Fkbp7 FK506 binding protein 7 [Mus musculus (house mouse)] - Gene

Summary

Official Symbol: Fkbp7provided by MGI
Official Full Name: FK506 binding protein 7provided by MGI
Primary source: MGI:MGI:1336879
See related: Ensembl:ENSMUSG00000002732 AllianceGenome:MGI:1336879
Gene type: protein coding
RefSeq status: VALIDATED
Organism: Mus musculus
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Mus; Mus
Also known as: 23kDa; FKBP-7; FKBP23
Summary: Enables calcium ion binding activity. Located in endoplasmic reticulum. Is expressed in several structures, including central nervous system; genitourinary system; jaw; retina; and skeleton. Orthologous to human FKBP7 (FKBP prolyl isomerase 7). [provided by Alliance of Genome Resources, Apr 2022]
Expression: Broad expression in bladder adult (RPKM 28.4), limb E14.5 (RPKM 18.1) and 15 other tissues See more
Orthologs: human all
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Genomic context

Location:: 2 C3; 2 45.09 cM

Exon count:: 5

Annotation release	Status	Assembly	Chr	Location
RS_2024_02	current	GRCm39 (GCF_000001635.27)	2	NC_000068.8 (76493378..76503442, complement)
108.20200622	previous assembly	GRCm38.p6 (GCF_000001635.26)	2	NC_000068.7 (76663034..76673098, complement)

Chromosome 2 - NC_000068.8 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Genomic Sequence:

Go to nucleotide: Graphics FASTA GenBank

Expression

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See details

Project title: Mouse ENCODE transcriptome data
Description: RNA profiling data sets generated by the Mouse ENCODE project.
BioProject: PRJNA66167
Publication: PMID 25409824
Analysis date: n/a

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

FKBP23 is demonstrated to mediate functions of BiP by catalyzing the Pro(117)cis/trans conformational interconversion in the ATPase domain of BiP.
Title: Mouse FKBP23 mediates conformer-specific functions of BiP by catalyzing Pro117 cis/trans isomerization.
In this study, we demonstrate the ability of mFKBP23 to modulate the ATPase activity of BiP, and that the bound mFKBP23, but not the free mFKBP23, can suppress the ATPase activity of mBiP through its PPIase activity.
Title: The binding of FKBP23 to BiP modulates BiP's ATPase activity with its PPIase activity.
binds to Grp78 (Bip) in endoplasmic reticulum.
Title: Binding of FKBP23 to BiP in ER shown by gel filtration chromatography.
mFKBP23 binds to immunoglobulin binding protein (mBiP,Hsp70); the binding of the C-terminus is Ca(2+)-dependent and the switch point is between 2 and 3 mM, no binding being detected at high concentration of calcium
Title: The mouse FKBP23 binds to BiP in ER and the binding of C-terminal domain is interrelated with Ca2+ concentration.

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Variation

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Alleles

Alleles of this type are documented at Mouse Genome Informatics (MGI)

Targeted (1)

Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Markers

Fkbp7 (e-PCR), detects polymorphism
- UniSTS:256975

Gene Ontology Provided by MGI

Function	Evidence Code	Pubs
enables calcium ion binding	IDA Inferred from Direct Assay more info	PubMed
enables isomerase activity	IEA Inferred from Electronic Annotation more info
enables metal ion binding	IEA Inferred from Electronic Annotation more info
enables peptidyl-prolyl cis-trans isomerase activity	IEA Inferred from Electronic Annotation more info
enables protein binding	IPI Inferred from Physical Interaction more info	PubMed

Component	Evidence Code	Pubs
located_in endoplasmic reticulum	IDA Inferred from Direct Assay more info	PubMed

General protein information

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Preferred Names: peptidyl-prolyl cis-trans isomerase FKBP7

Names: 23 kDa FK506-binding protein; 23 kDa FKBP; FKBP-23; PPIase FKBP7; rotamase

NP_001342008.1

EC 5.2.1.8

NP_001342009.1

EC 5.2.1.8

NP_034352.1

EC 5.2.1.8

NCBI Reference Sequences (RefSeq)

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RefSeqs maintained independently of Annotated Genomes

These reference sequences exist independently of genome builds. Explain

These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.

mRNA and Protein(s)

NM_001355079.1 → NP_001342008.1 peptidyl-prolyl cis-trans isomerase FKBP7 isoform 2 precursor

Status: VALIDATED

Description

Transcript Variant: This variant (2) uses an alternate in-frame splice junction compared to variant 1. The resulting isoform (2) has the same N- and C-termini but is 1 aa shorter compared to isoform 1.

Source sequence(s)

AI182368, AL928867

Conserved Domains (2) summary

pfam00254
Location:42 → 136

FKBP_C; FKBP-type peptidyl-prolyl cis-trans isomerase

pfam13499
Location:147 → 209

EF-hand_7; EF-hand domain pair
NM_001355080.1 → NP_001342009.1 peptidyl-prolyl cis-trans isomerase FKBP7 isoform 3

Status: VALIDATED

Description

Transcript Variant: This variant (3) contains an alternate exon compared to variant 1. The resulting isoform (3) has a shorter and distinct N-terminus compared to isoform 1.

Source sequence(s)

AL928867

Conserved Domains (2) summary

pfam13499
Location:40 → 102

EF-hand_7; EF-hand domain pair

cl19519
Location:12 → 29

FKBP_C; FKBP-type peptidyl-prolyl cis-trans isomerase
NM_010222.2 → NP_034352.1 peptidyl-prolyl cis-trans isomerase FKBP7 isoform 1 precursor

See identical proteins and their annotated locations for NP_034352.1

Status: VALIDATED

Description

Transcript Variant: This variant (1) represents the longest isoform (1).

Source sequence(s)

AL928867

Consensus CDS

CCDS16161.1

UniProtKB/Swiss-Prot

O54998

UniProtKB/TrEMBL

Q3UU11

Related

ENSMUSP00000002809.8, ENSMUST00000002809.14

Conserved Domains (3) summary

pfam00254
Location:42 → 137

FKBP_C; FKBP-type peptidyl-prolyl cis-trans isomerase

pfam13499
Location:148 → 210

EF-hand_7; EF-hand domain pair

cl08302
Location:148 → 209

EFh; EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal modulators; most examples in this alignment model have 2 active canonical EF hands. Ca2+ binding induces a conformational change in the EF-hand motif, leading to ...