ID A0A485PK19_LYNPA Unreviewed; 235 AA.
AC A0A485PK19;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 18-JUN-2025, entry version 20.
DE RecName: Full=Apoptosis regulator Bcl-2 {ECO:0000256|ARBA:ARBA00018573};
GN ORFNames=LYPA_23C017886 {ECO:0000313|EMBL:VFV45177.1};
OS Lynx pardinus (Iberian lynx) (Felis pardina).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Lynx.
OX NCBI_TaxID=191816 {ECO:0000313|EMBL:VFV45177.1, ECO:0000313|Proteomes:UP000386466};
RN [1] {ECO:0000313|EMBL:VFV45177.1, ECO:0000313|Proteomes:UP000386466}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Alioto T., Alioto T.;
RL Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Suppresses apoptosis in a variety of cell systems including
CC factor-dependent lymphohematopoietic and neural cells. Regulates cell
CC death by controlling the mitochondrial membrane permeability. Appears
CC to function in a feedback loop system with caspases. Inhibits caspase
CC activity either by preventing the release of cytochrome c from the
CC mitochondria and/or by binding to the apoptosis-activating factor
CC (APAF-1). Also acts as an inhibitor of autophagy: interacts with BECN1
CC and AMBRA1 during non-starvation conditions and inhibits their
CC autophagy function. May attenuate inflammation by impairing NLRP1-
CC inflammasome activation, hence CASP1 activation and IL1B release.
CC {ECO:0000256|ARBA:ARBA00045768}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004389}; Single-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004389}. Mitochondrion
CC outer membrane {ECO:0000256|ARBA:ARBA00004572}; Single-pass membrane
CC protein {ECO:0000256|ARBA:ARBA00004572}. Nucleus membrane
CC {ECO:0000256|ARBA:ARBA00004590}; Single-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004590}.
CC -!- SIMILARITY: Belongs to the Bcl-2 family.
CC {ECO:0000256|ARBA:ARBA00009458}.
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DR EMBL; CAAGRJ010037053; VFV45177.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A485PK19; -.
DR Proteomes; UP000386466; Unassembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0051400; F:BH domain binding; IEA:TreeGrafter.
DR GO; GO:0097192; P:extrinsic apoptotic signaling pathway in absence of ligand; IEA:TreeGrafter.
DR GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; IEA:TreeGrafter.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IEA:InterPro.
DR GO; GO:0001836; P:release of cytochrome c from mitochondria; IEA:TreeGrafter.
DR CDD; cd06845; Bcl-2_like; 1.
DR FunFam; 1.10.437.10:FF:000006; Apoptosis regulator Bcl-2; 1.
DR Gene3D; 1.10.437.10; Blc2-like; 1.
DR InterPro; IPR013278; Apop_reg_Bcl2.
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; IPR004725; Bcl2/BclX.
DR InterPro; IPR020717; Bcl2_BH1_motif_CS.
DR InterPro; IPR020726; Bcl2_BH2_motif_CS.
DR InterPro; IPR020728; Bcl2_BH3_motif_CS.
DR InterPro; IPR003093; Bcl2_BH4.
DR InterPro; IPR020731; Bcl2_BH4_motif_CS.
DR NCBIfam; TIGR00865; bcl-2; 1.
DR PANTHER; PTHR11256:SF11; APOPTOSIS REGULATOR BCL-2; 1.
DR PANTHER; PTHR11256; BCL-2 RELATED; 1.
DR Pfam; PF00452; Bcl-2; 1.
DR Pfam; PF02180; BH4; 1.
DR PRINTS; PR01863; APOPREGBCL2.
DR PRINTS; PR01862; BCL2FAMILY.
DR SMART; SM00337; BCL; 1.
DR SMART; SM00265; BH4; 1.
DR SUPFAM; SSF56854; Bcl-2 inhibitors of programmed cell death; 1.
DR PROSITE; PS50062; BCL2_FAMILY; 1.
DR PROSITE; PS01080; BH1; 1.
DR PROSITE; PS01258; BH2; 1.
DR PROSITE; PS01259; BH3; 1.
DR PROSITE; PS01260; BH4_1; 1.
DR PROSITE; PS50063; BH4_2; 1.
PE 3: Inferred from homology;
KW Apoptosis {ECO:0000256|ARBA:ARBA00022703, ECO:0000256|PROSITE-
KW ProRule:PRU00025}; Autophagy {ECO:0000256|ARBA:ARBA00023006};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Mitochondrion outer membrane {ECO:0000256|ARBA:ARBA00022787};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000386466};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 210..232
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 11..30
FT /note="Apoptosis regulator Bcl-2 family BH4"
FT /evidence="ECO:0000259|PROSITE:PS50063"
FT REGION 34..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 11..30
FT /note="BH4"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00025"
FT COMPBIAS 34..61
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 235 AA; 25640 MW; 7CC673F3FA9D9EC5 CRC64;
MAHAGRTGYD NREIVMKYIH YKLSQRGYEW DAGDAGAAPP GAAPAPGIFS SQPGRTPAPA
RTSPPPPPVA PAAAAAAAGP ALSPVPPVVH LTLRQAGDDF SRRYRRDFAE MSSQLHLTPF
TARGRFATVV EELFRDGVNW GRIVAFFEFG GVMCVESVNR EMSPLVDNIA LWMTEYLNRH
LHTWIQDNGG WDAFVELYGP SMQPLFDFSW LSLKALLSLA LVGACITLGA YLGHK
//
