BID_MOUSE
ID BID_MOUSE Reviewed; 195 AA.
AC P70444; Q99M39;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 21-FEB-2006, sequence version 2.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=BH3-interacting domain death agonist;
DE AltName: Full=p22 BID;
DE Short=BID;
DE Contains:
DE RecName: Full=BH3-interacting domain death agonist p15;
DE AltName: Full=p15 BID;
DE Contains:
DE RecName: Full=BH3-interacting domain death agonist p13;
DE AltName: Full=p13 BID;
DE Contains:
DE RecName: Full=BH3-interacting domain death agonist p11;
DE AltName: Full=p11 BID;
GN Name=Bid;
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], MUTAGENESIS OF BH3 MOTIF, AND SUBUNIT.
RC TISSUE=T-cell;
RX PubMed=8918887; DOI=10.1101/gad.10.22.2859;
RA Wang K., Yin X.-M., Chao D.T., Milliman C.L., Korsmeyer S.J.;
RT "BID: a novel BH3 domain-only death agonist.";
RL Genes Dev. 10:2859-2869(1996).
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 MRNA].
RC TISSUE=Mammary 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 [4]
RP CLEAVAGE SITES, SUBCELLULAR LOCATION, MUTAGENESIS OF ASP-98, AND FUNCTION.
RX PubMed=9873064; DOI=10.1074/jbc.274.2.1156;
RA Gross A., Yin X.-M., Wang K., Wei M.C., Jockel J., Milliman C.,
RA Erdjument-Bromage H., Tempst P., Korsmeyer S.J.;
RT "Caspase cleaved BID targets mitochondria and is required for cytochrome c
RT release, while BCL-XL prevents this release but not tumor necrosis factor-
RT R1/Fas death.";
RL J. Biol. Chem. 274:1156-1163(1999).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Liver, 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 [6]
RP INTERACTION WITH ITCH, AND UBIQUITINATION BY ITCH.
RX PubMed=20392206; DOI=10.1111/j.1742-4658.2010.07562.x;
RA Azakir B.A., Desrochers G., Angers A.;
RT "The ubiquitin ligase Itch mediates the antiapoptotic activity of epidermal
RT growth factor by promoting the ubiquitylation and degradation of the
RT truncated C-terminal portion of Bid.";
RL FEBS J. 277:1319-1330(2010).
RN [7]
RP STRUCTURE BY NMR.
RX PubMed=10089878; DOI=10.1016/s0092-8674(00)80573-5;
RA McDonnell J.M., Fushman D., Milliman C.L., Korsmeyer S.J., Cowburn D.;
RT "Solution structure of the proapoptotic molecule BID: a structural basis
RT for apoptotic agonists and antagonists.";
RL Cell 96:625-634(1999).
RN [8]
RP INTERACTION WITH MTCH2.
RX PubMed=15899861; DOI=10.1128/mcb.25.11.4579-4590.2005;
RA Grinberg M., Schwarz M., Zaltsman Y., Eini T., Niv H., Pietrokovski S.,
RA Gross A.;
RT "Mitochondrial carrier homolog 2 is a target of tBID in cells signaled to
RT die by tumor necrosis factor alpha.";
RL Mol. Cell. Biol. 25:4579-4590(2005).
CC -!- FUNCTION: Induces caspases and apoptosis. Counters the protective
CC effect of BCL2. {ECO:0000269|PubMed:9873064}.
CC -!- FUNCTION: [BH3-interacting domain death agonist p15]: Induces caspase
CC activation and apoptosis (By similarity). Allows the release of
CC cytochrome c (PubMed:9873064). {ECO:0000250|UniProtKB:P55957,
CC ECO:0000269|PubMed:9873064}.
CC -!- SUBUNIT: Forms heterodimers either with the pro-apoptotic protein BAX
CC or the anti-apoptotic protein BCL2 (PubMed:21183079). Interacts with
CC PLEKHN1 (By similarity). {ECO:0000250|UniProtKB:P55957,
CC ECO:0000269|PubMed:21183079}.
CC -!- SUBUNIT: [BH3-interacting domain death agonist p15]: Interacts with
CC ITCH (PubMed:20392206). Interacts with MTCH2 (PubMed:15899861).
CC {ECO:0000269|PubMed:15899861, ECO:0000269|PubMed:20392206}.
CC -!- INTERACTION:
CC P70444; Q07440: Bcl2a1; NbExp=2; IntAct=EBI-783400, EBI-707754;
CC P70444; Q07812: BAX; Xeno; NbExp=2; IntAct=EBI-783400, EBI-516580;
CC PRO_0000223236; Q07812: BAX; Xeno; NbExp=2; IntAct=EBI-2128640, EBI-516580;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9873064}.
CC Mitochondrion membrane {ECO:0000269|PubMed:9873064}. Mitochondrion
CC outer membrane {ECO:0000250|UniProtKB:P55957}. Note=When uncleaved, it
CC is predominantly cytoplasmic. {ECO:0000269|PubMed:9873064}.
CC -!- SUBCELLULAR LOCATION: [BH3-interacting domain death agonist p15]:
CC Mitochondrion membrane {ECO:0000269|PubMed:9873064}. Note=Translocates
CC to mitochondria as an integral membrane protein.
CC {ECO:0000269|PubMed:9873064}.
CC -!- SUBCELLULAR LOCATION: [BH3-interacting domain death agonist p13]:
CC Mitochondrion membrane {ECO:0000269|PubMed:9873064}. Note=Associated
CC with the mitochondrial membrane. {ECO:0000269|PubMed:9873064}.
CC -!- DOMAIN: Intact BH3 motif is required by BIK, BID, BAK, BAD and BAX for
CC their pro-apoptotic activity and for their interaction with anti-
CC apoptotic members of the Bcl-2 family. Apoptotic members of the Bcl-2
CC family.
CC -!- PTM: [BH3-interacting domain death agonist]: TNF-alpha induces caspase-
CC mediated cleavage into a major p15 and minor p13 and p11 products
CC (PubMed:9873064). Cleaved by CASP6 into a major p15 and minor p13
CC products, leading to release of cytochrome c and subsequent
CC nonalcoholic steatohepatitis (By similarity).
CC {ECO:0000250|UniProtKB:P55957, ECO:0000269|PubMed:9873064}.
CC -!- PTM: [BH3-interacting domain death agonist p15]: Ubiquitinated by ITCH;
CC ubiquitination results in proteasome-dependent degradation.
CC {ECO:0000269|PubMed:20392206}.
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DR EMBL; U75506; AAC71064.1; -; mRNA.
DR EMBL; AK045731; BAC32475.1; -; mRNA.
DR EMBL; AK051076; BAC34518.1; -; mRNA.
DR EMBL; AK052356; BAC34955.1; -; mRNA.
DR EMBL; AK077657; BAC36932.1; -; mRNA.
DR EMBL; AK161235; BAE36258.1; -; mRNA.
DR EMBL; BC002031; AAH02031.1; -; mRNA.
DR CCDS; CCDS20486.1; -.
DR RefSeq; NP_031570.2; NM_007544.3.
DR RefSeq; XP_006505472.1; XM_006505409.2.
DR RefSeq; XP_006505473.1; XM_006505410.3.
DR RefSeq; XP_006505474.1; XM_006505411.3.
DR PDB; 1DDB; NMR; -; A=1-195.
DR PDB; 2VOI; X-ray; 2.10 A; B=76-109.
DR PDBsum; 1DDB; -.
DR PDBsum; 2VOI; -.
DR AlphaFoldDB; P70444; -.
DR SMR; P70444; -.
DR BioGRID; 198349; 12.
DR ComplexPortal; CPX-2024; BID:BCL-2 complex.
DR ComplexPortal; CPX-2037; BID:BCL-XL complex.
DR CORUM; P70444; -.
DR DIP; DIP-29808N; -.
DR ELM; P70444; -.
DR IntAct; P70444; 8.
DR MINT; P70444; -.
DR STRING; 10090.ENSMUSP00000004560; -.
DR iPTMnet; P70444; -.
DR PhosphoSitePlus; P70444; -.
DR EPD; P70444; -.
DR MaxQB; P70444; -.
DR PaxDb; P70444; -.
DR PeptideAtlas; P70444; -.
DR PRIDE; P70444; -.
DR ProteomicsDB; 273689; -.
DR Antibodypedia; 263; 1351 antibodies from 50 providers.
DR DNASU; 12122; -.
DR Ensembl; ENSMUST00000004560; ENSMUSP00000004560; ENSMUSG00000004446.
DR Ensembl; ENSMUST00000160684; ENSMUSP00000125731; ENSMUSG00000004446.
DR GeneID; 12122; -.
DR KEGG; mmu:12122; -.
DR UCSC; uc009dnv.1; mouse.
DR CTD; 637; -.
DR MGI; MGI:108093; Bid.
DR VEuPathDB; HostDB:ENSMUSG00000004446; -.
DR eggNOG; ENOG502SAN7; Eukaryota.
DR GeneTree; ENSGT00390000002868; -.
DR HOGENOM; CLU_090524_0_0_1; -.
DR InParanoid; P70444; -.
DR OMA; QDEHITN; -.
DR OrthoDB; 1218538at2759; -.
DR PhylomeDB; P70444; -.
DR TreeFam; TF102047; -.
DR Reactome; R-MMU-111447; Activation of BAD and translocation to mitochondria.
DR Reactome; R-MMU-111452; Activation and oligomerization of BAK protein.
DR Reactome; R-MMU-111453; BH3-only proteins associate with and inactivate anti-apoptotic BCL-2 members.
DR Reactome; R-MMU-114294; Activation, translocation and oligomerization of BAX.
DR Reactome; R-MMU-75108; Activation, myristolyation of BID and translocation to mitochondria.
DR BioGRID-ORCS; 12122; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Bid; mouse.
DR EvolutionaryTrace; P70444; -.
DR PRO; PR:P70444; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; P70444; protein.
DR Bgee; ENSMUSG00000004446; Expressed in lumbar dorsal root ganglion and 214 other tissues.
DR ExpressionAtlas; P70444; baseline and differential.
DR Genevisible; P70444; MM.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0032592; C:integral component of mitochondrial membrane; IDA:BHF-UCL.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0005741; C:mitochondrial outer membrane; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB.
DR GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; IMP:MGI.
DR GO; GO:0008637; P:apoptotic mitochondrial changes; IBA:GO_Central.
DR GO; GO:0090150; P:establishment of protein localization to membrane; ISO:MGI.
DR GO; GO:0097191; P:extrinsic apoptotic signaling pathway; IMP:MGI.
DR GO; GO:0097284; P:hepatocyte apoptotic process; IGI:MGI.
DR GO; GO:0042775; P:mitochondrial ATP synthesis coupled electron transport; IMP:MGI.
DR GO; GO:0097345; P:mitochondrial outer membrane permeabilization; IGI:MGI.
DR GO; GO:1902230; P:negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage; IMP:MGI.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IDA:MGI.
DR GO; GO:2001235; P:positive regulation of apoptotic signaling pathway; IDA:MGI.
DR GO; GO:0034263; P:positive regulation of autophagy in response to ER overload; ISO:MGI.
DR GO; GO:2001238; P:positive regulation of extrinsic apoptotic signaling pathway; ISO:MGI.
DR GO; GO:2000271; P:positive regulation of fibroblast apoptotic process; IDA:MGI.
DR GO; GO:2001244; P:positive regulation of intrinsic apoptotic signaling pathway; ISO:MGI.
DR GO; GO:0010918; P:positive regulation of mitochondrial membrane potential; IMP:MGI.
DR GO; GO:0031334; P:positive regulation of protein-containing complex assembly; IDA:UniProtKB.
DR GO; GO:0090200; P:positive regulation of release of cytochrome c from mitochondria; IGI:BHF-UCL.
DR GO; GO:0006626; P:protein targeting to mitochondrion; IMP:MGI.
DR GO; GO:0065003; P:protein-containing complex assembly; IDA:BHF-UCL.
DR GO; GO:0042981; P:regulation of apoptotic process; IGI:MGI.
DR GO; GO:0050678; P:regulation of epithelial cell proliferation; IMP:MGI.
DR GO; GO:2000045; P:regulation of G1/S transition of mitotic cell cycle; IMP:MGI.
DR GO; GO:1902108; P:regulation of mitochondrial membrane permeability involved in apoptotic process; IGI:MGI.
DR GO; GO:0042129; P:regulation of T cell proliferation; IMP:MGI.
DR GO; GO:0001836; P:release of cytochrome c from mitochondria; IDA:CACAO.
DR GO; GO:0042770; P:signal transduction in response to DNA damage; TAS:UniProtKB.
DR GO; GO:0097435; P:supramolecular fiber organization; ISO:MGI.
DR DisProt; DP01661; -.
DR Gene3D; 1.10.437.10; -; 1.
DR InterPro; IPR036834; Bcl-2-like_sf.
DR InterPro; IPR020728; Bcl2_BH3_motif_CS.
DR InterPro; IPR010479; BID.
DR PANTHER; PTHR35447; PTHR35447; 1.
DR Pfam; PF06393; BID; 1.
DR PIRSF; PIRSF038018; BID; 1.
DR SUPFAM; SSF56854; SSF56854; 1.
DR PROSITE; PS01259; BH3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Apoptosis; Cytoplasm; Membrane; Mitochondrion;
KW Mitochondrion outer membrane; Phosphoprotein; Reference proteome;
KW Ubl conjugation.
FT CHAIN 1..195
FT /note="BH3-interacting domain death agonist"
FT /id="PRO_0000143102"
FT CHAIN 60..195
FT /note="BH3-interacting domain death agonist p15"
FT /id="PRO_0000223236"
FT CHAIN 76..195
FT /note="BH3-interacting domain death agonist p13"
FT /id="PRO_0000223235"
FT CHAIN 99..195
FT /note="BH3-interacting domain death agonist p11"
FT /id="PRO_0000223234"
FT REGION 58..77
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 87..100
FT /note="BH3"
FT /evidence="ECO:0000269|PubMed:8918887"
FT COMPBIAS 58..73
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 59..60
FT /note="Cleavage"
FT /evidence="ECO:0000269|PubMed:9873064"
FT SITE 75..76
FT /note="Cleavage"
FT /evidence="ECO:0000269|PubMed:9873064"
FT SITE 98..99
FT /note="Cleavage"
FT /evidence="ECO:0000269|PubMed:9873064"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P55957"
FT MOD_RES 78
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P55957"
FT MUTAGEN 98
FT /note="D->A: Loss of proteolytical cleavage leading to the
FT production of p11 BID."
FT /evidence="ECO:0000269|PubMed:9873064"
FT CONFLICT 14
FT /note="E -> K (in Ref. 1; AAC71064)"
FT /evidence="ECO:0000305"
FT HELIX 15..27
FT /evidence="ECO:0007829|PDB:1DDB"
FT STRAND 28..30
FT /evidence="ECO:0007829|PDB:1DDB"
FT HELIX 32..39
FT /evidence="ECO:0007829|PDB:1DDB"
FT HELIX 79..99
FT /evidence="ECO:0007829|PDB:2VOI"
FT STRAND 103..105
FT /evidence="ECO:0007829|PDB:1DDB"
FT HELIX 106..113
FT /evidence="ECO:0007829|PDB:1DDB"
FT STRAND 116..122
FT /evidence="ECO:0007829|PDB:1DDB"
FT HELIX 125..137
FT /evidence="ECO:0007829|PDB:1DDB"
FT HELIX 142..162
FT /evidence="ECO:0007829|PDB:1DDB"
FT HELIX 167..180
FT /evidence="ECO:0007829|PDB:1DDB"
FT HELIX 185..192
FT /evidence="ECO:0007829|PDB:1DDB"
SQ SEQUENCE 195 AA; 21952 MW; 52F412714FB867F3 CRC64;
MDSEVSNGSG LGAEHITDLL VFGFLQSSGC TRQELEVLGR ELPVQAYWEA DLEDELQTDG
SQASRSFNQG RIEPDSESQE EIIHNIARHL AQIGDEMDHN IQPTLVRQLA AQFMNGSLSE
EDKRNCLAKA LDEVKTAFPR DMENDKAMLI MTMLLAKKVA SHAPSLLRDV FHTTVNFINQ
NLFSYVRNLV RNEMD
