CIDEC_MOUSE
ID CIDEC_MOUSE Reviewed; 239 AA.
AC P56198; Q499X5; Q8BNV7;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 2.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Cell death activator CIDE-3;
DE AltName: Full=Cell death-inducing DFFA-like effector protein C;
DE AltName: Full=Fat-specific protein FSP27;
GN Name=Cidec; Synonyms=Fsp27;
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 [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=1339452; DOI=10.1016/s0021-9258(19)50555-5;
RA Danesch U., Hoeck W., Ringold G.M.;
RT "Cloning and transcriptional regulation of a novel adipocyte-specific gene,
RT FSP27. CAAT-enhancer-binding protein (C/EBP) and C/EBP-like proteins
RT interact with sequences required for differentiation-dependent
RT expression.";
RL J. Biol. Chem. 267:7185-7193(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Kidney;
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 [5]
RP TISSUE SPECIFICITY.
RX PubMed=12910269; DOI=10.1038/ng1225;
RA Zhou Z., Yon Toh S., Chen Z., Guo K., Ng C.P., Ponniah S., Lin S.C.,
RA Hong W., Li P.;
RT "Cidea-deficient mice have lean phenotype and are resistant to obesity.";
RL Nat. Genet. 35:49-56(2003).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=18334488; DOI=10.1074/jbc.m708323200;
RA Keller P., Petrie J.T., De Rose P., Gerin I., Wright W.S., Chiang S.H.,
RA Nielsen A.R., Fischer C.P., Pedersen B.K., MacDougald O.A.;
RT "Fat-specific protein 27 regulates storage of triacylglycerol.";
RL J. Biol. Chem. 283:14355-14365(2008).
RN [7]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=18654663; DOI=10.1172/jci34090;
RA Nishino N., Tamori Y., Tateya S., Kawaguchi T., Shibakusa T., Mizunoya W.,
RA Inoue K., Kitazawa R., Kitazawa S., Matsuki Y., Hiramatsu R., Masubuchi S.,
RA Omachi A., Kimura K., Saito M., Amo T., Ohta S., Yamaguchi T., Osumi T.,
RA Cheng J., Fujimoto T., Nakao H., Nakao K., Aiba A., Okamura H., Fushiki T.,
RA Kasuga M.;
RT "FSP27 contributes to efficient energy storage in murine white adipocytes
RT by promoting the formation of unilocular lipid droplets.";
RL J. Clin. Invest. 118:2808-2821(2008).
RN [8]
RP INDUCTION.
RX PubMed=18509062; DOI=10.1073/pnas.0802063105;
RA Puri V., Ranjit S., Konda S., Nicoloro S.M., Straubhaar J., Chawla A.,
RA Chouinard M., Lin C., Burkart A., Corvera S., Perugini R.A., Czech M.P.;
RT "Cidea is associated with lipid droplets and insulin sensitivity in
RT humans.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:7833-7838(2008).
RN [9]
RP SUBCELLULAR LOCATION, UBIQUITINATION, INDUCTION, AND MUTAGENESIS OF
RP LYS-224; LYS-226 AND LYS-236.
RX PubMed=20089860; DOI=10.1074/jbc.m109.043786;
RA Nian Z., Sun Z., Yu L., Toh S.Y., Sang J., Li P.;
RT "Fat-specific protein 27 undergoes ubiquitin-dependent degradation
RT regulated by triacylglycerol synthesis and lipid droplet formation.";
RL J. Biol. Chem. 285:9604-9615(2010).
RN [10]
RP FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-182; LYS-186 AND
RP ARG-190, AND CATALYTIC ACTIVITY.
RX PubMed=22144693; DOI=10.1083/jcb.201104142;
RA Gong J., Sun Z., Wu L., Xu W., Schieber N., Xu D., Shui G., Yang H.,
RA Parton R.G., Li P.;
RT "Fsp27 promotes lipid droplet growth by lipid exchange and transfer at
RT lipid droplet contact sites.";
RL J. Cell Biol. 195:953-963(2011).
RN [11]
RP FUNCTION AS A CEBPB COACTIVATOR, INTERACTION WITH CEBPB, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=22245780; DOI=10.1038/nm.2614;
RA Wang W., Lv N., Zhang S., Shui G., Qian H., Zhang J., Chen Y., Ye J.,
RA Xie Y., Shen Y., Wenk M.R., Li P.;
RT "Cidea is an essential transcriptional coactivator regulating mammary gland
RT secretion of milk lipids.";
RL Nat. Med. 18:235-243(2012).
RN [12]
RP FUNCTION IN UNILOCULAR LIPID DROPLET FORMATION, SUBUNIT, INTERACTION WITH
RP PLIN1, SUBCELLULAR LOCATION, AND MUTAGENESIS OF ARG-46; LYS-53; ARG-55;
RP LYS-75; LYS-77; 86-GLU--ASP-88; 87-GLU-ASP-88; LYS-112; LYS-115 AND
RP LYS-117.
RX PubMed=23481402; DOI=10.1038/ncomms2581;
RA Sun Z., Gong J., Wu H., Xu W., Wu L., Xu D., Gao J., Wu J.W., Yang H.,
RA Yang M., Li P.;
RT "Perilipin1 promotes unilocular lipid droplet formation through the
RT activation of Fsp27 in adipocytes.";
RL Nat. Commun. 4:1594-1594(2013).
RN [13]
RP TISSUE SPECIFICITY, AND INDUCTION BY OSMOTIC STRESS.
RX PubMed=23233732; DOI=10.1194/jlr.m033365;
RA Ueno M., Shen W.J., Patel S., Greenberg A.S., Azhar S., Kraemer F.B.;
RT "Fat-specific protein 27 modulates nuclear factor of activated T cells 5
RT and the cellular response to stress.";
RL J. Lipid Res. 54:734-743(2013).
CC -!- FUNCTION: Binds to lipid droplets and regulates their enlargement,
CC thereby restricting lipolysis and favoring storage. At focal contact
CC sites between lipid droplets, promotes directional net neutral lipid
CC transfer from the smaller to larger lipid droplets. The transfer
CC direction may be driven by the internal pressure difference between the
CC contacting lipid droplet pair. Its role in neutral lipid transfer and
CC lipid droplet enlargement is activated by the interaction with PLIN1.
CC May act as a CEBPB coactivator in the white adipose tissue to control
CC the expression of a subset of CEBPB downstream target genes, including
CC SOCS1, SOCS3, TGFB1, TGFBR1, ID2 and XDH. When overexpressed in
CC preadipocytes, induces apoptosis or increases cell susceptibility to
CC apoptosis induced by serum deprivation or TGFB treatment. As mature
CC adipocytes, that express high CIDEC levels, are quite resistant to
CC apoptotic stimuli, the physiological significance of its role in
CC apoptosis is unclear. May play a role in the modulation of the response
CC to osmotic stress by preventing NFAT5 to translocate into the nucleus
CC and activate its target genes expression. {ECO:0000269|PubMed:18334488,
CC ECO:0000269|PubMed:22144693, ECO:0000269|PubMed:22245780,
CC ECO:0000269|PubMed:23481402}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a triacyl-sn-glycerol(in) = a triacyl-sn-glycerol(out);
CC Xref=Rhea:RHEA:39011, ChEBI:CHEBI:64615;
CC Evidence={ECO:0000269|PubMed:22144693};
CC -!- SUBUNIT: Homodimer. Interacts with CIDEA. Interacts with NFAT5; this
CC interaction is direct and retains NFAT5 in the cytoplasm (By
CC similarity). Interacts with CEBPB. Interacts with PLIN1. {ECO:0000250,
CC ECO:0000269|PubMed:22245780, ECO:0000269|PubMed:23481402}.
CC -!- SUBCELLULAR LOCATION: Lipid droplet. Endoplasmic reticulum. Nucleus.
CC Note=Diffuses quickly on lipid droplet surface, but becomes trapped and
CC clustered at lipid droplet contact sites, thereby enabling its rapid
CC enrichment at lipid droplet contact sites.
CC -!- TISSUE SPECIFICITY: Expressed almost exclusively in adipose tissue,
CC including subcutaneous and epididymal white adipose tissue (at protein
CC level). Although abundantly present in brown adipose tissue at the mRNA
CC level, the protein is almost undetectable in this tissue
CC (PubMed:18654663), or at moderate levels (PubMed:22245780,
CC PubMed:12910269). Expressed in the mammary gland, in stromal adipose
CC tissue, but becomes undetectable at the end of pregnancy and during
CC lactation (at protein level). Expressed at low levels in skeletal
CC muscle and heart. {ECO:0000269|PubMed:12910269,
CC ECO:0000269|PubMed:1339452, ECO:0000269|PubMed:18654663,
CC ECO:0000269|PubMed:22245780, ECO:0000269|PubMed:23233732}.
CC -!- DEVELOPMENTAL STAGE: Up-regulated during differentiation into
CC adipocytes in various cell lines, including TA1 and 3T3-L1. Decreases
CC in the mammary gland during pregnancy from day 14.5 until 18.5, when it
CC becomes hardly detectable, and during lactation.
CC {ECO:0000269|PubMed:1339452, ECO:0000269|PubMed:18334488,
CC ECO:0000269|PubMed:18654663, ECO:0000269|PubMed:22245780}.
CC -!- INDUCTION: Up-regulated under conditions that enhance triacylglycerol
CC deposition, including rosiglitazone treatment and high-fat diet. This
CC up-regulation is mediated by PPARG. Up-regulated by isoproterenol, a
CC beta-agonist, and oleic acid treatment. This induction is due to
CC protein stabilization. Down-regulated upon hypertonic conditions.
CC {ECO:0000269|PubMed:18509062, ECO:0000269|PubMed:20089860,
CC ECO:0000269|PubMed:23233732}.
CC -!- DOMAIN: The CIDE-N domain is involved in homodimerization which is
CC crucial for its function in promoting lipid exchange and transfer.
CC {ECO:0000269|PubMed:23481402}.
CC -!- PTM: Ubiquitinated and targeted to proteasomal degradation, resulting
CC in a short half-life (about 15 minutes in 3T3-L1 cells). Protein
CC stability depends on triaclyglycerol synthesis, fatty acid availability
CC and lipid droplet formation. {ECO:0000269|PubMed:20089860}.
CC -!- DISRUPTION PHENOTYPE: Mutant animals are born in a Mendelian ratio and
CC appear physically normal at birth. The body weights of wild-type and
CC mutant mice fed a standard diet do not differ up to 14 weeks of age,
CC nor does food intake. From 16 weeks of age, the body weight of mutant
CC mice significantly decreases compared with that of wild-type mice. When
CC animals are fed a high-fat diet, the gain in body weight is
CC significantly smaller for mutant mice than for wild-type. Under these
CC feeding conditions, mutant mice are also protected from insulin
CC resistance and from accumulation of fat in the liver. The body
CC temperature do not differ significantly between mutant and wild-type
CC mice maintained at room temperature, but the basal rate of oxygen
CC consumption is significantly increased in mutants.
CC {ECO:0000269|PubMed:18654663}.
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DR EMBL; M61737; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK080133; BAC37830.1; -; mRNA.
DR EMBL; AC153910; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC099676; AAH99676.1; -; mRNA.
DR CCDS; CCDS20418.1; -.
DR PIR; A42445; A42445.
DR RefSeq; NP_001288224.1; NM_001301295.1.
DR RefSeq; NP_848460.1; NM_178373.3.
DR PDB; 4IKG; X-ray; 1.93 A; A=39-118.
DR PDB; 4MAC; X-ray; 2.00 A; A/B=32-120.
DR PDBsum; 4IKG; -.
DR PDBsum; 4MAC; -.
DR AlphaFoldDB; P56198; -.
DR SMR; P56198; -.
DR BioGRID; 199749; 1.
DR IntAct; P56198; 1.
DR MINT; P56198; -.
DR STRING; 10090.ENSMUSP00000032416; -.
DR iPTMnet; P56198; -.
DR PhosphoSitePlus; P56198; -.
DR PaxDb; P56198; -.
DR PRIDE; P56198; -.
DR ProteomicsDB; 283557; -.
DR Antibodypedia; 10363; 316 antibodies from 33 providers.
DR DNASU; 14311; -.
DR Ensembl; ENSMUST00000032416; ENSMUSP00000032416; ENSMUSG00000030278.
DR Ensembl; ENSMUST00000113089; ENSMUSP00000108712; ENSMUSG00000030278.
DR GeneID; 14311; -.
DR KEGG; mmu:14311; -.
DR UCSC; uc009dgb.2; mouse.
DR CTD; 63924; -.
DR MGI; MGI:95585; Cidec.
DR VEuPathDB; HostDB:ENSMUSG00000030278; -.
DR eggNOG; ENOG502QU28; Eukaryota.
DR GeneTree; ENSGT00390000018596; -.
DR HOGENOM; CLU_090011_1_0_1; -.
DR InParanoid; P56198; -.
DR TreeFam; TF334321; -.
DR Reactome; R-MMU-8964572; Lipid particle organization.
DR BioGRID-ORCS; 14311; 3 hits in 74 CRISPR screens.
DR ChiTaRS; Cidec; mouse.
DR PRO; PR:P56198; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; P56198; protein.
DR Bgee; ENSMUSG00000030278; Expressed in epididymal fat pad and 87 other tissues.
DR ExpressionAtlas; P56198; baseline and differential.
DR Genevisible; P56198; MM.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0005811; C:lipid droplet; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0006915; P:apoptotic process; ISO:MGI.
DR GO; GO:0097194; P:execution phase of apoptosis; ISS:UniProtKB.
DR GO; GO:0034389; P:lipid droplet organization; ISO:MGI.
DR GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR GO; GO:0042981; P:regulation of apoptotic process; IBA:GO_Central.
DR InterPro; IPR003508; CIDE-N_dom.
DR Pfam; PF02017; CIDE-N; 1.
DR SMART; SM00266; CAD; 1.
DR PROSITE; PS51135; CIDE_N; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Apoptosis; Endoplasmic reticulum; Lipid droplet;
KW Lipid transport; Nucleus; Reference proteome; Transcription;
KW Transcription regulation; Transport; Ubl conjugation.
FT CHAIN 1..239
FT /note="Cell death activator CIDE-3"
FT /id="PRO_0000144723"
FT DOMAIN 41..118
FT /note="CIDE-N"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00447"
FT MUTAGEN 46
FT /note="R->E: Abolishes CIDE-N/CIDE-N interaction between
FT the 2 homodimer subunits."
FT /evidence="ECO:0000269|PubMed:23481402"
FT MUTAGEN 53
FT /note="K->A: Slightly inhibits interaction with PLIN1."
FT /evidence="ECO:0000269|PubMed:23481402"
FT MUTAGEN 55
FT /note="R->E: Abolishes CIDE-N/CIDE-N interaction between
FT the 2 homodimer subunits."
FT /evidence="ECO:0000269|PubMed:23481402"
FT MUTAGEN 75
FT /note="K->A: Inhibits interaction with PLIN1; when
FT associated with A-77."
FT /evidence="ECO:0000269|PubMed:23481402"
FT MUTAGEN 77
FT /note="K->A: Inhibits interaction with PLIN1; when
FT associated with A-75."
FT /evidence="ECO:0000269|PubMed:23481402"
FT MUTAGEN 86..88
FT /note="EED->QQN: Abolishes CIDE-N/CIDE-N interaction
FT between the 2 homodimer subunits and inhibits lipid droplet
FT enlargement. No effect on homodimerization."
FT /evidence="ECO:0000269|PubMed:23481402"
FT MUTAGEN 87..88
FT /note="ED->QN: Reduces CIDE-N/CIDE-N interaction between
FT the 2 homodimer subunits and inhibits lipid droplet
FT enlargement."
FT /evidence="ECO:0000269|PubMed:23481402"
FT MUTAGEN 112
FT /note="K->A: Slightly inhibits interaction with PLIN1; when
FT associated with A-115."
FT /evidence="ECO:0000269|PubMed:23481402"
FT MUTAGEN 115
FT /note="K->A: Slightly inhibits interaction with PLIN1; when
FT associated with A-112 or A-117."
FT /evidence="ECO:0000269|PubMed:23481402"
FT MUTAGEN 117
FT /note="K->A: Slightly inhibits interaction with PLIN1; when
FT associated with A-115."
FT /evidence="ECO:0000269|PubMed:23481402"
FT MUTAGEN 182
FT /note="K->A: Abolishes lipid droplet enlargement activity,
FT but not localization to lipid droplets, nor enrichement at
FT contact sites; when associated with A-186 and A-190."
FT /evidence="ECO:0000269|PubMed:22144693"
FT MUTAGEN 186
FT /note="K->A: Abolishes lipid droplet enlargement activity,
FT but not localization to lipid droplets, nor enrichement at
FT contact sites; when associated with A-182 and A-190."
FT /evidence="ECO:0000269|PubMed:22144693"
FT MUTAGEN 190
FT /note="R->A: Abolishes lipid droplet enlargement activity,
FT but not localization to lipid droplets, nor enrichement at
FT contact sites; when associated with A-182 and A-186."
FT /evidence="ECO:0000269|PubMed:22144693"
FT MUTAGEN 224
FT /note="K->A: No effect on protein stability; when
FT associated with A-226. Drastically increased protein
FT stability and decreased ubiquitination; when associated
FT with A-226 and A-236."
FT /evidence="ECO:0000269|PubMed:20089860"
FT MUTAGEN 226
FT /note="K->A: No effect on protein stability; when
FT associated with A-226. Drastically increased protein
FT stability and decreased ubiquitination; when associated
FT with A-224 and A-236."
FT /evidence="ECO:0000269|PubMed:20089860"
FT MUTAGEN 236
FT /note="K->A: No effect on protein stability. Drastically
FT increased protein stability and decreased ubiquitination;
FT when associated with A-224 and A-226."
FT /evidence="ECO:0000269|PubMed:20089860"
FT CONFLICT 188..189
FT /note="ML -> IV (in Ref. 1; M61737)"
FT /evidence="ECO:0000305"
FT STRAND 44..48
FT /evidence="ECO:0007829|PDB:4IKG"
FT STRAND 55..59
FT /evidence="ECO:0007829|PDB:4IKG"
FT HELIX 63..73
FT /evidence="ECO:0007829|PDB:4IKG"
FT STRAND 82..85
FT /evidence="ECO:0007829|PDB:4IKG"
FT TURN 86..88
FT /evidence="ECO:0007829|PDB:4IKG"
FT HELIX 95..100
FT /evidence="ECO:0007829|PDB:4IKG"
FT STRAND 106..110
FT /evidence="ECO:0007829|PDB:4IKG"
SQ SEQUENCE 239 AA; 27324 MW; 7F4E6C5D2E24A161 CRC64;
MDYAMKSLSL LYPRSLSRHV AVSTAVVTQQ LVSKPSRETP RARPCRVSTA DRKVRKGIMA
HSLEDLLNKV QDILKLKDKP FSLVLEEDGT IVETEEYFQA LAKDTMFMVL LKGQKWKPPS
EQRKKRAQLA LSQKPTKKID VARVTFDLYK LNPQDFIGCL NVKATLYDTY SLSYDLHCYK
AKRIVKEMLR WTLFSMQATG HMLLGTSSYM QQFLDATEEE QPAKAKPSSL LPACLKMLQ
