ID   TAX4_YEAST              Reviewed;         604 AA.
AC   P47030; D6VWA0;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   24-JAN-2024, entry version 141.
DE   RecName: Full=Protein TAX4;
GN   Name=TAX4; OrderedLocusNames=YJL083W; ORFNames=J1002;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=7483841; DOI=10.1002/yea.320110709;
RA   Miosga T., Schaaff-Gerstenschlaeger I., Chalwatzis N., Baur A., Boles E.,
RA   Fournier C., Schmitt S., Velten C., Wilhelm N., Zimmermann F.K.;
RT   "Sequence analysis of a 33.1 kb fragment from the left arm of Saccharomyces
RT   cerevisiae chromosome X, including putative proteins with leucine zippers,
RT   a fungal Zn(II)2-Cys6 binuclear cluster domain and a putative alpha 2-SCB-
RT   alpha 2 binding site.";
RL   Yeast 11:681-689(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA   Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA   Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA   Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA   Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA   Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA   Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA   Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA   Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA   Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA   To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA   von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT   "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL   EMBO J. 15:2031-2049(1996).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [4]
RP   DOMAIN.
RX   PubMed=9822599; DOI=10.1093/emboj/17.22.6541;
RA   Paoluzi S., Castagnoli L., Lauro I., Salcini A.E., Coda L., Fre' S.,
RA   Confalonieri S., Pelicci P.G., Di Fiore P.P., Cesareni G.;
RT   "Recognition specificity of individual EH domains of mammals and yeast.";
RL   EMBO J. 17:6541-6550(1998).
RN   [5]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [6]
RP   FUNCTION, AND INTERACTION WITH INP51.
RX   PubMed=15265867; DOI=10.1074/jbc.m405589200;
RA   Morales-Johansson H., Jenoe P., Cooke F.T., Hall M.N.;
RT   "Negative regulation of phosphatidylinositol 4,5-bisphosphate levels by the
RT   INP51-associated proteins TAX4 and IRS4.";
RL   J. Biol. Chem. 279:39604-39610(2004).
CC   -!- FUNCTION: With IRS4, acts as a positive regulator of INP51 activity and
CC       phosphatidylinositol 4,5-bisphosphate turnover. Negatively regulates
CC       signaling through the cell integrity pathway, including the MAP kinase
CC       SLT2. {ECO:0000269|PubMed:15265867}.
CC   -!- SUBUNIT: Interacts with INP51. {ECO:0000269|PubMed:15265867}.
CC   -!- INTERACTION:
CC       P47030; P40559: INP51; NbExp=3; IntAct=EBI-25970, EBI-24915;
CC   -!- MISCELLANEOUS: Present with 396 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the IRS4 family. {ECO:0000305}.
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DR   EMBL; Z49358; CAA89376.1; -; Genomic_DNA.
DR   EMBL; X83502; CAA58487.1; -; Genomic_DNA.
DR   EMBL; X88851; CAA61318.1; -; Genomic_DNA.
DR   EMBL; BK006943; DAA08716.1; -; Genomic_DNA.
DR   PIR; S56027; S56027.
DR   RefSeq; NP_012452.1; NM_001181516.1.
DR   AlphaFoldDB; P47030; -.
DR   SMR; P47030; -.
DR   BioGRID; 33673; 121.
DR   IntAct; P47030; 5.
DR   MINT; P47030; -.
DR   STRING; 4932.YJL083W; -.
DR   MaxQB; P47030; -.
DR   PaxDb; 4932-YJL083W; -.
DR   PeptideAtlas; P47030; -.
DR   EnsemblFungi; YJL083W_mRNA; YJL083W; YJL083W.
DR   GeneID; 853362; -.
DR   KEGG; sce:YJL083W; -.
DR   AGR; SGD:S000003619; -.
DR   SGD; S000003619; TAX4.
DR   VEuPathDB; FungiDB:YJL083W; -.
DR   eggNOG; KOG0998; Eukaryota.
DR   GeneTree; ENSGT00940000176414; -.
DR   HOGENOM; CLU_452143_0_0_1; -.
DR   InParanoid; P47030; -.
DR   OMA; RSSXVGS; -.
DR   OrthoDB; 1333804at2759; -.
DR   BioCyc; YEAST:G3O-31540-MONOMER; -.
DR   BioGRID-ORCS; 853362; 1 hit in 10 CRISPR screens.
DR   PRO; PR:P47030; -.
DR   Proteomes; UP000002311; Chromosome X.
DR   RNAct; P47030; Protein.
DR   GO; GO:0000407; C:phagophore assembly site; IDA:SGD.
DR   GO; GO:0006914; P:autophagy; IGI:SGD.
DR   GO; GO:0009267; P:cellular response to starvation; IGI:SGD.
DR   GO; GO:0031505; P:fungal-type cell wall organization; IGI:SGD.
DR   GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd00052; EH; 1.
DR   Gene3D; 1.10.238.10; EF-hand; 1.
DR   InterPro; IPR011992; EF-hand-dom_pair.
DR   InterPro; IPR000261; EH_dom.
DR   SMART; SM00027; EH; 1.
DR   SUPFAM; SSF47473; EF-hand; 1.
PE   1: Evidence at protein level;
KW   Lipid metabolism; Reference proteome.
FT   CHAIN           1..604
FT                   /note="Protein TAX4"
FT                   /id="PRO_0000203050"
FT   DOMAIN          469..559
FT                   /note="EH"
FT   REGION          38..77
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          132..249
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          267..299
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          338..380
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          394..428
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        177..205
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        220..249
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        338..366
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        395..419
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   604 AA;  68768 MW;  E17C6C71D9FBFBD6 CRC64;
     MHFPKKKHSG NLSVVELPKE ALQDSLTAAQ ITFKRYAHPN GNAGSAERPR HLKVESAPVV
     KSEPSLPRMR QPEPRSINHQ YSRETLPGHS EAFSVPTTPL QTIHYDVRNK ASNSPSSIAA
     AETAAYLAHT NSFSNRSSGV GSRDPVMDTE TKPPRAPSAL KNELQLNRMR IPPPSYDNNV
     RSRSISPQVS YSTSLSSSCS ISSDGEETSY REKSTDEAFP PEPSMSSYSL ASKASAKASL
     TDPSQRQQES DYTAMNKLNG GNIIYKGTLP DLIPRSQRKT SKPRFKHRLL RSPEQQQENL
     SRVYSDQTQN GRAIINTQQN VKLKTTMRRG KYAITDNDET FPYDRKSVSS DSDTDEDSNV
     MEIKDKKKKS RRSKIKKGLK TTAAVVGSST SVLPFPHHHH HHHQLHNPNS HHLHTHHHTS
     SHKFNEDKPW KSHRDLGFIT EQERKRYESM WVSNRYSYLR LLPWWPSLAN EDDESHLQPL
     NLPQDGLMLN LVVKDIWYRS NLPRDLLVQI YNMVDTRKDG TLDRKSFIVG MWLVDQCLYG
     RKLTNELDQR VWNSVDGYVL GTINVKPATS DHYHNANNPL DKPSKLSVRQ ELKNIKRDLR
     NVRI
//