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Protein

Peptidyl-prolyl cis-trans isomerase FKBP8

Gene

Fkbp8

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

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).By similarity

Catalytic activityi

Peptidylproline (omega=180) = peptidylproline (omega=0).

Cofactori

Ca2+By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Isomerase, Rotamase

Keywords - Biological processi

Apoptosis

Keywords - Ligandi

Calcium

Names & Taxonomyi

Protein namesi
Recommended name:
Peptidyl-prolyl cis-trans isomerase FKBP8 (EC:5.2.1.8)
Short name:
PPIase FKBP8
Alternative name(s):
FK506-binding protein 8
Short name:
FKBP-8
Rotamase
Gene namesi
Name:Fkbp8
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 16

Organism-specific databases

RGDi1308670. Fkbp8.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei381 – 40121HelicalSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 403403Peptidyl-prolyl cis-trans isomerase FKBP8PRO_0000342530Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki240 – 240Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki262 – 262Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki264 – 264Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki275 – 275Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki298 – 298Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki305 – 305Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki325 – 325Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki331 – 331Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki339 – 339Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki342 – 342Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki343 – 343Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity

Post-translational modificationi

Ubiquitinated by PARK2 during mitophagy, leading to its degradation and enhancement of mitophagy. Deubiquitinated by USP30.By similarity

Keywords - PTMi

Isopeptide bond, Ubl conjugation

Proteomic databases

PaxDbiQ3B7U9.
PRIDEiQ3B7U9.

PTM databases

PhosphoSiteiQ3B7U9.

Expressioni

Gene expression databases

GenevisibleiQ3B7U9. RN.

Interactioni

Subunit structurei

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. Interacts with ZFYVE27; may negatively regulate ZFYVE27 phosphorylation (By similarity).By similarityCurated

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000027040.

Structurei

3D structure databases

ProteinModelPortaliQ3B7U9.
SMRiQ3B7U9. Positions 81-202.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini110 – 19586PPIase FKBP-typePROSITE-ProRule annotationAdd
BLAST
Repeati212 – 24534TPR 1Add
BLAST
Repeati263 – 29634TPR 2Add
BLAST
Repeati297 – 33034TPR 3Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi253 – 2575Poly-Glu

Sequence similaritiesi

Contains 1 PPIase FKBP-type domain.PROSITE-ProRule annotation
Contains 3 TPR repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, TPR repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG0543. Eukaryota.
COG0545. LUCA.
GeneTreeiENSGT00840000129912.
HOGENOMiHOG000112604.
HOVERGENiHBG051626.
InParanoidiQ3B7U9.
KOiK09574.
OMAiAMYKKML.
OrthoDBiEOG70S75T.
PhylomeDBiQ3B7U9.
TreeFamiTF105295.

Family and domain databases

Gene3Di1.10.150.160. 1 hit.
1.25.40.10. 1 hit.
InterProiIPR023114. Elongated_TPR_rpt_dom.
IPR023566. PPIase_FKBP.
IPR001179. PPIase_FKBP_dom.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical_dom.
IPR019734. TPR_repeat.
[Graphical view]
PANTHERiPTHR10516. PTHR10516. 1 hit.
PfamiPF00254. FKBP_C. 1 hit.
[Graphical view]
SMARTiSM00028. TPR. 3 hits.
[Graphical view]
SUPFAMiSSF48452. SSF48452. 1 hit.
PROSITEiPS50059. FKBP_PPIASE. 1 hit.
PS50005. TPR. 2 hits.
PS50293. TPR_REGION. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q3B7U9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASWAEPSEP AAQLLCGAPL LEGFEVLDGV DDAEEEDDLS GLPPLEDMGQ
60 70 80 90 100
PTVEEAEQPG ALAREFLAAT EPEPAPAPAP EEWLDILGNG LLRKKTLVPG
110 120 130 140 150
PTGSSRPLKG QVVTVHLQMS LENGTRVQEE PELAFTLGDC DVIQALDLSV
160 170 180 190 200
PLMHVGETAM VTADSKYCYG PQGSRSPYIP PHAALCLEVT LKTAEDGPDL
210 220 230 240 250
EMLSGQERVA LANRKRECGN AHYQRADFVL AANSYDLAIK AITSNAKVDM
260 270 280 290 300
TCEEEEELLQ LKVKCLNNLA ASQLKLDHYR AALRSCSQVL EHQPDNIKAL
310 320 330 340 350
FRKGKVLAQQ GEYSEAIPIL RAALKLEPSN KTIHAELSKL VKKRAAQRST
360 370 380 390 400
ETALYRKMLG NPSRLPAKCP GKGAWSIPWK WLFGATAVAL GGVALSVVIA

ARN
Length:403
Mass (Da):43,556
Last modified:November 22, 2005 - v1
Checksum:iF4E65E70D6155929
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC107454 mRNA. Translation: AAI07455.1.
RefSeqiNP_001032257.1. NM_001037180.1.
UniGeneiRn.99789.

Genome annotation databases

EnsembliENSRNOT00000077756; ENSRNOP00000074539; ENSRNOG00000058359.
GeneIDi290652.
KEGGirno:290652.
UCSCiRGD:1308670. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC107454 mRNA. Translation: AAI07455.1.
RefSeqiNP_001032257.1. NM_001037180.1.
UniGeneiRn.99789.

3D structure databases

ProteinModelPortaliQ3B7U9.
SMRiQ3B7U9. Positions 81-202.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000027040.

PTM databases

PhosphoSiteiQ3B7U9.

Proteomic databases

PaxDbiQ3B7U9.
PRIDEiQ3B7U9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000077756; ENSRNOP00000074539; ENSRNOG00000058359.
GeneIDi290652.
KEGGirno:290652.
UCSCiRGD:1308670. rat.

Organism-specific databases

CTDi23770.
RGDi1308670. Fkbp8.

Phylogenomic databases

eggNOGiKOG0543. Eukaryota.
COG0545. LUCA.
GeneTreeiENSGT00840000129912.
HOGENOMiHOG000112604.
HOVERGENiHBG051626.
InParanoidiQ3B7U9.
KOiK09574.
OMAiAMYKKML.
OrthoDBiEOG70S75T.
PhylomeDBiQ3B7U9.
TreeFamiTF105295.

Miscellaneous databases

NextBioi631421.
PROiQ3B7U9.

Gene expression databases

GenevisibleiQ3B7U9. RN.

Family and domain databases

Gene3Di1.10.150.160. 1 hit.
1.25.40.10. 1 hit.
InterProiIPR023114. Elongated_TPR_rpt_dom.
IPR023566. PPIase_FKBP.
IPR001179. PPIase_FKBP_dom.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical_dom.
IPR019734. TPR_repeat.
[Graphical view]
PANTHERiPTHR10516. PTHR10516. 1 hit.
PfamiPF00254. FKBP_C. 1 hit.
[Graphical view]
SMARTiSM00028. TPR. 3 hits.
[Graphical view]
SUPFAMiSSF48452. SSF48452. 1 hit.
PROSITEiPS50059. FKBP_PPIASE. 1 hit.
PS50005. TPR. 2 hits.
PS50293. TPR_REGION. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Spleen.

Entry informationi

Entry nameiFKBP8_RAT
AccessioniPrimary (citable) accession number: Q3B7U9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 2008
Last sequence update: November 22, 2005
Last modified: May 11, 2016
This is version 107 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

Binds the immunosuppressant FK506 only in its calmodulin/calcium activated form.By similarity

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.