FKBP4_NEUCR
ID FKBP4_NEUCR Reviewed; 467 AA.
AC Q7SCN0;
DT 18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 25-MAY-2022, entry version 107.
DE RecName: Full=FK506-binding protein 4;
DE Short=FKBP4;
DE EC=5.2.1.8 {ECO:0000250|UniProtKB:Q06205};
DE AltName: Full=FK506-resistance protein 4;
DE AltName: Full=Histone proline isomerase {ECO:0000250|UniProtKB:Q06205};
DE AltName: Full=Peptidyl-prolyl cis-trans isomerase fkr-4;
DE Short=PPIase fkr-4;
DE AltName: Full=Rotamase;
GN Name=fkr-4; ORFNames=NCU03241;
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(2003).
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; CM002236; EAA34497.1; -; Genomic_DNA.
DR RefSeq; XP_963733.1; XM_958640.3.
DR AlphaFoldDB; Q7SCN0; -.
DR SMR; Q7SCN0; -.
DR STRING; 5141.EFNCRP00000002989; -.
DR EnsemblFungi; EAA34497; EAA34497; NCU03241.
DR GeneID; 3879882; -.
DR KEGG; ncr:NCU03241; -.
DR VEuPathDB; FungiDB:NCU03241; -.
DR HOGENOM; CLU_022297_3_1_1; -.
DR InParanoid; Q7SCN0; -.
DR OMA; CPPHMAY; -.
DR Proteomes; UP000001805; Chromosome 1, Linkage Group I.
DR GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR GO; GO:0005730; C:nucleolus; IBA:GO_Central.
DR GO; GO:0005527; F:macrolide binding; IBA:GO_Central.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IBA:GO_Central.
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..467
FT /note="FK506-binding protein 4"
FT /id="PRO_0000233084"
FT DOMAIN 381..467
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00277"
FT REGION 64..163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 208..357
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 96..112
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 129..147
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 148..163
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 212..251
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 252..334
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 467 AA; 50774 MW; 69CEBC95C4E958EF CRC64;
MAPLMPVAVF GLEVPPGEIL IPAASEFPAI IHITMAALDP TKAPEADGQG NIPALPRSTL
KIIKATGHDH DDDDEEEDEY LQSLLGGGDS DDEANGGPSD PSKSKKAKQE AAIKKLMAAT
QEESDEEMED AKPNGKKGKG KGKASESDEE ESDEESDCCG DDDLQLEDYV VCTLDTERNY
QQPINITIGE GEKVFFCVQG THSVYLTGNF VVPEDDEEDS EDDEDESDDE DYDFPLGGED
DDSDDMSDEL DELDGTPRVK EITSEDEEEE APKLVDTSKK GKKRPAEDDA EGLDAMISKD
DKKLSKKQQK KQKVEEAKKE EPKKETKSDK KVQFAKNLEQ GPTGPAKDKL ENKKPTSTVK
VVQGVTIDDR KVGTGRAAKN GDRVGMRYIG KLQNGKVFDS NKKGAPFSFK LGKGEVIKGW
DIGVAGMAVG GERRLTIPAH LAYGSRALPG IPPNSTLIFD VKLLEIK
