ID A0A2K6GSR2_PROCO Unreviewed; 448 AA.
AC A0A2K6GSR2;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Beclin-1 {ECO:0000256|ARBA:ARBA00018490, ECO:0000256|RuleBase:RU367123};
GN Name=BECN1 {ECO:0000313|Ensembl:ENSPCOP00000029268.1};
OS Propithecus coquereli (Coquerel's sifaka) (Propithecus verreauxi
OS coquereli).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Strepsirrhini; Lemuriformes;
OC Indriidae; Propithecus.
OX NCBI_TaxID=379532 {ECO:0000313|Ensembl:ENSPCOP00000029268.1, ECO:0000313|Proteomes:UP000233160};
RN [1] {ECO:0000313|Ensembl:ENSPCOP00000029268.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 RefSeq; XP_012512150.1; XM_012656696.1.
DR AlphaFoldDB; A0A2K6GSR2; -.
DR STRING; 379532.ENSPCOP00000029268; -.
DR Ensembl; ENSPCOT00000040204.1; ENSPCOP00000029268.1; ENSPCOG00000027315.1.
DR GeneID; 105820245; -.
DR KEGG; pcoq:105820245; -.
DR CTD; 8678; -.
DR GeneTree; ENSGT00390000008164; -.
DR OMA; EWDVYKA; -.
DR OrthoDB; 11439at2759; -.
DR Proteomes; UP000233160; Unplaced.
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:Ensembl.
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:0000045; P:autophagosome assembly; IEA:Ensembl.
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:0045022; P:early endosome to late endosome transport; IEA:Ensembl.
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 GO; GO:0051707; P:response to other organism; 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:UP000233160};
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..443
FT /note="Atg6 BARA"
FT /evidence="ECO:0000259|Pfam:PF04111"
FT REGION 47..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 143..265
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 448 AA; 51715 MW; 6F25155D7062F52D CRC64;
MEGSKTSNST MQVSFVCQRC SQPLKLDTSF KILDRVTIQE LTAPLLTTAQ AKPGETQEEE
TNSGEEPFIE TRQDGVSRRF IPPARMMSTE SANSFTLIGE ASDGGTMENL SRRLKVTGDL
FDIMSGQTDV DHPLCEECTD TLLDQLDTQL NVTENECQNY KRCLEILEQM NEDDSEQLQM
ELKELALEEE RLIQELEDVE KNRKIVAENL EKVQAEAERL DQEEAQYQRE YSEFKRQQLE
LDDELKSVEN QMRYAQMQLD KLKKTNVFNA TFHIWHSGQF GTINNFRLGR LPSVPVEWNE
INAAWGQTVL LLHALANKMG LKFQRYRLVP YGNHSYLESL TDKSKELPLY CSGGLRFFWD
NKFDHAMVAF LDCVQQFKEE VEKGETRFCL PYRMDVEKGK IEDTGGSGGS YSIKTQFNSE
EQWTKALKFM LTNLKWGLAW VSSQFYNK
//
