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Peptidyl-prolyl cis-trans isomerase FKBP8 (PPIase FKBP8) (EC 5.2.1.8) (38 kDa FK506-binding protein) (38 kDa FKBP) (FKBP-38) (mFKBP38) (FK506-binding protein 8) (FKBP-8) (FKBPR38) (Rotamase)

 FKBP8_MOUSE             Reviewed;         402 AA.
O35465; Q3UK86; Q6GTX9; Q811M7; Q811R4; Q8C2F0; Q99L93;
27-APR-2001, integrated into UniProtKB/Swiss-Prot.
01-JUL-2008, sequence version 2.
23-MAY-2018, entry version 164.
RecName: Full=Peptidyl-prolyl cis-trans isomerase FKBP8;
Short=PPIase FKBP8;
EC=5.2.1.8;
AltName: Full=38 kDa FK506-binding protein;
Short=38 kDa FKBP;
Short=FKBP-38;
Short=mFKBP38;
AltName: Full=FK506-binding protein 8;
Short=FKBP-8;
AltName: Full=FKBPR38;
AltName: Full=Rotamase;
Name=Fkbp8; Synonyms=Fkbp38, Sam11;
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] (ISOFORM 1), AND INTERACTION WITH BCL2 AND
BCL2L1/BCLXL.
PubMed=12510191; DOI=10.1038/ncb894;
Shirane M., Nakayama K.I.;
"Inherent calcineurin inhibitor FKBP38 targets Bcl-2 to mitochondria
and inhibits apoptosis.";
Nat. Cell Biol. 5:28-37(2003).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, AND
TISSUE SPECIFICITY.
PubMed=15105374; DOI=10.1242/dev.01122;
Bulgakov O.V., Eggenschwiler J.T., Hong D.-H., Anderson K.V., Li T.;
"FKBP8 is a negative regulator of mouse sonic hedgehog signaling in
neural tissues.";
Development 131:2149-2159(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
STRAIN=BALB/cJ, C57BL/6J, and NOD;
TISSUE=Bone marrow macrophage, Placenta, Spleen, and Thymus;
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).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
STRAIN=FVB/N; TISSUE=Mammary 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).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 39-402 (ISOFORM 1), SUBUNIT, AND TISSUE
SPECIFICITY.
STRAIN=C57BL/6 X DBA/2;
PubMed=10197430;
DOI=10.1002/(SICI)1522-2683(19990201)20:2<249::AID-ELPS249>3.0.CO;2-F;
Pedersen K.M., Finsen B., Celis J.E., Jensen N.A.;
"muFKBP38: a novel murine immunophilin homolog differentially
expressed in Schwannoma cells and central nervous system neurons in
vivo.";
Electrophoresis 20:249-255(1999).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 48-402, SEQUENCE REVISION TO 100
AND 400, ALTERNATIVE SPLICING, AND TISSUE SPECIFICITY.
STRAIN=129/SvJ;
PubMed=14667822; DOI=10.1016/j.ygeno.2003.07.001;
Nielsen J.V., Mitchelmore C., Pedersen K.M., Kjaerulff K.M.,
Finsen B., Jensen N.A.;
"Fkbp8: novel isoforms, genomic organization, and characterization of
a forebrain promoter in transgenic mice.";
Genomics 83:181-192(2004).
[7]
DISRUPTION PHENOTYPE.
PubMed=18459960; DOI=10.1111/j.1365-2443.2008.01194.x;
Shirane M., Ogawa M., Motoyama J., Nakayama K.I.;
"Regulation of apoptosis and neurite extension by FKBP38 is required
for neural tube formation in the mouse.";
Genes Cells 13:635-651(2008).
[8]
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).
-!- FUNCTION: Constitutively inactive PPiase, which becomes active
when bound to calmodulin and calcium. Seems to act as a chaperone
for BCL2, targets it to the mitochondria and modulates its
phosphorylation state. The BCL2/FKBP8/calmodulin/calcium complex
probably interferes with the binding of BCL2 to its targets. The
active form of FKBP8 may therefore play a role in the regulation
of apoptosis (By similarity). Required for normal embryonic
development. {ECO:0000250}.
-!- CATALYTIC ACTIVITY: Peptidylproline (omega=180) = peptidylproline
(omega=0).
-!- COFACTOR:
Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
-!- SUBUNIT: Homomultimers or heteromultimers (Potential). Forms
heterodimer with calmodulin. When activated by calmodulin and
calcium, interacts with the BH4 domain of BCL2 and weakly with
BCLX isoform Bcl-X(L). Does not bind and inhibit calcineurin (By
similarity). Interacts with ZFYVE27; may negatively regulate
ZFYVE27 phosphorylation (By similarity). {ECO:0000250,
ECO:0000305}.
-!- SUBCELLULAR LOCATION: Mitochondrion membrane
{ECO:0000269|PubMed:15105374}; Single-pass membrane protein
{ECO:0000269|PubMed:15105374}; Cytoplasmic side
{ECO:0000269|PubMed:15105374}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=O35465-1; Sequence=Displayed;
Name=2;
IsoId=O35465-2; Sequence=VSP_034487;
-!- TISSUE SPECIFICITY: Detected throughout the embryonic body, in
caudal neural tube, limbs and head. Detected in adult retina,
brain, heart, kidney, liver, pancreas, lung, testis and urinary
bladder (at protein level). Detected in adult brain, kidney,
liver, testis and trigeminal nerve, and in embryo. Detected at
lower levels in lung, spleen, heart and ovary. Widely expressed in
forebrain. Detected in the Purkinje cell layer in the cerebellum
and in hippocampus neurons. {ECO:0000269|PubMed:10197430,
ECO:0000269|PubMed:14667822, ECO:0000269|PubMed:15105374}.
-!- PTM: Ubiquitinated by PRKN during mitophagy, leading to its
degradation and enhancement of mitophagy. Deubiquitinated by
USP30. {ECO:0000250|UniProtKB:Q14318}.
-!- DISRUPTION PHENOTYPE: Mice die shortly after birth. They display
neural tube and skeletal defects. The neuroepithelium is
disorganized and the formation of dorsal root ganglia is
defective, likely as a result of an increased frequency of
apoptosis and aberrant migration of neuronal cells. The extension
of nerve fibers in the spinal cord is also abnormal.
{ECO:0000269|PubMed:18459960}.
-!- MISCELLANEOUS: Binds the immunosuppressant FK506 only in its
calmodulin/calcium activated form. {ECO:0000250}.
-!- SEQUENCE CAUTION:
Sequence=AAB86422.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=AAH03739.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=AAH27808.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=AAO27795.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=BAC40541.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=BAE26916.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=BAE31027.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=BAE38118.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=BAE39713.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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EMBL; AY225340; AAO39021.1; -; mRNA.
EMBL; AY278608; AAQ84562.1; -; mRNA.
EMBL; AK088739; BAC40541.1; ALT_INIT; mRNA.
EMBL; AK146122; BAE26916.1; ALT_INIT; mRNA.
EMBL; AK152198; BAE31027.1; ALT_INIT; mRNA.
EMBL; AK165281; BAE38118.1; ALT_INIT; mRNA.
EMBL; AK167663; BAE39713.1; ALT_INIT; mRNA.
EMBL; BC003739; AAH03739.1; ALT_INIT; mRNA.
EMBL; BC027808; AAH27808.1; ALT_INIT; mRNA.
EMBL; AF030635; AAB86422.1; ALT_INIT; mRNA.
EMBL; AY187231; AAO27795.1; ALT_SEQ; Genomic_DNA.
CCDS; CCDS52575.1; -. [O35465-2]
CCDS; CCDS52576.1; -. [O35465-1]
RefSeq; NP_001104536.1; NM_001111066.1. [O35465-2]
RefSeq; NP_001186560.1; NM_001199631.1. [O35465-2]
RefSeq; NP_034353.2; NM_010223.2. [O35465-1]
RefSeq; XP_006509619.1; XM_006509556.2. [O35465-2]
RefSeq; XP_017168056.1; XM_017312567.1. [O35465-1]
RefSeq; XP_017168057.1; XM_017312568.1. [O35465-1]
UniGene; Mm.141864; -.
ProteinModelPortal; O35465; -.
SMR; O35465; -.
BioGrid; 199689; 2.
IntAct; O35465; 1.
STRING; 10090.ENSMUSP00000074935; -.
iPTMnet; O35465; -.
PhosphoSitePlus; O35465; -.
SwissPalm; O35465; -.
MaxQB; O35465; -.
PaxDb; O35465; -.
PeptideAtlas; O35465; -.
PRIDE; O35465; -.
Ensembl; ENSMUST00000075491; ENSMUSP00000074935; ENSMUSG00000019428. [O35465-2]
Ensembl; ENSMUST00000119353; ENSMUSP00000112527; ENSMUSG00000019428. [O35465-1]
Ensembl; ENSMUST00000119698; ENSMUSP00000114069; ENSMUSG00000019428. [O35465-2]
GeneID; 14232; -.
KEGG; mmu:14232; -.
UCSC; uc009mao.2; mouse. [O35465-2]
UCSC; uc009map.2; mouse. [O35465-1]
CTD; 23770; -.
MGI; MGI:1341070; Fkbp8.
eggNOG; KOG0543; Eukaryota.
eggNOG; COG0545; LUCA.
GeneTree; ENSGT00910000144255; -.
HOVERGEN; HBG051626; -.
InParanoid; O35465; -.
KO; K09574; -.
OMA; AIYRYKY; -.
OrthoDB; EOG091G0AS2; -.
TreeFam; TF105295; -.
Reactome; R-MMU-5689880; Ub-specific processing proteases.
ChiTaRS; Fkbp8; mouse.
PRO; PR:O35465; -.
Proteomes; UP000000589; Chromosome 8.
Bgee; ENSMUSG00000019428; -.
CleanEx; MM_FKBP8; -.
ExpressionAtlas; O35465; baseline and differential.
Genevisible; O35465; MM.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IDA:MGI.
GO; GO:0005740; C:mitochondrial envelope; IDA:MGI.
GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
GO; GO:0005739; C:mitochondrion; HDA:MGI.
GO; GO:0032991; C:protein-containing complex; ISO:MGI.
GO; GO:0097718; F:disordered domain specific binding; ISO:MGI.
GO; GO:0005528; F:FK506 binding; IBA:GO_Central.
GO; GO:0042802; F:identical protein binding; ISO:MGI.
GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IBA:GO_Central.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0043010; P:camera-type eye development; IMP:MGI.
GO; GO:0001708; P:cell fate specification; IMP:MGI.
GO; GO:0061077; P:chaperone-mediated protein folding; IBA:GO_Central.
GO; GO:0021904; P:dorsal/ventral neural tube patterning; IDA:MGI.
GO; GO:0009953; P:dorsal/ventral pattern formation; IMP:MGI.
GO; GO:0035264; P:multicellular organism growth; IGI:MGI.
GO; GO:0043066; P:negative regulation of apoptotic process; IMP:MGI.
GO; GO:0001933; P:negative regulation of protein phosphorylation; ISO:MGI.
GO; GO:0021915; P:neural tube development; IMP:MGI.
GO; GO:0030513; P:positive regulation of BMP signaling pathway; IMP:MGI.
GO; GO:0030510; P:regulation of BMP signaling pathway; IGI:MGI.
GO; GO:0010468; P:regulation of gene expression; IGI:MGI.
GO; GO:0007224; P:smoothened signaling pathway; IMP:MGI.
Gene3D; 1.25.40.10; -; 1.
InterPro; IPR023566; PPIase_FKBP.
InterPro; IPR001179; PPIase_FKBP_dom.
InterPro; IPR013026; TPR-contain_dom.
InterPro; IPR011990; TPR-like_helical_dom_sf.
InterPro; IPR019734; TPR_repeat.
PANTHER; PTHR10516; PTHR10516; 1.
Pfam; PF00254; FKBP_C; 1.
SMART; SM00028; TPR; 3.
SUPFAM; SSF48452; SSF48452; 1.
PROSITE; PS50059; FKBP_PPIASE; 1.
PROSITE; PS50005; TPR; 2.
PROSITE; PS50293; TPR_REGION; 1.
1: Evidence at protein level;
Alternative splicing; Apoptosis; Calcium; Complete proteome;
Isomerase; Isopeptide bond; Membrane; Mitochondrion; Phosphoprotein;
Reference proteome; Repeat; Rotamase; TPR repeat; Transmembrane;
Transmembrane helix; Ubl conjugation.
CHAIN 1 402 Peptidyl-prolyl cis-trans isomerase
FKBP8.
/FTId=PRO_0000075332.
TRANSMEM 380 400 Helical. {ECO:0000255}.
DOMAIN 110 194 PPIase FKBP-type. {ECO:0000255|PROSITE-
ProRule:PRU00277}.
REPEAT 211 244 TPR 1.
REPEAT 262 295 TPR 2.
REPEAT 296 329 TPR 3.
COMPBIAS 252 256 Poly-Glu.
MOD_RES 286 286 Phosphoserine.
{ECO:0000250|UniProtKB:Q14318}.
CROSSLNK 239 239 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:Q14318}.
CROSSLNK 261 261 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:Q14318}.
CROSSLNK 263 263 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:Q14318}.
CROSSLNK 274 274 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:Q14318}.
CROSSLNK 297 297 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:Q14318}.
CROSSLNK 304 304 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:Q14318}.
CROSSLNK 324 324 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:Q14318}.
CROSSLNK 330 330 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:Q14318}.
CROSSLNK 338 338 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:Q14318}.
CROSSLNK 341 341 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:Q14318}.
CROSSLNK 342 342 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:Q14318}.
VAR_SEQ 173 173 G -> GS (in isoform 2).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:16141072}.
/FTId=VSP_034487.
CONFLICT 100 100 G -> C (in Ref. 1; AAO39021, 2; AAQ84562,
4; AAH03739 and 5; AAB86422).
{ECO:0000305}.
CONFLICT 163 163 A -> T (in Ref. 3; BAE26916).
{ECO:0000305}.
CONFLICT 170 170 G -> A (in Ref. 3; BAC40541).
{ECO:0000305}.
CONFLICT 400 400 A -> G (in Ref. 1; AAO39021, 2; AAQ84562,
4; AAH03739 and 5; AAB86422).
{ECO:0000305}.
SEQUENCE 402 AA; 43529 MW; 609A954FAD3A76F8 CRC64;
MASWAEPSEP AALRLPGAPL LEGFEVLDGV DDAEEEDDLS GLPPLEDMGQ PTVEEAEQPG
ALAREFLAAT EPEPAPAPAP EEWLDILGNG LLRMKTLVPG PKGSSRPLKG QVVTVHLQMS
LENGTRVQEE PELAFTLGDC DVIQALDLSV PLMDVGETAM VTADSKYCYG PQGRSPYIPP
HAALCLEVTL KTAEDGPDLE MLSGQERVAL ANRKRECGNA HYQRADFVLA ANSYDLAIKA
ITSNTKVDMT CEEEEELLQL KVKCLNNLAA SQLKLDHYRA ALRSCSQVLE HQPDNIKALF
RKGKVLAQQG EYSEAIPILR AALKLEPSNK TIHAELSKLV KKRAAQRSTE TALYRKMLGN
PSRLPAKCPG KGAWSIPWKW LFGATAVALG GVALSVVIAA RN


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U0979m CLIA Cyclophilin A,Cyclosporin A-binding protein,Mouse,Mus musculus,Peptidyl-prolyl cis-trans isomerase A,Ppia,PPIase A,Rotamase A,SP18 96T
E0979m ELISA Cyclophilin A,Cyclosporin A-binding protein,Mouse,Mus musculus,Peptidyl-prolyl cis-trans isomerase A,Ppia,PPIase A,Rotamase A,SP18 96T


 

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