ID H0X1K7_OTOGA Unreviewed; 453 AA.
AC H0X1K7;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE RecName: Full=Beclin-1 {ECO:0000256|ARBA:ARBA00018490, ECO:0000256|RuleBase:RU367123};
GN Name=BECN1 {ECO:0000313|Ensembl:ENSOGAP00000008882.2};
OS Otolemur garnettii (Small-eared galago) (Garnett's greater bushbaby).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Strepsirrhini; Lorisiformes;
OC Galagidae; Otolemur.
OX NCBI_TaxID=30611 {ECO:0000313|Ensembl:ENSOGAP00000008882.2, ECO:0000313|Proteomes:UP000005225};
RN [1] {ECO:0000313|Proteomes:UP000005225}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG The Broad Institute Genome Sequencing Platform;
RA Di Palma F., Johnson J., Lander E.S., Lindblad-Toh K., Jaffe D.B.,
RA Gnerre S., MacCallum I., Przybylski D., Ribeiro F.J., Burton J.N.,
RA Walker B.J., Sharpe T., Hall G.;
RT "Version 3 of the genome sequence of Otolemur garnettii (Bushbaby).";
RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSOGAP00000008882.2}
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; AAQR03042662; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAQR03042663; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAQR03042664; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; H0X1K7; -.
DR STRING; 30611.ENSOGAP00000008882; -.
DR Ensembl; ENSOGAT00000009938.2; ENSOGAP00000008882.2; ENSOGAG00000009933.2.
DR eggNOG; KOG2751; Eukaryota.
DR GeneTree; ENSGT00390000008164; -.
DR HOGENOM; CLU_024219_4_1_1; -.
DR InParanoid; H0X1K7; -.
DR OMA; EWDVYKA; -.
DR TreeFam; TF314282; -.
DR Proteomes; UP000005225; Unassembled WGS sequence.
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:UP000005225};
KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}.
FT DOMAIN 103..127
FT /note="Beclin-1 BH3"
FT /evidence="ECO:0000259|Pfam:PF15285"
FT DOMAIN 133..259
FT /note="Atg6/beclin coiled-coil"
FT /evidence="ECO:0000259|Pfam:PF17675"
FT DOMAIN 262..448
FT /note="Atg6 BARA"
FT /evidence="ECO:0000259|Pfam:PF04111"
FT COILED 143..265
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 453 AA; 52030 MW; A99FA38520FE22B2 CRC64;
MEGSKTSNST MQVSFVCQRC SQPLKLDTSF KILDRVTIQE LTAPLLTTAQ VKPGETQEEE
ANSGEEPFIE TRQDGVSRRF IPPARMMSTE SANSFTLIGE ASDGGTMENL SRRLKVTGDL
FDIMSGQTDV DHPLCEECTD TLLDQLDTQL NVTENECQNY KRCLEILEQM NEDDSEQLQM
ELKELALEEE RLIQELEDVE KNRKIVAENL ETVQAEAERL DQEEAQYQRE YSEFKRQQLE
LDDELKSVEN QMRYAQMQLD KLKKTNVFNA TFHIWPCDGI GIVGIGILEL GDIHSSKNAT
LHLPAMWEMI WVKEGGIVNK ETGSRHLHSR YRLVPYGNHS YLESLTDKSK ELPLYCSGGL
RFFWDNKFDH AMVAFLDCVQ QFKEEVEKGE TRFCLPYRMD VEKGKIEDTG GSGGSYSIKT
QFNSEEQWTK ALKFMLTNLK WGLAWVSSQF YNK
//
