ATG40_YEAST
ID ATG40_YEAST Reviewed; 256 AA.
AC Q99325; D6W2K9;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Autophagy-related protein 40 {ECO:0000303|PubMed:26040717};
DE Flags: Precursor;
GN Name=ATG40 {ECO:0000303|PubMed:26040717};
GN OrderedLocusNames=YOR152C {ECO:0000312|SGD:S000005678};
GN ORFNames=O3536 {ECO:0000312|SGD:S000005678};
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 [GENOMIC DNA].
RC STRAIN=S288c / FY1678;
RX PubMed=9046089;
RX DOI=10.1002/(sici)1097-0061(199701)13:1<73::aid-yea52>3.0.co;2-m;
RA Bordonne R., Camasses A., Madania A., Poch O., Tarassov I.A., Winsor B.,
RA Martin R.P.;
RT "Analysis of a 35.6 kb region on the right arm of Saccharomyces cerevisiae
RT chromosome XV.";
RL Yeast 13:73-83(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [5]
RP INDUCTION.
RX PubMed=12788058; DOI=10.1016/s0006-291x(03)00907-0;
RA Ohkuni K., Shirahige K., Kikuchi A.;
RT "Genome-wide expression analysis of NAP1 in Saccharomyces cerevisiae.";
RL Biochem. Biophys. Res. Commun. 306:5-9(2003).
RN [6]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [7]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 208353 / W303-1A;
RX PubMed=16847258; DOI=10.1073/pnas.0604075103;
RA Kim H., Melen K., Oesterberg M., von Heijne G.;
RT "A global topology map of the Saccharomyces cerevisiae membrane proteome.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006).
RN [8]
RP INTERACTION WITH ATG8 AND ATG11, DOMAIN, DISRUPTION PHENOTYPE, SUBCELLULAR
RP LOCATION, FUNCTION, AND MUTAGENESIS OF TYR-242 AND MET-245.
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. Directs autophagic
CC sequestration of folded tubules/sheets derived from the cortical
CC endoplasmic reticulum (cER) and the cytoplasmic endoplasmic reticulum
CC (cytoER) into autophagosomes. Is not required for the cytoplasm-to-
CC vacuole targeting pathway, mitophagy, pexophagy, and non-selective
CC autophagy. {ECO:0000269|PubMed:26040717}.
CC -!- SUBUNIT: Interacts with ATG8 and ATG11. {ECO:0000269|PubMed:26040717}.
CC -!- INTERACTION:
CC Q99325; P38182: ATG8; NbExp=3; IntAct=EBI-3681992, 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: Induced in absence of NAP1 (PubMed:12788058). Expression is
CC increased by rapamycin, which mimics nitrogen starvation by
CC inactivating the TORC1 complex (PubMed:26040717).
CC {ECO:0000269|PubMed:12788058, ECO:0000269|PubMed:26040717}.
CC -!- DISRUPTION PHENOTYPE: Partially blocks reticulophagy, and the double
CC ATG39/ATG40 knockout almost completely blocks this pathway. Leads to a
CC more densely reticulated cytoplasmic endoplasmic reticulum (cER).
CC {ECO:0000269|PubMed:26040717}.
CC -!- MISCELLANEOUS: Present with 1890 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; U55020; AAC49638.1; -; Genomic_DNA.
DR EMBL; Z75060; CAA99358.1; -; Genomic_DNA.
DR EMBL; AY557755; AAS56081.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10925.1; -; Genomic_DNA.
DR PIR; S67040; S67040.
DR RefSeq; NP_014795.1; NM_001183571.1.
DR PDB; 7BRN; X-ray; 2.23 A; A=237-252.
DR PDBsum; 7BRN; -.
DR AlphaFoldDB; Q99325; -.
DR SMR; Q99325; -.
DR BioGRID; 34548; 38.
DR DIP; DIP-61576N; -.
DR IntAct; Q99325; 3.
DR STRING; 4932.YOR152C; -.
DR PaxDb; Q99325; -.
DR PRIDE; Q99325; -.
DR EnsemblFungi; YOR152C_mRNA; YOR152C; YOR152C.
DR GeneID; 854323; -.
DR KEGG; sce:YOR152C; -.
DR SGD; S000005678; ATG40.
DR VEuPathDB; FungiDB:YOR152C; -.
DR eggNOG; ENOG502S6VJ; Eukaryota.
DR HOGENOM; CLU_1103309_0_0_1; -.
DR InParanoid; Q99325; -.
DR OMA; TRELVYD; -.
DR BioCyc; YEAST:G3O-33669-MON; -.
DR PRO; PR:Q99325; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q99325; protein.
DR GO; GO:0032541; C:cortical endoplasmic reticulum; IDA:SGD.
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:0016020; C:membrane; 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:0061709; P:reticulophagy; IMP:SGD.
PE 1: Evidence at protein level;
KW 3D-structure; Autophagy; Endoplasmic reticulum; Membrane;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT CHAIN 17..256
FT /note="Autophagy-related protein 40"
FT /id="PRO_0000245280"
FT TOPO_DOM 17..67
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 68..88
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 89..256
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 197..243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 242..245
FT /note="ATG8-binding"
FT /evidence="ECO:0000305|PubMed:26040717"
FT COMPBIAS 210..239
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 242
FT /note="Y->A: Impairs interaction with ATG8 and decreases
FT subsequent reticulophagy; when associated with A-245."
FT /evidence="ECO:0000269|PubMed:26040717"
FT MUTAGEN 245
FT /note="M->A: Impairs interaction with ATG8 and decreases
FT subsequent reticulophagy; when associated with A-245."
FT /evidence="ECO:0000269|PubMed:26040717"
FT TURN 238..241
FT /evidence="ECO:0007829|PDB:7BRN"
FT HELIX 246..248
FT /evidence="ECO:0007829|PDB:7BRN"
SQ SEQUENCE 256 AA; 29693 MW; FD4951C817E2AD0F CRC64;
MFNLILWPLF LLTSVAIPLQ LTLEVVYLTS SVDFSKASAA KTATSLGQSP VVITIYKSLL
KYWSLYEFIH FIYLYTPIDA FLNFLPFTSL LMSFGSICLT RELVYDFIAF MESQNKLTGF
LNKITEPNFN SYLLFSSIYN IWFADDTNDK FLFGKLTQIL ISVTKRYEFP RTFYLAKVSD
FLQNLILTRL RPFVTEQPQG DKNRYQNGDR ESTKNGAAYQ KSSQQSSSFE QNFTSTEFPN
DYDFMEDILD ETTELD
