BECN1_XENLA
ID BECN1_XENLA Reviewed; 445 AA.
AC Q6GP52;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Beclin-1;
GN Name=becn1;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Spleen;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUN-2004) 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; BC073292; AAH73292.1; -; mRNA.
DR RefSeq; NP_001085751.1; NM_001092282.1.
DR AlphaFoldDB; Q6GP52; -.
DR SMR; Q6GP52; -.
DR DNASU; 444178; -.
DR GeneID; 444178; -.
DR KEGG; xla:444178; -.
DR CTD; 444178; -.
DR Xenbase; XB-GENE-999325; becn1.L.
DR OrthoDB; 1085752at2759; -.
DR Proteomes; UP000186698; Chromosome 9_10L.
DR Bgee; 444178; Expressed in internal ear and 19 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: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:0033554; P:cellular response to stress; IEA:UniProt.
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: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_0000316292"
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; 51294 MW; 441D357E1CFDA264 CRC64;
METSKSSTMQ VSFVCQRCSQ PLKLDTSFKI LDKVTMQELT APLVTTAAVK PGDIQEVDSN
IEETFAENRT DGVSRRLIPP ARMMSTESAT SFTLIGEASD GGTMENLSRR LKVTGDLFDI
MSGQTDVDHP LCEECTDTLL DQLDTQLNIT ENECQNYKRC LEILERMNED DKEKLEAKLK
ELAEDEERLI QELEEVERNR ELVAKDIEKV REEAERLEQE EARYQKEYSE FKRQQLELDD
DLKSVENQMR YAQIQLDKLK KTNVFNATFH IWHSGQFGTI NNFRLGRLPS VPVEWNEINA
AWGQTVLLLH ALANKMGLQF QRYRLVPFGN HSYLESLTDK SKELPLYCSG GLRFFWDNKF
DHAMVAFLDC VQQFKEEVEK GDTGFCLPYR MDVDKGKIED TGGSGGSYSI KTQFNSEEQW
TKALKFMLTN LKWGLAWVSS QFYNK
