ID   ATG17_SCHPO             Reviewed;         411 AA.
AC   O42651;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2012, sequence version 2.
DT   25-MAY-2022, entry version 128.
DE   RecName: Full=Autophagy-related protein 17;
GN   Name=atg17; ORFNames=SPAC10F6.11c;
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   REVISION OF GENE MODEL.
RX   PubMed=21511999; DOI=10.1126/science.1203357;
RA   Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N.,
RA   Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y.,
RA   Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K., Bayne E.H.,
RA   Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G.,
RA   French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A.,
RA   Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P.,
RA   Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R.,
RA   Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J.,
RA   Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W.,
RA   Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.;
RT   "Comparative functional genomics of the fission yeasts.";
RL   Science 332:930-936(2011).
RN   [3]
RP   DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
RX   PubMed=23950735; DOI=10.1371/journal.pgen.1003715;
RA   Sun L.L., Li M., Suo F., Liu X.M., Shen E.Z., Yang B., Dong M.Q., He W.Z.,
RA   Du L.L.;
RT   "Global analysis of fission yeast mating genes reveals new autophagy
RT   factors.";
RL   PLoS Genet. 9:E1003715-E1003715(2013).
CC   -!- FUNCTION: Autophagy-specific protein that functions in response to
CC       autophagy-inducing signals as a scaffold to recruit other ATG proteins
CC       to organize preautophagosomal structure (PAS) formation. Modulates the
CC       timing and magnitude of the autophagy response, such as the size of the
CC       sequestering vesicles. Plays particularly a role in pexophagy and
CC       nucleophagy (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Preautophagosomal
CC       structure membrane {ECO:0000269|PubMed:23950735}; Peripheral membrane
CC       protein {ECO:0000269|PubMed:23950735}.
CC   -!- DISRUPTION PHENOTYPE: Impairs atg8-processing.
CC       {ECO:0000269|PubMed:23950735}.
CC   -!- SIMILARITY: Belongs to the ATG17 family. {ECO:0000305}.
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DR   EMBL; CU329670; CAA15724.2; -; Genomic_DNA.
DR   PIR; T37505; T37505.
DR   RefSeq; NP_593262.2; NM_001018659.2.
DR   AlphaFoldDB; O42651; -.
DR   SMR; O42651; -.
DR   BioGRID; 279449; 32.
DR   IntAct; O42651; 1.
DR   STRING; 4896.SPAC10F6.11c.1; -.
DR   MaxQB; O42651; -.
DR   PaxDb; O42651; -.
DR   PRIDE; O42651; -.
DR   EnsemblFungi; SPAC10F6.11c.1; SPAC10F6.11c.1:pep; SPAC10F6.11c.
DR   GeneID; 2543011; -.
DR   KEGG; spo:SPAC10F6.11c; -.
DR   PomBase; SPAC10F6.11c; atg17.
DR   VEuPathDB; FungiDB:SPAC10F6.11c; -.
DR   eggNOG; ENOG502RW77; Eukaryota.
DR   HOGENOM; CLU_674655_0_0_1; -.
DR   InParanoid; O42651; -.
DR   OMA; YLPENIW; -.
DR   PRO; PR:O42651; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:1990316; C:Atg1/ULK1 kinase complex; EXP:PomBase.
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:0060090; F:molecular adaptor activity; ISO:PomBase.
DR   GO; GO:0030295; F:protein kinase activator activity; ISO:PomBase.
DR   GO; GO:0032147; P:activation of protein kinase activity; IBA:GO_Central.
DR   GO; GO:0000045; P:autophagosome assembly; ISO:PomBase.
DR   GO; GO:0000422; P:autophagy of mitochondrion; IMP:PomBase.
DR   GO; GO:0030242; P:autophagy of peroxisome; IBA:GO_Central.
DR   GO; GO:0044805; P:late nucleophagy; IBA:GO_Central.
DR   GO; GO:0016236; P:macroautophagy; IMP:PomBase.
DR   GO; GO:0034727; P:piecemeal microautophagy of the nucleus; IBA:GO_Central.
DR   InterPro; IPR007240; Atg17.
DR   InterPro; IPR045326; ATG17-like_dom.
DR   PANTHER; PTHR28005; PTHR28005; 1.
DR   Pfam; PF04108; ATG17_like; 1.
PE   3: Inferred from homology;
KW   Autophagy; Cytoplasm; Membrane; Reference proteome.
FT   CHAIN           1..411
FT                   /note="Autophagy-related protein 17"
FT                   /id="PRO_0000124564"
FT   REGION          388..411
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        389..411
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   411 AA;  47062 MW;  5E63B2764D515DFE CRC64;
     MELLQQWTQQ AKAALTQARQ LCGDAHKFNE DAKTDLRNSI KQHQQLKELA KLTASQCTRL
     DSSTALIKQL LDLVQNYPTF NQLNVLHDRL ESSLKRLRDC TLDPALGSEY TNLYAFVDDT
     ALEDLKTRLR GVTDGVWNAF EKLAGLLEED LCANYHKRLE AVSLDFLPPA YNDTAEELAD
     LLLQVAQHYD QCSEALNIYD TLSDAEKKDL QEVLQSDSNH VPSVLTELRS GLDQTIHYFN
     AVQSYKSKVD SATSILEALA EELNKNQLTN QRHEAAHELM RAQTGLEIPQ LAQELVQLER
     HYTHFAKAYT ALLQEIHRRQ TYENCVRSIV DEFVGRLEKE QQAEAKCRID FFNQYGDYLP
     QTLWGAVTDP PLHFEIIEHQ YTELPNVKVI PDKNDKKSKQ REKSSTTASK R