ATG27_LODEL
ID ATG27_LODEL Reviewed; 272 AA.
AC A5DZ34;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 2.
DT 25-MAY-2022, entry version 60.
DE RecName: Full=Autophagy-related protein 27;
DE Flags: Precursor;
GN Name=ATG27; ORFNames=LELG_02621;
OS Lodderomyces elongisporus (strain ATCC 11503 / CBS 2605 / JCM 1781 / NBRC
OS 1676 / NRRL YB-4239) (Yeast) (Saccharomyces elongisporus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade;
OC Lodderomyces.
OX NCBI_TaxID=379508;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11503 / BCRC 21390 / CBS 2605 / JCM 1781 / NBRC 1676 / NRRL
RC YB-4239;
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EDK44442.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR EMBL; CH981526; EDK44442.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_001526063.1; XM_001526013.1.
DR AlphaFoldDB; A5DZ34; -.
DR STRING; 36914.XP_001526063.1; -.
DR EnsemblFungi; EDK44442; EDK44442; LELG_02621.
DR GeneID; 5232914; -.
DR KEGG; lel:LELG_02621; -.
DR eggNOG; ENOG502S1VT; Eukaryota.
DR HOGENOM; CLU_089705_0_0_1; -.
DR InParanoid; A5DZ34; -.
DR OrthoDB; 1240091at2759; -.
DR Proteomes; UP000001996; 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..17
FT /evidence="ECO:0000255"
FT CHAIN 18..272
FT /note="Autophagy-related protein 27"
FT /id="PRO_0000318051"
FT TOPO_DOM 18..193
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 194..214
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 215..272
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 18..166
FT /note="MRH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 20..59
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 68..75
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 135..164
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
SQ SEQUENCE 272 AA; 30436 MW; 734684ACCF1E5092 CRC64;
MLNRLLIFIT LALAVRALDC SSKELQQYNL ESVKGTYSIS NIKSTPPSKT NITWSIGICE
PIKDVADCPQ NSDVCGITSI LIDGKSPVVS EIIGFNSNVQ KEYETIAEGD GGIIVKDKAV
NWGDSLIDAE IHFICDKNAK ENDLKLDKWD GQSVKLSFKS KAACITSDKD KKKNNGNNND
NNKNNDKKKD NGELWGWFTW IFIFLVLFLS IYYCGVRARG SSTIRETPFY FQSALKEVIE
NFIDLLKSLP SFIREIIERF TGSSGRAEYS AV
