ID A0A0D9S1G3_CHLSB Unreviewed; 450 AA.
AC A0A0D9S1G3;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=Beclin-1 {ECO:0000256|ARBA:ARBA00018490, ECO:0000256|RuleBase:RU367123};
GN Name=BECN1 {ECO:0000313|Ensembl:ENSCSAP00000014702.1};
OS Chlorocebus sabaeus (Green monkey) (Cercopithecus sabaeus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Chlorocebus.
OX NCBI_TaxID=60711 {ECO:0000313|Ensembl:ENSCSAP00000014702.1, ECO:0000313|Proteomes:UP000029965};
RN [1] {ECO:0000313|Ensembl:ENSCSAP00000014702.1, ECO:0000313|Proteomes:UP000029965}
RP NUCLEOTIDE SEQUENCE.
RA Warren W., Wilson R.K.;
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCSAP00000014702.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Beclin-1-C 35 kDa localized to mitochondria can promote
CC apoptosis; it induces the mitochondrial translocation of BAX and the
CC release of proapoptotic factors. {ECO:0000256|ARBA:ARBA00025121}.
CC -!- FUNCTION: Plays a central role in autophagy.
CC {ECO:0000256|RuleBase:RU367123}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU367123}. Golgi
CC apparatus, trans-Golgi network membrane {ECO:0000256|ARBA:ARBA00004150,
CC ECO:0000256|RuleBase:RU367123}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004150, ECO:0000256|RuleBase:RU367123}.
CC Endosome membrane {ECO:0000256|ARBA:ARBA00004481,
CC ECO:0000256|RuleBase:RU367123}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004481, ECO:0000256|RuleBase:RU367123}.
CC Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004406,
CC ECO:0000256|RuleBase:RU367123}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004406, ECO:0000256|RuleBase:RU367123}.
CC Mitochondrion membrane {ECO:0000256|ARBA:ARBA00004318,
CC ECO:0000256|RuleBase:RU367123}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004318, ECO:0000256|RuleBase:RU367123}.
CC Cytoplasmic vesicle, autophagosome {ECO:0000256|RuleBase:RU367123}.
CC Membrane {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004170}. Nucleus
CC {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the beclin family.
CC {ECO:0000256|ARBA:ARBA00005965, ECO:0000256|RuleBase:RU367123}.
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DR EMBL; AQIB01145567; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_008010774.1; XM_008012583.1.
DR RefSeq; XP_008010775.1; XM_008012584.1.
DR AlphaFoldDB; A0A0D9S1G3; -.
DR SMR; A0A0D9S1G3; -.
DR STRING; 60711.ENSCSAP00000014702; -.
DR Ensembl; ENSCSAT00000001374.1; ENSCSAP00000014702.1; ENSCSAG00000003347.1.
DR GeneID; 103243387; -.
DR CTD; 8678; -.
DR eggNOG; KOG2751; Eukaryota.
DR GeneTree; ENSGT00390000008164; -.
DR OMA; EWDVYKA; -.
DR OrthoDB; 11439at2759; -.
DR BioGRID-ORCS; 103243387; 5 hits in 16 CRISPR screens.
DR Proteomes; UP000029965; Chromosome 16.
DR Bgee; ENSCSAG00000003347; Expressed in blood and 7 other cell types or tissues.
DR GO; GO:0005776; C:autophagosome; IEA:UniProtKB-SubCell.
DR GO; GO:0032473; C:cytoplasmic side of mitochondrial outer membrane; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-UniRule.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016604; C:nuclear body; IEA:Ensembl.
DR GO; GO:0045335; C:phagocytic vesicle; IEA:Ensembl.
DR GO; GO:0035032; C:phosphatidylinositol 3-kinase complex, class III; IEA:Ensembl.
DR GO; GO:0005802; C:trans-Golgi network; IEA:Ensembl.
DR GO; GO:0051020; F:GTPase binding; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0043548; F:phosphatidylinositol 3-kinase binding; IEA:Ensembl.
DR GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IEA:Ensembl.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:Ensembl.
DR GO; GO:0050435; P:amyloid-beta metabolic process; IEA:Ensembl.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0000045; P:autophagosome assembly; IEA:UniProtKB-UniRule.
DR GO; GO:0097352; P:autophagosome maturation; IEA:Ensembl.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0042149; P:cellular response to glucose starvation; IEA:Ensembl.
DR GO; GO:0002753; P:cytoplasmic pattern recognition receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR GO; GO:0045022; P:early endosome to late endosome transport; IEA:UniProtKB-UniRule.
DR GO; GO:0043652; P:engulfment of apoptotic cell; IEA:Ensembl.
DR GO; GO:0007040; P:lysosome organization; IEA:Ensembl.
DR GO; GO:0000423; P:mitophagy; IEA:Ensembl.
DR GO; GO:0007080; P:mitotic metaphase chromosome alignment; IEA:Ensembl.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl.
DR GO; GO:1902902; P:negative regulation of autophagosome assembly; IEA:Ensembl.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IEA:Ensembl.
DR GO; GO:2000378; P:negative regulation of reactive oxygen species metabolic process; IEA:Ensembl.
DR GO; GO:0048666; P:neuron development; IEA:Ensembl.
DR GO; GO:0036092; P:phosphatidylinositol-3-phosphate biosynthetic process; IEA:Ensembl.
DR GO; GO:1902425; P:positive regulation of attachment of mitotic spindle microtubules to kinetochore; IEA:Ensembl.
DR GO; GO:0010508; P:positive regulation of autophagy; IEA:Ensembl.
DR GO; GO:0010613; P:positive regulation of cardiac muscle hypertrophy; IEA:Ensembl.
DR GO; GO:2001244; P:positive regulation of intrinsic apoptotic signaling pathway; IEA:Ensembl.
DR GO; GO:0065003; P:protein-containing complex assembly; IEA:Ensembl.
DR GO; GO:0032801; P:receptor catabolic process; IEA:Ensembl.
DR GO; GO:0032465; P:regulation of cytokinesis; IEA:Ensembl.
DR GO; GO:0098780; P:response to mitochondrial depolarisation; IEA:Ensembl.
DR Gene3D; 6.10.250.3110; -; 1.
DR Gene3D; 1.10.418.40; Autophagy protein 6/Beclin 1; 1.
DR InterPro; IPR007243; Atg6/Beclin.
DR InterPro; IPR038274; Atg6/Beclin_C_sf.
DR InterPro; IPR041691; Atg6/beclin_CC.
DR InterPro; IPR040455; Atg6_BARA.
DR InterPro; IPR029318; BH3_dom.
DR PANTHER; PTHR12768; BECLIN 1; 1.
DR PANTHER; PTHR12768:SF6; BECLIN-1; 1.
DR Pfam; PF04111; APG6; 1.
DR Pfam; PF17675; APG6_N; 1.
DR Pfam; PF15285; BH3; 1.
PE 3: Inferred from homology;
KW Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW Antiviral defense {ECO:0000256|ARBA:ARBA00023118};
KW Apoptosis {ECO:0000256|ARBA:ARBA00022703};
KW Autophagy {ECO:0000256|ARBA:ARBA00023006, ECO:0000256|RuleBase:RU367123};
KW Cell cycle {ECO:0000256|ARBA:ARBA00023306};
KW Cell division {ECO:0000256|ARBA:ARBA00022618};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|RuleBase:RU367123};
KW Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00023329,
KW ECO:0000256|RuleBase:RU367123};
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824,
KW ECO:0000256|RuleBase:RU367123};
KW Endosome {ECO:0000256|ARBA:ARBA00022753, ECO:0000256|RuleBase:RU367123};
KW Golgi apparatus {ECO:0000256|ARBA:ARBA00023034,
KW ECO:0000256|RuleBase:RU367123};
KW Isopeptide bond {ECO:0000256|ARBA:ARBA00022499};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU367123};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128,
KW ECO:0000256|RuleBase:RU367123}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000029965};
KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}.
FT DOMAIN 105..129
FT /note="Beclin-1 BH3"
FT /evidence="ECO:0000259|Pfam:PF15285"
FT DOMAIN 135..261
FT /note="Atg6/beclin coiled-coil"
FT /evidence="ECO:0000259|Pfam:PF17675"
FT DOMAIN 264..445
FT /note="Atg6 BARA"
FT /evidence="ECO:0000259|Pfam:PF04111"
FT REGION 48..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 145..267
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 450 AA; 51908 MW; 230B01FFB87756C0 CRC64;
MEGSKTSNNS TMQVSFVCQR CSQPLKLDTS FKILDRVTIQ ELTAPLLTTA QAKPGETQEE
ETNSGEEPFI ETPRQDGVSR RFIPPARMMS TESANSFTLI GEASDGGTME NLSRRLKVTG
DLFDIMSGQT DVDHPLCEEC TDTLLDQLDT QLNVTENECQ NYKRCLEILE QMNEDDSEQL
QMELKELALE EERLIQELED VEKNRKIVAE NLEKVQAEAE RLDQEEAQYQ REYSEFKRQQ
LELDDELKSV ENQMRYAQIQ LDKLKKTNVF NATFHIWHSG QFGTINNFRL GRLPSVPVEW
NEINAAWGQT VLLLHALANK MGLKFQRYRL VPYGNHSYLE SLTDKSKELP LYCSGGLRFF
WDNKFDHAMV AFLDCVQQFK EEVEKGETRF CLPYRMDVEK GKIEDTGGSG GSYSIKTQFN
SEEQWTKALK FMLTNLKWGL AWVSSQFYNK
//
