BECN1_ARATH
ID BECN1_ARATH Reviewed; 517 AA.
AC Q9M367; A8MRV3; F4JFF7; Q94BW8;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 2.
DT 25-MAY-2022, entry version 136.
DE RecName: Full=Beclin-1-like protein {ECO:0000305};
DE Short=AtBECLIN 1 {ECO:0000303|PubMed:17339883};
DE AltName: Full=Autophagy protein 6 {ECO:0000303|PubMed:25624505};
DE Short=AtATG6 {ECO:0000303|PubMed:17339883};
DE AltName: Full=Protein VPS30 homolog {ECO:0000303|PubMed:17339883};
DE Short=AtVPS30 {ECO:0000303|PubMed:17339883};
GN Name=ATG6 {ECO:0000303|PubMed:25624505};
GN Synonyms=VPS30 {ECO:0000303|PubMed:17339883};
GN OrderedLocusNames=At3g61710 {ECO:0000312|Araport:AT3G61710};
GN ORFNames=F15G16.100 {ECO:0000312|EMBL:CAB71101.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=17339883; DOI=10.1038/cr.2007.7;
RA Qin G., Ma Z., Zhang L., Xing S., Hou X., Deng J., Liu J., Chen Z.,
RA Qu L.J., Gu H.;
RT "Arabidopsis AtBECLIN 1/AtAtg6/AtVps30 is essential for pollen germination
RT and plant development.";
RL Cell Res. 17:249-263(2007).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=17259285; DOI=10.1104/pp.106.093864;
RA Fujiki Y., Yoshimoto K., Ohsumi Y.;
RT "An Arabidopsis homolog of yeast ATG6/VPS30 is essential for pollen
RT germination.";
RL Plant Physiol. 143:1132-1139(2007).
RN [6]
RP FUNCTION, AND INDUCTION BY PATHOGEN INFECTION.
RX PubMed=17932459; DOI=10.4161/auto.5056;
RA Patel S., Dinesh-Kumar S.P.;
RT "Arabidopsis ATG6 is required to limit the pathogen-associated cell death
RT response.";
RL Autophagy 4:20-27(2008).
RN [7]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=18227644; DOI=10.4161/auto.5629;
RA Harrison-Lowe N.J., Olsen L.J.;
RT "Autophagy protein 6 (ATG6) is required for pollen germination in
RT Arabidopsis thaliana.";
RL Autophagy 4:339-348(2008).
RN [8]
RP BIOTECHNOLOGY.
RX PubMed=21050365; DOI=10.1111/j.1467-7652.2010.00527.x;
RA Singh S.P., Pandey T., Srivastava R., Verma P.C., Singh P.K., Tuli R.,
RA Sawant S.V.;
RT "BECLIN1 from Arabidopsis thaliana under the generic control of regulated
RT expression systems, a strategy for developing male sterile plants.";
RL Plant Biotechnol. J. 8:1005-1022(2010).
RN [9]
RP INDUCTION BY FUNGAL PATHOGEN.
RX PubMed=21395886; DOI=10.1111/j.1365-313x.2011.04553.x;
RA Lai Z., Wang F., Zheng Z., Fan B., Chen Z.;
RT "A critical role of autophagy in plant resistance to necrotrophic fungal
RT pathogens.";
RL Plant J. 66:953-968(2011).
RN [10]
RP FUNCTION, INTERACTION WITH TUBB8/TUB8, AND SUBCELLULAR LOCATION.
RX PubMed=26566764; DOI=10.1080/15548627.2015.1113365;
RA Wang Y., Zheng X., Yu B., Han S., Guo J., Tang H., Yu A.Y., Deng H.,
RA Hong Y., Liu Y.;
RT "Disruption of microtubules in plants suppresses macroautophagy and
RT triggers starch excess-associated chloroplast autophagy.";
RL Autophagy 11:2259-2274(2015).
RN [11]
RP IDENTIFICATION IN A PI3K COMPLEX.
RX PubMed=25624505; DOI=10.1073/pnas.1421271112;
RA Gao C., Zhuang X., Cui Y., Fu X., He Y., Zhao Q., Zeng Y., Shen J., Luo M.,
RA Jiang L.;
RT "Dual roles of an Arabidopsis ESCRT component FREE1 in regulating vacuolar
RT protein transport and autophagic degradation.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:1886-1891(2015).
RN [12]
RP INTERACTION WITH SINAT1; SINAT2; SINAT5; SINAT6; TRAF1A AND TRAF1B,
RP UBIQUITINATION, AND DEGRADATION.
RX PubMed=28351989; DOI=10.1105/tpc.17.00056;
RA Qi H., Xia F.N., Xie L.J., Yu L.J., Chen Q.F., Zhuang X.H., Wang Q., Li F.,
RA Jiang L., Xie Q., Xiao S.;
RT "TRAF family proteins regulate autophagy dynamics by modulating AUTOPHAGY
RT PROTEIN6 stability in Arabidopsis.";
RL Plant Cell 29:890-911(2017).
CC -!- FUNCTION: Required for normal plant development (PubMed:17339883,
CC PubMed:17932459, PubMed:18227644). Required for pollen germination
CC (PubMed:17339883, PubMed:17259285, PubMed:18227644). Required for
CC autophagic activity. Required to limit the pathogen-associated cell
CC death response (PubMed:17932459). May be involved in vacuolar protein
CC sorting (PubMed:17259285). Binds to microtubules. May facilitate
CC efficient recruitment of other ATG proteins to assemble scaffolds for
CC autophagosome biogenesis (PubMed:26566764).
CC {ECO:0000269|PubMed:17259285, ECO:0000269|PubMed:17339883,
CC ECO:0000269|PubMed:17932459, ECO:0000269|PubMed:18227644,
CC ECO:0000269|PubMed:26566764}.
CC -!- SUBUNIT: Component of a phosphatidylinositol 3-kinase (PI3K) complex
CC composed of ATG6, SH3P2 and FREE1 (PubMed:25624505). Interacts with
CC SINAT1, SINAT2, SINAT5, SINAT6, TRAF1A and TRAF1B (PubMed:28351989).
CC Interacts with TUBB8/TUB8 (PubMed:26566764).
CC {ECO:0000269|PubMed:25624505, ECO:0000269|PubMed:26566764,
CC ECO:0000269|PubMed:28351989}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17259285}.
CC Cytoplasm, cytoskeleton {ECO:0000269|PubMed:26566764}. Note=Colocalizes
CC with ATG8I in punctuate structures (PubMed:17259285). Localizes in
CC punctuate structures and colocalizes with microtubules
CC (PubMed:26566764). {ECO:0000269|PubMed:17259285,
CC ECO:0000269|PubMed:26566764}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9M367-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9M367-2; Sequence=VSP_057914, VSP_057915;
CC Name=3;
CC IsoId=Q9M367-3; Sequence=VSP_057913, VSP_057914, VSP_057915;
CC -!- TISSUE SPECIFICITY: Highly expressed in mature pollen grains
CC (PubMed:17339883). Expressed in roots, leaves, stems, flowers and
CC siliques (PubMed:17259285, PubMed:18227644).
CC {ECO:0000269|PubMed:17259285, ECO:0000269|PubMed:17339883,
CC ECO:0000269|PubMed:18227644}.
CC -!- INDUCTION: Induced by infection with the bacterial pathogen Pseudomonas
CC syringae pv tomato strain DC3000 (PubMed:17932459). Induced by
CC infection with the fungal necrotrophic pathogen Botrytis cinerea
CC (PubMed:21395886). {ECO:0000269|PubMed:17932459,
CC ECO:0000269|PubMed:21395886}.
CC -!- PTM: Ubiquitinated (PubMed:28351989). The interaction with SINAT1 or
CC SINAT2, and the presence of TRAF1A/MUSE14 and TRAF1B/MUSE13, mediates
CC its proteasome-dependent degradation (PubMed:28351989).
CC {ECO:0000269|PubMed:28351989}.
CC -!- DISRUPTION PHENOTYPE: Male sterility due to pollen germination defect.
CC {ECO:0000269|PubMed:17259285, ECO:0000269|PubMed:17339883,
CC ECO:0000269|PubMed:18227644}.
CC -!- BIOTECHNOLOGY: Can be used to induced male sterility when expressed in
CC anther tapetum. Development of male sterile lines is important for
CC commercial hybrid seed production. {ECO:0000269|PubMed:21050365}.
CC -!- MISCELLANEOUS: Plants silencing ATG6 exhibit impaired autophagic
CC activity and accelerated senescence. {ECO:0000269|PubMed:17932459}.
CC -!- SIMILARITY: Belongs to the beclin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB71101.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL132959; CAB71101.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE80244.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE80245.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE80246.1; -; Genomic_DNA.
DR EMBL; AY039613; AAK62668.1; -; mRNA.
DR EMBL; BT000508; AAN18077.1; -; mRNA.
DR PIR; T47963; T47963.
DR RefSeq; NP_001030914.1; NM_001035837.1. [Q9M367-3]
DR RefSeq; NP_567116.1; NM_116036.4. [Q9M367-1]
DR RefSeq; NP_974475.1; NM_202746.2. [Q9M367-2]
DR AlphaFoldDB; Q9M367; -.
DR SMR; Q9M367; -.
DR BioGRID; 10658; 4.
DR STRING; 3702.AT3G61710.1; -.
DR TCDB; 9.A.15.3.1; the autophagy-related phagophore-formation transporter (apt) family.
DR PaxDb; Q9M367; -.
DR PRIDE; Q9M367; -.
DR ProteomicsDB; 241133; -. [Q9M367-1]
DR EnsemblPlants; AT3G61710.1; AT3G61710.1; AT3G61710. [Q9M367-1]
DR EnsemblPlants; AT3G61710.2; AT3G61710.2; AT3G61710. [Q9M367-2]
DR EnsemblPlants; AT3G61710.3; AT3G61710.3; AT3G61710. [Q9M367-3]
DR GeneID; 825344; -.
DR Gramene; AT3G61710.1; AT3G61710.1; AT3G61710. [Q9M367-1]
DR Gramene; AT3G61710.2; AT3G61710.2; AT3G61710. [Q9M367-2]
DR Gramene; AT3G61710.3; AT3G61710.3; AT3G61710. [Q9M367-3]
DR KEGG; ath:AT3G61710; -.
DR Araport; AT3G61710; -.
DR TAIR; locus:2076715; AT3G61710.
DR eggNOG; KOG2751; Eukaryota.
DR InParanoid; Q9M367; -.
DR OMA; DTFCIGH; -.
DR OrthoDB; 1085752at2759; -.
DR PhylomeDB; Q9M367; -.
DR PRO; PR:Q9M367; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9M367; baseline and differential.
DR Genevisible; Q9M367; AT.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0000407; C:phagophore assembly site; IDA: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:0000045; P:autophagosome assembly; IGI:UniProtKB.
DR GO; GO:0006995; P:cellular response to nitrogen starvation; IBA:GO_Central.
DR GO; GO:0050832; P:defense response to fungus; IEP:TAIR.
DR GO; GO:0045324; P:late endosome to vacuole transport; IBA:GO_Central.
DR GO; GO:0009846; P:pollen germination; IMP:TAIR.
DR GO; GO:0006623; P:protein targeting to vacuole; IGI:UniProtKB.
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 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Cytoplasm; Cytoskeleton;
KW Reference proteome; Ubl conjugation.
FT CHAIN 1..517
FT /note="Beclin-1-like protein"
FT /id="PRO_0000218558"
FT REGION 76..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 172..266
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..68
FT /note="Missing (in isoform 3)"
FT /id="VSP_057913"
FT VAR_SEQ 364..386
FT /note="CQVKIQPMGSYPRIVDSNNETYE -> YPYNYLTVLFLILPFLFDSVDCI
FT (in isoform 2 and isoform 3)"
FT /id="VSP_057914"
FT VAR_SEQ 387..517
FT /note="Missing (in isoform 2 and isoform 3)"
FT /id="VSP_057915"
SQ SEQUENCE 517 AA; 58504 MW; 15E3D9A40A5C15BE CRC64;
MRKEEIPDKS RTIPIDPNLP KWVCQNCHHS LTIVGVDSYA GKFFNDPPPS ATQGSSIHGA
NSVLGSTRMD NSFVVLPRHK PPQSQGIPPR PRGASSPQPD ATQSGKAMEE SFVVVYKSEP
VSDSGGSHNL SLEVGQNGPL HSNTSGFNAT INVLTRAFDI ARTQTQVEQP LCLECMRVLS
DKLEKEVEDV TRDVEAYEAC VQRLEGETQD VLSEADFLKE KKKIEEEERK LVAAIEETEK
QNAEVNHQLK ELEFKGNRFN ELEDRYWQEF NNFQFQLIAH QEERDAILAK IEVSQAHLEL
LNKTNVLIDA FPIRNDGEFG TINNFRLGRL PAIKVEWDEI NAAWGQACLL LHTMCNYFRP
KFQCQVKIQP MGSYPRIVDS NNETYELFGP VNLFWSTRYD KAMTLYLMCL KDFADFANSK
DQENNIPPDN CLNLPYKIEK DKVLGYSITQ SFNKQESWTK ALKYTLCNLK WALYWFVGNT
NFQPLSATVS LPSNISAAGS LYAKRGPDSS KPSCKKT
