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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   25-MAY-2022, entry version 101.
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 / NRRL
OS   Y-65) (Yeast) (Torulopsis glabrata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   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., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., 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:
CC       Reaction=[protein]-peptidylproline (omega=180) = [protein]-
CC         peptidylproline (omega=0); Xref=Rhea:RHEA:16237, Rhea:RHEA-
CC         COMP:10747, Rhea:RHEA-COMP:10748, ChEBI:CHEBI:83833,
CC         ChEBI:CHEBI:83834; EC=5.2.1.8;
CC         Evidence={ECO:0000250|UniProtKB:Q06205};
CC   -!- ACTIVITY REGULATION: Inhibited by both FK506 and rapamycin.
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Binds to histones H3 and H4. {ECO:0000250|UniProtKB:Q06205}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q06205}.
CC   -!- SIMILARITY: Belongs to the FKBP-type PPIase family. FKBP3/4 subfamily.
CC       {ECO:0000305}.
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DR   EMBL; CR380959; CAG62349.1; -; Genomic_DNA.
DR   RefSeq; XP_449373.1; XM_449373.1.
DR   AlphaFoldDB; Q6FK71; -.
DR   SMR; Q6FK71; -.
DR   STRING; 5478.XP_449373.1; -.
DR   EnsemblFungi; CAG62349; CAG62349; CAGL0M00638g.
DR   GeneID; 2891596; -.
DR   KEGG; cgr:CAGL0M00638g; -.
DR   CGD; CAL0136625; FPR4.
DR   VEuPathDB; FungiDB:CAGL0M00638g; -.
DR   eggNOG; KOG0552; Eukaryota.
DR   HOGENOM; CLU_022297_3_1_1; -.
DR   InParanoid; Q6FK71; -.
DR   OMA; YVKYVCM; -.
DR   Proteomes; UP000002428; Chromosome M.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.10.50.40; -; 1.
DR   InterPro; IPR041232; NPL.
DR   InterPro; IPR046357; PPIase_dom_sf.
DR   InterPro; IPR001179; PPIase_FKBP_dom.
DR   InterPro; IPR023566; PPIase_Fpr3/Fpr4-like.
DR   Pfam; PF00254; FKBP_C; 1.
DR   Pfam; PF17800; NPL; 1.
DR   PIRSF; PIRSF001473; FK506-bp_FPR3; 1.
DR   PROSITE; PS50059; FKBP_PPIASE; 1.
PE   3: Inferred from homology;
KW   Chaperone; Isomerase; Nucleus; Reference proteome; Rotamase.
FT   CHAIN           1..398
FT                   /note="FK506-binding protein 4"
FT                   /id="PRO_0000233078"
FT   DOMAIN          312..398
FT                   /note="PPIase FKBP-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00277"
FT   REGION          66..120
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          164..232
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          245..288
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        68..120
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        173..231
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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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