ATG27_PICAN
ID ATG27_PICAN Reviewed; 266 AA.
AC A7KAK7;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 25-MAY-2022, entry version 28.
DE RecName: Full=Autophagy-related protein 27;
DE Flags: Precursor;
GN Name=ATG27;
OS Pichia angusta (Yeast) (Hansenula polymorpha).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Pichiaceae; Ogataea.
OX NCBI_TaxID=870730;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=ATCC 34438 / CBS 4732 / DSM 70277 / JCM 3621 / NBRC 1476 / NRRL
RC Y-5445;
RX PubMed=17204848; DOI=10.4161/auto.3595;
RA Meijer W.H., van der Klei I.J., Veenhuis M., Kiel J.A.K.W.;
RT "ATG genes involved in non-selective autophagy are conserved from yeast to
RT man, but the selective Cvt and pexophagy pathways also require organism-
RT specific genes.";
RL Autophagy 3:106-116(2007).
CC -!- FUNCTION: Regulates the cytoplasm to vacuole transport (Cvt) vesicle
CC formation. {ECO:0000250, ECO:0000269|PubMed:17204848}.
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}. Note=Cycles among the pre-
CC autophagosomal structure (PAS), mitochondria 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; EF107729; ABO31067.1; -; Genomic_DNA.
DR AlphaFoldDB; A7KAK7; -.
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: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 PROSITE; PS51914; MRH; 1.
PE 3: Inferred from homology;
KW Autophagy; Cytoplasmic vesicle; Disulfide bond; Golgi apparatus; Membrane;
KW Mitochondrion; Protein transport; Signal; Transmembrane;
KW Transmembrane helix; Transport.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..266
FT /note="Autophagy-related protein 27"
FT /id="PRO_0000318052"
FT TOPO_DOM 19..192
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT TRANSMEM 193..213
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 214..266
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT DOMAIN 19..172
FT /note="MRH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT REGION 169..188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 77..84
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 141..170
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
SQ SEQUENCE 266 AA; 29537 MW; 15C4619C10B654AC CRC64;
MLHLITPLLL LLARFSMAID ISDEHFSAYP RMKELIGSHL VSRTEETPPS TKKITWYLKI
TDSGSGSPKD DTFPSECPKD SQLCGLTEIS LPNRDPVITE VFSFSNKLTP QFDVNTSSFI
VNLRGANWGA YTLDAEIEFV CASDDNAEGL KLVKFDYSTV SLQYKTSSAC KSNETPPKDG
KNKAPKDDDS NSWGVFTWLF ILLVIVMASY IIAQAWINAN RVGSSHEFLN ELVESIVETL
TKLPEFLREI ANKLFTSGSR GGYSAV
