FKB12_ARATH
ID FKB12_ARATH Reviewed; 112 AA.
AC Q8LGG0; O04263;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2005, sequence version 2.
DT 25-MAY-2022, entry version 119.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase FKBP12;
DE Short=PPIase FKBP12;
DE EC=5.2.1.8;
DE AltName: Full=12 kDa FK506-binding protein;
DE Short=12 kDa FKBP;
DE AltName: Full=FK506-binding protein 12;
DE Short=AtFKBP12;
DE AltName: Full=FKBP-12;
DE AltName: Full=Immunophilin FKBP12;
DE AltName: Full=Rotamase;
GN Name=FKBP12; Synonyms=FKP12; OrderedLocusNames=At5g64350; ORFNames=MSJ1.19;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=9753776; DOI=10.1046/j.1365-313x.1998.00232.x;
RA Xu Q., Liang S., Kudla J., Luan S.;
RT "Molecular characterization of a plant FKBP12 that does not mediate action
RT of FK506 and rapamycin.";
RL Plant J. 15:511-519(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9501997; DOI=10.1093/dnares/4.6.401;
RA Nakamura Y., Sato S., Kaneko T., Kotani H., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. III. Sequence
RT features of the regions of 1,191,918 bp covered by seventeen physically
RT assigned P1 clones.";
RL DNA Res. 4:401-414(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP INTERACTION WITH FIP37 AND FK506.
RC STRAIN=cv. Columbia;
RX PubMed=9807817; DOI=10.1046/j.1365-313x.1998.00248.x;
RA Faure J.-D., Gingerich D., Howell S.H.;
RT "An Arabidopsis immunophilin, AtFKBP12, binds to AtFIP37 (FKBP interacting
RT protein) in an interaction that is disrupted by FK506.";
RL Plant J. 15:783-789(1998).
RN [7]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=15047905; DOI=10.1104/pp.103.031005;
RA He Z., Li L., Luan S.;
RT "Immunophilins and parvulins. Superfamily of peptidyl prolyl isomerases in
RT Arabidopsis.";
RL Plant Physiol. 134:1248-1267(2004).
RN [8]
RP FUNCTION, AND INTERACTION WITH TOR.
RX PubMed=22134914; DOI=10.1074/jbc.m111.300749;
RA Xiong Y., Sheen J.;
RT "Rapamycin and glucose-target of rapamycin (TOR) protein signaling in
RT plants.";
RL J. Biol. Chem. 287:2836-2842(2012).
CC -!- FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the
CC cis-trans isomerization of proline imidic peptide bonds in
CC oligopeptides (By similarity). Mediates rapamycin inactivation of TOR
CC protein kinase activity. {ECO:0000250, ECO:0000269|PubMed:22134914}.
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 -!- SUBUNIT: Interacts with FIP37 and with the immunosuppressive drug
CC FK506. Its interaction with FIP37 is inhibited by FK506. Interacts with
CC TOR in a rapamycin-dependent manner. {ECO:0000269|PubMed:22134914,
CC ECO:0000269|PubMed:9807817}.
CC -!- INTERACTION:
CC Q8LGG0; Q9ZSZ8: FIP37; NbExp=3; IntAct=EBI-1641228, EBI-1641243;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the FKBP-type PPIase family. {ECO:0000305}.
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DR EMBL; U96924; AAB57847.1; -; mRNA.
DR EMBL; AB008268; BAB09866.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97876.1; -; Genomic_DNA.
DR EMBL; AY059928; AAL24410.1; -; mRNA.
DR EMBL; AY081564; AAM10126.1; -; mRNA.
DR EMBL; AY084289; AAM60880.1; -; mRNA.
DR RefSeq; NP_201240.1; NM_125831.3.
DR AlphaFoldDB; Q8LGG0; -.
DR SMR; Q8LGG0; -.
DR BioGRID; 21798; 4.
DR IntAct; Q8LGG0; 4.
DR STRING; 3702.AT5G64350.1; -.
DR PaxDb; Q8LGG0; -.
DR PRIDE; Q8LGG0; -.
DR ProteomicsDB; 228907; -.
DR EnsemblPlants; AT5G64350.1; AT5G64350.1; AT5G64350.
DR GeneID; 836556; -.
DR Gramene; AT5G64350.1; AT5G64350.1; AT5G64350.
DR KEGG; ath:AT5G64350; -.
DR Araport; AT5G64350; -.
DR TAIR; locus:2173438; AT5G64350.
DR eggNOG; KOG0544; Eukaryota.
DR HOGENOM; CLU_013615_12_2_1; -.
DR InParanoid; Q8LGG0; -.
DR OMA; RVIAGWD; -.
DR OrthoDB; 1328688at2759; -.
DR PhylomeDB; Q8LGG0; -.
DR PRO; PR:Q8LGG0; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q8LGG0; baseline and differential.
DR Genevisible; Q8LGG0; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IBA:GO_Central.
DR GO; GO:0061077; P:chaperone-mediated protein folding; IBA:GO_Central.
DR GO; GO:0000413; P:protein peptidyl-prolyl isomerization; IBA:GO_Central.
DR Gene3D; 3.10.50.40; -; 1.
DR InterPro; IPR046357; PPIase_dom_sf.
DR InterPro; IPR001179; PPIase_FKBP_dom.
DR Pfam; PF00254; FKBP_C; 1.
DR PROSITE; PS50059; FKBP_PPIASE; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Disulfide bond; Isomerase; Reference proteome; Rotamase.
FT CHAIN 1..112
FT /note="Peptidyl-prolyl cis-trans isomerase FKBP12"
FT /id="PRO_0000075300"
FT DOMAIN 19..112
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00277"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 26..80
FT /evidence="ECO:0000250"
FT CONFLICT 111
FT /note="V -> L (in Ref. 5; AAM60880)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 112 AA; 11988 MW; C0ED5DFEB6C8E1E2 CRC64;
MGVEKQVIRP GNGPKPAPGQ TVTVHCTGFG KDGDLSQKFW STKDEGQKPF SFQIGKGAVI
KGWDEGVIGM QIGEVARLRC SSDYAYGAGG FPAWGIQPNS VLDFEIEVLS VQ
