ATG27_ARTBC
ID ATG27_ARTBC Reviewed; 305 AA.
AC D4B086;
DT 11-NOV-2015, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 1.
DT 25-MAY-2022, entry version 43.
DE RecName: Full=Autophagy-related protein 27 {ECO:0000250|UniProtKB:P46989};
DE Flags: Precursor;
GN ORFNames=ARB_01857;
OS Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) (Trichophyton
OS mentagrophytes).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=663331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4681 / CBS 112371;
RX PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M.,
RA Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O.,
RA Schroeckh V., Hertweck C., Hube B., White T.C., Platzer M., Guthke R.,
RA Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.;
RT "Comparative and functional genomics provide insights into the
RT pathogenicity of dermatophytic fungi.";
RL Genome Biol. 12:R7.1-R7.16(2011).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=21919205; DOI=10.1002/pmic.201100234;
RA Sriranganadane D., Waridel P., Salamin K., Feuermann M., Mignon B.,
RA Staib P., Neuhaus J.M., Quadroni M., Monod M.;
RT "Identification of novel secreted proteases during extracellular
RT proteolysis by dermatophytes at acidic pH.";
RL Proteomics 11:4422-4433(2011).
CC -!- FUNCTION: Effector of phosphatidylinositol 3-phosphate kinase signaling
CC (By similarity). Regulates the cytoplasm to vacuole transport (Cvt)
CC vesicle formation. Plays a role in ATG protein retrieval from the pre-
CC autophagosomal structure (PAS) (By similarity).
CC {ECO:0000250|UniProtKB:P46989}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane
CC {ECO:0000250|UniProtKB:P46989}; Single-pass type I membrane protein
CC {ECO:0000255}. Golgi apparatus membrane {ECO:0000250|UniProtKB:P46989};
CC Single-pass type I membrane protein {ECO:0000255}. Mitochondrion
CC membrane {ECO:0000250|UniProtKB:P46989}; Single-pass membrane protein.
CC Preautophagosomal structure membrane {ECO:0000250|UniProtKB:P46989};
CC Single-pass type I membrane protein {ECO:0000255}. Note=Cycles among
CC the pre-autophagosomal structure (PAS), mitochondria and Golgi.
CC {ECO:0000250|UniProtKB:P46989}.
CC -!- SIMILARITY: Belongs to the ATG27 family. {ECO:0000305}.
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DR EMBL; ABSU01000023; EFE31238.1; -; Genomic_DNA.
DR RefSeq; XP_003011878.1; XM_003011832.1.
DR AlphaFoldDB; D4B086; -.
DR STRING; 63400.XP_003011878.1; -.
DR EnsemblFungi; EFE31238; EFE31238; ARB_01857.
DR GeneID; 9526430; -.
DR KEGG; abe:ARB_01857; -.
DR eggNOG; ENOG502S1VT; Eukaryota.
DR HOGENOM; CLU_047751_0_0_1; -.
DR OMA; AFDCKDI; -.
DR Proteomes; UP000008866; 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 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 1: Evidence at protein level;
KW Autophagy; Cytoplasmic vesicle; Disulfide bond; Glycoprotein;
KW Golgi apparatus; Membrane; Mitochondrion; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..305
FT /note="Autophagy-related protein 27"
FT /id="PRO_5003053810"
FT TOPO_DOM 23..242
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:P46989"
FT TRANSMEM 243..263
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 264..305
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P46989"
FT DOMAIN 24..231
FT /note="MRH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT REGION 163..202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 58
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 85
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 26..66
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 74..81
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 156..229
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
SQ SEQUENCE 305 AA; 33814 MW; 73B71E64AED9B51A CRC64;
MARYKGLSIL SLFAVFSSLA SAELDCSNIK VDGVMWNFGK LGGAHSISET ASSHEGYNTT
YTLDICKPLT KTLCKKGAFV CAVRNATDIN GIERTMDVID IAGNFVLNSG RTLDPIFTRL
KKEDPKTEGL KMELHGGKHK FGNLLKRQKA VITLLCDRER TGLEGLESPK PDGDKKKDGE
KKDDDKKDNK DKEGKSKRDG EENKRSLIFK SYNEEEGTLD LEWKTKYACE NVEDGGSAPS
GHWGFFTWVI VLYVVLVSLP LLSERVTNVR CHSQPVPVHF GLSDIRLVAQ LQPVWSSRVG
LASSQ
