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Peptidyl-prolyl cis-trans isomerase FKBP42 (PPIase FKBP42) (EC 5.2.1.8) (42 kDa peptidyl-prolyl isomerase) (FK506-binding protein 42) (AtFKBP42) (Immunophilin FKBP42) (Protein TWISTED DWARF 1) (Protein ULTRACURVATA 2) (Rotamase)

 FKB42_ARATH             Reviewed;         365 AA.
Q9LDC0; Q8RWM0;
07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
01-OCT-2000, sequence version 1.
07-NOV-2018, entry version 135.
RecName: Full=Peptidyl-prolyl cis-trans isomerase FKBP42;
Short=PPIase FKBP42;
EC=5.2.1.8;
AltName: Full=42 kDa peptidyl-prolyl isomerase;
AltName: Full=FK506-binding protein 42;
Short=AtFKBP42;
AltName: Full=Immunophilin FKBP42;
AltName: Full=Protein TWISTED DWARF 1;
AltName: Full=Protein ULTRACURVATA 2;
AltName: Full=Rotamase;
Name=FKBP42; Synonyms=TWD1, UCU2; OrderedLocusNames=At3g21640;
ORFNames=MIL23.21;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=cv. Columbia;
Kolukisaoglu U., Berger J., Eckhoff A., Moeller A., Saal B.,
Bellini C., Schulz B.;
"Structure and evolution of FKBP-like genes in Arabidopsis.";
Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=10819329; DOI=10.1093/dnares/7.2.131;
Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
"Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
features of the regions of 4,504,864 bp covered by sixty P1 and TAC
clones.";
DNA Res. 7:131-135(2000).
[3]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome.";
Plant J. 89:789-804(2017).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[5]
SUBCELLULAR LOCATION, INTERACTION WITH CALMODULIN AND SHD/HSP90, AND
DISRUPTION PHENOTYPE.
PubMed=12410806; DOI=10.1046/j.1365-313X.2002.01420.x;
Kamphausen T., Fanghaenel J., Neumann D., Schulz B., Rahfeld J.-U.;
"Characterization of Arabidopsis thaliana AtFKBP42 that is membrane-
bound and interacts with Hsp90.";
Plant J. 32:263-276(2002).
[6]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH MDR1/PGP1 AND
MDR11/PGP19.
PubMed=14517332; DOI=10.1091/mbc.E02-10-0698;
Geisler M., Kolukisaoglu H.U., Bouchard R., Billion K., Berger J.,
Saal B., Frangne N., Koncz-Kalman Z., Koncz C., Dudler R.,
Blakeslee J.J., Murphy A.S., Martinoia E., Schulz B.;
"TWISTED DWARF1, a unique plasma membrane-anchored immunophilin-like
protein, interacts with Arabidopsis multidrug resistance-like
transporters AtPGP1 and AtPGP19.";
Mol. Biol. Cell 14:4238-4249(2003).
[7]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH MRP1 AND MRP2.
PubMed=15133126; DOI=10.1091/mbc.E03-11-0831;
Geisler M., Girin M., Brandt S., Vincenzetti V., Plaza S., Paris N.,
Kobae Y., Maeshima M., Billion K., Kolukisaoglu U.H., Schulz B.,
Martinoia E.;
"Arabidopsis immunophilin-like TWD1 functionally interacts with
vacuolar ABC transporters.";
Mol. Biol. Cell 15:3393-3405(2004).
[8]
FUNCTION.
PubMed=14730066; DOI=10.1104/pp.103.032524;
Perez-Perez J.M., Ponce M.R., Micol J.L.;
"The ULTRACURVATA2 gene of Arabidopsis encodes an FK506-binding
protein involved in auxin and brassinosteroid signaling.";
Plant Physiol. 134:101-117(2004).
[9]
GENE FAMILY, AND NOMENCLATURE.
PubMed=15047905; DOI=10.1104/pp.103.031005;
He Z., Li L., Luan S.;
"Immunophilins and parvulins. Superfamily of peptidyl prolyl
isomerases in Arabidopsis.";
Plant Physiol. 134:1248-1267(2004).
[10]
FUNCTION.
PubMed=16887800; DOI=10.1074/jbc.M604604200;
Bouchard R., Bailly A., Blakeslee J.J., Oehring S.C., Vincenzetti V.,
Lee O.R., Paponov I., Palme K., Mancuso S., Murphy A.S., Schulz B.,
Geisler M.;
"Immunophilin-like TWISTED DWARF1 modulates auxin efflux activities of
Arabidopsis P-glycoproteins.";
J. Biol. Chem. 281:30603-30612(2006).
[11]
FUNCTION, AND INTERACTION WITH NPA.
PubMed=18499676; DOI=10.1074/jbc.M709655200;
Bailly A., Sovero V., Vincenzetti V., Santelia D., Bartnik D.,
Koenig B.W., Mancuso S., Martinoia E., Geisler M.;
"Modulation of P-glycoproteins by auxin transport inhibitors is
mediated by interaction with immunophilins.";
J. Biol. Chem. 283:21817-21826(2008).
[12]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=20971896; DOI=10.1105/tpc.110.078360;
Wu G., Otegui M.S., Spalding E.P.;
"The ER-localized TWD1 immunophilin is necessary for localization of
multidrug resistance-like proteins required for polar auxin transport
in Arabidopsis roots.";
Plant Cell 22:3295-3304(2010).
[13]
X-RAY CRYSTALLOGRAPHY (2.32 ANGSTROMS) OF 1-180.
PubMed=16364310; DOI=10.1016/j.febslet.2005.12.007;
Weiergraeber O.H., Eckhoff A., Granzin J.;
"Crystal structure of a plant immunophilin domain involved in
regulation of MDR-type ABC transporters.";
FEBS Lett. 580:251-255(2006).
[14]
X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS) OF 1-338.
PubMed=17045295; DOI=10.1016/j.jmb.2006.09.052;
Granzin J., Eckhoff A., Weiergraber O.H.;
"Crystal structure of a multi-domain immunophilin from Arabidopsis
thaliana: a paradigm for regulation of plant ABC transporters.";
J. Mol. Biol. 364:799-809(2006).
[15]
STRUCTURE BY NMR OF 335-365, AND MEMBRANE ANCHOR.
PubMed=17033777; DOI=10.1007/s00249-006-0094-2;
Scheidt H.A., Vogel A., Eckhoff A., Koenig B.W., Huster D.;
"Solid-state NMR characterization of the putative membrane anchor of
TWD1 from Arabidopsis thaliana.";
Eur. Biophys. J. 36:393-404(2007).
-!- FUNCTION: PPIases accelerate the folding of proteins. It catalyzes
the cis-trans isomerization of proline imidic peptide bonds in
oligopeptides (By similarity). Modulates the uptake of MRP
substrates into the vacuole; reduces metolachlor-GS (MOC-GS) and
enhances 17-beta-estradiol 17-(beta-D-glucuronide) (E(2)17betaG)
uptake. Regulates cell elongation and orientation. Functions as a
positive regulator of PGP1-mediated auxin transport. Confers drug
modulation of PGP1 efflux activity as interaction with NPA or
flavonol quercetin prevents its physical and functional
interaction with PGP1. Required for the proper localization of
auxin-related ABCB transporters. Plays a role in brassinosteroid
(BR) signaling pathway. {ECO:0000250, ECO:0000269|PubMed:14517332,
ECO:0000269|PubMed:14730066, ECO:0000269|PubMed:15133126,
ECO:0000269|PubMed:16887800, ECO:0000269|PubMed:18499676,
ECO:0000269|PubMed:20971896}.
-!- CATALYTIC ACTIVITY: Peptidylproline (omega=180) = peptidylproline
(omega=0).
-!- SUBUNIT: Interacts with calmodulin (CaM), MRP1, MRP2, MDR1/PGP1,
MDR11/PGP19 and SHD/HSP90. Interacts with 1-naphthylphthalamic
acid (NPA). {ECO:0000269|PubMed:12410806,
ECO:0000269|PubMed:14517332, ECO:0000269|PubMed:15133126,
ECO:0000269|PubMed:18499676}.
-!- INTERACTION:
Q9ZR72:ABCB1; NbExp=2; IntAct=EBI-360006, EBI-366396;
Q9C8G9:ABCC1; NbExp=4; IntAct=EBI-360006, EBI-637633;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12410806,
ECO:0000269|PubMed:14517332, ECO:0000269|PubMed:15133126}; Single-
pass type IV membrane protein. Vacuole membrane
{ECO:0000269|PubMed:12410806, ECO:0000269|PubMed:15133126};
Single-pass type IV membrane protein. Endoplasmic reticulum
{ECO:0000269|PubMed:20971896}.
-!- DISRUPTION PHENOTYPE: Plants display helical rotation of several
organs. {ECO:0000269|PubMed:12410806}.
-!- SIMILARITY: Belongs to the FKBP-type PPIase family. {ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; AJ224640; CAC00654.1; -; mRNA.
EMBL; AB019232; BAB02359.1; -; Genomic_DNA.
EMBL; CP002686; AEE76533.1; -; Genomic_DNA.
EMBL; AY093009; AAM13008.1; -; mRNA.
EMBL; BT001192; AAN65079.1; -; mRNA.
RefSeq; NP_188801.2; NM_113059.3.
UniGene; At.5664; -.
PDB; 2F4E; X-ray; 2.32 A; A/B=1-180.
PDB; 2IF4; X-ray; 2.85 A; A=1-338.
PDBsum; 2F4E; -.
PDBsum; 2IF4; -.
ProteinModelPortal; Q9LDC0; -.
SMR; Q9LDC0; -.
BioGrid; 7050; 31.
IntAct; Q9LDC0; 26.
STRING; 3702.AT3G21640.1; -.
TCDB; 8.A.11.1.1; the immunophilin-like prolyl:peptidyl isomerase regulator (i-ppi) family.
PaxDb; Q9LDC0; -.
PRIDE; Q9LDC0; -.
EnsemblPlants; AT3G21640.1; AT3G21640.1; AT3G21640.
GeneID; 821718; -.
Gramene; AT3G21640.1; AT3G21640.1; AT3G21640.
KEGG; ath:AT3G21640; -.
Araport; AT3G21640; -.
TAIR; locus:2089890; AT3G21640.
eggNOG; KOG0543; Eukaryota.
eggNOG; COG0545; LUCA.
HOGENOM; HOG000006189; -.
InParanoid; Q9LDC0; -.
OMA; AIYRYKY; -.
OrthoDB; EOG09360ESR; -.
PhylomeDB; Q9LDC0; -.
EvolutionaryTrace; Q9LDC0; -.
PRO; PR:Q9LDC0; -.
Proteomes; UP000006548; Chromosome 3.
ExpressionAtlas; Q9LDC0; baseline and differential.
Genevisible; Q9LDC0; AT.
GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IDA:TAIR.
GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
GO; GO:0005516; F:calmodulin binding; IDA:TAIR.
GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; ISS:TAIR.
GO; GO:0009734; P:auxin-activated signaling pathway; IEA:UniProtKB-KW.
GO; GO:0048366; P:leaf development; IMP:TAIR.
Gene3D; 1.25.40.10; -; 1.
InterPro; IPR001179; PPIase_FKBP_dom.
InterPro; IPR013026; TPR-contain_dom.
InterPro; IPR011990; TPR-like_helical_dom_sf.
InterPro; IPR019734; TPR_repeat.
Pfam; PF00254; FKBP_C; 1.
Pfam; PF13181; TPR_8; 1.
SMART; SM00028; TPR; 3.
SUPFAM; SSF48452; SSF48452; 1.
PROSITE; PS50059; FKBP_PPIASE; 1.
PROSITE; PS50005; TPR; 2.
PROSITE; PS50293; TPR_REGION; 2.
1: Evidence at protein level;
3D-structure; Auxin signaling pathway; Calmodulin-binding;
Cell membrane; Complete proteome; Endoplasmic reticulum; Isomerase;
Membrane; Reference proteome; Repeat; Rotamase; TPR repeat;
Transmembrane; Transmembrane helix; Vacuole.
CHAIN 1 365 Peptidyl-prolyl cis-trans isomerase
FKBP42.
/FTId=PRO_0000226087.
TRANSMEM 339 357 Helical; Anchor for type IV membrane
protein.
DOMAIN 67 159 PPIase FKBP-type. {ECO:0000255|PROSITE-
ProRule:PRU00277}.
REPEAT 179 212 TPR 1.
REPEAT 230 263 TPR 2.
REPEAT 264 297 TPR 3.
REGION 1 163 Interaction with MDR1/PGP1.
REGION 163 337 Interaction with MRP1.
{ECO:0000269|PubMed:15133126}.
REGION 310 326 Calmodulin-binding. {ECO:0000255}.
CONFLICT 107 107 A -> P (in Ref. 4; AAM13008/AAN65079).
{ECO:0000305}.
STRAND 45 48 {ECO:0000244|PDB:2F4E}.
STRAND 51 57 {ECO:0000244|PDB:2F4E}.
STRAND 69 78 {ECO:0000244|PDB:2F4E}.
TURN 79 81 {ECO:0000244|PDB:2F4E}.
STRAND 84 87 {ECO:0000244|PDB:2F4E}.
TURN 88 92 {ECO:0000244|PDB:2F4E}.
STRAND 95 98 {ECO:0000244|PDB:2F4E}.
HELIX 104 106 {ECO:0000244|PDB:2F4E}.
HELIX 107 113 {ECO:0000244|PDB:2F4E}.
STRAND 121 126 {ECO:0000244|PDB:2F4E}.
HELIX 128 130 {ECO:0000244|PDB:2F4E}.
TURN 131 135 {ECO:0000244|PDB:2F4E}.
STRAND 137 141 {ECO:0000244|PDB:2F4E}.
STRAND 149 159 {ECO:0000244|PDB:2F4E}.
TURN 166 168 {ECO:0000244|PDB:2IF4}.
HELIX 172 188 {ECO:0000244|PDB:2IF4}.
STRAND 191 193 {ECO:0000244|PDB:2IF4}.
HELIX 196 208 {ECO:0000244|PDB:2IF4}.
HELIX 211 215 {ECO:0000244|PDB:2IF4}.
HELIX 219 229 {ECO:0000244|PDB:2IF4}.
HELIX 231 241 {ECO:0000244|PDB:2IF4}.
TURN 242 244 {ECO:0000244|PDB:2IF4}.
HELIX 247 259 {ECO:0000244|PDB:2IF4}.
HELIX 264 275 {ECO:0000244|PDB:2IF4}.
TURN 276 278 {ECO:0000244|PDB:2IF4}.
HELIX 280 289 {ECO:0000244|PDB:2IF4}.
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


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