BID_RAT
ID BID_RAT Reviewed; 196 AA.
AC Q9JLT6; Q9JK60;
DT 21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-FEB-2006, sequence version 2.
DT 03-AUG-2022, entry version 132.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley;
RX PubMed=12787069; DOI=10.1046/j.1471-4159.2003.01795.x;
RA Itoh T., Itoh A., Pleasure D.;
RT "Bcl-2-related protein family gene expression during oligodendroglial
RT differentiation.";
RL J. Neurochem. 85:1500-1512(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley;
RA Chen D., Cao G., Chen J.;
RT "Cloning of rat apoptotic death agonist (BID) and its different expression
RT in ischemia and normal rat brain.";
RL Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-79, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Induces caspases and apoptosis. Counters the protective
CC effect of BCL2. {ECO:0000250|UniProtKB:P70444}.
CC -!- FUNCTION: [BH3-interacting domain death agonist p15]: Induces caspase
CC activation and apoptosis (By similarity). Allows the release of
CC cytochrome c (By similarity). {ECO:0000250|UniProtKB:P55957,
CC ECO:0000250|UniProtKB:P70444}.
CC -!- SUBUNIT: Forms heterodimers either with the pro-apoptotic protein BAX
CC or the anti-apoptotic protein BCL2. Interacts with PLEKHN1.
CC {ECO:0000250|UniProtKB:P55957, ECO:0000250|UniProtKB:P70444}.
CC -!- SUBUNIT: [BH3-interacting domain death agonist p15]: Interacts with
CC ITCH (By similarity). Interacts with MTCH2 (By similarity).
CC {ECO:0000250|UniProtKB:P55957, ECO:0000250|UniProtKB:P70444}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P70444}.
CC Mitochondrion membrane {ECO:0000250|UniProtKB:P70444}. Mitochondrion
CC outer membrane {ECO:0000250|UniProtKB:P55957}. Note=When uncleaved, it
CC is predominantly cytoplasmic (By similarity).
CC {ECO:0000250|UniProtKB:P70444}.
CC -!- SUBCELLULAR LOCATION: [BH3-interacting domain death agonist p15]:
CC Mitochondrion membrane {ECO:0000250|UniProtKB:P70444}.
CC Note=Translocates to mitochondria as an integral membrane protein.
CC {ECO:0000250|UniProtKB:P70444}.
CC -!- SUBCELLULAR LOCATION: [BH3-interacting domain death agonist p13]:
CC Mitochondrion membrane {ECO:0000250|UniProtKB:P70444}. Note=Associated
CC with the mitochondrial membrane. {ECO:0000250|UniProtKB:P70444}.
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.
CC -!- PTM: [BH3-interacting domain death agonist]: TNF-alpha induces caspase-
CC mediated cleavage into a major p15 and minor p13 and p11 products (By
CC similarity). Cleaved by CASP6 into a major p15 and minor p13 products,
CC leading to release of cytochrome c and subsequent nonalcoholic
CC steatohepatitis (By similarity). {ECO:0000250|UniProtKB:P55957,
CC ECO:0000250|UniProtKB:P70444}.
CC -!- PTM: [BH3-interacting domain death agonist p15]: Ubiquitinated by ITCH;
CC ubiquitination results in proteasome-dependent degradation.
CC {ECO:0000250|UniProtKB:P70444}.
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DR EMBL; AF259503; AAF71759.1; -; mRNA.
DR EMBL; AF136282; AAF61422.1; -; mRNA.
DR RefSeq; NP_073175.1; NM_022684.1.
DR RefSeq; XP_017448369.1; XM_017592880.1.
DR AlphaFoldDB; Q9JLT6; -.
DR SMR; Q9JLT6; -.
DR ComplexPortal; CPX-2023; BID:BCL-2 complex.
DR ComplexPortal; CPX-2038; BID:BCL-XL complex.
DR IntAct; Q9JLT6; 1.
DR MINT; Q9JLT6; -.
DR STRING; 10116.ENSRNOP00000016776; -.
DR iPTMnet; Q9JLT6; -.
DR PhosphoSitePlus; Q9JLT6; -.
DR jPOST; Q9JLT6; -.
DR PaxDb; Q9JLT6; -.
DR PRIDE; Q9JLT6; -.
DR Ensembl; ENSRNOT00000016776; ENSRNOP00000016776; ENSRNOG00000012439.
DR GeneID; 64625; -.
DR KEGG; rno:64625; -.
DR UCSC; RGD:620160; rat.
DR CTD; 637; -.
DR RGD; 620160; Bid.
DR eggNOG; ENOG502SAN7; Eukaryota.
DR GeneTree; ENSGT00390000002868; -.
DR HOGENOM; CLU_090524_0_0_1; -.
DR InParanoid; Q9JLT6; -.
DR OMA; QDEHITN; -.
DR OrthoDB; 1218538at2759; -.
DR PhylomeDB; Q9JLT6; -.
DR TreeFam; TF102047; -.
DR Reactome; R-RNO-111447; Activation of BAD and translocation to mitochondria.
DR Reactome; R-RNO-111452; Activation and oligomerization of BAK protein.
DR Reactome; R-RNO-111453; BH3-only proteins associate with and inactivate anti-apoptotic BCL-2 members.
DR Reactome; R-RNO-114294; Activation, translocation and oligomerization of BAX.
DR Reactome; R-RNO-75108; Activation, myristolyation of BID and translocation to mitochondria.
DR PRO; PR:Q9JLT6; -.
DR Proteomes; UP000002494; Chromosome 4.
DR Bgee; ENSRNOG00000012439; Expressed in thymus and 19 other tissues.
DR ExpressionAtlas; Q9JLT6; baseline and differential.
DR Genevisible; Q9JLT6; RN.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
DR GO; GO:0032592; C:integral component of mitochondrial membrane; ISO:RGD.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0005741; C:mitochondrial outer membrane; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:RGD.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:RGD.
DR GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; ISO:RGD.
DR GO; GO:0008637; P:apoptotic mitochondrial changes; IBA:GO_Central.
DR GO; GO:0007420; P:brain development; IEP:RGD.
DR GO; GO:0090150; P:establishment of protein localization to membrane; ISO:RGD.
DR GO; GO:0097191; P:extrinsic apoptotic signaling pathway; ISO:RGD.
DR GO; GO:0034349; P:glial cell apoptotic process; IEP:RGD.
DR GO; GO:0097284; P:hepatocyte apoptotic process; ISS:UniProtKB.
DR GO; GO:0042775; P:mitochondrial ATP synthesis coupled electron transport; ISO:RGD.
DR GO; GO:0097345; P:mitochondrial outer membrane permeabilization; ISO:RGD.
DR GO; GO:1902230; P:negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage; ISO:RGD.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISO:RGD.
DR GO; GO:2001235; P:positive regulation of apoptotic signaling pathway; ISO:RGD.
DR GO; GO:0034263; P:positive regulation of autophagy in response to ER overload; IMP:RGD.
DR GO; GO:2001238; P:positive regulation of extrinsic apoptotic signaling pathway; ISO:RGD.
DR GO; GO:2000271; P:positive regulation of fibroblast apoptotic process; ISO:RGD.
DR GO; GO:2001244; P:positive regulation of intrinsic apoptotic signaling pathway; ISO:RGD.
DR GO; GO:0010918; P:positive regulation of mitochondrial membrane potential; ISO:RGD.
DR GO; GO:0031334; P:positive regulation of protein-containing complex assembly; ISO:RGD.
DR GO; GO:0090200; P:positive regulation of release of cytochrome c from mitochondria; ISS:UniProtKB.
DR GO; GO:0006626; P:protein targeting to mitochondrion; ISO:RGD.
DR GO; GO:0065003; P:protein-containing complex assembly; ISO:RGD.
DR GO; GO:0042981; P:regulation of apoptotic process; ISO:RGD.
DR GO; GO:0042127; P:regulation of cell population proliferation; ISO:RGD.
DR GO; GO:2000045; P:regulation of G1/S transition of mitotic cell cycle; ISO:RGD.
DR GO; GO:1902108; P:regulation of mitochondrial membrane permeability involved in apoptotic process; ISO:RGD.
DR GO; GO:0001836; P:release of cytochrome c from mitochondria; IDA:RGD.
DR GO; GO:0032355; P:response to estradiol; IEP:RGD.
DR GO; GO:0002931; P:response to ischemia; IEP:RGD.
DR GO; GO:0097435; P:supramolecular fiber organization; ISO:RGD.
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 Acetylation; Apoptosis; Cytoplasm; Membrane; Mitochondrion;
KW Mitochondrion outer membrane; Phosphoprotein; Reference proteome;
KW Ubl conjugation.
FT CHAIN 1..196
FT /note="BH3-interacting domain death agonist"
FT /id="PRO_0000223369"
FT CHAIN 61..196
FT /note="BH3-interacting domain death agonist p15"
FT /evidence="ECO:0000250|UniProtKB:P70444"
FT /id="PRO_0000223370"
FT CHAIN 77..196
FT /note="BH3-interacting domain death agonist p13"
FT /evidence="ECO:0000250|UniProtKB:P70444"
FT /id="PRO_0000223371"
FT CHAIN 100..196
FT /note="BH3-interacting domain death agonist p11"
FT /evidence="ECO:0000250|UniProtKB:P70444"
FT /id="PRO_0000223372"
FT MOTIF 87..101
FT /note="BH3"
FT /evidence="ECO:0000250|UniProtKB:P70444"
FT SITE 60..61
FT /note="Cleavage"
FT /evidence="ECO:0000250|UniProtKB:P70444"
FT SITE 76..77
FT /note="Cleavage"
FT /evidence="ECO:0000250|UniProtKB:P70444"
FT SITE 99..100
FT /note="Cleavage"
FT /evidence="ECO:0000250|UniProtKB:P70444"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P55957"
FT MOD_RES 79
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT CONFLICT 176
FT /note="V -> A (in Ref. 2; AAF61422)"
FT /evidence="ECO:0000305"
FT CONFLICT 185
FT /note="S -> F (in Ref. 2; AAF61422)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 196 AA; 22249 MW; C5F6AD2F5D9B52E3 CRC64;
MDSEVSNGSG LGAEHITNLL VFGFLRNNDR DFHQELEVLG QELPVQVYLE GDREDELQTD
GSRASRSFYH GRIEPDSESQ DEVIHNIARH LAQAGDELDH SIQPTLVRQL AAQFMNGSLS
EEDKRNCLAK ALDEVKTSFP RDMENDKAML IMTMLLAKKV ASHAPSLLRD VFRTTVNFIN
QNLFSYVRDL VRNEMD
