ATG13_SCHPO
ID ATG13_SCHPO Reviewed; 758 AA.
AC O36019; Q9USA3;
DT 29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Autophagy protein 13;
DE AltName: Full=Meiotically up-regulated gene 78 protein;
GN Name=atg13; Synonyms=mug78; ORFNames=SPAC4F10.07c;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 108-302.
RC STRAIN=ATCC 38364 / 968;
RX PubMed=10759889; DOI=10.1046/j.1365-2443.2000.00317.x;
RA Ding D.-Q., Tomita Y., Yamamoto A., Chikashige Y., Haraguchi T.,
RA Hiraoka Y.;
RT "Large-scale screening of intracellular protein localization in living
RT fission yeast cells by the use of a GFP-fusion genomic DNA library.";
RL Genes Cells 5:169-190(2000).
RN [3]
RP FUNCTION IN MEIOSIS/SPORULATION.
RX PubMed=16303567; DOI=10.1016/j.cub.2005.10.038;
RA Martin-Castellanos C., Blanco M., Rozalen A.E., Perez-Hidalgo L.,
RA Garcia A.I., Conde F., Mata J., Ellermeier C., Davis L., San-Segundo P.,
RA Smith G.R., Moreno S.;
RT "A large-scale screen in S. pombe identifies seven novel genes required for
RT critical meiotic events.";
RL Curr. Biol. 15:2056-2062(2005).
RN [4]
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).
RN [5]
RP FUNCTION, PHOSPHORYLATION, AND DEPHOSPHORYLATION.
RX PubMed=17295836; DOI=10.1111/j.1365-2443.2007.01041.x;
RA Kohda T.A., Tanaka K., Konomi M., Sato M., Osumi M., Yamamoto M.;
RT "Fission yeast autophagy induced by nitrogen starvation generates a
RT nitrogen source that drives adaptation processes.";
RL Genes Cells 12:155-170(2007).
RN [6]
RP FUNCTION.
RX PubMed=19778961; DOI=10.1099/mic.0.034389-0;
RA Mukaiyama H., Kajiwara S., Hosomi A., Giga-Hama Y., Tanaka N., Nakamura T.,
RA Takegawa K.;
RT "Autophagy-deficient Schizosaccharomyces pombe mutants undergo partial
RT sporulation during nitrogen starvation.";
RL Microbiology 155:3816-3826(2009).
RN [7]
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: Activates the atg1 kinase in a nutritional condition
CC dependent manner through the TOR pathway, leading to autophagy. Also
CC involved in cytoplasm to vacuole transport (Cvt) and more specifically
CC in Cvt vesicle formation. Seems to play a role in the switching
CC machinery regulating the conversion between the Cvt pathway and
CC autophagy. Autophagy functions to supply nitrogen and is activated when
CC cells cannot access exogenous nitrogen, thus ensuring that they can
CC adapt and subsequently propagate. Finally, atg13 is also required for
CC glycogen storage during stationary phase and has a role in meiosis and
CC sporulation. {ECO:0000269|PubMed:16303567, ECO:0000269|PubMed:17295836,
CC ECO:0000269|PubMed:19778961}.
CC -!- SUBUNIT: Interacts with atg1 to form the atg1-atg13 kinase complex.
CC {ECO:0000250}.
CC -!- INTERACTION:
CC O36019; O13978: mug66; NbExp=6; IntAct=EBI-16158534, EBI-16158557;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}.
CC Preautophagosomal structure {ECO:0000269|PubMed:23950735}.
CC -!- PTM: Phosphorylated. Dephosphorylated under depletion of nitrogen.
CC -!- DISRUPTION PHENOTYPE: Impairs atg8-processing.
CC {ECO:0000269|PubMed:23950735}.
CC -!- SIMILARITY: Belongs to the ATG13 family. Fungi subfamily.
CC {ECO:0000305}.
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DR EMBL; CU329670; CAB11710.1; -; Genomic_DNA.
DR EMBL; AB027916; BAA87220.1; -; Genomic_DNA.
DR PIR; T38811; T38811.
DR RefSeq; NP_594750.1; NM_001020177.2.
DR PDB; 4YK8; X-ray; 3.00 A; B=32-269.
DR PDBsum; 4YK8; -.
DR AlphaFoldDB; O36019; -.
DR SMR; O36019; -.
DR BioGRID; 279845; 74.
DR DIP; DIP-61609N; -.
DR IntAct; O36019; 1.
DR STRING; 4896.SPAC4F10.07c.1; -.
DR iPTMnet; O36019; -.
DR PaxDb; O36019; -.
DR PRIDE; O36019; -.
DR EnsemblFungi; SPAC4F10.07c.1; SPAC4F10.07c.1:pep; SPAC4F10.07c.
DR GeneID; 2543425; -.
DR KEGG; spo:SPAC4F10.07c; -.
DR PomBase; SPAC4F10.07c; atg13.
DR VEuPathDB; FungiDB:SPAC4F10.07c; -.
DR eggNOG; KOG4573; Eukaryota.
DR HOGENOM; CLU_365689_0_0_1; -.
DR InParanoid; O36019; -.
DR OMA; GQVIHHC; -.
DR PhylomeDB; O36019; -.
DR Reactome; R-SPO-1632852; Macroautophagy.
DR PRO; PR:O36019; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:1990316; C:Atg1/ULK1 kinase complex; EXP:PomBase.
DR GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0019898; C:extrinsic component of membrane; IBA:GO_Central.
DR GO; GO:0000407; C:phagophore assembly site; IDA:PomBase.
DR GO; GO:0006914; P:autophagy; IMP:PomBase.
DR GO; GO:0000422; P:autophagy of mitochondrion; IMP:PomBase.
DR GO; GO:0016236; P:macroautophagy; IMP:PomBase.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0000423; P:mitophagy; IBA:GO_Central.
DR GO; GO:0034727; P:piecemeal microautophagy of the nucleus; IBA:GO_Central.
DR GO; GO:0034497; P:protein localization to phagophore assembly site; IBA:GO_Central.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR Gene3D; 3.30.900.10; -; 1.
DR InterPro; IPR040182; ATG13.
DR InterPro; IPR018731; Atg13_N.
DR InterPro; IPR036570; HORMA_dom_sf.
DR PANTHER; PTHR13430; PTHR13430; 1.
DR Pfam; PF10033; ATG13; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Autophagy; Cytoplasm; Meiosis; Phosphoprotein;
KW Protein transport; Reference proteome; Sporulation; Transport.
FT CHAIN 1..758
FT /note="Autophagy protein 13"
FT /id="PRO_0000116723"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 285..307
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 600..640
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT HELIX 36..57
FT /evidence="ECO:0007829|PDB:4YK8"
FT HELIX 77..79
FT /evidence="ECO:0007829|PDB:4YK8"
FT STRAND 80..82
FT /evidence="ECO:0007829|PDB:4YK8"
FT HELIX 86..97
FT /evidence="ECO:0007829|PDB:4YK8"
FT TURN 102..104
FT /evidence="ECO:0007829|PDB:4YK8"
FT STRAND 109..113
FT /evidence="ECO:0007829|PDB:4YK8"
FT STRAND 150..157
FT /evidence="ECO:0007829|PDB:4YK8"
FT HELIX 167..185
FT /evidence="ECO:0007829|PDB:4YK8"
FT HELIX 189..199
FT /evidence="ECO:0007829|PDB:4YK8"
FT STRAND 211..215
FT /evidence="ECO:0007829|PDB:4YK8"
FT STRAND 222..224
FT /evidence="ECO:0007829|PDB:4YK8"
FT STRAND 238..242
FT /evidence="ECO:0007829|PDB:4YK8"
FT STRAND 246..248
FT /evidence="ECO:0007829|PDB:4YK8"
FT STRAND 251..261
FT /evidence="ECO:0007829|PDB:4YK8"
SQ SEQUENCE 758 AA; 83710 MW; A6C9E32818607C84 CRC64;
MPRLNTQLPR MYSAPPGHSK AVSTELNKDL SSVGGRSAKL GQVIHHCFYK TGLIILESRL
NVFGTSRPRE SSKNNKWFNL EIVETELYAE QFKIWKNIEL SPSRKIPPMV LHTYLDISDL
SKNQTLSVSD GTHSHAINFN NMSTMKIVLE RWIVNLDGEA LSTPLELAVL YKKLVVLFRS
LYTYTHLMPL WKLKSKIHKL RAHGTSLKVG CALSTDDVLS NDFLPISAPI SSSLGSSIAT
FSFSPVGTPA GDFRISVQYR KNCHFEVHDS DALLSNQLLS ADKHQLAASN NSQDFEDGKQ
YDQPPPSFAT RLAKQSDPNS LLQSEIQHLA SIESITAQAA PLVTIHPFKS PSLSASPGSN
FDNMSISPKV AVNRYIHRGP SATSLNKFSM ISDAASKSRA KLPPLTSGSL KLNTLDISNT
PNLRRFSSSF GPRERKESFS SRNRLPLVNH PIRSIFKHNV SENPITDHSE HAVYDSEFAS
KDDLSGFIQL LDSHAHHLNA SEGSKSSGSF PGKVQTLTSG ISPVAHPHNS LGSSNEIFDI
DTYNHSIDNS GSRFTEAVKH NLGNSSHSIM RHHTLGTLRS RPSFSEKSTF PAPLTSISQA
STFQGDNRSP STVIPHTQTE VPSANDTSKQ LASLHDMRKS QSPICARSAT SAGLPRFEYH
TSLSKSLEHS STPASLQATK TPSPSFVLEP GIPQEYKKHF DNLSEERRQC LTPSTPTYEY
YNEHNPNYDD DLLFTMTDMT LEPHDVSAIR LGSPKSDD
