ATG27_DEBHA
ID ATG27_DEBHA Reviewed; 282 AA.
AC Q6BM18;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
DT 25-MAY-2022, entry version 90.
DE RecName: Full=Autophagy-related protein 27;
DE Flags: Precursor;
GN Name=ATG27; OrderedLocusNames=DEHA2F08998g;
OS Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX NCBI_TaxID=284592;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
CC -!- FUNCTION: Effector of VPS34 phosphatidylinositol 3-phosphate kinase
CC signaling. Regulates the cytoplasm to vacuole transport (Cvt) vesicle
CC formation. Plays a role in ATG protein retrieval from the pre-
CC autophagosomal structure (PAS) and is especially required for
CC autophagy-dependent cycling of ATG9 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane {ECO:0000250};
CC Single-pass type I membrane protein {ECO:0000250}. Golgi apparatus
CC membrane {ECO:0000250}; Single-pass type I membrane protein
CC {ECO:0000250}. Mitochondrion membrane {ECO:0000250}; Single-pass
CC membrane protein {ECO:0000250}. Preautophagosomal structure membrane
CC {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
CC Note=Cycles among the pre-autophagosomal structure (PAS), mitochondria
CC and Golgi. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ATG27 family. {ECO:0000305}.
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DR EMBL; CR382138; CAG89094.2; -; Genomic_DNA.
DR RefSeq; XP_460753.2; XM_460753.1.
DR AlphaFoldDB; Q6BM18; -.
DR STRING; 4959.XP_460753.2; -.
DR EnsemblFungi; CAG89094; CAG89094; DEHA2F08998g.
DR GeneID; 2903769; -.
DR KEGG; dha:DEHA2F08998g; -.
DR VEuPathDB; FungiDB:DEHA2F08998g; -.
DR eggNOG; ENOG502QVJJ; Eukaryota.
DR HOGENOM; CLU_089705_0_0_1; -.
DR InParanoid; Q6BM18; -.
DR OMA; NKGNAID; -.
DR OrthoDB; 1240091at2759; -.
DR Proteomes; UP000000599; Chromosome F.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0034045; C:phagophore assembly site membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR Gene3D; 2.70.130.10; -; 1.
DR InterPro; IPR018939; Autophagy-rel_prot_27.
DR InterPro; IPR009011; Man6P_isomerase_rcpt-bd_dom_sf.
DR InterPro; IPR044865; MRH_dom.
DR Pfam; PF09451; ATG27; 1.
DR SUPFAM; SSF50911; SSF50911; 1.
DR PROSITE; PS51914; MRH; 1.
PE 3: Inferred from homology;
KW Autophagy; Cytoplasmic vesicle; Disulfide bond; Glycoprotein;
KW Golgi apparatus; Membrane; Mitochondrion; Protein transport;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..282
FT /note="Autophagy-related protein 27"
FT /id="PRO_0000001777"
FT TOPO_DOM 20..206
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 207..227
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 228..282
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 20..180
FT /note="MRH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT CARBOHYD 53
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 22..61
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 71..78
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 145..178
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
SQ SEQUENCE 282 AA; 31673 MW; 7AEE71FBB101F5A7 CRC64;
MNYIYLISAA LGLIGGVSGI DCGVKELKEY DFESIKGIHS VTTLKDTPPT QTNVTWYIGI
CDTISEKIDH CPKNSDLCGI TSINLEKNSN KDAVVSEIVG FNTNLQKQYK PFTKDGDNNE
DGITIVYKGA NWGDNLVDAE LRFVCASSSD KDKDLDKFQL HQWDDKRLKV SVKTKAACIT
DKKDKKKPDN KKDNKKGNDK DDNGESWGWF TWIFIFLVLF LSIYIVGGAW FQYSKGNAID
FQSALREVLE NFVSLLKGLP SFVREIIEKF TGNSNRGEYS AV
