FIL1_SCHPO
ID FIL1_SCHPO Reviewed; 557 AA.
AC O94720;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Transcription factor fil1 {ECO:0000303|PubMed:29432178};
DE AltName: Full=GATA zinc finger domain-containing protein C1393.08;
DE AltName: Full=GCN four induction-like protein {ECO:0000303|PubMed:29432178};
DE AltName: Full=General control transcription factor fil1 {ECO:0000305};
GN Name=fil1 {ECO:0000303|PubMed:29432178, ECO:0000312|PomBase:SPCC1393.08};
GN ORFNames=SPCC1393.08 {ECO:0000312|PomBase:SPCC1393.08};
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] {ECO:0000312|EMBL:CAB38164.1}
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] {ECO:0000305}
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 [3]
RP FUNCTION, SUBCELLULAR LOCATION, INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=29432178; DOI=10.1073/pnas.1713991115;
RA Duncan C.D.S., Rodriguez-Lopez M., Ruis P., Baehler J., Mata J.;
RT "General amino acid control in fission yeast is regulated by a nonconserved
RT transcription factor, with functions analogous to Gcn4/Atf4.";
RL Proc. Natl. Acad. Sci. U.S.A. 115:E1829-E1838(2018).
CC -!- FUNCTION: Activates genes required for amino acid biosynthesis and acts
CC as a master transcriptional regulator during amino acid starvation
CC (PubMed:29432178). Binds variations of the DNA sequence 5'-GAT[AC]GC-3'
CC (PubMed:29432178). {ECO:0000269|PubMed:29432178}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16823372,
CC ECO:0000305|PubMed:29432178}. Cytoplasm {ECO:0000269|PubMed:16823372}.
CC -!- INDUCTION: Translation is induced by amino acid starvation
CC (PubMed:29432178). Translational repression during nutrient-rich
CC conditions is dependent on several uORFs (upstream open reading frames)
CC present in the 5'-UTR of the mRNA; these promote ribosome dissociation
CC (PubMed:29432178). Translational induction occurs in conditions
CC reducing translation machinery efficiency, leading to ribosomes
CC scanning over the uORFs, and increased translation of the mRNA (By
CC similarity). {ECO:0000250|UniProtKB:P03069,
CC ECO:0000269|PubMed:29432178}.
CC -!- DISRUPTION PHENOTYPE: Decreases the mRNA level of genes involved in
CC amino acid biosynthesis (PubMed:29432178). Increases the mRNA level of
CC genes involved in the response to nitrogen starvation, including genes
CC required for the mating response (PubMed:29432178). Decreases
CC vegetative cell population growth rate in low nutrient conditions
CC (PubMed:29432178). {ECO:0000269|PubMed:29432178}.
CC -!- MISCELLANEOUS: Functional homolog of the S. cerevisiae GCN4 and
CC mammalian ATF4 bZIP transcription factors.
CC {ECO:0000303|PubMed:29432178}.
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DR EMBL; CU329672; CAB38164.1; -; Genomic_DNA.
DR PIR; T40956; T40956.
DR RefSeq; NP_587966.1; NM_001022957.2.
DR AlphaFoldDB; O94720; -.
DR SMR; O94720; -.
DR BioGRID; 275462; 68.
DR STRING; 4896.SPCC1393.08.1; -.
DR iPTMnet; O94720; -.
DR MaxQB; O94720; -.
DR PaxDb; O94720; -.
DR PRIDE; O94720; -.
DR EnsemblFungi; SPCC1393.08.1; SPCC1393.08.1:pep; SPCC1393.08.
DR GeneID; 2538884; -.
DR KEGG; spo:SPCC1393.08; -.
DR PomBase; SPCC1393.08; -.
DR VEuPathDB; FungiDB:SPCC1393.08; -.
DR eggNOG; KOG1601; Eukaryota.
DR HOGENOM; CLU_531163_0_0_1; -.
DR InParanoid; O94720; -.
DR Reactome; R-SPO-9018519; Estrogen-dependent gene expression.
DR PRO; PR:O94720; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:PomBase.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISM:PomBase.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0034198; P:cellular response to amino acid starvation; IMP:PomBase.
DR GO; GO:1904262; P:negative regulation of TORC1 signaling; IMP:PomBase.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0010508; P:positive regulation of autophagy; IMP:PomBase.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:PomBase.
DR GO; GO:0061412; P:positive regulation of transcription from RNA polymerase II promoter in response to amino acid starvation; IMP:PomBase.
DR CDD; cd00202; ZnF_GATA; 2.
DR Gene3D; 3.30.50.10; -; 2.
DR InterPro; IPR039355; Transcription_factor_GATA.
DR InterPro; IPR000679; Znf_GATA.
DR InterPro; IPR013088; Znf_NHR/GATA.
DR PANTHER; PTHR10071; PTHR10071; 2.
DR Pfam; PF00320; GATA; 2.
DR PRINTS; PR00619; GATAZNFINGER.
DR SMART; SM00401; ZnF_GATA; 2.
DR PROSITE; PS00344; GATA_ZN_FINGER_1; 1.
DR PROSITE; PS50114; GATA_ZN_FINGER_2; 2.
PE 2: Evidence at transcript level;
KW Activator; Cytoplasm; DNA-binding; Metal-binding; Nucleus;
KW Reference proteome; Repeat; Transcription; Transcription regulation; Zinc;
KW Zinc-finger.
FT CHAIN 1..557
FT /note="Transcription factor fil1"
FT /id="PRO_0000310832"
FT ZN_FING 365..390
FT /note="GATA-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00094"
FT ZN_FING 419..443
FT /note="GATA-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00094"
FT REGION 234..258
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 557 AA; 60352 MW; C119968424A16051 CRC64;
MNYNDTTEFC FPFGQPSFPT SAMTEGSFDG QFSEFDPTFT SPADTALSDI ANLPIDLHKD
ALFANAPGKG DVDFDSVSML QLLSDYPLAF NSTENNQKLQ TNPSARWSLL DSMDFDNQRQ
CSDLESAQLG DSGLLKSTIL SNSHIDIAAL SSSKTSEPTP PFSYVQTPCI PTPSSALIDT
PFPGALDSEF GFDESQAPLF PASDGDCQRA FASISYPTNY GCKLSNLGFM SPQSPVKREL
NDSTSPSKLS ESSSSLTGSS SALLSQSEFL GSVPSLSDSI ATVDPFFSFE SFETDEKARS
LLMDASLKLP QFSTPNLSSN SSSLSLKSTL AEGMKGSTPL AAVKTEKASK AARVMKQKKH
REHVCFNCGV TETPLWRRTS DKLNFLCNAC GLYNKQYGVM RPLSPRNKGS SKALENLVCA
NCSSTKTSLW RKDRHGQTVC NACGLYARLH GHNRPIGLKK NKITRRRRGK GPGGEDGMSD
EVKSEFPVLS KSVTMAEILS SKGLESPQLT NSVSVSKMPN TDADVSLEHA KISFDSLDNS
VIVKKEEEIE NKFSVSC
