PUT3_YEAST
ID PUT3_YEAST Reviewed; 979 AA.
AC P25502; D6VXS1;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Proline utilization trans-activator;
GN Name=PUT3; OrderedLocusNames=YKL015W;
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].
RX PubMed=2017167; DOI=10.1128/mcb.11.5.2609-2619.1991;
RA Marczak J.E., Brandriss M.C.;
RT "Analysis of constitutive and noninducible mutations of the PUT3
RT transcriptional activator.";
RL Mol. Cell. Biol. 11:2609-2619(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8154185; DOI=10.1002/yea.320091208;
RA Wiemann S., Voss H., Schwager C., Rupp T., Stegemann J., Zimmermann J.,
RA Grothues D., Sensen C., Erfle H., Hewitt N., Banrevi A., Ansorge W.;
RT "Sequencing and analysis of 51.6 kilobases on the left arm of chromosome XI
RT from Saccharomyces cerevisiae reveals 23 open reading frames including the
RT FAS1 gene.";
RL Yeast 9:1343-1348(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8196765; DOI=10.1038/369371a0;
RA Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P.,
RA Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S.,
RA von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M.,
RA Becker I., Mewes H.-W.;
RT "Complete DNA sequence of yeast chromosome XI.";
RL Nature 369:371-378(1994).
RN [4]
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 [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 STRUCTURE BY NMR OF 30-100.
RX PubMed=9303003; DOI=10.1038/nsb0997-744;
RA Walters K.J., Dayie K.T., Reece R.J., Ptashne M., Wagner G.;
RT "Structure and mobility of the PUT3 dimer.";
RL Nat. Struct. Biol. 4:744-750(1997).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 31-100.
RX PubMed=9303004; DOI=10.1038/nsb0997-751;
RA Swaminathan K., Flynn P., Reece R.J., Marmorstein R.;
RT "Crystal structure of a PUT3-DNA complex reveals a novel mechanism for DNA
RT recognition by a protein containing a Zn2Cys6 binuclear cluster.";
RL Nat. Struct. Biol. 4:751-759(1997).
CC -!- FUNCTION: Positive activator of the proline utilization pathway. Binds
CC to the promoters of PUT1 and PUT2 genes. Recognizes and binds to the
CC DNA sequence 5'-CGG-N(10)-CCG-3'.
CC -!- SUBUNIT: Binds DNA as a homodimer.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- MISCELLANEOUS: Present with 736 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; X55384; CAA39055.1; -; Genomic_DNA.
DR EMBL; X74152; CAA52267.1; -; Genomic_DNA.
DR EMBL; Z28015; CAA81850.1; -; Genomic_DNA.
DR EMBL; BK006944; DAA09141.1; -; Genomic_DNA.
DR PIR; A39792; A39792.
DR RefSeq; NP_012910.1; NM_001179581.1.
DR PDB; 1AJY; NMR; -; A/B=31-100.
DR PDB; 1ZME; X-ray; 2.50 A; C/D=31-100.
DR PDBsum; 1AJY; -.
DR PDBsum; 1ZME; -.
DR AlphaFoldDB; P25502; -.
DR SMR; P25502; -.
DR BioGRID; 34117; 108.
DR DIP; DIP-1425N; -.
DR IntAct; P25502; 5.
DR MINT; P25502; -.
DR STRING; 4932.YKL015W; -.
DR iPTMnet; P25502; -.
DR MaxQB; P25502; -.
DR PaxDb; P25502; -.
DR PRIDE; P25502; -.
DR EnsemblFungi; YKL015W_mRNA; YKL015W; YKL015W.
DR GeneID; 853854; -.
DR KEGG; sce:YKL015W; -.
DR SGD; S000001498; PUT3.
DR VEuPathDB; FungiDB:YKL015W; -.
DR eggNOG; ENOG502QTA0; Eukaryota.
DR GeneTree; ENSGT00940000176304; -.
DR HOGENOM; CLU_006926_0_0_1; -.
DR InParanoid; P25502; -.
DR OMA; CTIASYF; -.
DR BioCyc; YEAST:G3O-31824-MON; -.
DR EvolutionaryTrace; P25502; -.
DR PRO; PR:P25502; -.
DR Proteomes; UP000002311; Chromosome XI.
DR RNAct; P25502; protein.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IMP:SGD.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:SGD.
DR GO; GO:0043565; F:sequence-specific DNA binding; HDA:SGD.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:2001158; P:positive regulation of proline catabolic process to glutamate; IMP:SGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:SGD.
DR GO; GO:0006560; P:proline metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR GO; GO:0000972; P:transcription-dependent tethering of RNA polymerase II gene DNA at nuclear periphery; IMP:SGD.
DR CDD; cd00067; GAL4; 1.
DR Gene3D; 4.10.240.10; -; 1.
DR InterPro; IPR046347; bZIP_sf.
DR InterPro; IPR007219; Transcription_factor_dom_fun.
DR InterPro; IPR001138; Zn2-C6_fun-type_DNA-bd.
DR InterPro; IPR036864; Zn2-C6_fun-type_DNA-bd_sf.
DR Pfam; PF04082; Fungal_trans; 1.
DR Pfam; PF00172; Zn_clus; 1.
DR SMART; SM00906; Fungal_trans; 1.
DR SMART; SM00066; GAL4; 1.
DR SUPFAM; SSF57701; SSF57701; 1.
DR SUPFAM; SSF57959; SSF57959; 1.
DR PROSITE; PS00463; ZN2_CY6_FUNGAL_1; 1.
DR PROSITE; PS50048; ZN2_CY6_FUNGAL_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; DNA-binding; Metal-binding; Nucleus;
KW Proline metabolism; Reference proteome; Transcription;
KW Transcription regulation; Zinc.
FT CHAIN 1..979
FT /note="Proline utilization trans-activator"
FT /id="PRO_0000114968"
FT DNA_BIND 34..60
FT /note="Zn(2)-C6 fungal-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00227"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 104..163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 183..207
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 805..825
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 104..120
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 136..150
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 34
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT BINDING 34
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT BINDING 37
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT BINDING 44
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT BINDING 50
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT BINDING 50
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT BINDING 53
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT BINDING 60
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT HELIX 35..40
FT /evidence="ECO:0007829|PDB:1ZME"
FT STRAND 47..49
FT /evidence="ECO:0007829|PDB:1ZME"
FT HELIX 51..55
FT /evidence="ECO:0007829|PDB:1ZME"
FT STRAND 68..72
FT /evidence="ECO:0007829|PDB:1ZME"
FT HELIX 73..96
FT /evidence="ECO:0007829|PDB:1ZME"
SQ SEQUENCE 979 AA; 111414 MW; 59FA19EFC79EE0C0 CRC64;
MVTDQGSRHS IQSKQPAYVN KQPQKRQQRS SVACLSCRKR HIKCPGGNPC QKCVTSNAIC
EYLEPSKKIV VSTKYLQQLQ KDLNDKTEEN NRLKALLLER PVSVRGKDNS DDDERHINNA
PSSDTLEVSS APAAPIFDLM SNSNTASDND NDDDNSNRIT NNRSYDHSLE KYYKKAISIF
KQPANANGEN GNGANGHEDD DEDDEEISTN FAQRSGRLIE SHNGFHYFVG SSSMTLFGLE
IQSLVTKYIS VKNFRPLPIN TKNKILNSNL NPAISSFINS NNYLFSSYNF LNPISTIVNL
NSINDNLSPL MFKIILKSDT DGSSGQEEVI QFQLPSYNYT KLLIDCFINY NDGCFYFFNE
GLVKCGINKL YLENKWLYYD NTKKALDNEN DPILQAVWFC KILLILAVGE MYLGSINNEM
LKNYSNQPKL PGSKFFQMGS KIFNCLFSSE RLENVTKKGG IEVLLLYAFF LQVADYTLAS
YFYFGQALRT CLILGLHVDS QSDTLSRYEI EHHRRLWWTV YMFERMLSSK AGLPLSFTDY
TISTALPADI DDETIEEKNS HYVFRKAELI SNCVTIVKIN AQILSKLYQR QPETNIIITL
KVVIKQLLEW RNNLSDSLQV DFTQKDEDFK ISRLSTNMFT EYFQGINLAV RPLLFHFASI
QLKRFKTSNT FVNLQNYSAT ISSLLTCSLH ASVNTIRSLW SLLQNSMLAM FSYMDREYLF
TSSCTLLLFN TAFGIHEQTL YHLDHSLEIF TQMRNLGNIP AGLRRAQLLT LMANLDFHGI
MNDLITKYND ILKFDSMNCE NDNIVEDSNE PKRETEKCKP HKDGDRIDPS IIDCDKSNTN
TNMIKNESIS NIVSILPEGA KPTLTDYSNG NNDVNDINVN NSEPSTFFDI ITASLENSYQ
TTLTEKGSQV MEKNMDQLDS VHNLNDDDLQ QLLEDLGNID HSDEKLWKEI TDQAMWLGNT
MDPTAAAGSE IDFTDYLGP
