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Protein

Beclin 1-associated autophagy-related key regulator

Gene

Atg14

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Required for both basal and inducible autophagy (PubMed:19270696, PubMed:19270693). Determines the localization of the autophagy-specific PI3-kinase complex PI3KC3-C1 (By similarity). Plays a role in autophagosome formation and MAP1LC3/LC3 conjugation to phosphatidylethanolamine (PubMed:19270696, PubMed:19270693). Promotes BECN1 translocation from the trans-Golgi network to autophagosomes (By similarity). Enhances PIK3C3 activity in a BECN1-dependent manner. Essential for the autophagy-dependent phosphorylation of BECN1 (By similarity). Stimulates the phosphorylation of BECN1, but suppresses the phosphorylation of PIK3C3 by AMPK (PubMed:23332761). Binds to STX17-SNAP29 binary t-SNARE complex on autophagosomes and primes it for VAMP8 interaction to promote autophagosome-endolysosome fusion (By similarity). Modulates the hepatic lipid metabolism (PubMed:22992773).By similarity4 Publications

GO - Biological processi

  • autophagosome assembly Source: MGI
  • autophagy Source: UniProtKB
  • cellular response to glucose starvation Source: UniProtKB
  • cellular response to starvation Source: MGI
  • endosome to lysosome transport Source: MGI
  • macroautophagy Source: MGI
  • mitophagy in response to mitochondrial depolarization Source: MGI
  • negative regulation of protein phosphorylation Source: UniProtKB
  • positive regulation of autophagy Source: CACAO
  • positive regulation of phosphatidylinositol 3-kinase activity Source: MGI
  • positive regulation of protein phosphorylation Source: UniProtKB
  • posttranscriptional regulation of gene expression Source: MGI
  • regulation of protein phosphorylation Source: MGI
  • regulation of triglyceride metabolic process Source: MGI
Complete GO annotation...

Keywords - Biological processi

Autophagy

Enzyme and pathway databases

ReactomeiR-MMU-1632852. Macroautophagy.

Names & Taxonomyi

Protein namesi
Recommended name:
Beclin 1-associated autophagy-related key regulatorBy similarity
Short name:
BarkorBy similarity
Alternative name(s):
Autophagy-related protein 14-like protein1 Publication
Short name:
Atg14L1 Publication
Gene namesi
Name:Atg14Imported
Synonyms:Atg14L1 Publication, D14Ertd436e, Kiaa0831
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 14

Organism-specific databases

MGIiMGI:1261775. Atg14.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoplasmic vesicle, Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 492492Beclin 1-associated autophagy-related key regulatorPRO_0000050775Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei29 – 291PhosphoserineBy similarity
Modified residuei416 – 4161PhosphoserineBy similarity
Modified residuei429 – 4291PhosphothreonineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ8CDJ3.
PaxDbiQ8CDJ3.
PRIDEiQ8CDJ3.

PTM databases

iPTMnetiQ8CDJ3.
PhosphoSiteiQ8CDJ3.

Expressioni

Tissue specificityi

Widely expressed.1 Publication

Inductioni

Expression is controlled by forkhead box O FoxO1 transcription factor and circadian rhythms.1 Publication

Gene expression databases

BgeeiQ8CDJ3.
CleanExiMM_D14ERTD436E.
GenevisibleiQ8CDJ3. MM.

Interactioni

Subunit structurei

Forms homooligomers; homo-oligomerization is essential for the roles in membrane tethering and enhancement of SNARE-mediated fusion (By similarity). Component of the PI3K (PI3KC3/PI3K-III/class III phosphatidylinositol 3-kinase) complex I (PI3KC3-C1) in which the core composed of the catalytic subunit PIK3C3, the regulatory subunit PIK3R4 and BECN1 is associated with ATG14 (PubMed:19270693, PubMed:22745922, PubMed:23332761). PI3KC3-C1 displays a V-shaped architecture with PIK3R4 serving as a bridge between PIK3C3 and the ATG14:BECN1 subcomplex (By similarity). PI3KC3-C1 can associate with further regulatory subunits (PubMed:24849286). Interacts with PIK3CB (PubMed:21059846). Interacts with BECN1P1/BECN2 (By similarity). Interacts with the STX17-SNAP29 binary t-SNARE complex (By similarity). Interacts with NRBF2 (PubMed:24849286).By similarity5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Nrbf2Q8VCQ37EBI-3506699,EBI-2365563

Protein-protein interaction databases

DIPiDIP-60849N.
IntActiQ8CDJ3. 10 interactions.
STRINGi10090.ENSMUSP00000039047.

Structurei

3D structure databases

ProteinModelPortaliQ8CDJ3.
SMRiQ8CDJ3. Positions 301-334.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni413 – 49280BATSAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili70 – 180111Sequence analysisAdd
BLAST

Domaini

The coiled-coil domain is required for BECN1- and PIK3C3-binding and for autophagy.By similarity
The final 80 residues in the C-terminus define a minimum required region for autophagosome binding called BATS.1 Publication
The N-terminal cysteine repeats are required for proper localization to the endoplasmic reticulum.By similarity

Sequence similaritiesi

Belongs to the ATG14 family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG4398. Eukaryota.
ENOG410Y9W5. LUCA.
GeneTreeiENSGT00390000011854.
HOGENOMiHOG000045344.
HOVERGENiHBG081828.
InParanoidiQ8CDJ3.
KOiK17889.
OMAiYSAYYSW.
OrthoDBiEOG7SV0WR.
PhylomeDBiQ8CDJ3.
TreeFamiTF323392.

Family and domain databases

InterProiIPR018791. UV_resistance/autophagy_Atg14.
[Graphical view]
PfamiPF10186. Atg14. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8CDJ3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASPSGKGSW TPEAPGFGPR ALARDLVDSV DDAEGLYVAV ERCPLCNTTR
60 70 80 90 100
RRLTCAKCVQ SGDFVYFDGR DRERFIDKKE RLSQLKNKQE EFQKEVLKAM
110 120 130 140 150
EGKRLTDQLR WKIMSCKMRI EQLKQTICKG NEEMKKNSEG LLKNKEKNQK
160 170 180 190 200
LYSRAQRHQE KKEKIQRHNR KLGDLVEKKT IDLKSHYERL ARLRRSHILE
210 220 230 240 250
LTSIIFPIDE VKTSGRDPAD VSSETDSAMT SSMVSKLAEA RRTTYLSGRW
260 270 280 290 300
VCDDHNGDTS ISITGPWISL PNNGDYSAYY NWVEEKKTTQ GPDMEHNNPA
310 320 330 340 350
YTISAALGYA TQLVNIVSHI LDINLPKKLC NSEFCGENLS KQKLTRAVRK
360 370 380 390 400
LNANILYLCS SQHVNLDQLQ PLHTLRNLMH LVSPRSEHLG RSGPFEVRAD
410 420 430 440 450
LEESMEFVDP GVAGESDASG DERVSDEETD LGTDWENLPS PRFCDIPSQP
460 470 480 490
VEVSQSQSTQ VSPPIASSSA GGMISSAAAS VTSWFKAYTG HR
Length:492
Mass (Da):55,388
Last modified:March 1, 2003 - v1
Checksum:iA221B3C03C8E2F9A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK029967 mRNA. Translation: BAC26705.1.
AK054196 mRNA. Translation: BAC35689.1.
BC025038 mRNA. Translation: AAH25038.1.
BC057360 mRNA. Translation: AAH57360.1.
BC090995 mRNA. Translation: AAH90995.1.
AK173037 mRNA. Translation: BAD32315.1.
CCDSiCCDS26989.1.
RefSeqiNP_766187.1. NM_172599.4.
UniGeneiMm.287279.
Mm.470462.

Genome annotation databases

EnsembliENSMUST00000042988; ENSMUSP00000039047; ENSMUSG00000037526.
GeneIDi100504663.
KEGGimmu:100504663.
UCSCiuc007tik.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK029967 mRNA. Translation: BAC26705.1.
AK054196 mRNA. Translation: BAC35689.1.
BC025038 mRNA. Translation: AAH25038.1.
BC057360 mRNA. Translation: AAH57360.1.
BC090995 mRNA. Translation: AAH90995.1.
AK173037 mRNA. Translation: BAD32315.1.
CCDSiCCDS26989.1.
RefSeqiNP_766187.1. NM_172599.4.
UniGeneiMm.287279.
Mm.470462.

3D structure databases

ProteinModelPortaliQ8CDJ3.
SMRiQ8CDJ3. Positions 301-334.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-60849N.
IntActiQ8CDJ3. 10 interactions.
STRINGi10090.ENSMUSP00000039047.

PTM databases

iPTMnetiQ8CDJ3.
PhosphoSiteiQ8CDJ3.

Proteomic databases

MaxQBiQ8CDJ3.
PaxDbiQ8CDJ3.
PRIDEiQ8CDJ3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000042988; ENSMUSP00000039047; ENSMUSG00000037526.
GeneIDi100504663.
KEGGimmu:100504663.
UCSCiuc007tik.2. mouse.

Organism-specific databases

CTDi22863.
MGIiMGI:1261775. Atg14.
RougeiSearch...

Phylogenomic databases

eggNOGiKOG4398. Eukaryota.
ENOG410Y9W5. LUCA.
GeneTreeiENSGT00390000011854.
HOGENOMiHOG000045344.
HOVERGENiHBG081828.
InParanoidiQ8CDJ3.
KOiK17889.
OMAiYSAYYSW.
OrthoDBiEOG7SV0WR.
PhylomeDBiQ8CDJ3.
TreeFamiTF323392.

Enzyme and pathway databases

ReactomeiR-MMU-1632852. Macroautophagy.

Miscellaneous databases

NextBioi33367523.
PROiQ8CDJ3.
SOURCEiSearch...

Gene expression databases

BgeeiQ8CDJ3.
CleanExiMM_D14ERTD436E.
GenevisibleiQ8CDJ3. MM.

Family and domain databases

InterProiIPR018791. UV_resistance/autophagy_Atg14.
[Graphical view]
PfamiPF10186. Atg14. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Oviduct and Testis.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J and FVB/N.
    Tissue: Embryonic brain, Heart and Mammary gland.
  3. "Prediction of the coding sequences of mouse homologues of KIAA gene: IV. The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
    Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H., Nagase T., Ohara O., Koga H.
    DNA Res. 11:205-218(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 307-492.
    Tissue: Spleen.
  4. "Beclin 1 forms two distinct phosphatidylinositol 3-kinase complexes with mammalian Atg14 and UVRAG."
    Itakura E., Kishi C., Inoue K., Mizushima N.
    Mol. Biol. Cell 19:5360-5372(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  5. "Two Beclin 1-binding proteins, Atg14L and Rubicon, reciprocally regulate autophagy at different stages."
    Matsunaga K., Saitoh T., Tabata K., Omori H., Satoh T., Kurotori N., Maejima I., Shirahama-Noda K., Ichimura T., Isobe T., Akira S., Noda T., Yoshimori T.
    Nat. Cell Biol. 11:385-396(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  6. "Distinct regulation of autophagic activity by Atg14L and Rubicon associated with Beclin 1-phosphatidylinositol-3-kinase complex."
    Zhong Y., Wang Q.J., Li X., Yan Y., Backer J.M., Chait B.T., Heintz N., Yue Z.
    Nat. Cell Biol. 11:468-476(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH BECN1 AND PIK3C3.
  7. "Characterization of autophagosome formation site by a hierarchical analysis of mammalian Atg proteins."
    Itakura E., Mizushima N.
    Autophagy 6:764-776(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  8. "The class IA phosphatidylinositol 3-kinase p110-beta subunit is a positive regulator of autophagy."
    Dou Z., Chattopadhyay M., Pan J.-A., Guerriero J.L., Jiang Y.-P., Ballou L.M., Yue Z., Lin R.Z., Zong W.-X.
    J. Cell Biol. 191:827-843(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PIK3CB.
  9. "Autophagosome targeting and membrane curvature sensing by Barkor/Atg14(L)."
    Fan W., Nassiri A., Zhong Q.
    Proc. Natl. Acad. Sci. U.S.A. 108:7769-7774(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: DOMAIN, SUBCELLULAR LOCATION.
  10. "The actin cytoskeleton participates in the early events of autophagosome formation upon starvation induced autophagy."
    Aguilera M.O., Beron W., Colombo M.I.
    Autophagy 8:1590-1603(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  11. "Mouse skeletal muscle fiber-type-specific macroautophagy and muscle wasting are regulated by a Fyn/STAT3/Vps34 signaling pathway."
    Yamada E., Bastie C.C., Koga H., Wang Y., Cuervo A.M., Pessin J.E.
    Cell Rep. 1:557-569(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE PI3-KINASE COMPLEX I.
  12. "The autophagy-related gene 14 (Atg14) is regulated by forkhead box O transcription factors and circadian rhythms and plays a critical role in hepatic autophagy and lipid metabolism."
    Xiong X., Tao R., DePinho R.A., Dong X.C.
    J. Biol. Chem. 287:39107-39114(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION, FUNCTION.
  13. "Differential regulation of distinct Vps34 complexes by AMPK in nutrient stress and autophagy."
    Kim J., Kim Y.C., Fang C., Russell R.C., Kim J.H., Fan W., Liu R., Zhong Q., Guan K.L.
    Cell 152:290-303(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION IN A COMPLEX WITH PIK3C3; PIK3R4 AND BECN1.
  14. Cited for: SUBCELLULAR LOCATION.
  15. "NRBF2 regulates autophagy and prevents liver injury by modulating Atg14L-linked phosphatidylinositol-3 kinase III activity."
    Lu J., He L., Behrends C., Araki M., Araki K., Jun Wang Q., Catanzaro J.M., Friedman S.L., Zong W.X., Fiel M.I., Li M., Yue Z.
    Nat. Commun. 5:3920-3920(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NRBF2.

Entry informationi

Entry nameiBAKOR_MOUSE
AccessioniPrimary (citable) accession number: Q8CDJ3
Secondary accession number(s): Q69ZY1
, Q6PFY6, Q8C6N0, Q8R3M3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: March 1, 2003
Last modified: May 11, 2016
This is version 94 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.