ID A0A401NJ83_SCYTO Unreviewed; 194 AA.
AC A0A401NJ83;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=BH3-interacting domain death agonist {ECO:0000256|ARBA:ARBA00015802, ECO:0000256|PIRNR:PIRNR038018};
GN ORFNames=scyTo_0004020 {ECO:0000313|EMBL:GCB60907.1};
OS Scyliorhinus torazame (Cloudy catshark).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC Elasmobranchii; Galeomorphii; Galeoidea; Carcharhiniformes; Scyliorhinidae;
OC Scyliorhinus.
OX NCBI_TaxID=75743 {ECO:0000313|EMBL:GCB60907.1, ECO:0000313|Proteomes:UP000288216};
RN [1] {ECO:0000313|EMBL:GCB60907.1, ECO:0000313|Proteomes:UP000288216}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=30297745; DOI=.1038/s41559-018-0673-5;
RA Hara Y, Yamaguchi K, Onimaru K, Kadota M, Koyanagi M, Keeley SD, Tatsumi K,
RA Tanaka K, Motone F, Kageyama Y, Nozu R, Adachi N, Nishimura O, Nakagawa R,
RA Tanegashima C, Kiyatake I, Matsumoto R, Murakumo K, Nishida K, Terakita A,
RA Kuratani S, Sato K, Hyodo S Kuraku.S.;
RT "Shark genomes provide insights into elasmobranch evolution and the origin
RT of vertebrates.";
RL Nat. Ecol. Evol. 2:1761-1771(2018).
CC -!- FUNCTION: Induces caspases and apoptosis. Counters the protective
CC effect of BCL2. {ECO:0000256|PIRNR:PIRNR038018}.
CC -!- SUBUNIT: Forms heterodimers either with the pro-apoptotic protein BAX
CC or the anti-apoptotic protein BCL2. {ECO:0000256|PIRNR:PIRNR038018}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|PIRNR:PIRNR038018}.
CC Mitochondrion outer membrane {ECO:0000256|PIRNR:PIRNR038018}. Membrane
CC {ECO:0000256|ARBA:ARBA00004370}.
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:0000256|PIRNR:PIRNR038018}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GCB60907.1}.
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DR EMBL; BFAA01001149; GCB60907.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A401NJ83; -.
DR STRING; 75743.A0A401NJ83; -.
DR OMA; LMNNLAM; -.
DR Proteomes; UP000288216; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-UniRule.
DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008637; P:apoptotic mitochondrial changes; IEA:UniProtKB-UniRule.
DR GO; GO:2001238; P:positive regulation of extrinsic apoptotic signaling pathway; IEA:UniProtKB-UniRule.
DR GO; GO:2001244; P:positive regulation of intrinsic apoptotic signaling pathway; IEA:UniProtKB-UniRule.
DR Gene3D; 1.10.437.10; Blc2-like; 1.
DR InterPro; IPR036834; Bcl-2-like_sf.
DR InterPro; IPR010479; BID.
DR PANTHER; PTHR35447; BH3-INTERACTING DOMAIN DEATH AGONIST; 1.
DR PANTHER; PTHR35447:SF1; BH3-INTERACTING DOMAIN DEATH AGONIST; 1.
DR Pfam; PF06393; BID; 1.
DR PIRSF; PIRSF038018; BID; 1.
DR SUPFAM; SSF56854; Bcl-2 inhibitors of programmed cell death; 1.
PE 4: Predicted;
KW Apoptosis {ECO:0000256|PIRNR:PIRNR038018};
KW Cytoplasm {ECO:0000256|PIRNR:PIRNR038018};
KW Membrane {ECO:0000256|PIRNR:PIRNR038018};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00022787,
KW ECO:0000256|PIRNR:PIRNR038018};
KW Mitochondrion outer membrane {ECO:0000256|ARBA:ARBA00022787,
KW ECO:0000256|PIRNR:PIRNR038018};
KW Reference proteome {ECO:0000313|Proteomes:UP000288216}.
SQ SEQUENCE 194 AA; 22479 MW; 033F0BDC55C2F7F5 CRC64;
MSGRLTHPFA EQTQLILLKF LQEKKVENRI YQQEIEKLET ELGSGPRFDD DIQTDGHCPP
GSLHAADYPG VEAVNEELYR QIAAHLADIG DRLDQSINRD LVEEFIRETE RIQPQMDGTI
IMSSMITRLT NQRIDATQDM PQEKVFLLLA LMLFKKTVVE KPVLLSRIFR TTVQYINNRL
QDYIRNIGGW QNIH
//