BECN1_KLUMD
ID BECN1_KLUMD Reviewed; 466 AA.
AC W0TD11;
DT 25-APR-2018, integrated into UniProtKB/Swiss-Prot.
DT 19-MAR-2014, sequence version 1.
DT 25-MAY-2022, entry version 28.
DE RecName: Full=Vacuolar protein sorting-associated protein 30 {ECO:0000250|UniProtKB:Q02948};
DE AltName: Full=Autophagy-related protein 6 {ECO:0000303|PubMed:26442587};
GN Name=VPS30 {ECO:0000250|UniProtKB:Q02948};
GN Synonyms=ATG6 {ECO:0000303|PubMed:26442587};
GN ORFNames=KLMA_50047 {ECO:0000312|EMBL:BAO40701.1};
OS Kluyveromyces marxianus (strain DMKU3-1042 / BCC 29191 / NBRC 104275)
OS (Yeast) (Candida kefyr).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=1003335;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DMKU3-1042 / BCC 29191 / NBRC 104275;
RX PubMed=25834639; DOI=10.1186/s13068-015-0227-x;
RA Lertwattanasakul N., Kosaka T., Hosoyama A., Suzuki Y., Rodrussamee N.,
RA Matsutani M., Murata M., Fujimoto N., Suprayogi X., Tsuchikane K.,
RA Limtong S., Fujita N., Yamada M.;
RT "Genetic basis of the highly efficient yeast Kluyveromyces marxianus:
RT complete genome sequence and transcriptome analyses.";
RL Biotechnol. Biofuels 8:47-47(2015).
RN [2]
RP IDENTIFICATION, AND DISRUPTION PHENOTYPE.
RX PubMed=26442587; DOI=10.1074/jbc.m115.684233;
RA Yamamoto H., Shima T., Yamaguchi M., Mochizuki Y., Hoshida H., Kakuta S.,
RA Kondo-Kakuta C., Noda N.N., Inagaki F., Itoh T., Akada R., Ohsumi Y.;
RT "The thermotolerant yeast Kluyveromyces marxianus is a useful organism for
RT structural and biochemical studies of autophagy.";
RL J. Biol. Chem. 290:29506-29518(2015).
CC -!- FUNCTION: Required for cytoplasm to vacuole transport (Cvt), autophagy,
CC nucleophagy, and mitophagy, as a part of the autophagy-specific VPS34
CC PI3-kinase complex I (By similarity). This complex is essential to
CC recruit the ATG8-phosphatidylinositol conjugate and the ATG12-ATG5
CC conjugate to the pre-autophagosomal structure (By similarity). Also
CC involved in endosome-to-Golgi retrograde transport as part of the VPS34
CC PI3-kinase complex II (By similarity). {ECO:0000250|UniProtKB:Q02948}.
CC -!- SUBUNIT: Component of the autophagy-specific VPS34 PI3-kinase complex
CC I; and of the VPS34 PI3-kinase complex II (By similarity).
CC {ECO:0000250|UniProtKB:Q02948}.
CC -!- SUBCELLULAR LOCATION: Endosome membrane {ECO:0000250|UniProtKB:Q02948};
CC Peripheral membrane protein {ECO:0000250|UniProtKB:Q02948}. Vacuole
CC membrane {ECO:0000250|UniProtKB:Q02948}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q02948}. Preautophagosomal structure membrane
CC {ECO:0000250|UniProtKB:Q02948}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q02948}. Note=With the VPS34 PI3-kinase complex
CC I, localizes to the vacuole-isolation membrane contact site (VICS)
CC during isolation membrane (IM) expansion (By similarity). The IM is a
CC membrane sac generated from the pre-autophagosomal structure that
CC ultimately expands to become a mature autophagosome (By similarity).
CC {ECO:0000250|UniProtKB:Q02948}.
CC -!- DOMAIN: The C-terminal domain called the BARA domain is dispensable for
CC the construction of both VPS34 PI3-kinase complexes, but is
CC specifically required for autophagy through the targeting of complex I
CC to the pre-autophagosomal structure (By similarity).
CC {ECO:0000250|UniProtKB:Q02948}.
CC -!- DISRUPTION PHENOTYPE: Still forms preautophagosomal structures (PAS) in
CC proximity to the vacuolar membrane (PubMed:26442587).
CC {ECO:0000269|PubMed:26442587}.
CC -!- SIMILARITY: Belongs to the beclin family. {ECO:0000305}.
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DR EMBL; AP012217; BAO40701.1; -; Genomic_DNA.
DR AlphaFoldDB; W0TD11; -.
DR SMR; W0TD11; -.
DR EnsemblFungi; BAO40701; BAO40701; KLMA_50047.
DR OrthoDB; 1085752at2759; -.
DR Proteomes; UP000065495; Chromosome 5.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0034045; C:phagophore assembly site membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0034271; C:phosphatidylinositol 3-kinase complex, class III, type I; IEA:EnsemblFungi.
DR GO; GO:0034272; C:phosphatidylinositol 3-kinase complex, class III, type II; IEA:EnsemblFungi.
DR GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0120095; C:vacuole-isolation membrane contact site; IEA:EnsemblFungi.
DR GO; GO:0000045; P:autophagosome assembly; IEA:EnsemblFungi.
DR GO; GO:0030242; P:autophagy of peroxisome; IEA:EnsemblFungi.
DR GO; GO:0032258; P:cytoplasm to vacuole transport by the Cvt pathway; IEA:EnsemblFungi.
DR GO; GO:0045324; P:late endosome to vacuole transport; IEA:EnsemblFungi.
DR GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IEA:EnsemblFungi.
DR GO; GO:0034727; P:piecemeal microautophagy of the nucleus; IEA:EnsemblFungi.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; IEA:EnsemblFungi.
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 PANTHER; PTHR12768; PTHR12768; 1.
DR Pfam; PF04111; APG6; 1.
DR Pfam; PF17675; APG6_N; 1.
PE 3: Inferred from homology;
KW Autophagy; Coiled coil; Endosome; Membrane; Protein transport; Transport;
KW Vacuole.
FT CHAIN 1..466
FT /note="Vacuolar protein sorting-associated protein 30"
FT /id="PRO_0000443879"
FT REGION 35..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 279..463
FT /note="BARA"
FT /evidence="ECO:0000250|UniProtKB:Q02948"
FT REGION 439..464
FT /note="Required for membrane-association, autophagic
FT function during starvation and normal autophagosome
FT morphology"
FT /evidence="ECO:0000250|UniProtKB:Q02948"
FT COILED 149..258
FT /evidence="ECO:0000255"
SQ SEQUENCE 466 AA; 53321 MW; C30892BDCCB65937 CRC64;
MGDLTLRCMN CRSLLDIDSS LVDLSMAQRD LLLNSETNTD NSDNNKHNGE NDRNIIPQEK
LKIINQVKSP SQLRIGQAKN VTAESYVFLT DTEFSLTKFK NNGDEFVDDE DYDERNKTLS
SRISALSNIF NILSCKSNID YPVCQGCCDT LLEKLKEEYN QELKKRDTYH EFMKRIQEQN
NSVEIYSDGN KGPKELKNLK REKEELLRQL QELEGENDLL QNDIQTLQSQ LKEKQEQQLE
QLREKNVQQM EHLSFIKDIQ SLKNQRVVTL NHIDSLRKLN IYNETFRISH KGPFGTINEL
RLGSVPKIQV PWTEINAALG QVVLLLSLIV EKTSLPLPDY NLKPMGSTSV IEKRDLQTDQ
WFVLKAYGGS EFSLSSLFHK ENPIDKALLA ILEIIKKLSE NVSSNTSEPA SIELPYDISD
DKINGLSILL KSSSPSLEWT TACKFLLTNI KWLLAFSTSR INKAKP
