas; Q9UHD4; -. DR ProteomicsDB; 84324; -. DR Antibodypedia; 9150; 385 antibodies from 35 providers. DR DNASU; 27141; -. DR Ensembl; ENST00000258807.5; ENSP00000258807.5; ENSG00000136305.12. DR Ensembl; ENST00000336557.9; ENSP00000337731.5; ENSG00000136305.12. DR Ensembl; ENST00000554411.6; ENSP00000451089.1; ENSG00000136305.12. DR Ensembl; ENST00000642223.1; ENSP00000493738.1; ENSG00000285199.1. DR Ensembl; ENST00000644519.1; ENSP00000494868.1; ENSG00000285199.1. DR Ensembl; ENST00000644672.1; ENSP00000495235.1; ENSG00000285199.1. DR GeneID; 27141; -. DR KEGG; hsa:27141; -. DR MANE-Select; ENST00000554411.6; ENSP00000451089.1; NM_001393339.1; NP_001380268.1. DR UCSC; uc001won.4; human. DR AGR; HGNC:1977; -. DR CTD; 27141; -. DR DisGeNET; 27141; -. DR GeneCards; CIDEB; -. DR HGNC; HGNC:1977; CIDEB. DR HPA; ENSG00000136305; Tissue enhanced (intestine, liver). DR MIM; 604441; gene. DR neXtProt; NX_Q9UHD4; -. DR OpenTargets; ENSG00000136305; -. DR PharmGKB; PA26515; -. DR VEuPathDB; HostDB:ENSG00000136305; -. DR eggNOG; ENOG502RUS7; Eukaryota. DR GeneTree; ENSGT00390000018596; -. DR HOGENOM; CLU_090011_0_0_1; -. DR InParanoid; Q9UHD4; -. DR OMA; PFRICCN; -. DR OrthoDB; 4218882at2759; -. DR PhylomeDB; Q9UHD4; -. DR TreeFam; TF334321; -. DR PathwayCommons; Q9UHD4; -. DR SignaLink; Q9UHD4; -. DR BioGRID-ORCS; 27141; 18 hits in 1079 CRISPR screens. DR ChiTaRS; CIDEB; human. DR EvolutionaryTrace; Q9UHD4; -. DR GenomeRNAi; 27141; -. DR Pharos; Q9UHD4; Tbio. DR PRO; PR:Q9UHD4; -. DR Proteomes; UP000005640; Chromosome 14. DR RNAct; Q9UHD4; Protein. DR Bgee; ENSG00000136305; Expressed in right lobe of liver and 100 other cell types or tissues. DR ExpressionAtlas; Q9UHD4; baseline and differential. DR GO; GO:0030137; C:COPI-coated vesicle; IEA:UniProtKB-SubCell. DR GO; GO:0030127; C:COPII vesicle coat; ISS:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:MGI. DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB. DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB. DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell. DR GO; GO:0005811; C:lipid droplet; IDA:UniProtKB. DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:AgBase. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0120013; F:lipid transfer activity; ISS:UniProtKB. DR GO; GO:0060090; F:molecular adaptor activity; ISS:UniProtKB. DR GO; GO:0070300; F:phosphatidic acid binding; IEA:Ensembl. DR GO; GO:0006915; P:apoptotic process; IDA:MGI. DR GO; GO:0038183; P:bile acid signaling pathway; IEA:Ensembl. DR GO; GO:0090110; P:COPII-coated vesicle cargo loading; ISS:UniProtKB. DR GO; GO:0097194; P:execution phase of apoptosis; ISS:BHF-UCL. DR GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; TAS:ProtInc. DR GO; GO:0160077; P:lipid droplet fusion; IMP:UniProtKB. DR GO; GO:0019915; P:lipid storage; IEA:Ensembl. DR GO; GO:0043065; P:positive regulation of apoptotic process; IDA:AgBase. DR GO; GO:0042981; P:regulation of apoptotic process; IBA:GO_Central. DR GO; GO:0090207; P:regulation of triglyceride metabolic process; ISS:UniProtKB. DR GO; GO:0031667; P:response to nutrient levels; IEA:Ensembl. DR GO; GO:0034379; P:very-low-density lipoprotein particle assembly; ISS:UniProtKB. DR CDD; cd06537; CIDE_N_B; 1. DR Gene3D; 3.10.20.10; -; 1. DR InterPro; IPR003508; CIDE-N_dom. DR PANTHER; PTHR12306; CELL DEATH ACTIVATOR CIDE; 1. DR PANTHER; PTHR12306:SF10; CELL DEATH ACTIVATOR CIDE-B; 1. DR Pfam; PF02017; CIDE-N; 1. DR SMART; SM00266; CAD; 1. DR SUPFAM; SSF54277; CAD & PB1 domains; 1. DR PROSITE; PS51135; CIDE_N; 1. DR Genevisible; Q9UHD4; HS. PE 1: Evidence at protein level; KW 3D-structure; Apoptosis; Cytoplasmic vesicle; Endoplasmic reticulum; KW Golgi apparatus; Host-virus interaction; Lipid droplet; Membrane; KW Phosphoprotein; Reference proteome. FT CHAIN 1..219 FT /note="Lipid transferase CIDEB" FT /id="PRO_0000144720" FT DOMAIN 34..110 FT /note="CIDE-N" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00447" FT CONFLICT 120 FT /note="L -> P (in Ref. 1; AAF23324)" FT /evidence="ECO:0000305" FT CONFLICT 124 FT /note="R -> S (in Ref. 1; AAF23324)" FT /evidence="ECO:0000305" FT CONFLICT 132 FT /note="A -> G (in Ref. 1; AAF23324)" FT /evidence="ECO:0000305" FT STRAND 9..12 FT /evidence="ECO:0007829|PDB:1D4B" FT STRAND 36..41 FT /evidence="ECO:0007829|PDB:1D4B" FT STRAND 43..46 FT /evidence="ECO:0007829|PDB:1D4B" FT STRAND 48..53 FT /evidence="ECO:0007829|PDB:1D4B" FT HELIX 59..67 FT /evidence="ECO:0007829|PDB:1D4B" FT STRAND 74..77 FT /evidence="ECO:0007829|PDB:1D4B" FT TURN 78..81 FT /evidence="ECO:0007829|PDB:1D4B" FT STRAND 82..84 FT /evidence="ECO:0007829|PDB:1D4B" FT HELIX 88..92 FT /evidence="ECO:0007829|PDB:1D4B" FT STRAND 93..95 FT /evidence="ECO:0007829|PDB:1D4B" SQ SEQUENCE 219 AA; 24678 MW; E0B4E5EF1F7C912D CRC64; MEYLSALNPS DLLRSVSNIS SEFGRRVWTS APPPQRPFRV CDHKRTIRKG LTAATRQELL AKALETLLLN GVLTLVLEED GTAVDSEDFF QLLEDDTCLM VLQSGQSWSP TRSGVLSYGL GRERPKHSKD IARFTFDVYK QNPRDLFGSL NVKATFYGLY SMSCDFQGLG PKKVLRELLR WTSTLLQGLG HMLLGISSTL RHAVEGAEQW QQKGRLHSY //