ATG39_YEAST
ID ATG39_YEAST Reviewed; 398 AA.
AC Q06159; D6VYV5;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Autophagy-related protein 39 {ECO:0000303|PubMed:26040717};
GN Name=ATG39 {ECO:0000303|PubMed:26040717};
GN OrderedLocusNames=YLR312C {ECO:0000312|SGD:S000004303};
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP INTERACTION WITH ATG8 AND ATG11, INDUCTION, DISRUPTION PHENOTYPE,
RP SUBCELLULAR LOCATION, FUNCTION, AND MUTAGENESIS OF 52-ASP--SER-59.
RX PubMed=26040717; DOI=10.1038/nature14506;
RA Mochida K., Oikawa Y., Kimura Y., Kirisako H., Hirano H., Ohsumi Y.,
RA Nakatogawa H.;
RT "Receptor-mediated selective autophagy degrades the endoplasmic reticulum
RT and the nucleus.";
RL Nature 522:359-362(2015).
CC -!- FUNCTION: Acts as a receptor for reticulophagy and nucleophagy. Directs
CC autophagic sequestration of double-membrane vesicles derived from the
CC nuclear envelope and perinuclear endoplasmic reticulum (pnER) into
CC autophagosomes. Is not required for the cytoplasm-to-vacuole targeting
CC pathway, mitophagy, pexophagy, and non-selective autophagy.
CC {ECO:0000269|PubMed:26040717}.
CC -!- SUBUNIT: Interacts with ATG8 and ATG11. {ECO:0000269|PubMed:26040717}.
CC -!- INTERACTION:
CC Q06159; Q12527: ATG11; NbExp=2; IntAct=EBI-33888, EBI-31977;
CC Q06159; P38182: ATG8; NbExp=3; IntAct=EBI-33888, EBI-2684;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:26040717}; Single-pass membrane protein
CC {ECO:0000255}. Preautophagosomal structure membrane
CC {ECO:0000269|PubMed:26040717}; Single-pass membrane protein
CC {ECO:0000255}.
CC -!- INDUCTION: Expression is increased by rapamycin, which mimics nitrogen
CC starvation by inactivating the TORC1 complex.
CC {ECO:0000269|PubMed:26040717}.
CC -!- DISRUPTION PHENOTYPE: Partially blocks reticulophagy, and the double
CC ATG39/ATG40 knockout almost completely blocks this pathway. Leads to
CC abnormal morphology in the nucleus/pnER, when exposed to prolonged
CC nitrogen starvation. {ECO:0000269|PubMed:26040717}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U20618; AAB64517.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09621.1; -; Genomic_DNA.
DR PIR; S53391; S53391.
DR RefSeq; NP_013415.1; NM_001182200.1.
DR AlphaFoldDB; Q06159; -.
DR BioGRID; 31576; 94.
DR DIP; DIP-1453N; -.
DR IntAct; Q06159; 3.
DR MINT; Q06159; -.
DR STRING; 4932.YLR312C; -.
DR TCDB; 1.I.1.1.1; the nuclear pore complex (npc) family.
DR MaxQB; Q06159; -.
DR PaxDb; Q06159; -.
DR PRIDE; Q06159; -.
DR EnsemblFungi; YLR312C_mRNA; YLR312C; YLR312C.
DR GeneID; 851021; -.
DR KEGG; sce:YLR312C; -.
DR SGD; S000004303; ATG39.
DR VEuPathDB; FungiDB:YLR312C; -.
DR eggNOG; ENOG502S3QX; Eukaryota.
DR HOGENOM; CLU_683620_0_0_1; -.
DR InParanoid; Q06159; -.
DR OMA; HIAYPLK; -.
DR BioCyc; YEAST:G3O-32397-MON; -.
DR PRO; PR:Q06159; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; Q06159; protein.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0097038; C:perinuclear endoplasmic reticulum; IDA:SGD.
DR GO; GO:0034045; C:phagophore assembly site membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IMP:SGD.
DR GO; GO:0044804; P:autophagy of nucleus; IMP:SGD.
DR GO; GO:0061709; P:reticulophagy; IMP:SGD.
PE 1: Evidence at protein level;
KW Autophagy; Endoplasmic reticulum; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..398
FT /note="Autophagy-related protein 39"
FT /id="PRO_0000268627"
FT TRANSMEM 148..164
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 15..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 8..11
FT /note="ATG8-binding"
FT /evidence="ECO:0000305|PubMed:26040717"
FT MOTIF 52..59
FT /note="ATG11-binding"
FT /evidence="ECO:0000305|PubMed:26040717"
FT COMPBIAS 15..31
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 52..59
FT /note="DVLSNTSS->AAAAAAAAA: Impairs interaction with ATG8
FT and decreases subsequent reticulophagy."
FT /evidence="ECO:0000269|PubMed:26040717"
SQ SEQUENCE 398 AA; 46628 MW; 0592D785516D9F90 CRC64;
MSEEDDHWNL VRLRRLRKGR EGEEQSSKSE ISLDSLHESS FAGEDDEDFD ADVLSNTSSE
ESAQMNRIYD FRTSNEFSNA GVNIDQTGVP TISESFDTLS GSNVGGTVLP SMEGSKLKDS
TIRNSSTLSD HIIDKSEGKS AKLKMWHVIM LSSLLSMTFS YLALEYSLTG DVLAGFKSQQ
SLRNNERKLL YGNIDFVDKK SYDSSSDSLS QWAPSGKYYV DFDNHIAYPL KDDDLMGWRR
YKTDLVILWY TTKARMKDGW HKRINKINGG RIKLHLFLKN SFKSAQESLR VLHKEQKRRW
KRLFVLLHNK YRQFSPHIKR YFDHSCQKAK QCWSGSRLQL RKLRFKSMKP FRVFQFKVRK
DTNWFVKQLK RFGLKLQHSR MYKAMSECRK KNYFKCKH
