ATG11_SCHPO
ID ATG11_SCHPO Reviewed; 926 AA.
AC O14261;
DT 11-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 2.
DT 25-MAY-2022, entry version 121.
DE RecName: Full=Taz1-interacting factor 1;
DE Short=Protein taf1;
DE AltName: Full=Autophagy-related protein 11;
DE AltName: Full=Cytoplasm to vacuole targeting protein 9;
GN Name=taf1; Synonyms=atg11, cvt9; ORFNames=SPAC7D4.04;
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] {ECO:0000305}
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] {ECO:0000305}
RP FUNCTION, AND INTERACTION WITH TAZ1.
RX PubMed=11270572; DOI=10.1007/s002940000168;
RA Ueno M., Kurokawa R., Renauld H., Watanabe K., Ushimaru T., Uritani M.,
RA Yoshinaga K., Hiraoka Y.;
RT "Schizosaccharomyces pombe taf1+ is required for nitrogen starvation-
RT induced sexual development and for entering the dormant GO state.";
RL Curr. Genet. 38:307-313(2001).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-548; THR-550 AND SER-552, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
RN [4]
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: Involved in cytoplasm to vacuole transport (Cvt), pexophagy,
CC mitophagy and nucleophagy. Recruits mitochondria for their selective
CC degradation via autophagy (mitophagy) during starvation. Works as
CC scaffold proteins that recruit ATG proteins to the preautophagosome
CC (PAS), the site of vesicle/autophagosome formation. Required for atg9
CC anterograde transport from the mitochondria to the PAS (By similarity).
CC Required for nitrogen starvation-induced sexual development and for
CC entering the dormant G0 state (By similarity). {ECO:0000250,
CC ECO:0000269|PubMed:11270572}.
CC -!- SUBUNIT: Homodimer and potential homooligomers (By similarity).
CC Interacts with taz1. {ECO:0000250, ECO:0000269|PubMed:11270572}.
CC -!- SUBCELLULAR LOCATION: Preautophagosomal structure membrane
CC {ECO:0000269|PubMed:23950735}; Peripheral membrane protein
CC {ECO:0000269|PubMed:23950735}. Vacuole membrane
CC {ECO:0000269|PubMed:23950735}; Peripheral membrane protein
CC {ECO:0000269|PubMed:23950735}.
CC -!- DISRUPTION PHENOTYPE: Impairs atg8-processing.
CC {ECO:0000269|PubMed:23950735}.
CC -!- SIMILARITY: Belongs to the ATG11 family. {ECO:0000305}.
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DR EMBL; CU329670; CAB16721.2; -; Genomic_DNA.
DR PIR; T39082; T39082.
DR RefSeq; NP_593855.1; NM_001019284.2.
DR AlphaFoldDB; O14261; -.
DR SMR; O14261; -.
DR BioGRID; 278229; 85.
DR IntAct; O14261; 10.
DR STRING; 4896.SPAC7D4.04.1; -.
DR iPTMnet; O14261; -.
DR MaxQB; O14261; -.
DR PaxDb; O14261; -.
DR PRIDE; O14261; -.
DR EnsemblFungi; SPAC7D4.04.1; SPAC7D4.04.1:pep; SPAC7D4.04.
DR GeneID; 2541735; -.
DR KEGG; spo:SPAC7D4.04; -.
DR PomBase; SPAC7D4.04; -.
DR VEuPathDB; FungiDB:SPAC7D4.04; -.
DR eggNOG; ENOG502QVZE; Eukaryota.
DR HOGENOM; CLU_318616_0_0_1; -.
DR InParanoid; O14261; -.
DR OMA; WKREFQS; -.
DR PhylomeDB; O14261; -.
DR Reactome; R-SPO-1632852; Macroautophagy.
DR PRO; PR:O14261; -.
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:0019898; C:extrinsic component of membrane; IBA:GO_Central.
DR GO; GO:0000329; C:fungal-type vacuole membrane; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0000407; C:phagophore assembly site; IDA:PomBase.
DR GO; GO:0034045; C:phagophore assembly site membrane; IBA:GO_Central.
DR GO; GO:0060090; F:molecular adaptor activity; IBA:GO_Central.
DR GO; GO:0019901; F:protein kinase binding; IBA:GO_Central.
DR GO; GO:0043539; F:protein serine/threonine kinase activator activity; IDA:PomBase.
DR GO; GO:0000045; P:autophagosome assembly; IBA:GO_Central.
DR GO; GO:0000422; P:autophagy of mitochondrion; IMP:PomBase.
DR GO; GO:0030242; P:autophagy of peroxisome; IBA:GO_Central.
DR GO; GO:0006995; P:cellular response to nitrogen starvation; IMP:UniProtKB.
DR GO; GO:0016236; P:macroautophagy; IMP:PomBase.
DR GO; GO:0034727; P:piecemeal microautophagy of the nucleus; IBA:GO_Central.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IBA:GO_Central.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0061709; P:reticulophagy; IBA:GO_Central.
DR InterPro; IPR040040; ATG11.
DR InterPro; IPR019460; Atg11_C.
DR InterPro; IPR045593; Atg11_middle.
DR InterPro; IPR045326; ATG17-like_dom.
DR PANTHER; PTHR13222; PTHR13222; 1.
DR Pfam; PF10377; ATG11; 1.
DR Pfam; PF19697; Atg11_middle; 1.
DR Pfam; PF04108; ATG17_like; 1.
PE 1: Evidence at protein level;
KW Autophagy; Coiled coil; Membrane; Phosphoprotein; Protein transport;
KW Reference proteome; Transport; Vacuole.
FT CHAIN 1..926
FT /note="Taz1-interacting factor 1"
FT /id="PRO_0000072418"
FT COILED 461..496
FT /evidence="ECO:0000255"
FT COILED 548..671
FT /evidence="ECO:0000255"
FT MOD_RES 548
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 550
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 552
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 926 AA; 106770 MW; EB3F366872877CA0 CRC64;
MRFRLNDSFS GKSWTIDNVQ WTPQNLVAWI MELNIGLSDE AKLLLPNGMS LNETVLNSES
DVVIYVLDQN LLTFTYDGDK IPSIPSLKGQ PISNVLTGII ADSSSDQWKD KISKCLSLLS
DILESSSKIH NQLSVCHDEY STSIVSPEVA MNYLQRRQSG MKDLLFVFYE RLDRVSVSDL
LHDFLALPTG SLPITPLKIL STNWTKLDSW LNSISARYAE AQKRVQQCIG AANSIIVSPF
KEVPSIKEGD DAYYHLRSVA QDAANILQEI LKIESTSTTS QIKPKCNYET EITDCMEKLQ
SNLSELKSSR KSSLISLKSF WLSFYKVSLR YDALYEYLRQ IAEELDRSKF VLSQSRNIFS
LYIDILMEAL RRTEWQESYN VSHDSSLPLD QEKELSLRKS WLSHFSNLLF NHGQLKYLPV
LTRDEISNYL LNIQAHPNYQ TFHQMLSNRL SEYLGFPGSP REAVSNTVQA NNSLHEKLAM
YQNRCNNLEA MLSHQNGFNY NINNDGLSPN APHPPINEQS NSSQPFYRVS PSIVPLNVIR
KLTNRKTSFT DSHILRLQDE VNQLRNELDL VNKRNEDLLI ELQGKEEKIQ YLETENEEVL
QKYENLQEEL SSTRKLLTKN EAAVAEQQSN EEMHSNEPNI LNLYSVFEGK VDSLQELYNA
FKLQLTSLKQ KGEYATLAKD AEAVQHIIEE RDYALAEKAD LLKLSENRKE QCKILTQKLY
TIVFRCNELQ SVLRECVTQP GFDSDNERDG HASIPDRQIE FNSKDLQYLY WMDGEDADRN
FQEFLNRMSS LDFDSFHNFV VSVLTQAHNH ELRWKREFQS NRDKALKAIL DSQSKVSLRN
FKQGSLVLFL PTRRTAGNKK VWAAFNVNAP HYYLNTQPHL KLESRDWMLG RVTSIEDRTA
DDSTDKWLRL PSGTIWHLVE AIDERF
