ID Q53F78_HUMAN Unreviewed; 450 AA.
AC Q53F78;
DT 24-MAY-2005, integrated into UniProtKB/TrEMBL.
DT 24-MAY-2005, sequence version 1.
DT 24-JAN-2024, entry version 74.
DE RecName: Full=Beclin-1 {ECO:0000256|ARBA:ARBA00018490, ECO:0000256|RuleBase:RU367123};
DE Flags: Fragment;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606 {ECO:0000313|EMBL:BAD97131.1};
RN [1] {ECO:0000313|EMBL:BAD97131.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=8125298; DOI=10.1016/0378-1119(94)90802-8;
RA Maruyama K., Sugano S.;
RT "Oligo-capping: a simple method to replace the cap structure of eukaryotic
RT mRNAs with oligoribonucleotides.";
RL Gene 138:171-174(1994).
RN [2] {ECO:0000313|EMBL:BAD97131.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=9373149; DOI=10.1016/S0378-1119(97)00411-3;
RA Suzuki Y., Yoshitomo K., Maruyama K., Suyama A., Sugano S.;
RT "Construction and characterization of a full length-enriched and a 5'-end-
RT enriched cDNA library.";
RL Gene 200:149-156(1997).
RN [3] {ECO:0000313|EMBL:BAD97131.1}
RP NUCLEOTIDE SEQUENCE.
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
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; AK223411; BAD97131.1; -; mRNA.
DR AlphaFoldDB; Q53F78; -.
DR PeptideAtlas; Q53F78; -.
DR GO; GO:0005776; C:autophagosome; IEA:UniProtKB-SubCell.
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:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000045; P:autophagosome assembly; IEA:UniProtKB-UniRule.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0045022; P:early endosome to late endosome transport; IEA:UniProtKB-UniRule.
DR GO; GO:0048583; P:regulation of response to stimulus; IEA:UniProt.
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 2: Evidence at transcript level;
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 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"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:BAD97131.1"
SQ SEQUENCE 450 AA; 51949 MW; A45E76C8749DE98C CRC64;
MEGSKTSNNS TMQVSFVCQR CSQPLKLDTS FKILDRVTIQ ELTAPLLTTA QAKPGETQEE
ETNSGEEPFI ETPRQDGVSR RFIPPARMMS TESANSFTLI GEASDGGTME NLSRRLKVTG
DLFDIMSGQT DVDHPLREEC TDTLLDQLDT QLNVTENECQ NYKRCLEILE QMNEDDSEQL
QMELKELALE EERLIQELED VEKNRKIVAE NLEKVQAEAE RLDQEEAQYQ REYSEFKRQQ
LELDDELKSV ENQMRYAQTQ LDKLKKTNVF NATFHIWHSG QFGTINNFRL GRLPSVPVEW
NEINAAWGQT VLLLHALANK MGLKFQRYRL VPYGNHSYLE SLTDKSKELP LYCSGGLRFF
WDNKFDHAMV AFLDCVQQFK EEVEKGETRF CLPYRMDVEK GKIEDTGGSG GSYSIKTQFN
SEEQWTKALK FMLTNLKWGL AWVSSQFYNK
//