BECN1_RAT
ID BECN1_RAT Reviewed; 448 AA.
AC Q91XJ1;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Beclin-1;
DE AltName: Full=Coiled-coil myosin-like BCL2-interacting protein;
DE AltName: Full=Protein GT197;
DE Contains:
DE RecName: Full=Beclin-1-C 35 kDa;
DE Contains:
DE RecName: Full=Beclin-1-C 37 kDa;
GN Name=Becn1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Ovary;
RA Paredes A.H., Tapia V., Ojeda S.R.;
RT "Beclin mRNA in the developing rat ovary.";
RL Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP INTERACTION WITH VMP1.
RX PubMed=17724469; DOI=10.1038/sj.onc.1210743;
RA Sauermann M., Sahin O., Sultmann H., Hahne F., Blaszkiewicz S., Majety M.,
RA Zatloukal K., Fuzesi L., Poustka A., Wiemann S., Arlt D.;
RT "Reduced expression of vacuole membrane protein 1 affects the invasion
RT capacity of tumor cells.";
RL Oncogene 27:1320-1326(2008).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 174-264, SUBUNIT, DOMAIN, AND
RP MUTAGENESIS OF LEU-178; GLU-189; LEU-192; LEU-196; ALA-217; GLU-224;
RP ALA-255 AND LEU-259.
RX PubMed=22314358; DOI=10.1038/ncomms1648;
RA Li X., He L., Che K.H., Funderburk S.F., Pan L., Pan N., Zhang M., Yue Z.,
RA Zhao Y.;
RT "Imperfect interface of Beclin1 coiled-coil domain regulates homodimer and
RT heterodimer formation with Atg14L and UVRAG.";
RL Nat. Commun. 3:662-662(2012).
CC -!- FUNCTION: Plays a central role in autophagy. Acts as core subunit of
CC the PI3K complex that mediates formation of phosphatidylinositol 3-
CC phosphate; different complex forms 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. Involved in regulation of degradative
CC endocytic trafficking and required for the abcission step in
CC cytokinesis, probably in the context of PI3KC3-C2. Essential for the
CC formation of PI3KC3-C2 but not PI3KC3-C1 PI3K complex forms. Involved
CC in endocytosis. May play a role in antiviral host defense (By
CC similarity). {ECO:0000250|UniProtKB:O88597,
CC ECO:0000250|UniProtKB:Q14457}.
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:0000250|UniProtKB:O88597,
CC ECO:0000250|UniProtKB:Q14457}.
CC -!- SUBUNIT: A homodimeric form is proposed to exist; this metastable form
CC readily transits to ATG14- or UVRAG-containing complexes with
CC BECN1:UVRAG being more stable than BECN1:ATG14 (PubMed:22314358).
CC Component of the PI3K (PI3KC3/PI3K-III/class III phosphatidylinositol
CC 3-kinase) complex the core of which is composed of the catalytic
CC subunit PIK3C3, the regulatory subunit PIK3R4 and BECN1 associating
CC with additional regulatory/auxilliary subunits to form alternative
CC complex forms. Alternative complex forms containing a forth regulatory
CC subunit in a mutually exclusive manner are PI3K complex I (PI3KC3-C1)
CC containing ATG14, and PI3K complex II (PI3KC3-C2) containing UVRAG.
CC PI3KC3-C1 displays a V-shaped architecture with PIK3R4 serving as a
CC bridge between PIK3C3 and the ATG14:BECN1 subcomplex. Both, PI3KC3-C1
CC and PI3KC3-C2, can associate with further regulatory subunits, such as
CC RUBCN, SH3GLB1/Bif-1 and AMBRA1. PI3KC3-C1 probably associates with
CC PIK3CB. Interacts with AMBRA1, GOPC, GRID2. Forms a complex with PPP2CA
CC and AMBRA1; AMBRA1 and BECN1 components of the complex regulate MYC
CC stability via different pathways (By similarity). Interacts with BCL2
CC and BCL2L1 isoform Bcl-X(L); the interaction inhibits BECN1 function in
CC promoting autophagy by interfering with the formation of the PI3K
CC complex. Interacts with cytosolic HMGB1; inhibits the interaction of
CC BECN1 and BCL2 leading to promotion of autophagy. Interacts with USP10,
CC USP13, DAPK1, RAB39A. Interacts with SLAMF1 (By similarity). Interacts
CC with the poly-Gln domain of ATXN3; the interaction causes
CC deubiquitination at Lys-400 and stabilizes BECN1. Interacts with VMP1
CC (PubMed:17724469). Interacts with TRIM5; the interaction causes
CC activation of BECN1 by causing its dissociation from its inhibitors
CC BCL2 and TAB2 (By similarity). Interacts with active ULK1
CC (phosphorylated on 'Ser-317') and MEFV simultaneously (By similarity).
CC Interacts with WDR81 and WDR91; negatively regulates the PI3
CC kinase/PI3K activity associated with endosomal membranes (By
CC similarity). Interacts with LAPTM4B; competes with EGFR for LAPTM4B
CC binding; regulates EGFR activity (By similarity). Interacts with TRIM50
CC (By similarity). Interacts with TRIM16 (By similarity). Interacts with
CC ATG14; this interaction is increased in the absence of TMEM39A (By
CC similarity). Interacts with WASHC1; preventing interaction with AMBRA1
CC and the DCX(AMBRA1) complex and subsequent ubiquitination (By
CC similarity). Interacts with TRIM17 (By similarity). Interacts with
CC BCL2L10/BCL-B (via BH1 domain) (By similarity).
CC {ECO:0000250|UniProtKB:O88597, ECO:0000250|UniProtKB:Q14457,
CC ECO:0000269|PubMed:17724469}.
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}. Note=Interaction with ATG14 promotes translocation to
CC autophagosomes. Expressed in dendrites and cell bodies of cerebellar
CC Purkinje cells. {ECO:0000250|UniProtKB:O88597,
CC ECO:0000250|UniProtKB:Q14457}.
CC -!- SUBCELLULAR LOCATION: [Beclin-1-C 35 kDa]: Mitochondrion
CC {ECO:0000250|UniProtKB:O88597, ECO:0000250|UniProtKB:Q14457}. Nucleus
CC {ECO:0000250|UniProtKB:Q14457}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q14457}.
CC -!- SUBCELLULAR LOCATION: [Beclin-1-C 37 kDa]: Mitochondrion
CC {ECO:0000250|UniProtKB:O88597}.
CC -!- DOMAIN: The C-terminal evolutionary conserved domain (ECD) contains
CC poly-Gln-binding domains such as the ATXN3 poly-Gln motif, consistent
CC with structural docking models revealing two highly scored poly-Gln-
CC binding pockets in the ECD (By similarity). As some binding is observed
CC with BECN1 lacking the ECD, other domains of BECN1 may also interact
CC with ATXN3 (By similarity). {ECO:0000250|UniProtKB:Q14457}.
CC -!- DOMAIN: The coiled coil domain can form antiparallel homodimers and
CC mediates dimerization with the coiled coil domains of ATG14 or UVRAG
CC involved in the formation of PI3K complexes.
CC {ECO:0000269|PubMed:22314358}.
CC -!- PTM: Phosphorylation at Thr-117 by DAPK1 reduces its interaction with
CC BCL2 and BCL2L1 and promotes induction of autophagy. In response to
CC autophagic stimuli, phosphorylated at serine residues by AMPK in an
CC ATG14-dependent manner, and this phosphorylation is critical for
CC maximally efficient autophagy. {ECO:0000250|UniProtKB:O88597,
CC ECO:0000250|UniProtKB:Q14457}.
CC -!- PTM: Polyubiquitinated by NEDD4, both with 'Lys-11'- and 'Lys-63'-
CC linkages (By similarity). 'Lys-11'-linked polyubiquitination leads to
CC degradation and is enhanced when the stabilizing interaction partner
CC VPS34 is depleted (By similarity). Deubiquitinated by USP10 and USP13,
CC leading to stabilize the PIK3C3/VPS34-containing complexes (By
CC similarity). Polyubiquitinated at Lys-400 with 'Lys-48'-linkages (By
CC similarity). 'Lys-48'-linked polyubiquitination of Lys-400 leads to
CC degradation (By similarity). Deubiquitinated by ATXN3, leading to
CC stabilization (By similarity). Ubiquitinated at Lys-435 via 'Lys-63'-
CC linkage by the DCX(AMBRA1) complex, thereby increasing the association
CC between BECN1 and PIK3C3 to promote PIK3C3 activity (By similarity).
CC {ECO:0000250|UniProtKB:Q14457}.
CC -!- PTM: Proteolytically processed by caspases including CASP8 and CASP3;
CC the C-terminal fragments lack autophagy-inducing capacity and are
CC proposed to induce apoptosis. Thus the cleavage is proposed to be an
CC determinant to switch from autophagy to apoptosis pathways affecting
CC cellular homeostasis including viral infections and survival of tumor
CC cells. {ECO:0000250|UniProtKB:O88597, ECO:0000250|UniProtKB:Q14457}.
CC -!- MISCELLANEOUS: Expanded poly-Gln tracts inhibit ATXN3-BECN1
CC interaction, decrease BECN1 levels and impair starvation-induced
CC autophagy (By similarity). {ECO:0000250|UniProtKB:Q14457}.
CC -!- SIMILARITY: Belongs to the beclin family. {ECO:0000305}.
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DR EMBL; AY033824; AAK56548.1; -; mRNA.
DR EMBL; BC074011; AAH74011.1; -; mRNA.
DR RefSeq; NP_001029289.1; NM_001034117.1.
DR RefSeq; NP_446191.1; NM_053739.2.
DR PDB; 3Q8T; X-ray; 1.90 A; A/B=174-264.
DR PDBsum; 3Q8T; -.
DR AlphaFoldDB; Q91XJ1; -.
DR SMR; Q91XJ1; -.
DR BioGRID; 250376; 1.
DR DIP; DIP-61888N; -.
DR IntAct; Q91XJ1; 1.
DR STRING; 10116.ENSRNOP00000027868; -.
DR iPTMnet; Q91XJ1; -.
DR PhosphoSitePlus; Q91XJ1; -.
DR PaxDb; Q91XJ1; -.
DR Ensembl; ENSRNOT00000082010; ENSRNOP00000071966; ENSRNOG00000020513.
DR GeneID; 114558; -.
DR KEGG; rno:114558; -.
DR UCSC; RGD:620190; rat.
DR CTD; 8678; -.
DR RGD; 620190; Becn1.
DR eggNOG; KOG2751; Eukaryota.
DR GeneTree; ENSGT00390000008164; -.
DR HOGENOM; CLU_024219_4_1_1; -.
DR InParanoid; Q91XJ1; -.
DR OMA; DTFCIGH; -.
DR OrthoDB; 1085752at2759; -.
DR PhylomeDB; Q91XJ1; -.
DR TreeFam; TF314282; -.
DR Reactome; R-RNO-1632852; Macroautophagy.
DR Reactome; R-RNO-5689880; Ub-specific processing proteases.
DR PRO; PR:Q91XJ1; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000020513; Expressed in colon and 20 other tissues.
DR Genevisible; Q91XJ1; RN.
DR GO; GO:0005776; C:autophagosome; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0031410; C:cytoplasmic vesicle; ISO:RGD.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0030425; C:dendrite; IDA:RGD.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:RGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005768; C:endosome; ISO:RGD.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0019898; C:extrinsic component of membrane; ISO:RGD.
DR GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016604; C:nuclear body; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0045335; C:phagocytic vesicle; ISO:RGD.
DR GO; GO:0000407; C:phagophore assembly site; IBA:GO_Central.
DR GO; GO:0035032; C:phosphatidylinositol 3-kinase complex, class III; ISS:UniProtKB.
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:0032991; C:protein-containing complex; ISO:RGD.
DR GO; GO:0005802; C:trans-Golgi network; ISO:RGD.
DR GO; GO:0051020; F:GTPase binding; ISO:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0043548; F:phosphatidylinositol 3-kinase binding; ISO:RGD.
DR GO; GO:0019901; F:protein kinase binding; ISO:RGD.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:RGD.
DR GO; GO:0007568; P:aging; IEP:RGD.
DR GO; GO:0050435; P:amyloid-beta metabolic process; ISO:RGD.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0000045; P:autophagosome assembly; IMP:RGD.
DR GO; GO:0097352; P:autophagosome maturation; ISO:RGD.
DR GO; GO:0006914; P:autophagy; IMP:RGD.
DR GO; GO:0000422; P:autophagy of mitochondrion; ISO:RGD.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0071275; P:cellular response to aluminum ion; IEP:RGD.
DR GO; GO:0034198; P:cellular response to amino acid starvation; IEP:RGD.
DR GO; GO:0071280; P:cellular response to copper ion; IEP:RGD.
DR GO; GO:0071364; P:cellular response to epidermal growth factor stimulus; IEP:RGD.
DR GO; GO:0042149; P:cellular response to glucose starvation; ISS:UniProtKB.
DR GO; GO:0070301; P:cellular response to hydrogen peroxide; IEP:RGD.
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:0043652; P:engulfment of apoptotic cell; ISO:RGD.
DR GO; GO:0045324; P:late endosome to vacuole transport; IBA:GO_Central.
DR GO; GO:0007040; P:lysosome organization; ISO:RGD.
DR GO; GO:0016236; P:macroautophagy; ISS:UniProtKB.
DR GO; GO:0000423; P:mitophagy; ISO:RGD.
DR GO; GO:0007080; P:mitotic metaphase plate congression; ISO:RGD.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:RGD.
DR GO; GO:1902902; P:negative regulation of autophagosome assembly; ISO:RGD.
DR GO; GO:0010507; P:negative regulation of autophagy; ISO:RGD.
DR GO; GO:0060548; P:negative regulation of cell death; IMP:RGD.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISO:RGD.
DR GO; GO:1905672; P:negative regulation of lysosome organization; IMP:RGD.
DR GO; GO:2000378; P:negative regulation of reactive oxygen species metabolic process; ISO:RGD.
DR GO; GO:0048666; P:neuron development; ISO:RGD.
DR GO; GO:0036092; P:phosphatidylinositol-3-phosphate biosynthetic process; ISO:RGD.
DR GO; GO:1902425; P:positive regulation of attachment of mitotic spindle microtubules to kinetochore; ISO:RGD.
DR GO; GO:2000786; P:positive regulation of autophagosome assembly; IMP:RGD.
DR GO; GO:0010508; P:positive regulation of autophagy; IMP:RGD.
DR GO; GO:0010613; P:positive regulation of cardiac muscle hypertrophy; ISO:RGD.
DR GO; GO:2001244; P:positive regulation of intrinsic apoptotic signaling pathway; IMP:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; ISO:RGD.
DR GO; GO:0032801; P:receptor catabolic process; ISO:RGD.
DR GO; GO:0010506; P:regulation of autophagy; ISO:RGD.
DR GO; GO:0050790; P:regulation of catalytic activity; ISO:RGD.
DR GO; GO:0032465; P:regulation of cytokinesis; ISS:UniProtKB.
DR GO; GO:0016241; P:regulation of macroautophagy; ISO:RGD.
DR GO; GO:0001666; P:response to hypoxia; IEP:RGD.
DR GO; GO:0010040; P:response to iron(II) ion; IEP:RGD.
DR GO; GO:0010288; P:response to lead ion; IEP:RGD.
DR GO; GO:0098780; P:response to mitochondrial depolarisation; ISO:RGD.
DR GO; GO:0031667; P:response to nutrient levels; IEP:RGD.
DR GO; GO:0051707; P:response to other organism; ISO:RGD.
DR GO; GO:0033197; P:response to vitamin E; IEP:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
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 1: Evidence at protein level;
KW 3D-structure; Acetylation; Antiviral defense; Apoptosis; Autophagy;
KW Cell cycle; Cell division; Coiled coil; Cytoplasm; Cytoplasmic vesicle;
KW Endoplasmic reticulum; Endosome; Golgi apparatus; Isopeptide bond;
KW Membrane; Mitochondrion; Nucleus; Phosphoprotein; Reference proteome;
KW Ubl conjugation.
FT CHAIN 1..448
FT /note="Beclin-1"
FT /id="PRO_0000316290"
FT CHAIN 132..448
FT /note="Beclin-1-C 37 kDa"
FT /evidence="ECO:0000250|UniProtKB:Q14457"
FT /id="PRO_0000435044"
FT CHAIN 148..448
FT /note="Beclin-1-C 35 kDa"
FT /evidence="ECO:0000250|UniProtKB:Q14457"
FT /id="PRO_0000435045"
FT REGION 47..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 110..157
FT /note="Interaction with BCL2 and BCL2L1 isoform Bcl-X(L)"
FT /evidence="ECO:0000250|UniProtKB:Q14457"
FT REGION 243..448
FT /note="Evolutionary conserved domain (ECD)"
FT /evidence="ECO:0000250|UniProtKB:Q14457"
FT REGION 423..448
FT /note="Required for membrane-association"
FT /evidence="ECO:0000250|UniProtKB:Q14457"
FT COILED 140..267
FT /evidence="ECO:0000255"
FT MOTIF 106..125
FT /note="BH3"
FT /evidence="ECO:0000250|UniProtKB:Q14457"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q14457"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14457"
FT MOD_RES 29
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14457"
FT MOD_RES 88
FT /note="Phosphoserine; by AMPK"
FT /evidence="ECO:0000250|UniProtKB:Q14457"
FT MOD_RES 91
FT /note="Phosphoserine; by AMPK"
FT /evidence="ECO:0000250|UniProtKB:Q14457"
FT MOD_RES 94
FT /note="Phosphoserine; by AMPK"
FT /evidence="ECO:0000250|UniProtKB:O88597"
FT MOD_RES 117
FT /note="Phosphothreonine; by DAPK1"
FT /evidence="ECO:0000250|UniProtKB:Q14457"
FT CROSSLNK 400
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q14457"
FT CROSSLNK 435
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q14457"
FT MUTAGEN 178
FT /note="L->A: Disrupts homodimerization, no effect on
FT interaction with ATG14 and UVRAG; when associated with A-
FT 192."
FT /evidence="ECO:0000269|PubMed:22314358"
FT MUTAGEN 178
FT /note="L->A: Disrupts homodimerization, no effect on
FT interaction with ATG14 and UVRAG; when associated with A-
FT 196."
FT /evidence="ECO:0000269|PubMed:22314358"
FT MUTAGEN 178
FT /note="L->A: Disrupts homodimerization, no effect on
FT interaction with ATG14 and UVRAG; when associated with A-
FT 259."
FT /evidence="ECO:0000269|PubMed:22314358"
FT MUTAGEN 189
FT /note="E->L: Decreases interaction with ATG14, no effect on
FT interaction with UVRAG; when associated with L-217, L-224
FT and L-255."
FT /evidence="ECO:0000269|PubMed:22314358"
FT MUTAGEN 192
FT /note="L->A: Disrupts homodimerization, no effect on
FT interaction with ATG14 and UVRAG; when associated with A-
FT 178."
FT /evidence="ECO:0000269|PubMed:22314358"
FT MUTAGEN 196
FT /note="L->A: Disrupts homodimerization, no effect on
FT interaction with ATG14 and UVRAG; when associated with A-
FT 178."
FT /evidence="ECO:0000269|PubMed:22314358"
FT MUTAGEN 217
FT /note="A->L: Decreases interaction with ATG14, no effect on
FT interaction with UVRAG; when associated with L-189, L-224
FT and L-255."
FT /evidence="ECO:0000269|PubMed:22314358"
FT MUTAGEN 224
FT /note="E->L: Decreases interaction with ATG14, no effect on
FT interaction with UVRAG; when associated with L-189, L-217
FT and L-255."
FT /evidence="ECO:0000269|PubMed:22314358"
FT MUTAGEN 255
FT /note="A->L: Decreases interaction with ATG14, no effect on
FT interaction with UVRAG; when associated with L-189, L-217
FT and L-224."
FT /evidence="ECO:0000269|PubMed:22314358"
FT MUTAGEN 259
FT /note="L->A: Disrupts homodimerization, no effect on
FT interaction with ATG14 and UVRAG; when associated with A-
FT 178."
FT /evidence="ECO:0000269|PubMed:22314358"
FT HELIX 174..263
FT /evidence="ECO:0007829|PDB:3Q8T"
SQ SEQUENCE 448 AA; 51557 MW; 34981BE560F3354B CRC64;
MEGSKASSST MQVSFVCQRC SQPLKLDTSF KILDRVTIQE LTAPLLTTAQ AKPGESQEEE
ANSGEEPFIE TRQDGVSRRF IPPARMMSTE SANSFTLIGE ASDGGTMENL SRRLKVTGDL
FDIMSGQTDV DHPLCEECTD TLLDQLDTQL NVTENECQNY KRCLEMLEQM NEGDSEQLQR
ELKELALEEE RLIQELEDVE KNRKVVAENL EKVQAEAERL DQEEAQYQRE YSEFKRQQLE
LDDELKSVEN QMRYAQMQLD KLKKTNVFNA TFHIWHSGQF GTINNFRLGR LPSAPVEWNE
INAAWGQTVL LLHALANKMG LKFQRYRLVP YGNHSYLESL TDKSKELPLY CSGGLRFFWD
NKFDHAMVAF LDCVQQFKEE VEKGETRFCL PYRMDVEKGK IEDTGGSGGS YSIKTQFNSE
EQWTKALKFM LTNLKWGLAW VSSQFYNK
