BAKOR_RAT
ID BAKOR_RAT Reviewed; 492 AA.
AC D4A4K3;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Beclin 1-associated autophagy-related key regulator {ECO:0000250|UniProtKB:Q6ZNE5};
DE Short=Barkor {ECO:0000250|UniProtKB:Q6ZNE5};
DE AltName: Full=Autophagy-related protein 14-like protein {ECO:0000250|UniProtKB:Q6ZNE5};
DE Short=Atg14L {ECO:0000250|UniProtKB:Q6ZNE5};
GN Name=Atg14 {ECO:0000250|UniProtKB:Q6ZNE5};
GN Synonyms=Atg14L {ECO:0000250|UniProtKB:Q6ZNE5};
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 [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Required for both basal and inducible autophagy. Determines
CC the localization of the autophagy-specific PI3-kinase complex. Plays a
CC role in autophagosome formation and MAP1LC3/LC3 conjugation to
CC phosphatidylethanolamine. Promotes BECN1 translocation from the trans-
CC Golgi network to autophagosomes. Enhances PIK3C3 activity in a BECN1-
CC dependent manner. Essential for the autophagy-dependent phosphorylation
CC of BECN1. Stimulates the phosphorylation of BECN1, but suppresses the
CC phosphorylation PIK3C3 by AMPK. Binds to STX17-SNAP29 binary t-SNARE
CC complex on autophagosomes and primes it for VAMP8 interaction to
CC promote autophagosome-endolysosome fusion. Modulates the hepatic lipid
CC metabolism (By similarity). {ECO:0000250|UniProtKB:Q6ZNE5,
CC ECO:0000250|UniProtKB:Q8CDJ3}.
CC -!- SUBUNIT: Forms homooligomers; homo-oligomerization is essential for the
CC roles in membrane tethering and enhancement of SNARE-mediated fusion.
CC Component of the PI3K (PI3KC3/PI3K-III/class III phosphatidylinositol
CC 3-kinase) complex I (PI3KC3-C1) in which the core composed of the
CC catalytic subunit PIK3C3, the regulatory subunit PIK3R4 and BECN1 is
CC associated with ATG14. PI3KC3-C1 displays a V-shaped architecture with
CC PIK3R4 serving as a bridge between PIK3C3 and the ATG14:BECN1
CC subcomplex. PI3KC3-C1 can associate with further regulatory subunits.
CC Interacts with PIK3CB. Interacts (via coiled-coil domain) with BECN2
CC (via coiled-coil domain); this interaction is tighter than BECN2 self-
CC association (By similarity). Interacts with the STX17-SNAP29 binary t-
CC SNARE complex (By similarity). Interacts with NRBF2 (By similarity).
CC Interacts with PIK3C3 and BECN1; this interaction is increased in the
CC absence of TMEM39A (By similarity). Interacts with STEEP1; the
CC interaction is required for trafficking of STING1 from the endoplasmic
CC reticulum (By similarity). {ECO:0000250|UniProtKB:Q6ZNE5,
CC ECO:0000250|UniProtKB:Q8CDJ3}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q6ZNE5}.
CC Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q6ZNE5};
CC Peripheral membrane protein {ECO:0000305}. Preautophagosomal structure
CC membrane {ECO:0000250|UniProtKB:Q6ZNE5}; Peripheral membrane protein
CC {ECO:0000305}. Note=Cytosolic under nutrient-rich conditions (By
CC similarity). Following autophagy stimuli, such as starvation or
CC rapamycin induction, predominantly detected in cytoplasmic foci,
CC identified as isolation membranes and autophagosomes (By similarity).
CC Accumulates on highly curved PtdIns(3)P enriched autophagic membrane
CC via its BATS domain to sense and maintain membrane curvature (By
CC similarity). Localizes also to discrete punctae along the ciliary
CC axoneme and to the base of the ciliary axoneme (By similarity).
CC {ECO:0000250|UniProtKB:Q6ZNE5, ECO:0000250|UniProtKB:Q8CDJ3}.
CC -!- DOMAIN: The coiled-coil domain is required for BECN1- and PIK3C3-
CC binding and for autophagy. {ECO:0000250|UniProtKB:Q6ZNE5}.
CC -!- DOMAIN: The final 80 residues in the C-terminus define a minimum
CC required region for autophagosome binding called BATS.
CC {ECO:0000250|UniProtKB:Q6ZNE5}.
CC -!- DOMAIN: The N-terminal cysteine repeats are required for proper
CC localization to the endoplasmic reticulum.
CC {ECO:0000250|UniProtKB:Q6ZNE5}.
CC -!- SIMILARITY: Belongs to the ATG14 family. {ECO:0000305}.
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DR EMBL; CH474040; EDL88360.1; -; Genomic_DNA.
DR RefSeq; NP_001100728.1; NM_001107258.1.
DR AlphaFoldDB; D4A4K3; -.
DR SMR; D4A4K3; -.
DR DIP; DIP-60850N; -.
DR IntAct; D4A4K3; 1.
DR STRING; 10116.ENSRNOP00000016274; -.
DR PhosphoSitePlus; D4A4K3; -.
DR PaxDb; D4A4K3; -.
DR PeptideAtlas; D4A4K3; -.
DR Ensembl; ENSRNOT00000016274; ENSRNOP00000016274; ENSRNOG00000011873.
DR GeneID; 305831; -.
DR KEGG; rno:305831; -.
DR UCSC; RGD:1304610; rat.
DR CTD; 22863; -.
DR RGD; 1304610; Atg14.
DR eggNOG; KOG4398; Eukaryota.
DR GeneTree; ENSGT00390000011854; -.
DR HOGENOM; CLU_046719_1_0_1; -.
DR InParanoid; D4A4K3; -.
DR OMA; PWITLPN; -.
DR OrthoDB; 1332122at2759; -.
DR PhylomeDB; D4A4K3; -.
DR TreeFam; TF323392; -.
DR Reactome; R-RNO-1632852; Macroautophagy.
DR PRO; PR:D4A4K3; -.
DR Proteomes; UP000002494; Chromosome 15.
DR Proteomes; UP000234681; Chromosome 15.
DR Bgee; ENSRNOG00000011873; Expressed in skeletal muscle tissue and 19 other tissues.
DR Genevisible; D4A4K3; RN.
DR GO; GO:0005776; C:autophagosome; ISO:RGD.
DR GO; GO:0005930; C:axoneme; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0097629; C:extrinsic component of omegasome membrane; ISO:RGD.
DR GO; GO:0097632; C:extrinsic component of phagophore assembly site membrane; ISO:RGD.
DR GO; GO:0044233; C:mitochondria-associated endoplasmic reticulum membrane; ISO:RGD.
DR GO; GO:0045335; C:phagocytic vesicle; ISO:RGD.
DR GO; GO:0034045; C:phagophore assembly site membrane; ISO:RGD.
DR GO; GO:0035032; C:phosphatidylinositol 3-kinase complex, class III; ISS:UniProtKB.
DR GO; GO:0051020; F:GTPase binding; ISO:RGD.
DR GO; GO:0000045; P:autophagosome assembly; ISO:RGD.
DR GO; GO:0097352; P:autophagosome maturation; ISO:RGD.
DR GO; GO:0016240; P:autophagosome membrane docking; ISO:RGD.
DR GO; GO:0006914; P:autophagy; ISO:RGD.
DR GO; GO:0042149; P:cellular response to glucose starvation; ISS:UniProtKB.
DR GO; GO:0009267; P:cellular response to starvation; ISO:RGD.
DR GO; GO:0045022; P:early endosome to late endosome transport; ISO:RGD.
DR GO; GO:0008333; P:endosome to lysosome transport; ISO:RGD.
DR GO; GO:0016236; P:macroautophagy; ISO:RGD.
DR GO; GO:0000423; P:mitophagy; ISO:RGD.
DR GO; GO:0001933; P:negative regulation of protein phosphorylation; ISS:UniProtKB.
DR GO; GO:0036092; P:phosphatidylinositol-3-phosphate biosynthetic process; ISO:RGD.
DR GO; GO:0043552; P:positive regulation of phosphatidylinositol 3-kinase activity; ISO:RGD.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; ISS:UniProtKB.
DR GO; GO:0010608; P:post-transcriptional regulation of gene expression; ISO:RGD.
DR GO; GO:0006468; P:protein phosphorylation; ISO:RGD.
DR GO; GO:0016241; P:regulation of macroautophagy; ISO:RGD.
DR GO; GO:0001932; P:regulation of protein phosphorylation; ISO:RGD.
DR GO; GO:0090207; P:regulation of triglyceride metabolic process; ISO:RGD.
DR GO; GO:0098780; P:response to mitochondrial depolarisation; ISO:RGD.
DR InterPro; IPR018791; UV_resistance/autophagy_Atg14.
DR Pfam; PF10186; ATG14; 1.
PE 3: Inferred from homology;
KW Autophagy; Coiled coil; Cytoplasm; Endoplasmic reticulum; Membrane;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..492
FT /note="Beclin 1-associated autophagy-related key regulator"
FT /id="PRO_0000401194"
FT REGION 213..232
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 411..473
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 70..180
FT /evidence="ECO:0000255"
FT COMPBIAS 449..473
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 29
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6ZNE5"
FT MOD_RES 416
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6ZNE5"
FT MOD_RES 429
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q6ZNE5"
SQ SEQUENCE 492 AA; 55345 MW; F7647AFDDE3E7FA6 CRC64;
MASPSGKGSW TPEAPGFGPR ALAPDLVDSV DDAEGLYVAV ERCPLCNTTR RRLTCAKCVQ
SGDFVYFDGR DRERFIDKKE RLSQLKNKQE EFQKEVLKAM EGKRLTDQLR WKIMSCKMRI
EQLKQTICKG NEEMKKNSEG LLKNKEKNQK LYSRAQRHQE KKEKIQRHNR KLGDLVEKKT
SDLREHYDRL ACLRRLHILE LTSVIFPMDE VKTSGRDPAD VSSETDSAMT SSMVSKLAEA
RRTTYLSGRW VCDDHNGDTS ISITGPWISL PNNGDYSAYY NWVEEKKTTQ GPDMEHNNPA
YTISAALGYA TQLVNIVSHI LDINLPKKLC NSEFCGENLS KQRLTRAVRK LNANILYLCS
SQHVNLDQLQ PLHTLRNLMH LVSPHSEHLG RSGPFEVRAD LEESMEFVDP GVAGESDVSG
DERVSDEETD LGTDWENLPS PRFCDIPSQP VEVSQSQSTQ ASPPIASSSA GGMISSAAAS
VTSWFKAYTG HR
