BECN1_CHICK
ID BECN1_CHICK Reviewed; 447 AA.
AC Q5ZKS6;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Beclin-1;
GN Name=BECN1; ORFNames=RCJMB04_9f22;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
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 such as initiation of
CC autophagosomes, maturation of autophagosomes and endocytosis (By
CC similarity). Involved in regulation of degradative endocytic
CC trafficking and required for the abcission step in cytokinesis,
CC probably in the context of PI3KC3-C2 (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; AJ720008; CAG31667.1; -; mRNA.
DR RefSeq; NP_001006332.1; NM_001006332.1.
DR AlphaFoldDB; Q5ZKS6; -.
DR SMR; Q5ZKS6; -.
DR STRING; 9031.ENSGALP00000004697; -.
DR PaxDb; Q5ZKS6; -.
DR PRIDE; Q5ZKS6; -.
DR GeneID; 420018; -.
DR KEGG; gga:420018; -.
DR CTD; 8678; -.
DR VEuPathDB; HostDB:geneid_420018; -.
DR eggNOG; KOG2751; Eukaryota.
DR InParanoid; Q5ZKS6; -.
DR OrthoDB; 1085752at2759; -.
DR PhylomeDB; Q5ZKS6; -.
DR PRO; PR:Q5ZKS6; -.
DR Proteomes; UP000000539; Unplaced.
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: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..447
FT /note="Beclin-1"
FT /id="PRO_0000316291"
FT REGION 44..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 242..447
FT /note="Evolutionary conserved domain (ECD)"
FT /evidence="ECO:0000250|UniProtKB:Q14457"
FT REGION 422..447
FT /note="Required for membrane-association"
FT /evidence="ECO:0000250|UniProtKB:Q14457"
FT COILED 139..266
FT /evidence="ECO:0000255"
FT MOTIF 105..124
FT /note="BH3"
FT /evidence="ECO:0000250|UniProtKB:Q14457"
SQ SEQUENCE 447 AA; 51435 MW; B4B28EA95CB7463A CRC64;
MEGGRAPACT TQVSFVCQRC SQPLKLDTSF KILDRLTIQE LTAPPLTAAP ARPGDAQEES
ALSEEAFTEG RQDGVSRRFI PPARMMSTES ANSFTLIGEA SDGGTMENLS RRLKVTGDLF
DIMSGQTDVD HPLCEECTDT LLDQLDTQLN ITENECQNYK RCLEILEKMN EDDKEKLQTE
LKELALEEEQ LIQELEDVEK NRKIVAEDFE RVRAEAERLE QEEAQYQKEY CEFKRQQLEL
DDELKSVENQ MRYAQMQLDK LKKTNVFNAT FHIWHSGQFG TINNFRLGRL PSVPVEWNEI
NAAWGQTVLL LHALANKMGL KFQRYRLVPY GNHSYLESLT DKSKELPLYC SGGLRFFWDN
KFDHAMVAFL DCVQQFKEEV EKGETRFCLP YRMDVEKGKI EDTGGSGGSY SIKTQFNSEE
QWTKALKFML TNLKWGLAWV SSQFYNK
