BID_PIG
ID BID_PIG Reviewed; 192 AA.
AC Q4JHS0; Q56VC1;
DT 21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2005, sequence version 1.
DT 03-AUG-2022, entry version 88.
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 Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Diaz-Gil G., Fernandez-Zapatero P., Hernaez B., Bouillet P.,
RA Escribano J.M., Alonso C.;
RT "A179L, a viral apoptosis inhibitor acting via interaction with
RT proapoptotic cellular Bcl-2 proteins.";
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Sakamaki K.;
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000250|UniProtKB:Q9JLT6}.
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}.
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; DQ087226; AAY82900.1; -; mRNA.
DR EMBL; AY521564; AAT01900.1; -; mRNA.
DR RefSeq; NP_001025706.1; NM_001030535.1.
DR RefSeq; XP_005664186.1; XM_005664129.2.
DR RefSeq; XP_005664187.1; XM_005664130.2.
DR RefSeq; XP_013853374.1; XM_013997920.1.
DR PDB; 5UA4; X-ray; 2.60 A; B=73-106.
DR PDBsum; 5UA4; -.
DR AlphaFoldDB; Q4JHS0; -.
DR SMR; Q4JHS0; -.
DR STRING; 9823.ENSSSCP00000000817; -.
DR PaxDb; Q4JHS0; -.
DR PeptideAtlas; Q4JHS0; -.
DR PRIDE; Q4JHS0; -.
DR Ensembl; ENSSSCT00000000833; ENSSSCP00000000817; ENSSSCG00000000769.
DR Ensembl; ENSSSCT00005012978; ENSSSCP00005007675; ENSSSCG00005008383.
DR Ensembl; ENSSSCT00015043931; ENSSSCP00015017367; ENSSSCG00015031932.
DR Ensembl; ENSSSCT00040095675; ENSSSCP00040042415; ENSSSCG00040069597.
DR Ensembl; ENSSSCT00055050354; ENSSSCP00055040249; ENSSSCG00055025501.
DR Ensembl; ENSSSCT00065110276; ENSSSCP00065049686; ENSSSCG00065079295.
DR Ensembl; ENSSSCT00070031406; ENSSSCP00070026177; ENSSSCG00070015991.
DR GeneID; 594852; -.
DR KEGG; ssc:594852; -.
DR CTD; 637; -.
DR VGNC; VGNC:85824; BID.
DR eggNOG; ENOG502SAN7; Eukaryota.
DR GeneTree; ENSGT00390000002868; -.
DR HOGENOM; CLU_090524_0_0_1; -.
DR InParanoid; Q4JHS0; -.
DR OrthoDB; 1218538at2759; -.
DR TreeFam; TF102047; -.
DR Reactome; R-SSC-111452; Activation and oligomerization of BAK protein.
DR Reactome; R-SSC-114294; Activation, translocation and oligomerization of BAX.
DR Reactome; R-SSC-75108; Activation, myristolyation of BID and translocation to mitochondria.
DR Proteomes; UP000008227; Chromosome 5.
DR Proteomes; UP000314985; Chromosome 5.
DR Bgee; ENSSSCG00000000769; Expressed in blood and 43 other tissues.
DR ExpressionAtlas; Q4JHS0; baseline and differential.
DR Genevisible; Q4JHS0; SS.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005741; C:mitochondrial outer membrane; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; IBA:GO_Central.
DR GO; GO:0008637; P:apoptotic mitochondrial changes; IBA:GO_Central.
DR GO; GO:0097284; P:hepatocyte apoptotic process; ISS:UniProtKB.
DR GO; GO:2001238; P:positive regulation of extrinsic apoptotic signaling pathway; IBA:GO_Central.
DR GO; GO:2001244; P:positive regulation of intrinsic apoptotic signaling pathway; IBA:GO_Central.
DR GO; GO:0090200; P:positive regulation of release of cytochrome c from mitochondria; ISS:UniProtKB.
DR Gene3D; 1.10.437.10; -; 1.
DR InterPro; IPR036834; Bcl-2-like_sf.
DR InterPro; IPR010479; BID.
DR PANTHER; PTHR35447; PTHR35447; 1.
DR Pfam; PF06393; BID; 1.
DR PIRSF; PIRSF038018; BID; 1.
DR SUPFAM; SSF56854; SSF56854; 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..192
FT /note="BH3-interacting domain death agonist"
FT /id="PRO_0000223368"
FT CHAIN 58..192
FT /note="BH3-interacting domain death agonist p15"
FT /evidence="ECO:0000250|UniProtKB:P70444"
FT /id="PRO_0000445272"
FT CHAIN 73..192
FT /note="BH3-interacting domain death agonist p13"
FT /evidence="ECO:0000250|UniProtKB:P70444"
FT /id="PRO_0000445273"
FT CHAIN 96..192
FT /note="BH3-interacting domain death agonist p11"
FT /evidence="ECO:0000250|UniProtKB:P70444"
FT /id="PRO_0000445274"
FT MOTIF 83..97
FT /note="BH3"
FT /evidence="ECO:0000250|UniProtKB:P70444"
FT SITE 57..58
FT /note="Cleavage"
FT /evidence="ECO:0000250|UniProtKB:P70444"
FT SITE 72..73
FT /note="Cleavage"
FT /evidence="ECO:0000250|UniProtKB:P70444"
FT SITE 95..96
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 75
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P55957"
FT CONFLICT 190..192
FT /note="EMD -> VRASVAAPHVSLFPSH (in Ref. 2; AAT01900)"
FT /evidence="ECO:0000305"
FT HELIX 76..95
FT /evidence="ECO:0007829|PDB:5UA4"
SQ SEQUENCE 192 AA; 21569 MW; 6D379006E938EF19 CRC64;
MDSKVSNGSS LQDERITNLL VFGFLQSCPH ASFHKELEVL GHELPVHTSG SDELQTDGNR
CSYFMEDAAE TDSESQEAVI RDIARHLARI GDRMEYGIRP GLVDSLAAQF RNQSLSEEDR
RQGLAAVLQQ LVHSYPADMG QEKTLLVLTM LLARKVAEHS PALLRDVFHT TVNFINQNLL
TYLRNLVQSE MD
