MCL1_MOUSE
ID MCL1_MOUSE Reviewed; 331 AA.
AC P97287; D2K6L9; Q3TUS0; Q792P0; Q9CRI4;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 3.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=Induced myeloid leukemia cell differentiation protein Mcl-1 homolog;
DE AltName: Full=Bcl-2-related protein EAT/mcl1;
GN Name=Mcl1;
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] (ISOFORM 1), AND INDUCTION.
RC TISSUE=Fetus;
RX PubMed=9655929; DOI=10.1016/s0167-4781(98)00059-1;
RA Okita H., Umezawa A., Suzuki A., Hata J.;
RT "Up-regulated expression of murine Mcl1/EAT, a bcl-2 related gene, in the
RT early stage of differentiation of murine embryonal carcinoma cells and
RT embryonic stem cells.";
RL Biochim. Biophys. Acta 1398:335-341(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, AND SUBCELLULAR
RP LOCALIZATION.
RC STRAIN=C57BL/6J;
RX PubMed=19919825; DOI=10.1016/j.bbrc.2009.11.086;
RA Kojima S., Hyakutake A., Koshikawa N., Nakagawara A., Takenaga K.;
RT "MCL-1V, a novel mouse antiapoptotic MCL-1 variant, generated by RNA
RT splicing at a non-canonical splicing pair.";
RL Biochem. Biophys. Res. Commun. 391:492-497(2010).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Embryo, and Embryonic stem cell;
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=Czech II, and FVB/N; TISSUE=Mammary tumor, and Salivary gland;
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 [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-65, AND INDUCTION.
RC STRAIN=129/SvJ;
RX PubMed=9671497; DOI=10.1128/mcb.18.8.4883;
RA Chao J.-R., Wang J.-M., Lee S.-F., Peng H.-W., Lin Y.-H., Chou C.-H.,
RA Li J.-C., Huang H.-M., Chou C.-K., Kuo M.-L., Yen J.J.-Y., Yang-Yen H.-F.;
RT "Mcl-1 is an immediate-early gene activated by the granulocyte-macrophage
RT colony-stimulating factor (GM-CSF) signaling pathway and is one component
RT of the GM-CSF viability response.";
RL Mol. Cell. Biol. 18:4883-4898(1998).
RN [7]
RP FUNCTION AS INHIBITOR OF APOPTOSIS, PHOSPHORYLATION AT SER-140 BY
RP GSK3-ALPHA AND GSK3-BETA, AND INTERACTION WITH BCL2L11.
RX PubMed=16543145; DOI=10.1016/j.molcel.2006.02.009;
RA Maurer U., Charvet C., Wagman A.S., Dejardin E., Green D.R.;
RT "Glycogen synthase kinase-3 regulates mitochondrial outer membrane
RT permeabilization and apoptosis by destabilization of MCL-1.";
RL Mol. Cell 21:749-760(2006).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [9]
RP INTERACTION WITH HIF3A.
RX PubMed=21546903; DOI=10.1038/cdd.2011.47;
RA Torii S., Goto Y., Ishizawa T., Hoshi H., Goryo K., Yasumoto K.,
RA Fukumura H., Sogawa K.;
RT "Pro-apoptotic activity of inhibitory PAS domain protein (IPAS), a negative
RT regulator of HIF-1, through binding to pro-survival Bcl-2 family
RT proteins.";
RL Cell Death Differ. 18:1711-1725(2011).
RN [10]
RP INTERACTION WITH GIMAP5 AND HSPA8.
RX PubMed=21502331; DOI=10.1084/jem.20101192;
RA Chen Y., Yu M., Dai X., Zogg M., Wen R., Weiler H., Wang D.;
RT "Critical role for Gimap5 in the survival of mouse hematopoietic stem and
RT progenitor cells.";
RL J. Exp. Med. 208:923-935(2011).
RN [11]
RP INTERACTION WITH BCL2L11.
RX PubMed=27013495; DOI=10.15252/embr.201541392;
RA Weber A., Heinlein M., Dengjel J., Alber C., Singh P.K., Haecker G.;
RT "The deubiquitinase Usp27x stabilizes the BH3-only protein Bim and enhances
RT apoptosis.";
RL EMBO Rep. 17:724-738(2016).
RN [12]
RP STRUCTURE BY NMR OF 152-308, AND INTERACTION WITH BCL2L11; BMF AND PMAIP.
RX PubMed=15550399; DOI=10.1074/jbc.m411434200;
RA Day C.L., Chen L., Richardson S.J., Harrison P.J., Huang D.C.S.,
RA Hinds M.G.;
RT "Solution structure of prosurvival Mcl-1 and characterization of its
RT binding by proapoptotic BH3-only ligands.";
RL J. Biol. Chem. 280:4738-4744(2005).
RN [13]
RP STRUCTURE BY NMR OF 148-308 IN COMPLEXES WITH BBC3 AND PMAIP1.
RX PubMed=18589438; DOI=10.1016/j.jmb.2008.05.071;
RA Day C.L., Smits C., Fan F.C., Lee E.F., Fairlie W.D., Hinds M.G.;
RT "Structure of the BH3 domains from the p53-inducible BH3-only proteins Noxa
RT and Puma in complex with Mcl-1.";
RL J. Mol. Biol. 380:958-971(2008).
CC -!- FUNCTION: Involved in the regulation of apoptosis versus cell survival,
CC and in the maintenance of viability but not of proliferation. Mediates
CC its effects by interactions with a number of other regulators of
CC apoptosis. Isoform 2 has antiapoptotic activity.
CC {ECO:0000269|PubMed:16543145, ECO:0000269|PubMed:19919825}.
CC -!- SUBUNIT: Interacts with HIF3A isoform 2 (via C-terminus domain)
CC (PubMed:21546903). Interacts with BAD, BOK, BIK, BAX, BAK1, and TPT1.
CC Interacts with BBC3, BMF and PMAIP1 (PubMed:15550399, PubMed:18589438).
CC Interacts with BOP. Interacts with BCL2L11; this interaction may
CC sequester BCL2L11 and prevent its pro-apoptotic activity
CC (PubMed:16543145, PubMed:27013495, PubMed:15550399). Interacts with
CC GIMAP5 and HSPA8/HSC70; the interaction between HSPA8 and MCL1 is
CC impaired in the absence of GIMAP5 (PubMed:21502331).
CC {ECO:0000269|PubMed:15550399, ECO:0000269|PubMed:16543145,
CC ECO:0000269|PubMed:18589438, ECO:0000269|PubMed:21502331,
CC ECO:0000269|PubMed:21546903, ECO:0000269|PubMed:27013495}.
CC -!- INTERACTION:
CC P97287; O08734: Bak1; NbExp=2; IntAct=EBI-707292, EBI-822441;
CC P97287; Q99ML1: Bbc3; NbExp=2; IntAct=EBI-707292, EBI-727801;
CC P97287; O54918: Bcl2l11; NbExp=5; IntAct=EBI-707292, EBI-526067;
CC P97287; Q9JM54: Pmaip1; NbExp=14; IntAct=EBI-707292, EBI-709183;
CC P97287; Q16611: BAK1; Xeno; NbExp=3; IntAct=EBI-707292, EBI-519866;
CC P97287; Q07812: BAX; Xeno; NbExp=2; IntAct=EBI-707292, EBI-516580;
CC P97287; Q9BXH1: BBC3; Xeno; NbExp=5; IntAct=EBI-707292, EBI-519884;
CC P97287; O43521: BCL2L11; Xeno; NbExp=7; IntAct=EBI-707292, EBI-526406;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass membrane
CC protein {ECO:0000250}. Cytoplasm {ECO:0000250}. Mitochondrion. Nucleus,
CC nucleoplasm {ECO:0000250}. Note=Cytoplasmic, associated with
CC mitochondria.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P97287-1; Sequence=Displayed;
CC Name=2; Synonyms=Mck-1V;
CC IsoId=P97287-2; Sequence=VSP_046443;
CC -!- INDUCTION: Up-regulated by IL3 and CSF2. Up-regulated in murine
CC embryonal carcinoma cells in response to retinoic acid treatment.
CC Levels reach a maximum after 4 hours, are decreased after 8 hours and
CC are back to maximum after 12 hours. Levels are decreased after 24 hours
CC and back to basal levels after 48 hours. Expression remains constant in
CC retinoic acid-treated embryonic stem cells.
CC {ECO:0000269|PubMed:9655929, ECO:0000269|PubMed:9671497}.
CC -!- PTM: Cleaved by CASP3 during apoptosis, yielding a pro-apoptotic C-
CC terminal fragment. {ECO:0000250}.
CC -!- PTM: Rapidly degraded in the absence of phosphorylation in the PEST
CC region. {ECO:0000250}.
CC -!- PTM: Phosphorylated on Ser-140, by GSK3, in response to
CC IL3/interleukin-3 withdrawal. Phosphorylation at Ser-140 induces
CC ubiquitination and proteasomal degradation, abrogating the anti-
CC apoptotic activity. Treatment with taxol or okadaic acid induces
CC phosphorylation on additional sites. {ECO:0000269|PubMed:16543145}.
CC -!- PTM: Ubiquitinated. Ubiquitination is induced by phosphorylation at
CC Ser-140 (By similarity). {ECO:0000250}.
CC -!- MISCELLANEOUS: [Isoform 2]: This isoform is more stable than isoform 1
CC in cells undergoing apoptosis. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the Bcl-2 family. {ECO:0000305}.
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DR EMBL; U35623; AAC31790.1; -; mRNA.
DR EMBL; GU182318; ACZ54910.1; -; mRNA.
DR EMBL; AK010424; BAB26927.1; -; mRNA.
DR EMBL; AK159504; BAE35137.1; -; mRNA.
DR EMBL; AK160594; BAE35901.1; -; mRNA.
DR EMBL; AC092479; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; FO082281; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC003839; AAH03839.1; -; mRNA.
DR EMBL; BC005427; AAH05427.1; -; mRNA.
DR EMBL; BC021638; AAH21638.1; -; mRNA.
DR EMBL; AF063886; AAC27929.1; -; Genomic_DNA.
DR CCDS; CCDS57236.1; -. [P97287-1]
DR RefSeq; NP_032588.1; NM_008562.3. [P97287-1]
DR PDB; 1WSX; NMR; -; A=152-308.
DR PDB; 2JM6; NMR; -; B=152-308.
DR PDB; 2NL9; X-ray; 1.55 A; A=152-189.
DR PDB; 2NLA; X-ray; 2.80 A; A=152-189.
DR PDB; 2ROC; NMR; -; A=152-308.
DR PDB; 2ROD; NMR; -; A=152-308.
DR PDB; 3D7V; X-ray; 2.03 A; A=152-189.
DR PDB; 3IO9; X-ray; 2.40 A; A=152-189.
DR PDB; 4BPI; X-ray; 1.98 A; A=152-189.
DR PDB; 4BPJ; X-ray; 1.60 A; A=152-189.
DR PDB; 4G35; X-ray; 2.00 A; A=152-308.
DR PDB; 5KU9; X-ray; 2.20 A; A/B=152-308.
DR PDB; 5MES; X-ray; 2.24 A; A=153-221.
DR PDB; 5MEV; X-ray; 2.94 A; A=153-221.
DR PDB; 5VX2; X-ray; 1.85 A; A/C=152-221.
DR PDB; 6DM8; X-ray; 2.70 A; A/B/C/D/E/F/G/H=154-302.
DR PDBsum; 1WSX; -.
DR PDBsum; 2JM6; -.
DR PDBsum; 2NL9; -.
DR PDBsum; 2NLA; -.
DR PDBsum; 2ROC; -.
DR PDBsum; 2ROD; -.
DR PDBsum; 3D7V; -.
DR PDBsum; 3IO9; -.
DR PDBsum; 4BPI; -.
DR PDBsum; 4BPJ; -.
DR PDBsum; 4G35; -.
DR PDBsum; 5KU9; -.
DR PDBsum; 5MES; -.
DR PDBsum; 5MEV; -.
DR PDBsum; 5VX2; -.
DR PDBsum; 6DM8; -.
DR AlphaFoldDB; P97287; -.
DR SMR; P97287; -.
DR BioGRID; 201344; 19.
DR ComplexPortal; CPX-305; MCL1:PMAIP1 complex.
DR ComplexPortal; CPX-629; MCL-1-BIM complex.
DR CORUM; P97287; -.
DR DIP; DIP-33343N; -.
DR ELM; P97287; -.
DR IntAct; P97287; 18.
DR MINT; P97287; -.
DR STRING; 10090.ENSMUSP00000044048; -.
DR BindingDB; P97287; -.
DR ChEMBL; CHEMBL5768; -.
DR iPTMnet; P97287; -.
DR PhosphoSitePlus; P97287; -.
DR EPD; P97287; -.
DR jPOST; P97287; -.
DR MaxQB; P97287; -.
DR PaxDb; P97287; -.
DR PeptideAtlas; P97287; -.
DR PRIDE; P97287; -.
DR ProteomicsDB; 252747; -. [P97287-1]
DR ProteomicsDB; 252748; -. [P97287-2]
DR ABCD; P97287; 1 sequenced antibody.
DR Antibodypedia; 1508; 1456 antibodies from 50 providers.
DR DNASU; 17210; -.
DR Ensembl; ENSMUST00000037947; ENSMUSP00000044048; ENSMUSG00000038612. [P97287-1]
DR Ensembl; ENSMUST00000178686; ENSMUSP00000135915; ENSMUSG00000038612. [P97287-2]
DR GeneID; 17210; -.
DR KEGG; mmu:17210; -.
DR UCSC; uc029unp.1; mouse. [P97287-1]
DR CTD; 4170; -.
DR MGI; MGI:101769; Mcl1.
DR VEuPathDB; HostDB:ENSMUSG00000038612; -.
DR eggNOG; KOG4728; Eukaryota.
DR GeneTree; ENSGT01050000244872; -.
DR HOGENOM; CLU_046711_0_0_1; -.
DR InParanoid; P97287; -.
DR OMA; TKPMGGS; -.
DR OrthoDB; 1218929at2759; -.
DR PhylomeDB; P97287; -.
DR TreeFam; TF315834; -.
DR BioGRID-ORCS; 17210; 21 hits in 75 CRISPR screens.
DR ChiTaRS; Mcl1; mouse.
DR EvolutionaryTrace; P97287; -.
DR PRO; PR:P97287; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; P97287; protein.
DR Bgee; ENSMUSG00000038612; Expressed in otic placode and 263 other tissues.
DR Genevisible; P97287; MM.
DR GO; GO:0097136; C:Bcl-2 family protein complex; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR GO; GO:0005741; C:mitochondrial outer membrane; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IDA:ParkinsonsUK-UCL.
DR GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0051400; F:BH domain binding; ISO:MGI.
DR GO; GO:0051434; F:BH3 domain binding; IPI:UniProtKB.
DR GO; GO:0046983; F:protein dimerization activity; ISO:MGI.
DR GO; GO:0046982; F:protein heterodimerization activity; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; IBA:GO_Central.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0097192; P:extrinsic apoptotic signaling pathway in absence of ligand; IMP:UniProtKB.
DR GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; IDA:MGI.
DR GO; GO:2000811; P:negative regulation of anoikis; ISO:MGI.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB.
DR GO; GO:0010507; P:negative regulation of autophagy; ISO:MGI.
DR GO; GO:2001240; P:negative regulation of extrinsic apoptotic signaling pathway in absence of ligand; ISO:MGI.
DR GO; GO:2001243; P:negative regulation of intrinsic apoptotic signaling pathway; IBA:GO_Central.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISO:MGI.
DR GO; GO:1903378; P:positive regulation of oxidative stress-induced neuron intrinsic apoptotic signaling pathway; IMP:ParkinsonsUK-UCL.
DR GO; GO:0042981; P:regulation of apoptotic process; ISO:MGI.
DR GO; GO:2001020; P:regulation of response to DNA damage stimulus; ISO:MGI.
DR GO; GO:0034097; P:response to cytokine; ISO:MGI.
DR CDD; cd06845; Bcl-2_like; 1.
DR Gene3D; 1.10.437.10; -; 1.
DR InterPro; IPR013281; Apop_reg_Mc1.
DR InterPro; IPR036834; Bcl-2-like_sf.
DR InterPro; IPR046371; Bcl-2_BH1-3.
DR InterPro; IPR026298; Bcl-2_fam.
DR InterPro; IPR002475; Bcl2-like.
DR InterPro; IPR020717; Bcl2_BH1_motif_CS.
DR InterPro; IPR020726; Bcl2_BH2_motif_CS.
DR InterPro; IPR020728; Bcl2_BH3_motif_CS.
DR PANTHER; PTHR11256; PTHR11256; 1.
DR PANTHER; PTHR11256:SF46; PTHR11256:SF46; 1.
DR Pfam; PF00452; Bcl-2; 1.
DR PRINTS; PR01866; APOPREGMCL1.
DR PRINTS; PR01862; BCL2FAMILY.
DR SMART; SM00337; BCL; 1.
DR SUPFAM; SSF56854; SSF56854; 1.
DR PROSITE; PS50062; BCL2_FAMILY; 1.
DR PROSITE; PS01080; BH1; 1.
DR PROSITE; PS01258; BH2; 1.
DR PROSITE; PS01259; BH3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Apoptosis; Cytoplasm;
KW Developmental protein; Differentiation; Isopeptide bond; Membrane;
KW Mitochondrion; Nucleus; Phosphoprotein; Reference proteome; Transmembrane;
KW Transmembrane helix; Ubl conjugation.
FT CHAIN 1..331
FT /note="Induced myeloid leukemia cell differentiation
FT protein Mcl-1 homolog"
FT /id="PRO_0000143081"
FT TRANSMEM 308..330
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 85..156
FT /note="PEST-like"
FT /evidence="ECO:0000250"
FT REGION 130..154
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 190..204
FT /note="BH3"
FT MOTIF 234..253
FT /note="BH1"
FT MOTIF 285..300
FT /note="BH2"
FT SITE 108..109
FT /note="Cleavage; by caspase-3"
FT /evidence="ECO:0000250"
FT SITE 138..139
FT /note="Cleavage; by caspase-3"
FT /evidence="ECO:0000250"
FT MOD_RES 102
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q07820"
FT MOD_RES 140
FT /note="Phosphoserine; by GSK3-alpha and GSK3-beta"
FT /evidence="ECO:0000269|PubMed:16543145"
FT MOD_RES 143
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q07820"
FT MOD_RES 144
FT /note="Phosphothreonine; by MAPK"
FT /evidence="ECO:0000250|UniProtKB:Q07820"
FT CROSSLNK 117
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q07820"
FT CROSSLNK 175
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q07820"
FT CROSSLNK 178
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q07820"
FT VAR_SEQ 18..63
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:19919825"
FT /id="VSP_046443"
FT HELIX 154..172
FT /evidence="ECO:0007829|PDB:2NL9"
FT STRAND 181..183
FT /evidence="ECO:0007829|PDB:5VX2"
FT HELIX 185..202
FT /evidence="ECO:0007829|PDB:2NL9"
FT HELIX 206..216
FT /evidence="ECO:0007829|PDB:2NL9"
FT HELIX 221..225
FT /evidence="ECO:0007829|PDB:6DM8"
FT HELIX 227..234
FT /evidence="ECO:0007829|PDB:4G35"
FT TURN 235..237
FT /evidence="ECO:0007829|PDB:4G35"
FT HELIX 242..261
FT /evidence="ECO:0007829|PDB:4G35"
FT HELIX 265..267
FT /evidence="ECO:0007829|PDB:4G35"
FT HELIX 268..289
FT /evidence="ECO:0007829|PDB:4G35"
FT HELIX 292..300
FT /evidence="ECO:0007829|PDB:4G35"
FT TURN 301..303
FT /evidence="ECO:0007829|PDB:2ROC"
SQ SEQUENCE 331 AA; 35217 MW; E4FD369DB0EC6723 CRC64;
MFGLRRNAVI GLNLYCGGAS LGAGGGSPAG ARLVAEEAKA RREGGGEAAL LPGARVVARP
PPVGAEDPDV TASAERRLHK SPGLLAVPPE EMAASAAAAI VSPEEELDGC EPEAIGKRPA
VLPLLERVSE AAKSSGADGS LPSTPPPPEE EEDDLYRQSL EIISRYLREQ ATGSKDSKPL
GEAGAAGRRA LETLRRVGDG VQRNHETAFQ GMLRKLDIKN EGDVKSFSRV MVHVFKDGVT
NWGRIVTLIS FGAFVAKHLK SVNQESFIEP LAETITDVLV RTKRDWLVKQ RGWDGFVEFF
HVQDLEGGIR NVLLAFAGVA GVGAGLAYLI R
