FKBP4_SPOFR
ID FKBP4_SPOFR Reviewed; 412 AA.
AC Q26486;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 77.
DE RecName: Full=46 kDa FK506-binding nuclear protein;
DE EC=5.2.1.8;
DE AltName: Full=Peptidyl-prolyl cis-trans isomerase;
DE Short=PPIase;
DE AltName: Full=Rotamase;
GN Name=FKBP46;
OS Spodoptera frugiperda (Fall armyworm).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Noctuoidea;
OC Noctuidae; Amphipyrinae; Spodoptera.
OX NCBI_TaxID=7108;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7527037; DOI=10.1016/s0021-9258(18)47356-5;
RA Alnemri E.S., Fernandes-Alnemri T., Pomerenke K., Robertson N.M.,
RA Dudley K., Dubois G.C., Litwack G.;
RT "FKBP46, a novel Sf9 insect cell nuclear immunophilin that forms a protein-
RT kinase complex.";
RL J. Biol. Chem. 269:30828-30834(1994).
CC -!- FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the
CC cis-trans isomerization of proline imidic peptide bonds in
CC oligopeptides. Binds double-stranded DNA in vitro.
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 -!- ACTIVITY REGULATION: Inhibited by both FK506 and rapamycin.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- PTM: Phosphorylated by a nuclear kinase in the presence of Mg(2+) and
CC ATP.
CC -!- SIMILARITY: Belongs to the FKBP-type PPIase family. {ECO:0000305}.
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DR EMBL; U15038; AAA58962.1; -; mRNA.
DR PIR; A55320; A55320.
DR AlphaFoldDB; Q26486; -.
DR SMR; Q26486; -.
DR PRIDE; Q26486; -.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
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 2: Evidence at transcript level;
KW DNA-binding; Isomerase; Nucleus; Phosphoprotein; Rotamase.
FT CHAIN 1..412
FT /note="46 kDa FK506-binding nuclear protein"
FT /id="PRO_0000075311"
FT DOMAIN 324..412
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00277"
FT REGION 95..304
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 95..113
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 114..147
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 153..177
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 189..214
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 215..247
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 269..304
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 412 AA; 45810 MW; F2A69159AEF4FE22 CRC64;
MFWGLIMEPN KRYTQVVEKP FHISQAAMDI STGDNDPCQV MVVVDGKNFL VCTLQKGKII
QVPLDLYFKS GDSVSFLTNG KCNVHLTGYL DPEFEEDLED EEEAEEEEEE EEAPPLVPAK
NKRKLENAND ATANKKAKPD KKAGKNSAPA AESDSDDDDE DQLQKFLDGE DIDTDENDES
FKMNTSAEGD DSDEEDDDED EEDEEDDDED DEEEEEAPKK KKKQPAAEQD STLDTSKESV
DMSKLSKSQK RRLKKKLQQQ AKQQPQVNGV DKPKKEEPQQ KAEKKKPEAK KEEAPVEKKE
KKQIAGGVSI EDLKVGSGPV AKAGKVVMVY YEGRLKQNNK MFDNCVKGPG FKFRLGSKEV
ISGWDVGIAG MKVGGKRKIV CPPAMAYGAK GSPPVIPPNS TLVFEVDLKN VK
