FKBP3_MOUSE
ID FKBP3_MOUSE Reviewed; 224 AA.
AC Q62446; Q9WTJ7;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2001, sequence version 2.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase FKBP3;
DE Short=PPIase FKBP3;
DE EC=5.2.1.8;
DE AltName: Full=25 kDa FK506-binding protein;
DE Short=25 kDa FKBP;
DE Short=FKBP-25;
DE AltName: Full=FK506-binding protein 3;
DE Short=FKBP-3;
DE AltName: Full=Immunophilin FKBP25;
DE AltName: Full=Rapamycin-selective 25 kDa immunophilin;
DE AltName: Full=Rotamase;
GN Name=Fkbp3; Synonyms=Fkbp25;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Telencephalon;
RA Mas C., Bourgeois F., Simonneau M.;
RT "Isolation and mapping assignment of cDNAs differentially expressed in
RT embryonic telencephalon.";
RL Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Ahn J., Kratowicz S., Murphy M., Wang A., Levine A.J., George D.L.;
RT "Down-regulation of the Stathmin/Op18 and FKBP25 genes following p53
RT expression.";
RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PROTEIN SEQUENCE OF 100-110, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 168-224.
RX PubMed=8956998; DOI=10.1101/gad.10.23.2971;
RA Murphy M., Hinman A., Levine A.J.;
RT "Wild-type p53 negatively regulates the expression of a microtubule-
RT associated protein.";
RL Genes Dev. 10:2971-2980(1996).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-99, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
CC -!- FUNCTION: FK506- and rapamycin-binding proteins (FKBPs) constitute a
CC family of receptors for the two immunosuppressants which inhibit T-cell
CC proliferation by arresting two distinct cytoplasmic signal transmission
CC pathways. PPIases accelerate the folding of proteins (By similarity).
CC {ECO:0000250}.
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 preferentially by rapamycin over FK506.
CC {ECO:0000250}.
CC -!- INTERACTION:
CC Q62446; Q00987: MDM2; Xeno; NbExp=4; IntAct=EBI-8313562, EBI-389668;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the FKBP-type PPIase family. {ECO:0000305}.
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DR EMBL; AF135595; AAD25097.1; -; mRNA.
DR EMBL; AF110812; AAD20598.1; -; mRNA.
DR EMBL; BC002122; AAH02122.1; -; mRNA.
DR EMBL; U62545; AAB05769.1; -; mRNA.
DR CCDS; CCDS25940.1; -.
DR RefSeq; NP_038930.1; NM_013902.4.
DR PDB; 3KZ7; X-ray; 1.95 A; A=106-224.
DR PDBsum; 3KZ7; -.
DR AlphaFoldDB; Q62446; -.
DR SMR; Q62446; -.
DR BioGRID; 205966; 12.
DR IntAct; Q62446; 2.
DR MINT; Q62446; -.
DR STRING; 10090.ENSMUSP00000021332; -.
DR iPTMnet; Q62446; -.
DR PhosphoSitePlus; Q62446; -.
DR EPD; Q62446; -.
DR jPOST; Q62446; -.
DR MaxQB; Q62446; -.
DR PaxDb; Q62446; -.
DR PRIDE; Q62446; -.
DR ProteomicsDB; 267478; -.
DR Antibodypedia; 56; 239 antibodies from 33 providers.
DR DNASU; 30795; -.
DR Ensembl; ENSMUST00000021332; ENSMUSP00000021332; ENSMUSG00000020949.
DR GeneID; 30795; -.
DR KEGG; mmu:30795; -.
DR UCSC; uc007nrb.1; mouse.
DR CTD; 2287; -.
DR MGI; MGI:1353460; Fkbp3.
DR VEuPathDB; HostDB:ENSMUSG00000020949; -.
DR eggNOG; KOG0544; Eukaryota.
DR GeneTree; ENSGT00940000154514; -.
DR HOGENOM; CLU_013615_12_2_1; -.
DR InParanoid; Q62446; -.
DR OMA; FKGTEPV; -.
DR OrthoDB; 1328688at2759; -.
DR PhylomeDB; Q62446; -.
DR TreeFam; TF105293; -.
DR BioGRID-ORCS; 30795; 4 hits in 73 CRISPR screens.
DR ChiTaRS; Fkbp3; mouse.
DR PRO; PR:Q62446; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q62446; protein.
DR Bgee; ENSMUSG00000020949; Expressed in optic fissure and 287 other tissues.
DR ExpressionAtlas; Q62446; baseline and differential.
DR Genevisible; Q62446; MM.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.10.50.40; -; 1.
DR InterPro; IPR043368; FKBP3.
DR InterPro; IPR041200; FKBP3_BTHB.
DR InterPro; IPR046357; PPIase_dom_sf.
DR InterPro; IPR001179; PPIase_FKBP_dom.
DR PANTHER; PTHR46493; PTHR46493; 1.
DR Pfam; PF18410; BTHB; 1.
DR Pfam; PF00254; FKBP_C; 1.
DR PROSITE; PS50059; FKBP_PPIASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Direct protein sequencing; Isomerase; Nucleus;
KW Phosphoprotein; Reference proteome; Rotamase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q00688"
FT CHAIN 2..224
FT /note="Peptidyl-prolyl cis-trans isomerase FKBP3"
FT /id="PRO_0000075308"
FT DOMAIN 128..224
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00277"
FT REGION 88..118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q00688"
FT MOD_RES 36
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q00688"
FT MOD_RES 99
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 152
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q00688"
FT MOD_RES 170
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q00688"
FT CONFLICT 219
FT /note="E -> G (in Ref. 5; AAB05769)"
FT /evidence="ECO:0000305"
FT STRAND 110..117
FT /evidence="ECO:0007829|PDB:3KZ7"
FT STRAND 130..138
FT /evidence="ECO:0007829|PDB:3KZ7"
FT STRAND 144..147
FT /evidence="ECO:0007829|PDB:3KZ7"
FT STRAND 152..154
FT /evidence="ECO:0007829|PDB:3KZ7"
FT TURN 155..158
FT /evidence="ECO:0007829|PDB:3KZ7"
FT STRAND 162..165
FT /evidence="ECO:0007829|PDB:3KZ7"
FT STRAND 168..171
FT /evidence="ECO:0007829|PDB:3KZ7"
FT HELIX 173..179
FT /evidence="ECO:0007829|PDB:3KZ7"
FT STRAND 187..192
FT /evidence="ECO:0007829|PDB:3KZ7"
FT HELIX 194..196
FT /evidence="ECO:0007829|PDB:3KZ7"
FT HELIX 204..206
FT /evidence="ECO:0007829|PDB:3KZ7"
FT STRAND 214..224
FT /evidence="ECO:0007829|PDB:3KZ7"
SQ SEQUENCE 224 AA; 25148 MW; FCA2058CC4E97DAC CRC64;
MAAAVPQRAW TVEQLRSEQL PKKDIIKFLQ DHGSDSFLAE HKLLGNIKNV AKTANKDHLV
NAYNHLFESK RFKGTETISK VSEQVKNVKL SDDKPKDSKS EETLDEGPPK YTKSILKKGD
KTNFPKKGDV VHCWYTGTLP DGTVFDTNIQ TSSKKKKNAK PLSFKVGVGK VIRGWDEALL
TMSKGEKARL EIEPEWAYGK KGQPDAKIPP NTKLIFEVEL VDID
