ATG27_CANGA
ID ATG27_CANGA Reviewed; 276 AA.
AC Q6FIW0;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 92.
DE RecName: Full=Autophagy-related protein 27;
DE Flags: Precursor;
GN Name=ATG27; OrderedLocusNames=CAGL0M11352g;
OS Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS Y-65) (Yeast) (Torulopsis glabrata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC Nakaseomyces/Candida clade.
OX NCBI_TaxID=284593;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
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; CR380959; CAG62814.1; -; Genomic_DNA.
DR RefSeq; XP_449834.1; XM_449834.1.
DR AlphaFoldDB; Q6FIW0; -.
DR STRING; 5478.XP_449834.1; -.
DR EnsemblFungi; CAG62814; CAG62814; CAGL0M11352g.
DR GeneID; 2891403; -.
DR KEGG; cgr:CAGL0M11352g; -.
DR CGD; CAL0136241; CAGL0M11352g.
DR VEuPathDB; FungiDB:CAGL0M11352g; -.
DR eggNOG; ENOG502QVJJ; Eukaryota.
DR HOGENOM; CLU_089705_0_0_1; -.
DR InParanoid; Q6FIW0; -.
DR OMA; NKGNAID; -.
DR Proteomes; UP000002428; Chromosome M.
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:0005802; C:trans-Golgi network; IEA:EnsemblFungi.
DR GO; GO:0005774; C:vacuolar membrane; IEA:EnsemblFungi.
DR GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; IEA:EnsemblFungi.
DR GO; GO:0030242; P:autophagy of peroxisome; IEA:EnsemblFungi.
DR GO; GO:0032258; P:cytoplasm to vacuole transport by the Cvt pathway; IEA:EnsemblFungi.
DR GO; GO:0034497; P:protein localization to phagophore assembly site; IEA:EnsemblFungi.
DR GO; GO:0016050; P:vesicle organization; IEA:EnsemblFungi.
DR InterPro; IPR018939; Autophagy-rel_prot_27.
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; Glycoprotein;
KW Golgi apparatus; Membrane; Mitochondrion; Protein transport;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..276
FT /note="Autophagy-related protein 27"
FT /id="PRO_0000001776"
FT TOPO_DOM 19..200
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 201..221
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 222..276
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 19..166
FT /note="MRH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT REGION 162..196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 165..188
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 189
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 21..59
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 276 AA; 30428 MW; 269379AD631E5BD9 CRC64;
MVMLGQVVAL AMASSAVALN CKNHNVLSNY NVANKDILLK NELDTPPSKT SEMWYLAPCE
DGSRRQRPSE CSSDDLMCAI RHVKVDGSDH LTQKLDVHKS AKYEVEEVES GGFDIRFLGV
KWGSNTIDAT LSYSCDTNLK TDELVTTIWN SEYVLIEMSG PSGCKRDGNS DSGDNGNGNG
NGNDPDNNNN TGKDKKSKKT SWFTWLFVYA ILFTVIYLMV VSYLNTKGGS FQDFRNEFVE
RGTEFITSLP TFVKEVVTKT LGTRDSSASR GGYSAV
