(data stored in ACNUC7421 zone)

SWISSPROT: ATG27_ASHGO

ID   ATG27_ASHGO             Reviewed;         251 AA.
AC   Q757Z8;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2013, sequence version 2.
DT   11-DEC-2019, entry version 87.
DE   RecName: Full=Autophagy-related protein 27;
DE   Flags: Precursor;
GN   Name=ATG27; OrderedLocusNames=AEL138C;
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2]
RP   GENOME REANNOTATION, AND SEQUENCE REVISION TO 237-239; 243-245 AND
RP   C-TERMINUS.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
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}.
DR   EMBL; AE016818; AAS52547.2; -; Genomic_DNA.
DR   RefSeq; NP_984723.2; NM_210077.2.
DR   STRING; 33169.AAS52547; -.
DR   EnsemblFungi; AAS52547; AAS52547; AGOS_AEL138C.
DR   GeneID; 4620910; -.
DR   KEGG; ago:AGOS_AEL138C; -.
DR   HOGENOM; HOG000034146; -.
DR   InParanoid; Q757Z8; -.
DR   KO; K21141; -.
DR   OMA; WICGFIS; -.
DR   Proteomes; UP000000591; Chromosome V.
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   Pfam; PF09451; ATG27; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q757Z8.
DR   SWISS-2DPAGE; Q757Z8.
KW   Autophagy; Cytoplasmic vesicle; Golgi apparatus; Membrane; Mitochondrion;
KW   Protein transport; Reference proteome; Signal; Transmembrane;
KW   Transmembrane helix; Transport.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..251
FT                   /note="Autophagy-related protein 27"
FT                   /id="PRO_0000001774"
FT   TOPO_DOM        20..175
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        176..196
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        197..251
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   251 AA;  27782 MW;  B7F6264F25B893E6 CRC64;
     MKYVRCVLLT GALFNIAAGL KCADSKVLSR YKVSQHAAKG KFTESTPPSE TTDFWWINLC
     EEHSEPVPDK CKDDAMFCHR QQVKLDDGKE YVTQVFDVPR NQEVDVEELR DGFQVSFTGK
     WGERERKVKV RYTCADDKAE DEVSAEGAFG AHTTPVEVAL RGPSGCIQAT EKSSGIGGWI
     TWLVIYAVLL TLIYLLAKSY MSVGHGSMQD FREEFVERST NLVSSLPEFA KEVMGKVVGG
     GPSSRGGYSA V
//

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