ATG27_CANAL
ID ATG27_CANAL Reviewed; 252 AA.
AC Q5A5S7; A0A1D8PIQ3;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Autophagy-related protein 27;
DE Flags: Precursor;
GN Name=ATG27; OrderedLocusNames=CAALFM_C210470CA;
GN ORFNames=CaO19.12782, CaO19.5322;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(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}.
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DR EMBL; CP017624; AOW28019.1; -; Genomic_DNA.
DR RefSeq; XP_717125.1; XM_712032.1.
DR AlphaFoldDB; Q5A5S7; -.
DR STRING; 237561.Q5A5S7; -.
DR GeneID; 3641196; -.
DR KEGG; cal:CAALFM_C210470CA; -.
DR CGD; CAL0000194879; orf19.12782.
DR VEuPathDB; FungiDB:C2_10470C_A; -.
DR eggNOG; ENOG502QVJJ; Eukaryota.
DR HOGENOM; CLU_047751_0_0_1; -.
DR InParanoid; Q5A5S7; -.
DR OMA; NKGNAID; -.
DR OrthoDB; 1240091at2759; -.
DR PRO; PR:Q5A5S7; -.
DR Proteomes; UP000000559; Chromosome 2.
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:0005770; C:late endosome; IBA:GO_Central.
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; Glycoprotein;
KW Golgi apparatus; Membrane; Mitochondrion; Protein transport;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..15
FT /evidence="ECO:0000255"
FT CHAIN 16..252
FT /note="Autophagy-related protein 27"
FT /id="PRO_0000001775"
FT TOPO_DOM 16..176
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 177..197
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 198..252
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 16..161
FT /note="MRH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT CARBOHYD 49
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 18..57
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 66..73
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 130..159
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
SQ SEQUENCE 252 AA; 28278 MW; 6BBA16F1A4FF4133 CRC64;
MILASLLTFA TAALAFDCSD KELERYNFES IKGVHSYTTL KNTPPSQTNV TWNVGICQPI
SAIKDCPANS DICGVTSILR KDEKPVVSEV VSFKSDLQKA YESSDNGIKV IYKGANWGDV
LVNAELNFQC DKDSQNNEFT LDQWDGTNLK LSMKTKAACI TSKEDKKKEK HDNGESWGWF
TWIFIFLVLF LSIYIIGGAW FQYNKGNAID FQSALKEVVE NFIELLKGLP SFGKEIIEKF
TGRSNRGEYS AV
