BECN1_XENTR
ID BECN1_XENTR Reviewed; 445 AA.
AC Q4A1L3;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Beclin-1;
GN Name=becn1;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Botti J., Djavaheri-Mergny M., Codogno P., Oriol R.;
RT "Phylogeny and biochemistry of the autophagy protein beclin 1.";
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Plays a central role in autophagy (By similarity). Acts as
CC core subunit of different PI3K complex forms that mediate formation of
CC phosphatidylinositol 3-phosphate and are believed to play a role in
CC multiple membrane trafficking pathways: PI3KC3-C1 is involved in
CC initiation of autophagosomes and PI3KC3-C2 in maturation of
CC autophagosomes and endocytosis (By similarity). Involved in regulation
CC of degradative endocytic trafficking and required for the abcission
CC step in cytokinesis, probably in the context of PI3KC3-C2 (By
CC similarity). Essential for the formation of PI3KC3-C2 but not PI3KC3-C1
CC PI3K complex forms (By similarity). Involved in endocytosis including
CC endosome formation in neuronal cells (By similarity).
CC {ECO:0000250|UniProtKB:Q14457}.
CC -!- SUBUNIT: Component of the PI3K (PI3KC3/PI3K-III/class III
CC phosphatidylinositol 3-kinase) complex (By similarity).
CC {ECO:0000250|UniProtKB:Q14457}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O88597}. Golgi
CC apparatus, trans-Golgi network membrane {ECO:0000250|UniProtKB:Q14457};
CC Peripheral membrane protein {ECO:0000250|UniProtKB:Q14457}. Endosome
CC membrane {ECO:0000250|UniProtKB:Q14457}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q14457}. Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q14457}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q14457}. Mitochondrion membrane
CC {ECO:0000250|UniProtKB:Q14457}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q14457}. Cytoplasmic vesicle, autophagosome
CC {ECO:0000305}.
CC -!- PTM: May be proteolytically processed by caspases; the C-terminal
CC fragment(s) may induce apoptosis. {ECO:0000250|UniProtKB:O88597,
CC ECO:0000250|UniProtKB:Q14457}.
CC -!- SIMILARITY: Belongs to the beclin family. {ECO:0000305}.
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DR EMBL; AM051356; CAJ19734.1; -; mRNA.
DR EMBL; BC135115; AAI35116.1; -; mRNA.
DR RefSeq; NP_001029112.1; NM_001033940.2.
DR AlphaFoldDB; Q4A1L3; -.
DR SMR; Q4A1L3; -.
DR STRING; 8364.ENSXETP00000032566; -.
DR PaxDb; Q4A1L3; -.
DR DNASU; 619357; -.
DR Ensembl; ENSXETT00000027611; ENSXETP00000027611; ENSXETG00000012613.
DR GeneID; 619357; -.
DR KEGG; xtr:619357; -.
DR CTD; 8678; -.
DR Xenbase; XB-GENE-999318; becn1.
DR eggNOG; KOG2751; Eukaryota.
DR HOGENOM; CLU_024219_4_1_1; -.
DR InParanoid; Q4A1L3; -.
DR OMA; AWASQRY; -.
DR OrthoDB; 1085752at2759; -.
DR PhylomeDB; Q4A1L3; -.
DR TreeFam; TF314282; -.
DR Reactome; R-XTR-1632852; Macroautophagy.
DR Proteomes; UP000008143; Chromosome 10.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000012613; Expressed in heart and 16 other tissues.
DR GO; GO:0005776; C:autophagosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
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:0000407; C:phagophore assembly site; IBA:GO_Central.
DR GO; GO:0034271; C:phosphatidylinositol 3-kinase complex, class III, type I; IBA:GO_Central.
DR GO; GO:0034272; C:phosphatidylinositol 3-kinase complex, class III, type II; IBA:GO_Central.
DR GO; GO:0000045; P:autophagosome assembly; IBA:GO_Central.
DR GO; GO:0006914; P:autophagy; ISS:UniProtKB.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0006995; P:cellular response to nitrogen starvation; IBA:GO_Central.
DR GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR GO; GO:0045022; P:early endosome to late endosome transport; ISS:UniProtKB.
DR GO; GO:0006897; P:endocytosis; IEA:InterPro.
DR GO; GO:0045324; P:late endosome to vacuole transport; IBA:GO_Central.
DR GO; GO:0010508; P:positive regulation of autophagy; ISS:UniProtKB.
DR GO; GO:0032465; P:regulation of cytokinesis; ISS:UniProtKB.
DR GO; GO:0048583; P:regulation of response to stimulus; IEA:UniProt.
DR Gene3D; 1.10.418.40; -; 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; IPR032913; BECN1.
DR InterPro; IPR029318; BH3_dom.
DR PANTHER; PTHR12768; PTHR12768; 1.
DR PANTHER; PTHR12768:SF6; PTHR12768:SF6; 1.
DR Pfam; PF04111; APG6; 1.
DR Pfam; PF17675; APG6_N; 1.
DR Pfam; PF15285; BH3; 1.
PE 2: Evidence at transcript level;
KW Antiviral defense; Autophagy; Cell cycle; Cell division; Coiled coil;
KW Cytoplasm; Cytoplasmic vesicle; Endoplasmic reticulum; Endosome;
KW Golgi apparatus; Membrane; Mitochondrion; Reference proteome.
FT CHAIN 1..445
FT /note="Beclin-1"
FT /id="PRO_0000316293"
FT REGION 240..445
FT /note="Evolutionary conserved domain (ECD)"
FT /evidence="ECO:0000250|UniProtKB:Q14457"
FT REGION 420..445
FT /note="Required for membrane-association"
FT /evidence="ECO:0000250|UniProtKB:Q14457"
FT COILED 137..264
FT /evidence="ECO:0000255"
FT MOTIF 103..122
FT /note="BH3"
FT /evidence="ECO:0000250|UniProtKB:Q14457"
SQ SEQUENCE 445 AA; 51326 MW; 44063514AA3DCEEA CRC64;
METSKSSTMQ VSFVCQRCSQ PLKLDTSFKI LDKVTMQELT APLVTTAAVK PGDIQEVDSN
IEETFAENRT DGVSRRLIPP ARMMSTESAT SFTLIGEASD GGTMENLSRR LKVTGDLFDI
MSGQTDVDHP LCEECTDTLL DQLDTQLNIT ENECQNYKRC LEILERMNED DKEKLEAKLK
ELAEDEDRLI QELEEVERNR ELVAKDIEKV REEAERLEQE EARYQKEYSE FKRQQLELDD
DLKSVENQMR YAQIQLDKLK KTNVFNATFH IWHSGQFGTI NNFRLGRLPS VPVEWNEINA
AWGQTVLLLH ALANKMGLQF QRYRLMPFGN HSYLESLTDK SKELPLYCSG GLRFFWDNKF
DHAMVAFLDC VQQFKEEVEK GDTGFCLPYR MDVEKGKIED TGGSGGSYSI KTQFNSEEQW
TKALKFMLTN LKWGLAWVSS QFYNK
