FKBP8_RAT
ID FKBP8_RAT Reviewed; 403 AA.
AC Q3B7U9;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase FKBP8;
DE Short=PPIase FKBP8;
DE EC=5.2.1.8;
DE AltName: Full=FK506-binding protein 8;
DE Short=FKBP-8;
DE AltName: Full=Rotamase;
GN Name=Fkbp8;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Spleen;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Constitutively inactive PPiase, which becomes active when
CC bound to calmodulin and calcium. Seems to act as a chaperone for BCL2,
CC targets it to the mitochondria and modulates its phosphorylation state.
CC The BCL2/FKBP8/calmodulin/calcium complex probably interferes with the
CC binding of BCL2 to its targets. The active form of FKBP8 may therefore
CC play a role in the regulation of apoptosis (By similarity).
CC {ECO:0000250}.
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 -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC -!- SUBUNIT: Homomultimers or heteromultimers (Potential). Forms
CC heterodimer with calmodulin. When activated by calmodulin and calcium,
CC interacts with the BH4 domain of BCL2 and weakly with BCLX isoform Bcl-
CC X(L). Does not bind and inhibit calcineurin. Interacts with ZFYVE27;
CC may negatively regulate ZFYVE27 phosphorylation (By similarity).
CC {ECO:0000250, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion membrane {ECO:0000250}; Single-pass
CC membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}.
CC -!- PTM: Ubiquitinated by PRKN during mitophagy, leading to its degradation
CC and enhancement of mitophagy. Deubiquitinated by USP30.
CC {ECO:0000250|UniProtKB:Q14318}.
CC -!- MISCELLANEOUS: Binds the immunosuppressant FK506 only in its
CC calmodulin/calcium activated form. {ECO:0000250}.
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DR EMBL; BC107454; AAI07455.1; -; mRNA.
DR RefSeq; NP_001032257.1; NM_001037180.1.
DR AlphaFoldDB; Q3B7U9; -.
DR SMR; Q3B7U9; -.
DR BioGRID; 253272; 1.
DR STRING; 10116.ENSRNOP00000027040; -.
DR iPTMnet; Q3B7U9; -.
DR PhosphoSitePlus; Q3B7U9; -.
DR jPOST; Q3B7U9; -.
DR PaxDb; Q3B7U9; -.
DR PRIDE; Q3B7U9; -.
DR Ensembl; ENSRNOT00000077756; ENSRNOP00000074539; ENSRNOG00000058359.
DR GeneID; 290652; -.
DR KEGG; rno:290652; -.
DR UCSC; RGD:1308670; rat.
DR CTD; 23770; -.
DR RGD; 1308670; Fkbp8.
DR eggNOG; KOG0543; Eukaryota.
DR GeneTree; ENSGT00940000156705; -.
DR HOGENOM; CLU_013615_1_3_1; -.
DR InParanoid; Q3B7U9; -.
DR OMA; RRDQHNE; -.
DR OrthoDB; 787673at2759; -.
DR PhylomeDB; Q3B7U9; -.
DR TreeFam; TF105295; -.
DR Reactome; R-RNO-5689880; Ub-specific processing proteases.
DR PRO; PR:Q3B7U9; -.
DR Proteomes; UP000002494; Chromosome 16.
DR Bgee; ENSRNOG00000058359; Expressed in frontal cortex and 19 other tissues.
DR Genevisible; Q3B7U9; RN.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0012505; C:endomembrane system; IBA:GO_Central.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; ISO:RGD.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005740; C:mitochondrial envelope; ISO:RGD.
DR GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0032991; C:protein-containing complex; ISO:RGD.
DR GO; GO:0097718; F:disordered domain specific binding; ISO:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0044183; F:protein folding chaperone; ISO:RGD.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0030509; P:BMP signaling pathway; IEA:Ensembl.
DR GO; GO:0043010; P:camera-type eye development; ISO:RGD.
DR GO; GO:0001708; P:cell fate specification; ISO:RGD.
DR GO; GO:0021904; P:dorsal/ventral neural tube patterning; ISO:RGD.
DR GO; GO:0009953; P:dorsal/ventral pattern formation; ISO:RGD.
DR GO; GO:0035264; P:multicellular organism growth; ISO:RGD.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:RGD.
DR GO; GO:0001933; P:negative regulation of protein phosphorylation; ISO:RGD.
DR GO; GO:0021915; P:neural tube development; ISO:RGD.
DR GO; GO:0048665; P:neuron fate specification; IEA:Ensembl.
DR GO; GO:0030513; P:positive regulation of BMP signaling pathway; ISO:RGD.
DR GO; GO:0006457; P:protein folding; ISO:RGD.
DR GO; GO:0030510; P:regulation of BMP signaling pathway; ISO:RGD.
DR GO; GO:0010468; P:regulation of gene expression; ISO:RGD.
DR GO; GO:0007224; P:smoothened signaling pathway; ISO:RGD.
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 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; 1.
PE 2: Evidence at transcript level;
KW Apoptosis; Calcium; Isomerase; Isopeptide bond; Membrane; Mitochondrion;
KW Phosphoprotein; Reference proteome; Repeat; Rotamase; TPR repeat;
KW Transmembrane; Transmembrane helix; Ubl conjugation.
FT CHAIN 1..403
FT /note="Peptidyl-prolyl cis-trans isomerase FKBP8"
FT /id="PRO_0000342530"
FT TRANSMEM 381..401
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 110..195
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00277"
FT REPEAT 212..245
FT /note="TPR 1"
FT REPEAT 263..296
FT /note="TPR 2"
FT REPEAT 297..330
FT /note="TPR 3"
FT REGION 26..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..42
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 287
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14318"
FT CROSSLNK 240
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q14318"
FT CROSSLNK 262
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q14318"
FT CROSSLNK 264
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q14318"
FT CROSSLNK 275
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q14318"
FT CROSSLNK 298
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q14318"
FT CROSSLNK 305
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q14318"
FT CROSSLNK 325
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q14318"
FT CROSSLNK 331
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q14318"
FT CROSSLNK 339
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q14318"
FT CROSSLNK 342
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q14318"
FT CROSSLNK 343
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q14318"
SQ SEQUENCE 403 AA; 43556 MW; F4E65E70D6155929 CRC64;
MASWAEPSEP AAQLLCGAPL LEGFEVLDGV DDAEEEDDLS GLPPLEDMGQ PTVEEAEQPG
ALAREFLAAT EPEPAPAPAP EEWLDILGNG LLRKKTLVPG PTGSSRPLKG QVVTVHLQMS
LENGTRVQEE PELAFTLGDC DVIQALDLSV PLMHVGETAM VTADSKYCYG PQGSRSPYIP
PHAALCLEVT LKTAEDGPDL EMLSGQERVA LANRKRECGN AHYQRADFVL AANSYDLAIK
AITSNAKVDM TCEEEEELLQ LKVKCLNNLA ASQLKLDHYR AALRSCSQVL EHQPDNIKAL
FRKGKVLAQQ GEYSEAIPIL RAALKLEPSN KTIHAELSKL VKKRAAQRST ETALYRKMLG
NPSRLPAKCP GKGAWSIPWK WLFGATAVAL GGVALSVVIA ARN
