ATG27_PICST
ID ATG27_PICST Reviewed; 269 AA.
AC A3LW83;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 2.
DT 25-MAY-2022, entry version 71.
DE RecName: Full=Autophagy-related protein 27;
DE Flags: Precursor;
GN Name=ATG27; ORFNames=PICST_46861;
OS Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL
OS Y-11545) (Yeast) (Pichia stipitis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Scheffersomyces.
OX NCBI_TaxID=322104;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545;
RX PubMed=17334359; DOI=10.1038/nbt1290;
RA Jeffries T.W., Grigoriev I.V., Grimwood J., Laplaza J.M., Aerts A.,
RA Salamov A., Schmutz J., Lindquist E., Dehal P., Shapiro H., Jin Y.-S.,
RA Passoth V., Richardson P.M.;
RT "Genome sequence of the lignocellulose-bioconverting and xylose-fermenting
RT yeast Pichia stipitis.";
RL Nat. Biotechnol. 25:319-326(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 -!- 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}.
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; CP000499; ABN67240.2; -; Genomic_DNA.
DR RefSeq; XP_001385269.2; XM_001385232.1.
DR AlphaFoldDB; A3LW83; -.
DR STRING; 4924.XP_001385269.2; -.
DR EnsemblFungi; ABN67240; ABN67240; PICST_46861.
DR GeneID; 4839593; -.
DR KEGG; pic:PICST_46861; -.
DR eggNOG; ENOG502QVJJ; Eukaryota.
DR HOGENOM; CLU_089705_0_0_1; -.
DR InParanoid; A3LW83; -.
DR OMA; NKGNAID; -.
DR OrthoDB; 1240091at2759; -.
DR Proteomes; UP000002258; Chromosome 5.
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; Golgi apparatus; Membrane;
KW Mitochondrion; Protein transport; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..269
FT /note="Autophagy-related protein 27"
FT /id="PRO_0000318054"
FT TOPO_DOM 18..193
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT TRANSMEM 194..214
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 215..269
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT DOMAIN 18..175
FT /note="MRH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 20..59
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 69..76
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 141..173
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
SQ SEQUENCE 269 AA; 29937 MW; FC3BFD0900DC46CE CRC64;
MWAIAGLISV LLAQAAAFDC SAKELEHYNF ELLKGIHSVT SLKDTPPSQT NLTWYFGICE
PIKEGLDACP QNSDVCGITS IILKGDSKNR VISEIVSFNT NLQKTYEPFS DSEIDSTGIA
ISYTGATWGD NSINAALRFV CPPKNNEHIL DKFKLDSWDG KKLKASMYSK AACITSDKDK
LKPPPKKPDN GESWGWFTWI FIFLVLFLSI YIVGGAWFQY NKGNAIDFSS ALREVLDNFV
ELLKGIPAFS REIIEKFTSN SNRGEYSAV
