FKB42_ARATH
ID FKB42_ARATH Reviewed; 365 AA.
AC Q9LDC0; Q8RWM0;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 152.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase FKBP42;
DE Short=PPIase FKBP42;
DE EC=5.2.1.8;
DE AltName: Full=42 kDa peptidyl-prolyl isomerase;
DE AltName: Full=FK506-binding protein 42;
DE Short=AtFKBP42;
DE AltName: Full=Immunophilin FKBP42;
DE AltName: Full=Protein TWISTED DWARF 1;
DE AltName: Full=Protein ULTRACURVATA 2;
DE AltName: Full=Rotamase;
GN Name=FKBP42; Synonyms=TWD1, UCU2; OrderedLocusNames=At3g21640;
GN ORFNames=MIL23.21;
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;
RA Kolukisaoglu U., Berger J., Eckhoff A., Moeller A., Saal B., Bellini C.,
RA Schulz B.;
RT "Structure and evolution of FKBP-like genes in Arabidopsis.";
RL Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(2000).
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 SUBCELLULAR LOCATION, INTERACTION WITH CALMODULIN AND SHD/HSP90, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=12410806; DOI=10.1046/j.1365-313x.2002.01420.x;
RA Kamphausen T., Fanghaenel J., Neumann D., Schulz B., Rahfeld J.-U.;
RT "Characterization of Arabidopsis thaliana AtFKBP42 that is membrane-bound
RT and interacts with Hsp90.";
RL Plant J. 32:263-276(2002).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH MDR1/PGP1 AND
RP MDR11/PGP19.
RX PubMed=14517332; DOI=10.1091/mbc.e02-10-0698;
RA Geisler M., Kolukisaoglu H.U., Bouchard R., Billion K., Berger J., Saal B.,
RA Frangne N., Koncz-Kalman Z., Koncz C., Dudler R., Blakeslee J.J.,
RA Murphy A.S., Martinoia E., Schulz B.;
RT "TWISTED DWARF1, a unique plasma membrane-anchored immunophilin-like
RT protein, interacts with Arabidopsis multidrug resistance-like transporters
RT AtPGP1 and AtPGP19.";
RL Mol. Biol. Cell 14:4238-4249(2003).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH MRP1 AND MRP2.
RX PubMed=15133126; DOI=10.1091/mbc.e03-11-0831;
RA Geisler M., Girin M., Brandt S., Vincenzetti V., Plaza S., Paris N.,
RA Kobae Y., Maeshima M., Billion K., Kolukisaoglu U.H., Schulz B.,
RA Martinoia E.;
RT "Arabidopsis immunophilin-like TWD1 functionally interacts with vacuolar
RT ABC transporters.";
RL Mol. Biol. Cell 15:3393-3405(2004).
RN [8]
RP FUNCTION.
RX PubMed=14730066; DOI=10.1104/pp.103.032524;
RA Perez-Perez J.M., Ponce M.R., Micol J.L.;
RT "The ULTRACURVATA2 gene of Arabidopsis encodes an FK506-binding protein
RT involved in auxin and brassinosteroid signaling.";
RL Plant Physiol. 134:101-117(2004).
RN [9]
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 [10]
RP FUNCTION.
RX PubMed=16887800; DOI=10.1074/jbc.m604604200;
RA Bouchard R., Bailly A., Blakeslee J.J., Oehring S.C., Vincenzetti V.,
RA Lee O.R., Paponov I., Palme K., Mancuso S., Murphy A.S., Schulz B.,
RA Geisler M.;
RT "Immunophilin-like TWISTED DWARF1 modulates auxin efflux activities of
RT Arabidopsis P-glycoproteins.";
RL J. Biol. Chem. 281:30603-30612(2006).
RN [11]
RP FUNCTION, AND INTERACTION WITH NPA.
RX PubMed=18499676; DOI=10.1074/jbc.m709655200;
RA Bailly A., Sovero V., Vincenzetti V., Santelia D., Bartnik D., Koenig B.W.,
RA Mancuso S., Martinoia E., Geisler M.;
RT "Modulation of P-glycoproteins by auxin transport inhibitors is mediated by
RT interaction with immunophilins.";
RL J. Biol. Chem. 283:21817-21826(2008).
RN [12]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=20971896; DOI=10.1105/tpc.110.078360;
RA Wu G., Otegui M.S., Spalding E.P.;
RT "The ER-localized TWD1 immunophilin is necessary for localization of
RT multidrug resistance-like proteins required for polar auxin transport in
RT Arabidopsis roots.";
RL Plant Cell 22:3295-3304(2010).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.32 ANGSTROMS) OF 1-180.
RX PubMed=16364310; DOI=10.1016/j.febslet.2005.12.007;
RA Weiergraeber O.H., Eckhoff A., Granzin J.;
RT "Crystal structure of a plant immunophilin domain involved in regulation of
RT MDR-type ABC transporters.";
RL FEBS Lett. 580:251-255(2006).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS) OF 1-338.
RX PubMed=17045295; DOI=10.1016/j.jmb.2006.09.052;
RA Granzin J., Eckhoff A., Weiergraber O.H.;
RT "Crystal structure of a multi-domain immunophilin from Arabidopsis
RT thaliana: a paradigm for regulation of plant ABC transporters.";
RL J. Mol. Biol. 364:799-809(2006).
RN [15]
RP STRUCTURE BY NMR OF 335-365, AND MEMBRANE ANCHOR.
RX PubMed=17033777; DOI=10.1007/s00249-006-0094-2;
RA Scheidt H.A., Vogel A., Eckhoff A., Koenig B.W., Huster D.;
RT "Solid-state NMR characterization of the putative membrane anchor of TWD1
RT from Arabidopsis thaliana.";
RL Eur. Biophys. J. 36:393-404(2007).
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). Modulates the uptake of MRP substrates
CC into the vacuole; reduces metolachlor-GS (MOC-GS) and enhances 17-beta-
CC estradiol 17-(beta-D-glucuronide) (E(2)17betaG) uptake. Regulates cell
CC elongation and orientation. Functions as a positive regulator of PGP1-
CC mediated auxin transport. Confers drug modulation of PGP1 efflux
CC activity as interaction with NPA or flavonol quercetin prevents its
CC physical and functional interaction with PGP1. Required for the proper
CC localization of auxin-related ABCB transporters. Plays a role in
CC brassinosteroid (BR) signaling pathway. {ECO:0000250,
CC ECO:0000269|PubMed:14517332, ECO:0000269|PubMed:14730066,
CC ECO:0000269|PubMed:15133126, ECO:0000269|PubMed:16887800,
CC ECO:0000269|PubMed:18499676, ECO:0000269|PubMed:20971896}.
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 calmodulin (CaM), MRP1, MRP2, MDR1/PGP1,
CC MDR11/PGP19 and SHD/HSP90. Interacts with 1-naphthylphthalamic acid
CC (NPA). {ECO:0000269|PubMed:12410806, ECO:0000269|PubMed:14517332,
CC ECO:0000269|PubMed:15133126, ECO:0000269|PubMed:18499676}.
CC -!- INTERACTION:
CC Q9LDC0; Q9ZR72: ABCB1; NbExp=2; IntAct=EBI-360006, EBI-366396;
CC Q9LDC0; Q9C8G9: ABCC1; NbExp=4; IntAct=EBI-360006, EBI-637633;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12410806,
CC ECO:0000269|PubMed:14517332, ECO:0000269|PubMed:15133126}; Single-pass
CC type IV membrane protein. Vacuole membrane
CC {ECO:0000269|PubMed:12410806, ECO:0000269|PubMed:15133126}; Single-pass
CC type IV membrane protein. Endoplasmic reticulum
CC {ECO:0000269|PubMed:20971896}.
CC -!- DISRUPTION PHENOTYPE: Plants display helical rotation of several
CC organs. {ECO:0000269|PubMed:12410806}.
CC -!- SIMILARITY: Belongs to the FKBP-type PPIase family. {ECO:0000305}.
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DR EMBL; AJ224640; CAC00654.1; -; mRNA.
DR EMBL; AB019232; BAB02359.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE76533.1; -; Genomic_DNA.
DR EMBL; AY093009; AAM13008.1; -; mRNA.
DR EMBL; BT001192; AAN65079.1; -; mRNA.
DR RefSeq; NP_188801.2; NM_113059.3.
DR PDB; 2F4E; X-ray; 2.32 A; A/B=1-180.
DR PDB; 2IF4; X-ray; 2.85 A; A=1-338.
DR PDBsum; 2F4E; -.
DR PDBsum; 2IF4; -.
DR AlphaFoldDB; Q9LDC0; -.
DR BMRB; Q9LDC0; -.
DR SMR; Q9LDC0; -.
DR BioGRID; 7050; 31.
DR IntAct; Q9LDC0; 26.
DR STRING; 3702.AT3G21640.1; -.
DR TCDB; 8.A.11.1.1; the immunophilin-like prolyl:peptidyl isomerase regulator (i-ppi) family.
DR PaxDb; Q9LDC0; -.
DR PRIDE; Q9LDC0; -.
DR ProteomicsDB; 230585; -.
DR EnsemblPlants; AT3G21640.1; AT3G21640.1; AT3G21640.
DR GeneID; 821718; -.
DR Gramene; AT3G21640.1; AT3G21640.1; AT3G21640.
DR KEGG; ath:AT3G21640; -.
DR Araport; AT3G21640; -.
DR TAIR; locus:2089890; AT3G21640.
DR eggNOG; KOG0543; Eukaryota.
DR HOGENOM; CLU_013615_4_0_1; -.
DR InParanoid; Q9LDC0; -.
DR OMA; GCPPRIK; -.
DR OrthoDB; 897391at2759; -.
DR PhylomeDB; Q9LDC0; -.
DR EvolutionaryTrace; Q9LDC0; -.
DR PRO; PR:Q9LDC0; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LDC0; baseline and differential.
DR Genevisible; Q9LDC0; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005516; F:calmodulin binding; IDA:TAIR.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; ISS:TAIR.
DR GO; GO:0009734; P:auxin-activated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0048366; P:leaf development; IMP:TAIR.
DR Gene3D; 1.25.40.10; -; 1.
DR Gene3D; 3.10.50.40; -; 1.
DR InterPro; IPR046357; PPIase_dom_sf.
DR InterPro; IPR001179; PPIase_FKBP_dom.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR Pfam; PF00254; FKBP_C; 1.
DR Pfam; PF13181; TPR_8; 1.
DR SMART; SM00028; TPR; 3.
DR SUPFAM; SSF48452; SSF48452; 1.
DR PROSITE; PS50059; FKBP_PPIASE; 1.
DR PROSITE; PS50005; TPR; 2.
DR PROSITE; PS50293; TPR_REGION; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Auxin signaling pathway; Calmodulin-binding; Cell membrane;
KW Endoplasmic reticulum; Isomerase; Membrane; Reference proteome; Repeat;
KW Rotamase; TPR repeat; Transmembrane; Transmembrane helix; Vacuole.
FT CHAIN 1..365
FT /note="Peptidyl-prolyl cis-trans isomerase FKBP42"
FT /id="PRO_0000226087"
FT TRANSMEM 339..357
FT /note="Helical; Anchor for type IV membrane protein"
FT DOMAIN 67..159
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00277"
FT REPEAT 179..212
FT /note="TPR 1"
FT REPEAT 230..263
FT /note="TPR 2"
FT REPEAT 264..297
FT /note="TPR 3"
FT REGION 1..163
FT /note="Interaction with MDR1/PGP1"
FT REGION 1..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 163..337
FT /note="Interaction with MRP1"
FT /evidence="ECO:0000269|PubMed:15133126"
FT REGION 310..326
FT /note="Calmodulin-binding"
FT /evidence="ECO:0000255"
FT CONFLICT 107
FT /note="A -> P (in Ref. 4; AAM13008/AAN65079)"
FT /evidence="ECO:0000305"
FT STRAND 45..48
FT /evidence="ECO:0007829|PDB:2F4E"
FT STRAND 51..57
FT /evidence="ECO:0007829|PDB:2F4E"
FT STRAND 69..78
FT /evidence="ECO:0007829|PDB:2F4E"
FT TURN 79..81
FT /evidence="ECO:0007829|PDB:2F4E"
FT STRAND 84..87
FT /evidence="ECO:0007829|PDB:2F4E"
FT TURN 88..92
FT /evidence="ECO:0007829|PDB:2F4E"
FT STRAND 95..98
FT /evidence="ECO:0007829|PDB:2F4E"
FT HELIX 104..106
FT /evidence="ECO:0007829|PDB:2F4E"
FT HELIX 107..113
FT /evidence="ECO:0007829|PDB:2F4E"
FT STRAND 121..126
FT /evidence="ECO:0007829|PDB:2F4E"
FT HELIX 128..130
FT /evidence="ECO:0007829|PDB:2F4E"
FT TURN 131..135
FT /evidence="ECO:0007829|PDB:2F4E"
FT STRAND 137..141
FT /evidence="ECO:0007829|PDB:2F4E"
FT STRAND 149..159
FT /evidence="ECO:0007829|PDB:2F4E"
FT TURN 166..168
FT /evidence="ECO:0007829|PDB:2IF4"
FT HELIX 172..188
FT /evidence="ECO:0007829|PDB:2IF4"
FT STRAND 191..193
FT /evidence="ECO:0007829|PDB:2IF4"
FT HELIX 196..208
FT /evidence="ECO:0007829|PDB:2IF4"
FT HELIX 211..215
FT /evidence="ECO:0007829|PDB:2IF4"
FT HELIX 219..229
FT /evidence="ECO:0007829|PDB:2IF4"
FT HELIX 231..241
FT /evidence="ECO:0007829|PDB:2IF4"
FT TURN 242..244
FT /evidence="ECO:0007829|PDB:2IF4"
FT HELIX 247..259
FT /evidence="ECO:0007829|PDB:2IF4"
FT HELIX 264..275
FT /evidence="ECO:0007829|PDB:2IF4"
FT TURN 276..278
FT /evidence="ECO:0007829|PDB:2IF4"
FT HELIX 280..289
FT /evidence="ECO:0007829|PDB:2IF4"
SQ SEQUENCE 365 AA; 41806 MW; C939B75EEC79EA87 CRC64;
MDESLEHQTQ THDQESEIVT EGSAVVHSEP SQEGNVPPKV DSEAEVLDEK VSKQIIKEGH
GSKPSKYSTC FLHYRAWTKN SQHKFEDTWH EQQPIELVLG KEKKELAGLA IGVASMKSGE
RALVHVGWEL AYGKEGNFSF PNVPPMADLL YEVEVIGFDE TKEGKARSDM TVEERIGAAD
RRKMDGNSLF KEEKLEEAMQ QYEMAIAYMG DDFMFQLYGK YQDMALAVKN PCHLNIAACL
IKLKRYDEAI GHCNIVLTEE EKNPKALFRR GKAKAELGQM DSARDDFRKA QKYAPDDKAI
RRELRALAEQ EKALYQKQKE MYKGIFKGKD EGGAKSKSLF WLIVLWQWFV SLFSRIFRRH
RVKAD
