ID   BECN2_MOUSE             Reviewed;         447 AA.
AC   P0DM65; S5WDD2;
DT   16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT   26-NOV-2014, sequence version 2.
DT   03-AUG-2022, entry version 54.
DE   RecName: Full=Beclin-2 {ECO:0000303|PubMed:23954414};
GN   Name=Becn2 {ECO:0000303|PubMed:23954414, ECO:0000312|MGI:MGI:2684950};
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH ATG14; AMBRA1;
RP   GPRASP1; UVRAG AND PIK3C3, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RC   STRAIN=C57BL/6J {ECO:0000312|EMBL:AGS82805.1};
RX   PubMed=23954414; DOI=10.1016/j.cell.2013.07.035;
RA   He C., Wei Y., Sun K., Li B., Dong X., Zou Z., Liu Y., Kinch L.N., Khan S.,
RA   Sinha S., Xavier R.J., Grishin N.V., Xiao G., Eskelinen E.L., Scherer P.E.,
RA   Whistler J.L., Levine B.;
RT   "Beclin 2 functions in autophagy, degradation of G protein-coupled
RT   receptors, and metabolism.";
RL   Cell 154:1085-1099(2013).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
CC   -!- FUNCTION: Involved in 2 distinct lysosomal degradation pathways: acts
CC       as a regulator of autophagy and as a regulator of G-protein coupled
CC       receptors turnover. Regulates degradation in lysosomes of a variety of
CC       G-protein coupled receptors via its interaction with GPRASP1/GASP1.
CC       {ECO:0000269|PubMed:23954414}.
CC   -!- SUBUNIT: Homodimer (via coiled-coil domain) (By similarity). Interacts
CC       (via coiled-coil domain) with ATG14 (via coiled-coil domain); this
CC       interaction is tighter than BECN2 self-association (PubMed:23954414).
CC       Interacts with AMBRA1, UVRAG and PIK3C3/VPS34; these interactions are
CC       not disrupted by starvation (PubMed:23954414). Does not interact with
CC       RUBCN. Interacts (via N-terminus) with GPRASP1/GASP1; the interaction
CC       is direct (PubMed:23954414). {ECO:0000250|UniProtKB:A8MW95,
CC       ECO:0000269|PubMed:23954414}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Expressed in brain, skeletal muscle, placenta,
CC       thymus and uterus. Expressed at a lower level in liver, testis,
CC       stomach, and 17-day-old embryos. {ECO:0000269|PubMed:23954414}.
CC   -!- DISRUPTION PHENOTYPE: Decreased embryonic viability: embryonic and
CC       postnatal survival rates of homozygous mutant mice are markedly lower.
CC       Heterozygous knockout mice show defects in autophagy, increased levels
CC       of Cnr1 receptor, elevated food intake, and obesity and insulin
CC       resistance. {ECO:0000269|PubMed:23954414}.
CC   -!- SIMILARITY: Belongs to the beclin family. {ECO:0000305}.
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DR   EMBL; KF511582; AGS82805.1; -; mRNA.
DR   EMBL; GL456087; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   CCDS; CCDS78757.1; -.
DR   RefSeq; NP_001277621.1; NM_001290692.1.
DR   AlphaFoldDB; P0DM65; -.
DR   SMR; P0DM65; -.
DR   BioGRID; 230547; 5.
DR   IntAct; P0DM65; 6.
DR   PhosphoSitePlus; P0DM65; -.
DR   PRIDE; P0DM65; -.
DR   Antibodypedia; 77840; 347 antibodies from 17 providers.
DR   DNASU; 226720; -.
DR   Ensembl; ENSMUST00000201297; ENSMUSP00000143887; ENSMUSG00000104158.
DR   GeneID; 226720; -.
DR   KEGG; mmu:226720; -.
DR   UCSC; uc033fof.2; mouse.
DR   CTD; 441925; -.
DR   MGI; MGI:2684950; Becn2.
DR   VEuPathDB; HostDB:ENSMUSG00000104158; -.
DR   GeneTree; ENSGT00390000008164; -.
DR   OMA; AWASQRY; -.
DR   OrthoDB; 1085752at2759; -.
DR   PRO; PR:P0DM65; -.
DR   Proteomes; UP000000589; Chromosome 1.
DR   RNAct; P0DM65; protein.
DR   Bgee; ENSMUSG00000104158; Expressed in morula and 6 other tissues.
DR   ExpressionAtlas; P0DM65; baseline and differential.
DR   Genevisible; P0DM65; MM.
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:0044877; F:protein-containing complex binding; IDA:MGI.
DR   GO; GO:0000045; P:autophagosome assembly; IBA:GO_Central.
DR   GO; GO:0006914; P:autophagy; IMP:UniProtKB.
DR   GO; GO:0006995; P:cellular response to nitrogen starvation; IBA:GO_Central.
DR   GO; GO:0008333; P:endosome to lysosome transport; IMP:UniProtKB.
DR   GO; GO:1990172; P:G protein-coupled receptor catabolic process; IMP:UniProtKB.
DR   GO; GO:0042593; P:glucose homeostasis; IGI:MGI.
DR   GO; GO:0045324; P:late endosome to vacuole transport; IBA:GO_Central.
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; IPR032912; BECN2.
DR   PANTHER; PTHR12768; PTHR12768; 1.
DR   PANTHER; PTHR12768:SF5; PTHR12768:SF5; 1.
DR   Pfam; PF04111; APG6; 1.
DR   Pfam; PF17675; APG6_N; 1.
PE   1: Evidence at protein level;
KW   Autophagy; Coiled coil; Cytoplasm; Reference proteome.
FT   CHAIN           1..447
FT                   /note="Beclin-2"
FT                   /id="PRO_0000424159"
FT   REGION          186..256
FT                   /note="Required for homodimer formation"
FT                   /evidence="ECO:0000250|UniProtKB:A8MW95"
FT   COILED          169..228
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   447 AA;  50287 MW;  F5114EB9DB6320B9 CRC64;
     MSPALFLCQR CKEPLKLLQQ QGGPLEVQHH ANTPTEIPVS AESQVRTSGR PHSDGGRVSQ
     GSALCTFTLL TSGGPDSEGG TTSQGNACCT FTLLGESASM RTMNTIQNTV LETFEILSDQ
     KVVDHPLCVD CTDHLLMQLD DQLALLASDN QKYKSFQDRE LLVSEEEREA LHAELCAELS
     SLEQEEARLT QELEDLDGHH ARVAAELRAA QAESKELYKQ HEQHRVEYSV FKMEQLELMD
     QLSSVENQLT YALSQQYRLR QTNIFNATFT ISDEGPLGVI NNFRLGCLPG VRVGWTEISS
     AWGQTVLLLF SLSKIAGLQF QRYQLVPFGD HSYLKSLTGD GVLPLFSDGS HSVFLNNKFD
     CGMKAFLDCL QQFVEEIERD ERCPCLPYRI HVKEGLMEDV WDSGECCSIR THLNTEEEWS
     RALKFMLSDL KLILAWASLR FSRVQRP