ATG20_SCHPO
ID ATG20_SCHPO Reviewed; 534 AA.
AC Q9USM8;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Autophagy-related protein 20;
GN Name=atg20; ORFNames=SPCC16A11.08;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
CC -!- FUNCTION: Required for cytoplasm to vacuole transport (Cvt), pexophagy
CC and mitophagy. Also involved in endoplasmic reticulum-specific
CC autophagic process and is essential for the survival of cells subjected
CC to severe ER stress. Functions in protein retrieval from the endocytic
CC pathway (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Endosome
CC membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
CC Preautophagosomal structure membrane {ECO:0000250}; Peripheral membrane
CC protein {ECO:0000250}.
CC -!- DOMAIN: The PX domain binds phosphatidylinositol 3-phosphate which is
CC necessary for peripheral membrane localization of ATG20 to the
CC perivacuolar punctate structures.
CC -!- SIMILARITY: Belongs to the sorting nexin family. {ECO:0000305}.
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DR EMBL; CU329672; CAB53080.1; -; Genomic_DNA.
DR PIR; T41081; T41081.
DR RefSeq; NP_587995.1; NM_001022986.2.
DR AlphaFoldDB; Q9USM8; -.
DR BioGRID; 275883; 27.
DR STRING; 4896.SPCC16A11.08.1; -.
DR iPTMnet; Q9USM8; -.
DR MaxQB; Q9USM8; -.
DR PaxDb; Q9USM8; -.
DR PRIDE; Q9USM8; -.
DR EnsemblFungi; SPCC16A11.08.1; SPCC16A11.08.1:pep; SPCC16A11.08.
DR GeneID; 2539317; -.
DR KEGG; spo:SPCC16A11.08; -.
DR PomBase; SPCC16A11.08; atg20.
DR VEuPathDB; FungiDB:SPCC16A11.08; -.
DR eggNOG; KOG2273; Eukaryota.
DR HOGENOM; CLU_504485_0_0_1; -.
DR InParanoid; Q9USM8; -.
DR OMA; FEFSGMY; -.
DR PhylomeDB; Q9USM8; -.
DR PRO; PR:Q9USM8; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0005768; C:endosome; ISO:PomBase.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000407; C:phagophore assembly site; IDA:PomBase.
DR GO; GO:0034045; C:phagophore assembly site membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; ISO:PomBase.
DR GO; GO:0000422; P:autophagy of mitochondrion; IMP:PomBase.
DR GO; GO:0034498; P:early endosome to Golgi transport; ISO:PomBase.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0061709; P:reticulophagy; IMP:PomBase.
DR CDD; cd06867; PX_SNX41_42; 1.
DR Gene3D; 3.30.1520.10; -; 1.
DR InterPro; IPR001683; PX_dom.
DR InterPro; IPR036871; PX_dom_sf.
DR InterPro; IPR044106; PX_Snx41/Atg20.
DR Pfam; PF00787; PX; 1.
DR SMART; SM00312; PX; 1.
DR SUPFAM; SSF64268; SSF64268; 1.
DR PROSITE; PS50195; PX; 1.
PE 3: Inferred from homology;
KW Autophagy; Cytoplasm; Endosome; Lipid-binding; Membrane; Protein transport;
KW Reference proteome; Transport.
FT CHAIN 1..534
FT /note="Autophagy-related protein 20"
FT /id="PRO_0000314769"
FT DOMAIN 1..137
FT /note="PX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00147"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 179..272
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 179..210
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 224..266
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 55
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-3-phosphate)"
FT /ligand_id="ChEBI:CHEBI:58088"
FT /evidence="ECO:0000250"
FT BINDING 57
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-3-phosphate)"
FT /ligand_id="ChEBI:CHEBI:58088"
FT /evidence="ECO:0000250"
FT BINDING 81
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-3-phosphate)"
FT /ligand_id="ChEBI:CHEBI:58088"
FT /evidence="ECO:0000250"
FT BINDING 104
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-3-phosphate)"
FT /ligand_id="ChEBI:CHEBI:58088"
FT /evidence="ECO:0000250"
SQ SEQUENCE 534 AA; 60194 MW; 3315176D929B9B53 CRC64;
MAQDDSYEEK PEVISSDSGG SGYSTEIQIV GTVTSSDGSY VEYEIVHQKR SVWRRYSDFE
SLVKLMRRQY PAAIVPPIPG KQSLLSYAKH PRKAKSDAEF LNFRSRMLEL FLRQCLLHPC
IRSNPIFDKF IHSTVSWHVT LSSLDLPKDS NTDPLRLPPI ATEHDPFAHL RSSMPLVMAN
SLSPPSSRAL KPIHSLSNPS TASSLEPSSP LGSEDECHPP TSDMQPTHEL NESPSTPTAP
DFPHYNSSPS ELSPTQRRSS ISNGKDAPSP VLKDLTSYTQ EVIVCRKFLH HSLSPSIHST
LSSISKMESC LSKLGSAFHS LTALNEIQLA NHLQVIANAF EFSGMYAKEF EQEFNSSVYE
KMVQSMQLAK CAADALKYKQ LKIQQRDFLQ DQLIHSNTMS ATDSMVAASP TIHPATRLNT
IQRAVVSQAK KGYTIFGRLQ NVLHDFVEGE TSISKESLQQ HKNTIENQLA AANWDCQKID
EFMDAELKFY KECQTSQWEE IIKSVHECIY KWAQTNLQRW LRTREELENL SKDI
