ID BAKOR_MOUSE Reviewed; 492 AA.
AC Q8CDJ3; Q69ZY1; Q6PFY6; Q8C6N0; Q8R3M3;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 27-MAR-2024, entry version 140.
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:0000303|PubMed:19270696};
DE Short=Atg14L {ECO:0000303|PubMed:19270696};
GN Name=Atg14 {ECO:0000312|MGI:MGI:1261775};
GN Synonyms=Atg14L {ECO:0000303|PubMed:19270696}, D14Ertd436e, Kiaa0831;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Oviduct, and Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and FVB/N;
RC TISSUE=Embryonic brain, Heart, and Mammary gland;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 307-492.
RC TISSUE=Spleen;
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 11:205-218(2004).
RN [4]
RP TISSUE SPECIFICITY.
RX PubMed=18843052; DOI=10.1091/mbc.e08-01-0080;
RA Itakura E., Kishi C., Inoue K., Mizushima N.;
RT "Beclin 1 forms two distinct phosphatidylinositol 3-kinase complexes with
RT mammalian Atg14 and UVRAG.";
RL Mol. Biol. Cell 19:5360-5372(2008).
RN [5]
RP FUNCTION.
RX PubMed=19270696; DOI=10.1038/ncb1846;
RA Matsunaga K., Saitoh T., Tabata K., Omori H., Satoh T., Kurotori N.,
RA Maejima I., Shirahama-Noda K., Ichimura T., Isobe T., Akira S., Noda T.,
RA Yoshimori T.;
RT "Two Beclin 1-binding proteins, Atg14L and Rubicon, reciprocally regulate
RT autophagy at different stages.";
RL Nat. Cell Biol. 11:385-396(2009).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH BECN1 AND PIK3C3.
RX PubMed=19270693; DOI=10.1038/ncb1854;
RA Zhong Y., Wang Q.J., Li X., Yan Y., Backer J.M., Chait B.T., Heintz N.,
RA Yue Z.;
RT "Distinct regulation of autophagic activity by Atg14L and Rubicon
RT associated with Beclin 1-phosphatidylinositol-3-kinase complex.";
RL Nat. Cell Biol. 11:468-476(2009).
RN [7]
RP SUBCELLULAR LOCATION.
RX PubMed=20639694; DOI=10.4161/auto.6.6.12709;
RA Itakura E., Mizushima N.;
RT "Characterization of autophagosome formation site by a hierarchical
RT analysis of mammalian Atg proteins.";
RL Autophagy 6:764-776(2010).
RN [8]
RP INTERACTION WITH PIK3CB.
RX PubMed=21059846; DOI=10.1083/jcb.201006056;
RA Dou Z., Chattopadhyay M., Pan J.-A., Guerriero J.L., Jiang Y.-P.,
RA Ballou L.M., Yue Z., Lin R.Z., Zong W.-X.;
RT "The class IA phosphatidylinositol 3-kinase p110-beta subunit is a positive
RT regulator of autophagy.";
RL J. Cell Biol. 191:827-843(2010).
RN [9]
RP DOMAIN, AND SUBCELLULAR LOCATION.
RX PubMed=21518905; DOI=10.1073/pnas.1016472108;
RA Fan W., Nassiri A., Zhong Q.;
RT "Autophagosome targeting and membrane curvature sensing by
RT Barkor/Atg14(L).";
RL Proc. Natl. Acad. Sci. U.S.A. 108:7769-7774(2011).
RN [10]
RP SUBCELLULAR LOCATION.
RX PubMed=22863730; DOI=10.4161/auto.21459;
RA Aguilera M.O., Beron W., Colombo M.I.;
RT "The actin cytoskeleton participates in the early events of autophagosome
RT formation upon starvation induced autophagy.";
RL Autophagy 8:1590-1603(2012).
RN [11]
RP IDENTIFICATION IN THE PI3-KINASE COMPLEX I.
RX PubMed=22745922; DOI=10.1016/j.celrep.2012.03.014;
RA Yamada E., Bastie C.C., Koga H., Wang Y., Cuervo A.M., Pessin J.E.;
RT "Mouse skeletal muscle fiber-type-specific macroautophagy and muscle
RT wasting are regulated by a Fyn/STAT3/Vps34 signaling pathway.";
RL Cell Rep. 1:557-569(2012).
RN [12]
RP INDUCTION, AND FUNCTION.
RX PubMed=22992773; DOI=10.1074/jbc.m112.412569;
RA Xiong X., Tao R., DePinho R.A., Dong X.C.;
RT "The autophagy-related gene 14 (Atg14) is regulated by forkhead box O
RT transcription factors and circadian rhythms and plays a critical role in
RT hepatic autophagy and lipid metabolism.";
RL J. Biol. Chem. 287:39107-39114(2012).
RN [13]
RP FUNCTION, AND IDENTIFICATION IN A COMPLEX WITH PIK3C3; PIK3R4 AND BECN1.
RX PubMed=23332761; DOI=10.1016/j.cell.2012.12.016;
RA Kim J., Kim Y.C., Fang C., Russell R.C., Kim J.H., Fan W., Liu R.,
RA Zhong Q., Guan K.L.;
RT "Differential regulation of distinct Vps34 complexes by AMPK in nutrient
RT stress and autophagy.";
RL Cell 152:290-303(2013).
RN [14]
RP SUBCELLULAR LOCATION.
RX PubMed=24089209; DOI=10.1038/nature12639;
RA Pampliega O., Orhon I., Patel B., Sridhar S., Diaz-Carretero A., Beau I.,
RA Codogno P., Satir B.H., Satir P., Cuervo A.M.;
RT "Functional interaction between autophagy and ciliogenesis.";
RL Nature 502:194-200(2013).
RN [15]
RP INTERACTION WITH NRBF2.
RX PubMed=24849286; DOI=10.1038/ncomms4920;
RA Lu J., He L., Behrends C., Araki M., Araki K., Jun Wang Q., Catanzaro J.M.,
RA Friedman S.L., Zong W.X., Fiel M.I., Li M., Yue Z.;
RT "NRBF2 regulates autophagy and prevents liver injury by modulating Atg14L-
RT linked phosphatidylinositol-3 kinase III activity.";
RL Nat. Commun. 5:3920-3920(2014).
RN [16]
RP INTERACTION WITH ARMC3.
RX PubMed=34428398; DOI=10.1016/j.devcel.2021.07.015;
RA Lei Y., Zhang X., Xu Q., Liu S., Li C., Jiang H., Lin H., Kong E., Liu J.,
RA Qi S., Li H., Xu W., Lu K.;
RT "Autophagic elimination of ribosomes during spermiogenesis provides energy
RT for flagellar motility.";
RL Dev. Cell 56:2313-2328(2021).
CC -!- FUNCTION: Required for both basal and inducible autophagy
CC (PubMed:19270696, PubMed:19270693). Determines the localization of the
CC autophagy-specific PI3-kinase complex PI3KC3-C1 (By similarity). Plays
CC a role in autophagosome formation and MAP1LC3/LC3 conjugation to
CC phosphatidylethanolamine (PubMed:19270696, PubMed:19270693). Promotes
CC BECN1 translocation from the trans-Golgi network to autophagosomes (By
CC similarity). Enhances PIK3C3 activity in a BECN1-dependent manner.
CC Essential for the autophagy-dependent phosphorylation of BECN1 (By
CC similarity). Stimulates the phosphorylation of BECN1, but suppresses
CC the phosphorylation of PIK3C3 by AMPK (PubMed:23332761). Binds to
CC STX17-SNAP29 binary t-SNARE complex on autophagosomes and primes it for
CC VAMP8 interaction to promote autophagosome-endolysosome fusion (By
CC similarity). Modulates the hepatic lipid metabolism (PubMed:22992773).
CC {ECO:0000250|UniProtKB:Q6ZNE5, ECO:0000269|PubMed:19270693,
CC ECO:0000269|PubMed:19270696, ECO:0000269|PubMed:22992773,
CC ECO:0000269|PubMed:23332761}.
CC -!- SUBUNIT: Forms homooligomers; homo-oligomerization is essential for the
CC roles in membrane tethering and enhancement of SNARE-mediated fusion
CC (By similarity). Component of the PI3K (PI3KC3/PI3K-III/class III
CC phosphatidylinositol 3-kinase) complex I (PI3KC3-C1) in which the core
CC composed of the catalytic subunit PIK3C3, the regulatory subunit PIK3R4
CC and BECN1 is associated with ATG14 (PubMed:19270693, PubMed:22745922,
CC PubMed:23332761). PI3KC3-C1 displays a V-shaped architecture with
CC PIK3R4 serving as a bridge between PIK3C3 and the ATG14:BECN1
CC subcomplex (By similarity). PI3KC3-C1 can associate with further
CC regulatory subunits (PubMed:24849286). Interacts with PIK3CB
CC (PubMed:21059846). Interacts (via coiled-coil domain) with BECN2 (via
CC 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 (PubMed:24849286)
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). Interacts with ARMC3 (via ARM domains)
CC (PubMed:34428398). {ECO:0000250|UniProtKB:Q6ZNE5,
CC ECO:0000269|PubMed:19270693, ECO:0000269|PubMed:21059846,
CC ECO:0000269|PubMed:22745922, ECO:0000269|PubMed:23332761,
CC ECO:0000269|PubMed:24849286, ECO:0000269|PubMed:34428398}.
CC -!- INTERACTION:
CC Q8CDJ3; P23242: Gja1; NbExp=2; IntAct=EBI-3506699, EBI-298630;
CC Q8CDJ3; Q8VCQ3: Nrbf2; NbExp=7; IntAct=EBI-3506699, EBI-2365563;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20639694}.
CC Endoplasmic reticulum membrane {ECO:0000269|PubMed:20639694};
CC Peripheral membrane protein {ECO:0000305}. Preautophagosomal structure
CC membrane {ECO:0000269|PubMed:19270693, ECO:0000269|PubMed:20639694,
CC ECO:0000269|PubMed:22863730}; Peripheral membrane protein
CC {ECO:0000305}. Cytoplasmic vesicle, autophagosome membrane
CC {ECO:0000250|UniProtKB:Q6ZNE5}; Peripheral membrane protein
CC {ECO:0000305}. Note=Cytosolic under nutrient-rich conditions
CC (PubMed:20639694). Following autophagy stimuli, such as starvation or
CC rapamycin induction, predominantly detected in cytoplasmic foci,
CC identified as isolation membranes and autophagosomes (PubMed:20639694).
CC Accumulates on highly curved PtdIns(3)P enriched autophagic membrane
CC via its BATS domain to sense and maintain membrane curvature
CC (PubMed:21518905). Localizes also to discrete punctae along the ciliary
CC axoneme and to the base of the ciliary axoneme (PubMed:24089209).
CC {ECO:0000269|PubMed:20639694, ECO:0000269|PubMed:21518905,
CC ECO:0000269|PubMed:24089209}.
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:18843052}.
CC -!- INDUCTION: Expression is controlled by forkhead box O FoxO1
CC transcription factor and circadian rhythms.
CC {ECO:0000269|PubMed:22992773}.
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:0000269|PubMed:21518905}.
CC -!- DOMAIN: The N-terminal cysteine repeats are required for proper
CC localization to the endoplasmic reticulum.
CC {ECO:0000250|UniProtKB:Q6ZNE5}.
CC -!- PTM: Ubiquitinated via 'Lys-6', 'Lys-11' and 'Lys-63'-linked
CC polyubiquitin chains on multiple lysines by MARCHF7, leading to ATG14
CC aggregation and loss of interaction with STX17.
CC {ECO:0000250|UniProtKB:Q6ZNE5}.
CC -!- SIMILARITY: Belongs to the ATG14 family. {ECO:0000305}.
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DR EMBL; AK029967; BAC26705.1; -; mRNA.
DR EMBL; AK054196; BAC35689.1; -; mRNA.
DR EMBL; BC025038; AAH25038.1; -; mRNA.
DR EMBL; BC057360; AAH57360.1; -; mRNA.
DR EMBL; BC090995; AAH90995.1; -; mRNA.
DR EMBL; AK173037; BAD32315.1; -; mRNA.
DR CCDS; CCDS26989.1; -.
DR RefSeq; NP_766187.1; NM_172599.4.
DR PDB; 8GU7; X-ray; 2.60 A; A/B=101-154.
DR PDBsum; 8GU7; -.
DR AlphaFoldDB; Q8CDJ3; -.
DR SMR; Q8CDJ3; -.
DR BioGRID; 425286; 5.
DR ComplexPortal; CPX-75; Phosphatidylinositol 3-kinase complex, class III, ATG14 variant.
DR DIP; DIP-60849N; -.
DR IntAct; Q8CDJ3; 13.
DR MINT; Q8CDJ3; -.
DR STRING; 10090.ENSMUSP00000153718; -.
DR iPTMnet; Q8CDJ3; -.
DR PhosphoSitePlus; Q8CDJ3; -.
DR SwissPalm; Q8CDJ3; -.
DR EPD; Q8CDJ3; -.
DR MaxQB; Q8CDJ3; -.
DR PaxDb; 10090-ENSMUSP00000039047; -.
DR PeptideAtlas; Q8CDJ3; -.
DR ProteomicsDB; 273597; -.
DR Antibodypedia; 24031; 255 antibodies from 32 providers.
DR Ensembl; ENSMUST00000042988.7; ENSMUSP00000039047.7; ENSMUSG00000037526.8.
DR Ensembl; ENSMUST00000226299.2; ENSMUSP00000153718.2; ENSMUSG00000037526.8.
DR GeneID; 100504663; -.
DR KEGG; mmu:100504663; -.
DR UCSC; uc007tik.2; mouse.
DR AGR; MGI:1261775; -.
DR CTD; 22863; -.
DR MGI; MGI:1261775; Atg14.
DR VEuPathDB; HostDB:ENSMUSG00000037526; -.
DR eggNOG; KOG4398; Eukaryota.
DR GeneTree; ENSGT00390000011854; -.
DR HOGENOM; CLU_046719_1_0_1; -.
DR InParanoid; Q8CDJ3; -.
DR OMA; KTQHEHL; -.
DR OrthoDB; 3674063at2759; -.
DR PhylomeDB; Q8CDJ3; -.
DR TreeFam; TF323392; -.
DR Reactome; R-MMU-1632852; Macroautophagy.
DR BioGRID-ORCS; 100504663; 22 hits in 77 CRISPR screens.
DR PRO; PR:Q8CDJ3; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q8CDJ3; Protein.
DR Bgee; ENSMUSG00000037526; Expressed in morula and 251 other cell types or tissues.
DR ExpressionAtlas; Q8CDJ3; baseline and differential.
DR Genevisible; Q8CDJ3; MM.
DR GO; GO:0005776; C:autophagosome; ISO:MGI.
DR GO; GO:0000421; C:autophagosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005930; C:axoneme; IDA: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:MGI.
DR GO; GO:0097632; C:extrinsic component of phagophore assembly site membrane; ISO:MGI.
DR GO; GO:0044233; C:mitochondria-associated endoplasmic reticulum membrane; IDA:MGI.
DR GO; GO:0045335; C:phagocytic vesicle; IDA:MGI.
DR GO; GO:0000407; C:phagophore assembly site; ISO:MGI.
DR GO; GO:0034045; C:phagophore assembly site membrane; ISO:MGI.
DR GO; GO:0035032; C:phosphatidylinositol 3-kinase complex, class III; IDA:UniProtKB.
DR GO; GO:0051020; F:GTPase binding; ISO:MGI.
DR GO; GO:0141039; F:phosphatidylinositol 3-kinase inhibitor activity; ISO:MGI.
DR GO; GO:0043495; F:protein-membrane adaptor activity; ISO:MGI.
DR GO; GO:0000045; P:autophagosome assembly; ISO:MGI.
DR GO; GO:0097352; P:autophagosome maturation; ISO:MGI.
DR GO; GO:0016240; P:autophagosome membrane docking; ISO:MGI.
DR GO; GO:0006914; P:autophagy; IMP:UniProtKB.
DR GO; GO:0042149; P:cellular response to glucose starvation; IDA:UniProtKB.
DR GO; GO:0009267; P:cellular response to starvation; ISO:MGI.
DR GO; GO:0045022; P:early endosome to late endosome transport; ISO:MGI.
DR GO; GO:0008333; P:endosome to lysosome transport; ISO:MGI.
DR GO; GO:0016236; P:macroautophagy; ISO:MGI.
DR GO; GO:0000423; P:mitophagy; ISO:MGI.
DR GO; GO:0001933; P:negative regulation of protein phosphorylation; IDA:UniProtKB.
DR GO; GO:0043491; P:phosphatidylinositol 3-kinase/protein kinase B signal transduction; ISO:MGI.
DR GO; GO:0036092; P:phosphatidylinositol-3-phosphate biosynthetic process; ISO:MGI.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IDA:UniProtKB.
DR GO; GO:0010608; P:post-transcriptional regulation of gene expression; ISO:MGI.
DR GO; GO:0006622; P:protein targeting to lysosome; NAS:ComplexPortal.
DR GO; GO:0016241; P:regulation of macroautophagy; ISO:MGI.
DR GO; GO:0001932; P:regulation of protein phosphorylation; ISO:MGI.
DR GO; GO:0090207; P:regulation of triglyceride metabolic process; IMP:MGI.
DR GO; GO:0098780; P:response to mitochondrial depolarisation; ISO:MGI.
DR InterPro; IPR018791; UV_resistance/autophagy_Atg14.
DR PANTHER; PTHR13664; BECLIN 1-ASSOCIATED AUTOPHAGY-RELATED KEY REGULATOR; 1.
DR PANTHER; PTHR13664:SF0; BECLIN 1-ASSOCIATED AUTOPHAGY-RELATED KEY REGULATOR; 1.
DR Pfam; PF10186; ATG14; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Autophagy; Coiled coil; Cytoplasm; Cytoplasmic vesicle;
KW Endoplasmic reticulum; Membrane; Phosphoprotein; Reference proteome;
KW Ubl conjugation.
FT CHAIN 1..492
FT /note="Beclin 1-associated autophagy-related key regulator"
FT /id="PRO_0000050775"
FT REGION 410..439
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 413..492
FT /note="BATS"
FT REGION 451..471
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 70..180
FT /evidence="ECO:0000255"
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"
FT HELIX 101..133
FT /evidence="ECO:0007829|PDB:8GU7"
SQ SEQUENCE 492 AA; 55388 MW; A221B3C03C8E2F9A CRC64;
MASPSGKGSW TPEAPGFGPR ALARDLVDSV DDAEGLYVAV ERCPLCNTTR RRLTCAKCVQ
SGDFVYFDGR DRERFIDKKE RLSQLKNKQE EFQKEVLKAM EGKRLTDQLR WKIMSCKMRI
EQLKQTICKG NEEMKKNSEG LLKNKEKNQK LYSRAQRHQE KKEKIQRHNR KLGDLVEKKT
IDLKSHYERL ARLRRSHILE LTSIIFPIDE VKTSGRDPAD VSSETDSAMT SSMVSKLAEA
RRTTYLSGRW VCDDHNGDTS ISITGPWISL PNNGDYSAYY NWVEEKKTTQ GPDMEHNNPA
YTISAALGYA TQLVNIVSHI LDINLPKKLC NSEFCGENLS KQKLTRAVRK LNANILYLCS
SQHVNLDQLQ PLHTLRNLMH LVSPRSEHLG RSGPFEVRAD LEESMEFVDP GVAGESDASG
DERVSDEETD LGTDWENLPS PRFCDIPSQP VEVSQSQSTQ VSPPIASSSA GGMISSAAAS
VTSWFKAYTG HR
//
