ID   ATG27_YEAS7             Reviewed;         271 AA.
AC   A6ZQF6;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   03-AUG-2022, entry version 47.
DE   RecName: Full=Autophagy-related protein 27;
DE   Flags: Precursor;
GN   Name=ATG27; ORFNames=SCY_3117;
OS   Saccharomyces cerevisiae (strain YJM789) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=307796;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YJM789;
RX   PubMed=17652520; DOI=10.1073/pnas.0701291104;
RA   Wei W., McCusker J.H., Hyman R.W., Jones T., Ning Y., Cao Z., Gu Z.,
RA   Bruno D., Miranda M., Nguyen M., Wilhelmy J., Komp C., Tamse R., Wang X.,
RA   Jia P., Luedi P., Oefner P.J., David L., Dietrich F.S., Li Y., Davis R.W.,
RA   Steinmetz L.M.;
RT   "Genome sequencing and comparative analysis of Saccharomyces cerevisiae
RT   strain YJM789.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:12825-12830(2007).
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   -!- SUBUNIT: Forms a complex with ATG9 and ATG23.
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; AAFW02000044; EDN63208.1; -; Genomic_DNA.
DR   AlphaFoldDB; A6ZQF6; -.
DR   PRIDE; A6ZQF6; -.
DR   EnsemblFungi; EDN63208; EDN63208; SCY_3117.
DR   HOGENOM; CLU_089705_0_0_1; -.
DR   Proteomes; UP000007060; Unassembled WGS sequence.
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   PROSITE; PS51914; MRH; 1.
PE   3: Inferred from homology;
KW   Autophagy; Cytoplasmic vesicle; Disulfide bond; Golgi apparatus; Membrane;
KW   Mitochondrion; Protein transport; Signal; Transmembrane;
KW   Transmembrane helix; Transport.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..271
FT                   /note="Autophagy-related protein 27"
FT                   /id="PRO_0000318056"
FT   TOPO_DOM        20..197
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        198..218
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        219..271
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   DOMAIN          20..166
FT                   /note="MRH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT   REGION          161..190
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        164..190
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        22..60
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT   DISULFID        71..78
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT   DISULFID        135..164
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
SQ   SEQUENCE   271 AA;  30255 MW;  4136A20E4C3797FE CRC64;
     MVSKTWICGF ISIITVVQAL SCEKHDVLKK YQVGKFSSLT STERDTPPST TIEKWWINVC
     EEHTVEPPED CKKNDMLCGL TDVILPGKDA ITTQIIDFDK NIGFNVEETE SALTLTLKGA
     TWGANSFDAK LEFQCNDNMK QDELTSHTWA DKSIQLTLKG PSGCLKSKDD DKKNGDGDNG
     KDGDNEGKKP AKKAGGTLWF TWLFLYALLF TLIYLMVVSF LNTRGGSFQD FRAEFIQRST
     QFLTSLPEFC REVVSRILGR STAQRGGYSA V