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Peptidyl-prolyl cis-trans isomerase FKBP4 (PPIase FKBP4) (EC 5.2.1.8) (52 kDa FK506-binding protein) (52 kDa FKBP) (FKBP-52) (59 kDa immunophilin) (p59) (FK506-binding protein 4) (FKBP-4) (FKBP59) (HSP-binding immunophilin) (HBI) (Immunophilin FKBP52) (Rotamase) [Cleaved into: Peptidyl-prolyl cis-trans isomerase FKBP4, N-terminally processed]

 FKBP4_MOUSE             Reviewed;         458 AA.
P30416; Q3TVC9;
01-APR-1993, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 5.
23-MAY-2018, entry version 181.
RecName: Full=Peptidyl-prolyl cis-trans isomerase FKBP4;
Short=PPIase FKBP4;
EC=5.2.1.8;
AltName: Full=52 kDa FK506-binding protein;
Short=52 kDa FKBP;
Short=FKBP-52;
AltName: Full=59 kDa immunophilin;
Short=p59;
AltName: Full=FK506-binding protein 4;
Short=FKBP-4;
AltName: Full=FKBP59;
AltName: Full=HSP-binding immunophilin;
Short=HBI;
AltName: Full=Immunophilin FKBP52;
AltName: Full=Rotamase;
Contains:
RecName: Full=Peptidyl-prolyl cis-trans isomerase FKBP4, N-terminally processed;
Name=Fkbp4; Synonyms=Fkpb52;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=7693550; DOI=10.1016/0378-1119(93)90206-I;
Schmitt J., Stunnenberg H.G.;
"Cloning and expression of a mouse cDNA encoding p59, an immunophilin
that associates with the glucocorticoid receptor.";
Gene 132:267-271(1993).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Embryo, and Spinal ganglion;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lung tumor;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 6-458, PARTIAL PROTEIN SEQUENCE,
FUNCTION, AND SUBCELLULAR LOCATION.
STRAIN=C57BL/6J; TISSUE=Testis;
PubMed=8341706; DOI=10.1073/pnas.90.14.6839;
Alnemri E.S., Fernandes-Alnemri T., Nelki D.S., Dudley K.,
Dubois G.C., Litwack G.;
"Overexpression, characterization, and purification of a recombinant
mouse immunophilin FKBP-52 and identification of an associated
phosphoprotein.";
Proc. Natl. Acad. Sci. U.S.A. 90:6839-6843(1993).
[5]
IDENTIFICATION IN A COMPLEX WITH NR3C1 AND HSP90AA1.
PubMed=9195923; DOI=10.1074/jbc.272.26.16224;
Silverstein A.M., Galigniana M.D., Chen M.S., Owens-Grillo J.K.,
Chinkers M., Pratt W.B.;
"Protein phosphatase 5 is a major component of glucocorticoid
receptor.hsp90 complexes with properties of an FK506-binding
immunophilin.";
J. Biol. Chem. 272:16224-16230(1997).
[6]
FUNCTION IN INTRACELLULAR TRAFFICKING, IDENTIFICATION IN A COMPLEX
WITH HSP90AA1 AND NR3C1, AND INTERACTION WITH DYNEIN.
PubMed=11278753; DOI=10.1074/jbc.M010809200;
Galigniana M.D., Radanyi C., Renoir J.-M., Housley P.R., Pratt W.B.;
"Evidence that the peptidylprolyl isomerase domain of the hsp90-
binding immunophilin FKBP52 is involved in both dynein interaction and
glucocorticoid receptor movement to the nucleus.";
J. Biol. Chem. 276:14884-14889(2001).
[7]
FUNCTION IN INTRACELLULAR TRAFFICKING, IDENTIFICATION IN A COMPLEX
WITH HSP90AA1 AND NR3C1, SUBCELLULAR LOCATION, AND INTERACTION WITH
DYNEIN.
PubMed=11751894; DOI=10.1074/jbc.C100531200;
Davies T.H., Ning Y.M., Sanchez E.R.;
"A new first step in activation of steroid receptors: hormone-induced
switching of FKBP51 and FKBP52 immunophilins.";
J. Biol. Chem. 277:4597-4600(2002).
[8]
PROTEIN SEQUENCE OF 235-244.
TISSUE=Brain;
Lubec G., Yang J.W., Zigmond M.;
Submitted (JUL-2007) to UniProtKB.
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[10]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-373, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain;
PubMed=24129315; DOI=10.1074/mcp.O113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V.,
Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
Vemulapalli V., Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
-!- FUNCTION: Immunophilin protein with PPIase and co-chaperone
activities. Component of steroid receptors heterocomplexes through
interaction with heat-shock protein 90 (HSP90). May play a role in
the intracellular trafficking of heterooligomeric forms of steroid
hormone receptors between cytoplasm and nuclear compartments. The
isomerase activity controls neuronal growth cones via regulation
of TRPC1 channel opening. Acts also as a regulator of microtubule
dynamics by inhibiting MAPT/TAU ability to promote microtubule
assembly. May have a protective role against oxidative stress in
mitochondria. {ECO:0000269|PubMed:11278753,
ECO:0000269|PubMed:11751894, ECO:0000269|PubMed:8341706}.
-!- CATALYTIC ACTIVITY: Peptidylproline (omega=180) = peptidylproline
(omega=0).
-!- ENZYME REGULATION: Inhibited by FK506. {ECO:0000250}.
-!- SUBUNIT: Homodimer (By similarity). Associates with HSP90AA1 and
HSPA1A/HSPA1B in steroid hormone receptor complexes. Also
interacts with peroxisomal phytanoyl-CoA alpha-hydroxylase (PHYH).
Interacts with NR3C1 and dynein. Interacts with HSF1 in the HSP90
complex. Associates with tubulin. Interacts with MAPT/TAU.
Interacts (via TPR domain) with S100A1, S100A2 and S100A6; the
interaction is Ca(2+) dependent. Interaction with S100A1 and
S100A2 (but not with S100A6) leads to inhibition of FKBP4-HSP90
interaction. Interacts with dynein; contributes to NR3C1 transport
to the nucleus. {ECO:0000250, ECO:0000269|PubMed:11278753,
ECO:0000269|PubMed:11751894, ECO:0000269|PubMed:9195923}.
-!- INTERACTION:
P06537:Nr3c1; NbExp=3; IntAct=EBI-492746, EBI-492753;
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
{ECO:0000269|PubMed:11751894}. Mitochondrion
{ECO:0000250|UniProtKB:Q02790}. Nucleus
{ECO:0000269|PubMed:11751894, ECO:0000269|PubMed:8341706}.
Cytoplasm, cytoskeleton {ECO:0000250}. Note=Shuttles from
mitochondria to nucleus; co-localizes in mitochondria with the
glucocorticoid receptor. Colocalized with MAPT/TAU in the distal
part of the primary cortical neurons.
{ECO:0000250|UniProtKB:Q02790, ECO:0000250|UniProtKB:Q9QVC8}.
-!- DOMAIN: The PPIase activity is mainly due to the fisrt PPIase
FKBP-type domain (1-138 AA). {ECO:0000250}.
-!- DOMAIN: The C-terminal region (AA 375-458) is required to prevent
tubulin polymerization. {ECO:0000250}.
-!- DOMAIN: The chaperone activity resides in the C-terminal region,
mainly between amino acids 264 and 400. {ECO:0000250}.
-!- DOMAIN: The TPR repeats mediate mitochondrial localization.
{ECO:0000250}.
-!- PTM: Phosphorylation by CK2 results in loss of HSP90 binding
activity.
-!- SEQUENCE CAUTION:
Sequence=CAA34914.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=CAA34914.1; Type=Frameshift; Positions=16, 156, 204, 265; Evidence={ECO:0000305};
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EMBL; X70887; CAA50231.1; -; mRNA.
EMBL; AK083912; BAC39057.1; -; mRNA.
EMBL; AK160202; BAE35690.1; -; mRNA.
EMBL; BC003447; AAH03447.1; -; mRNA.
EMBL; X17069; CAC39452.1; -; mRNA.
EMBL; X17068; CAA34914.1; ALT_SEQ; mRNA.
CCDS; CCDS20573.1; -.
PIR; JN0873; JN0873.
RefSeq; NP_034349.1; NM_010219.3.
UniGene; Mm.12758; -.
ProteinModelPortal; P30416; -.
SMR; P30416; -.
BioGrid; 199685; 3.
IntAct; P30416; 4.
MINT; P30416; -.
STRING; 10090.ENSMUSP00000032508; -.
iPTMnet; P30416; -.
PhosphoSitePlus; P30416; -.
SwissPalm; P30416; -.
REPRODUCTION-2DPAGE; P30416; -.
EPD; P30416; -.
MaxQB; P30416; -.
PaxDb; P30416; -.
PeptideAtlas; P30416; -.
PRIDE; P30416; -.
Ensembl; ENSMUST00000032508; ENSMUSP00000032508; ENSMUSG00000030357.
GeneID; 14228; -.
KEGG; mmu:14228; -.
UCSC; uc009edr.1; mouse.
CTD; 2288; -.
MGI; MGI:95543; Fkbp4.
eggNOG; KOG0543; Eukaryota.
eggNOG; COG0545; LUCA.
GeneTree; ENSGT00760000119159; -.
HOGENOM; HOG000256916; -.
HOVERGEN; HBG051624; -.
InParanoid; P30416; -.
KO; K09571; -.
OMA; ELEMLGW; -.
OrthoDB; EOG091G07OA; -.
PhylomeDB; P30416; -.
TreeFam; TF354214; -.
Reactome; R-MMU-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR).
Reactome; R-MMU-8939211; ESR-mediated signaling.
ChiTaRS; Fkbp4; mouse.
PRO; PR:P30416; -.
Proteomes; UP000000589; Chromosome 6.
Bgee; ENSMUSG00000030357; -.
CleanEx; MM_FKBP4; -.
ExpressionAtlas; P30416; baseline and differential.
Genevisible; P30416; MM.
GO; GO:0044295; C:axonal growth cone; ISS:UniProtKB.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0005829; C:cytosol; ISS:UniProtKB.
GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
GO; GO:0032991; C:protein-containing complex; IEA:Ensembl.
GO; GO:0005524; F:ATP binding; IDA:MGI.
GO; GO:0005528; F:FK506 binding; IBA:GO_Central.
GO; GO:0035259; F:glucocorticoid receptor binding; IDA:MGI.
GO; GO:0005525; F:GTP binding; IDA:MGI.
GO; GO:0031072; F:heat shock protein binding; IDA:MGI.
GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; ISS:UniProtKB.
GO; GO:0051219; F:phosphoprotein binding; IDA:MGI.
GO; GO:0048156; F:tau protein binding; IEA:Ensembl.
GO; GO:0030521; P:androgen receptor signaling pathway; IMP:MGI.
GO; GO:0061077; P:chaperone-mediated protein folding; ISS:UniProtKB.
GO; GO:0006825; P:copper ion transport; IEA:Ensembl.
GO; GO:0007566; P:embryo implantation; IMP:MGI.
GO; GO:0046661; P:male sex differentiation; IMP:MGI.
GO; GO:0031115; P:negative regulation of microtubule polymerization; IEA:Ensembl.
GO; GO:0031111; P:negative regulation of microtubule polymerization or depolymerization; ISS:UniProtKB.
GO; GO:0010977; P:negative regulation of neuron projection development; ISS:UniProtKB.
GO; GO:0030850; P:prostate gland development; IMP:MGI.
GO; GO:0031503; P:protein-containing complex localization; IDA:MGI.
GO; GO:0048608; P:reproductive structure development; IMP:MGI.
GO; GO:0006463; P:steroid hormone receptor complex assembly; IDA:MGI.
Gene3D; 1.25.40.10; -; 1.
InterPro; IPR031212; FKBP4.
InterPro; IPR023566; PPIase_FKBP.
InterPro; IPR001179; PPIase_FKBP_dom.
InterPro; IPR013026; TPR-contain_dom.
InterPro; IPR011990; TPR-like_helical_dom_sf.
InterPro; IPR001440; TPR_1.
InterPro; IPR013105; TPR_2.
InterPro; IPR019734; TPR_repeat.
PANTHER; PTHR10516; PTHR10516; 1.
PANTHER; PTHR10516:SF25; PTHR10516:SF25; 1.
Pfam; PF00254; FKBP_C; 2.
Pfam; PF00515; TPR_1; 1.
Pfam; PF07719; TPR_2; 1.
SMART; SM00028; TPR; 3.
SUPFAM; SSF48452; SSF48452; 1.
PROSITE; PS50059; FKBP_PPIASE; 2.
PROSITE; PS50005; TPR; 3.
PROSITE; PS50293; TPR_REGION; 2.
1: Evidence at protein level;
Acetylation; Chaperone; Complete proteome; Cytoplasm; Cytoskeleton;
Direct protein sequencing; Isomerase; Isopeptide bond; Methylation;
Microtubule; Mitochondrion; Nucleus; Phosphoprotein;
Reference proteome; Repeat; Rotamase; TPR repeat; Ubl conjugation.
CHAIN 1 458 Peptidyl-prolyl cis-trans isomerase
FKBP4.
/FTId=PRO_0000391469.
INIT_MET 1 1 Removed; alternate.
{ECO:0000250|UniProtKB:Q02790}.
CHAIN 2 458 Peptidyl-prolyl cis-trans isomerase
FKBP4, N-terminally processed.
/FTId=PRO_0000075319.
DOMAIN 50 138 PPIase FKBP-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00277}.
DOMAIN 167 253 PPIase FKBP-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00277}.
REPEAT 270 303 TPR 1.
REPEAT 319 352 TPR 2.
REPEAT 353 386 TPR 3.
REGION 267 400 Interaction with tubulin. {ECO:0000250}.
MOD_RES 1 1 N-acetylmethionine; in peptidyl-prolyl
cis-trans isomerase FKBP4; alternate.
{ECO:0000250|UniProtKB:Q02790}.
MOD_RES 2 2 N-acetylthreonine; in peptidyl-prolyl
cis-trans isomerase FKBP4, N-terminally
processed; partial.
{ECO:0000250|UniProtKB:Q02790}.
MOD_RES 143 143 Phosphothreonine; by CK2.
{ECO:0000250|UniProtKB:P27124}.
MOD_RES 220 220 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q02790}.
MOD_RES 282 282 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q02790}.
MOD_RES 373 373 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 436 436 Phosphothreonine.
{ECO:0000250|UniProtKB:Q02790}.
MOD_RES 452 452 Phosphoserine.
{ECO:0000250|UniProtKB:Q02790}.
CROSSLNK 441 441 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1).
{ECO:0000250|UniProtKB:Q02790}.
CONFLICT 6 7 MK -> HE (in Ref. 4; CAC39452).
{ECO:0000305}.
CONFLICT 156 163 TRGEGYAR -> LGVKAMQG (in Ref. 4;
CAC39452). {ECO:0000305}.
CONFLICT 203 240 GLEEAIQRMEKGEHSIVYLKPSYAFGSVGKERFQIPPH ->
AWRRPFSAWRKESIPSCTSNLAMLLAVWGRRGSRSHRT
(in Ref. 4; CAC39452/CAA34914).
{ECO:0000305}.
CONFLICT 265 272 EKLEQSNI -> RSWSRATY (in Ref. 4;
CAC39452). {ECO:0000305}.
CONFLICT 315 315 H -> R (in Ref. 3; AAH03447).
{ECO:0000305}.
CONFLICT 360 360 G -> R (in Ref. 2; BAE35690).
{ECO:0000305}.
SEQUENCE 458 AA; 51572 MW; CFB2ED49E9B6BA7A CRC64;
MTAEEMKAAE NGAQSAPLPL EGVDISPKQD EGVLKVIKRE GTGTETPMIG DRVFVHYTGW
LLDGTKFDSS LDRKDKFSFD LGKGEVIKAW DIAVATMKVG EVCHITCKPE YAYGAAGSPP
KIPPNATLVF EVELFEFKGE DLTEEEDGGI IRRIRTRGEG YARPNDGAMV EVALEGYHKD
RLFDQRELCF EVGEGESLDL PCGLEEAIQR MEKGEHSIVY LKPSYAFGSV GKERFQIPPH
AELRYEVRLK SFEKAKESWE MSSAEKLEQS NIVKERGTAY FKEGKYKQAL LQYKKIVSWL
EYESSFSGEE MQKVHALRLA SHLNLAMCHL KLQAFSAAIE SCNKALELDS NNEKGLFRRG
EAHLAVNDFD LARADFQKVL QLYPSNKAAK TQLAVCQQRT RRQLAREKKL YANMFERLAE
EEHKVKAEVA AGDHPTDAEM KGERNNVAEN QSRVETEA


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