(data stored in ACNUC8465 zone)

SWISSPROT: FKBP4_CANGA

ID   FKBP4_CANGA             Reviewed;         398 AA.
AC   Q6FK71;
DT   18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   30-AUG-2017, entry version 82.
DE   RecName: Full=FK506-binding protein 4;
DE            EC=5.2.1.8 {ECO:0000250|UniProtKB:Q06205};
DE   AltName: Full=Histone proline isomerase {ECO:0000250|UniProtKB:Q06205};
DE   AltName: Full=Peptidyl-prolyl cis-trans isomerase;
DE            Short=PPIase;
DE   AltName: Full=Rotamase;
GN   Name=FPR4; OrderedLocusNames=CAGL0M00638g;
OS   Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 /
OS   NRRL Y-65) (Yeast) (Torulopsis glabrata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC   Nakaseomyces/Candida clade.
OX   NCBI_TaxID=284593;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S.,
RA   Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E.,
RA   Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V.,
RA   Barnay S., Blanchin S., Beckerich J.-M., Beyne E., Bleykasten C.,
RA   Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A.,
RA   Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A.,
RA   Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R.,
RA   Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H.,
RA   Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O.,
RA   Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A.,
RA   Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B.,
RA   Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A.,
RA   Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA   Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- FUNCTION: PPIase that acts as a histone chaperone. Histone proline
CC       isomerase that increases the rate of cis-trans isomerization at
CC       prolines on the histone H3 N-terminal tail. Proline isomerization
CC       influences H3 methylation thereby regulating gene expression.
CC       {ECO:0000250|UniProtKB:Q06205}.
CC   -!- CATALYTIC ACTIVITY: Peptidylproline (omega=180) = peptidylproline
CC       (omega=0). {ECO:0000250|UniProtKB:Q06205}.
CC   -!- ENZYME REGULATION: Inhibited by both FK506 and rapamycin.
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Binds to histones H3 and H4.
CC       {ECO:0000250|UniProtKB:Q06205}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q06205}.
CC   -!- SIMILARITY: Belongs to the FKBP-type PPIase family. FKBP3/4
CC       subfamily. {ECO:0000305}.
DR   EMBL; CR380959; CAG62349.1; -; Genomic_DNA.
DR   RefSeq; XP_449373.1; XM_449373.1.
DR   ProteinModelPortal; Q6FK71; -.
DR   SMR; Q6FK71; -.
DR   STRING; 284593.XP_449373.1; -.
DR   PRIDE; Q6FK71; -.
DR   EnsemblFungi; CAG62349; CAG62349; CAGL0M00638g.
DR   KEGG; cgr:CAGL0M00638g; -.
DR   CGD; CAL0136625; CAGL0M00638g.
DR   EuPathDB; FungiDB:CAGL0M00638g; -.
DR   eggNOG; KOG0552; Eukaryota.
DR   eggNOG; COG0545; LUCA.
DR   HOGENOM; HOG000216214; -.
DR   InParanoid; Q6FK71; -.
DR   KO; K14826; -.
DR   OMA; MEIAEMG; -.
DR   OrthoDB; EOG092C52SD; -.
DR   Proteomes; UP000002428; Chromosome M.
DR   GO; GO:0000785; C:chromatin; IEA:EnsemblFungi.
DR   GO; GO:0005730; C:nucleolus; IEA:InterPro.
DR   GO; GO:0005528; F:FK506 binding; IEA:InterPro.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0000412; P:histone peptidyl-prolyl isomerization; IEA:EnsemblFungi.
DR   GO; GO:0000415; P:negative regulation of histone H3-K36 methylation; IEA:EnsemblFungi.
DR   GO; GO:0006334; P:nucleosome assembly; IEA:EnsemblFungi.
DR   InterPro; IPR026257; FK506_BP.
DR   InterPro; IPR023566; PPIase_FKBP.
DR   InterPro; IPR001179; PPIase_FKBP_dom.
DR   PANTHER; PTHR43811; PTHR43811; 1.
DR   Pfam; PF00254; FKBP_C; 1.
DR   PIRSF; PIRSF001473; FK506-bp_FPR3; 1.
DR   PROSITE; PS50059; FKBP_PPIASE; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q6FK71.
DR   SWISS-2DPAGE; Q6FK71.
KW   Chaperone; Complete proteome; Isomerase; Nucleus; Reference proteome;
KW   Rotamase.
FT   CHAIN         1    398       FK506-binding protein 4.
FT                                /FTId=PRO_0000233078.
FT   DOMAIN      312    398       PPIase FKBP-type. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00277}.
FT   COMPBIAS     66    244       Asp/Glu-rich.
SQ   SEQUENCE   398 AA;  44834 MW;  5B454925CFFBA57A CRC64;
     MSDMLPLAMY ALNVEPYTHT PAVLLDTPVT VRITMAAIDP EPFDEDKKPS TLRIIRRNPV
     YLDAGEVDEE KLIEELEGDE AAEDGDEASD DDKEEEDEDE DVDEDDEDDD EDDDGEDEYE
     ECVVVTLSPE TRCQQAIDIT IAPEEDVQFL VTGSYTISLT GNYVKHPFDE PLEDLYSDED
     SEEYSDDELD QEIEEDDELD HDEASSEESD EDQEFYDAIS EGDEDIDEQL AKLEETSDVE
     AHLEDLIAKD NKKKRKQEQL DEQPETKKSK KTKDEKNTKA TENEKKNKAQ VLEGGVIIED
     RKIGEGPKAK KGSKVGMRYI GKLKNGKVFD KNTSGKPFYF KLHRGEVIKG WDIGVTGMAI
     GGERRIVIPA PYAYGKQTLP GIPANSELTF DVKLVSLK
//

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