ATG27_PICGU
ID ATG27_PICGU Reviewed; 259 AA.
AC A5DE01;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 2.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=Autophagy-related protein 27;
DE Flags: Precursor;
GN Name=ATG27; ORFNames=PGUG_01502;
OS Meyerozyma guilliermondii (strain ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539
OS / NBRC 10279 / NRRL Y-324) (Yeast) (Candida guilliermondii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Meyerozyma.
OX NCBI_TaxID=294746;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539 / NBRC 10279 / NRRL Y-324;
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W.J., Harris D., Hoyer L.L., Hube B.,
RA Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M.,
RA Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F.,
RA Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D.,
RA Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T.,
RA Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C.,
RA Birren B.W., Kellis M., Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
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; CH408156; EDK37404.2; -; Genomic_DNA.
DR RefSeq; XP_001485831.1; XM_001485781.1.
DR AlphaFoldDB; A5DE01; -.
DR SMR; A5DE01; -.
DR STRING; 4929.XP_001485831.1; -.
DR EnsemblFungi; EDK37404; EDK37404; PGUG_01502.
DR GeneID; 5127456; -.
DR KEGG; pgu:PGUG_01502; -.
DR VEuPathDB; FungiDB:PGUG_01502; -.
DR eggNOG; ENOG502QVJJ; Eukaryota.
DR HOGENOM; CLU_089705_0_0_1; -.
DR InParanoid; A5DE01; -.
DR OMA; NKGNAID; -.
DR OrthoDB; 1240091at2759; -.
DR Proteomes; UP000001997; 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 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..15
FT /evidence="ECO:0000255"
FT CHAIN 16..259
FT /note="Autophagy-related protein 27"
FT /id="PRO_0000318053"
FT TOPO_DOM 16..184
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT TRANSMEM 185..205
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 206..259
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT DOMAIN 16..167
FT /note="MRH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 18..57
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 68..75
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 135..165
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
SQ SEQUENCE 259 AA; 29027 MW; 0EB4967D882A7770 CRC64;
MWFPILTWLV ATAVALDCSA KDLDSYNFAL LQGTHAVESV KDTPPSTTKT TWYFGICESV
SSKKAPACPK NVDICGVTEV KVDKDYIVTQ VVGFNSNLEK KYTPVESKNE NGIKISYKGA
NWGSSLVNAE VYYICAEDKD GDDTFTVESW DDEMLFAQVK SKAACVTSKD DKKKPKKPED
NGESWGWFTW IFIFMVLFLS IYIIGGAWFQ YNKGNAIDFQ SALREVLENF VDLVRGLPSF
IREIIEKVTG SNRGEYSAV
