ID A0A2K5ZSR0_MANLE Unreviewed; 485 AA.
AC A0A2K5ZSR0;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE SubName: Full=BCL2 like 13 {ECO:0000313|Ensembl:ENSMLEP00000030813.1};
GN Name=BCL2L13 {ECO:0000313|Ensembl:ENSMLEP00000030813.1};
OS Mandrillus leucophaeus (Drill) (Papio leucophaeus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Mandrillus.
OX NCBI_TaxID=9568 {ECO:0000313|Ensembl:ENSMLEP00000030813.1, ECO:0000313|Proteomes:UP000233140};
RN [1] {ECO:0000313|Ensembl:ENSMLEP00000030813.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the Bcl-2 family.
CC {ECO:0000256|ARBA:ARBA00009458}.
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DR RefSeq; XP_011840014.1; XM_011984624.1.
DR AlphaFoldDB; A0A2K5ZSR0; -.
DR Ensembl; ENSMLET00000054378.1; ENSMLEP00000030813.1; ENSMLEG00000039559.1.
DR GeneID; 105542918; -.
DR KEGG; mleu:105542918; -.
DR CTD; 23786; -.
DR GeneTree; ENSGT00390000015552; -.
DR OMA; MHEALQT; -.
DR OrthoDB; 5399330at2759; -.
DR Proteomes; UP000233140; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0042981; P:regulation of apoptotic process; IEA:InterPro.
DR Gene3D; 1.10.437.10; Blc2-like; 1.
DR InterPro; IPR036834; Bcl-2-like_sf.
DR InterPro; IPR046371; Bcl-2_BH1-3.
DR InterPro; IPR002475; Bcl2-like.
DR InterPro; IPR042398; BCL2L13.
DR PANTHER; PTHR15758; BCL-2-LIKE PROTEIN 13; 1.
DR PANTHER; PTHR15758:SF2; BCL-2-LIKE PROTEIN 13; 1.
DR Pfam; PF00452; Bcl-2; 1.
DR SUPFAM; SSF56854; Bcl-2 inhibitors of programmed cell death; 1.
DR PROSITE; PS50062; BCL2_FAMILY; 1.
PE 3: Inferred from homology;
KW Apoptosis {ECO:0000256|ARBA:ARBA00022703};
KW Coiled coil {ECO:0000256|SAM:Coils}; Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000233140};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 460..482
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 104..200
FT /note="Bcl-2 Bcl-2 homology region 1-3"
FT /evidence="ECO:0000259|Pfam:PF00452"
FT REGION 218..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 401..448
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 53..80
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 224..248
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 410..425
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 485 AA; 52513 MW; 9AC4DEFE19AE8CE3 CRC64;
MASSSTVPLG FHYETKYVVL SYLGLLSQEK LQEQHLSSPQ GVQLDIASQS LDQEILLKVK
TEIEEELKSL DKEISEAFTS TGFDRHTSPV FSPANPESSM EDCLAHLGEK VSQELKEPLH
TALQMLLSQP VTYQAFRECT LETTVHASGW NKILVPLVLL RHMLLELTRR GQEPLSALLQ
FGVTYLEDYS AEYIIQQGGW GTVFSLESEE EEYPGITAED SNDIYILPSD NSGQVSPPES
PTVTTSWQSE SLPVSLSASQ SWHTESLPVS LGPESWQQIA MDPEEVKSLD SNGAGEKSEN
NSSNSDIVHV EKEEVPEGME EAAVASVVLP AGELPEALPE APAPLLPHIT ATSLLGTREP
DTEVITVEKS SPATSLFVEL DEEEVKAATV EPTEVKEVVP APEPTETLLS EKETNAREES
LGEELSPPGE MKPLPLSEGK SRLSPAGEMK PLPLSEGKSI LLFGGAAAVA ILAVAIGVAL
ALRKK
//
