Ppib peptidylprolyl isomerase B [Mus musculus (house mouse)] - Gene

Summary

Official Symbol: Ppibprovided by MGI
Official Full Name: peptidylprolyl isomerase Bprovided by MGI
Primary source: MGI:MGI:97750
See related: Ensembl:ENSMUSG00000032383 AllianceGenome:MGI:97750
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: Cphn2; Cphn-2; CyP-20b
Summary: Predicted to enable RNA polymerase binding activity; cyclosporin A binding activity; and peptidyl-prolyl cis-trans isomerase activity. Predicted to contribute to collagen binding activity. Predicted to be involved in several processes, including neutrophil chemotaxis; positive regulation by host of viral genome replication; and protein peptidyl-prolyl isomerization. Part of endoplasmic reticulum chaperone complex. Is expressed in several structures, including axial skeleton; cranium; otic capsule; and pancreas tip epithelium. Used to study osteogenesis imperfecta type 9. Human ortholog(s) of this gene implicated in osteogenesis imperfecta type 9. Orthologous to human PPIB (peptidylprolyl isomerase B). [provided by Alliance of Genome Resources, Nov 2024]
Expression: Ubiquitous expression in placenta adult (RPKM 354.3), liver E18 (RPKM 213.8) and 28 other tissues See more
Orthologs: human all
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Genomic context

Location:: 9 C; 9 35.69 cM

Exon count:: 5

Annotation release	Status	Assembly	Chr	Location
RS_2024_02	current	GRCm39 (GCF_000001635.27)	9	NC_000075.7 (65967451..65973911)
108.20200622	previous assembly	GRCm38.p6 (GCF_000001635.26)	9	NC_000075.6 (66060169..66066629)

Chromosome 9 - NC_000075.7 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 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?

Mice lacking cyclophilin B, but not cyclophilin A, are protected from the development of NASH in a diet and chemical-induced model.
Title: Mice lacking cyclophilin B, but not cyclophilin A, are protected from the development of NASH in a diet and chemical-induced model.
These data demonstrate that CypB deficiency profoundly affects Lys post-translational modifications of collagen likely by modulating LH chaperone complexes. Together, our study underscores the critical role of CypB in Lys modifications of collagen, cross-linking and mechanical properties of skin.
Title: Cyclophilin B control of lysine post-translational modifications of skin type I collagen.
a critical role of CypB in dentin matrix formation, suggesting a possible association between recessive osteogenesis imperfecta and dentin defects
Title: Cyclophilin B Deficiency Causes Abnormal Dentin Collagen Matrix.
These studies demonstrate novel consequences of the indirect regulatory effect of CyPB on collagen hydroxylation, impacting collagen glycosylation, crosslinking and fibrillogenesis
Title: Abnormal type I collagen post-translational modification and crosslinking in a cyclophilin B KO mouse model of recessive osteogenesis imperfecta.
An additional function of the rough endoplasmic reticulum protein complex prolyl 3-hydroxylase 1.cartilage-associated protein.cyclophilin B: the CXXXC motif reveals disulfide isomerase activity in vitro.
Title: An additional function of the rough endoplasmic reticulum protein complex prolyl 3-hydroxylase 1·cartilage-associated protein·cyclophilin B: the CXXXC motif reveals disulfide isomerase activity in vitro.
Cyclophilin B activity regulated secretion and activity of ADAMTS13.
Title: Cyclosporin A impairs the secretion and activity of ADAMTS13 (a disintegrin and metalloprotease with thrombospondin type 1 repeat).
These data provide significant new mechanistic insight into the pathophysiology of Osteogenesis Imperfecta and reveal how the members of the P3H1/CRTAP/CypB complex interact to direct proper formation of collagen and bone.
Title: Severe osteogenesis imperfecta in cyclophilin B-deficient mice.
The protein identified was cyclophilin (Ppib).
Title: Evaluation of the SELDI-TOF MS technique for protein profiling of pancreatic islets exposed to glucose and oleate.
These results suggest that immunophilins are involved in the complex protein networks operating at the presynaptic level and implicate the interaction between cyclophilin B and synapsins in presynaptic function.
Title: Synapsin associates with cyclophilin B in an ATP- and cyclosporin A-dependent manner.

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Variation

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Alleles

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

Endonuclease-mediated (2)
Gene trapped (2)
Targeted (2) 1 citation

Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Markers

AI844835 (e-PCR)
- UniSTS:165643

px-44d3 (e-PCR)
- UniSTS:257814

RH124798 (e-PCR)
- UniSTS:161620

RH124325 (e-PCR)
- UniSTS:161147

Ppib (e-PCR), detects polymorphism
- UniSTS:144252

px-42d4 (e-PCR)
- UniSTS:257776

Gene Ontology Provided by MGI

Function	Evidence Code	Pubs
enables RNA polymerase binding	IEA Inferred from Electronic Annotation more info
enables RNA polymerase binding	ISO Inferred from Sequence Orthology more info
contributes_to collagen binding	ISS Inferred from Sequence or Structural Similarity more info
enables cyclosporin A binding	IBA Inferred from Biological aspect of Ancestor more info
enables cyclosporin A binding	ISO Inferred from Sequence Orthology more info
enables peptidyl-prolyl cis-trans isomerase activity	IBA Inferred from Biological aspect of Ancestor more info
enables peptidyl-prolyl cis-trans isomerase activity	ISO Inferred from Sequence Orthology more info
enables peptidyl-prolyl cis-trans isomerase activity	ISS Inferred from Sequence or Structural Similarity more info
enables protein binding	IPI Inferred from Physical Interaction more info	PubMed
enables protein binding	ISS Inferred from Sequence or Structural Similarity more info

Process	Evidence Code	Pubs
involved_in bone development	IEA Inferred from Electronic Annotation more info
involved_in bone development	ISO Inferred from Sequence Orthology more info
involved_in chaperone-mediated protein folding	ISO Inferred from Sequence Orthology more info
involved_in chaperone-mediated protein folding	ISS Inferred from Sequence or Structural Similarity more info
involved_in neutrophil chemotaxis	IEA Inferred from Electronic Annotation more info
involved_in neutrophil chemotaxis	ISO Inferred from Sequence Orthology more info
involved_in positive regulation by host of viral genome replication	IEA Inferred from Electronic Annotation more info
involved_in positive regulation by host of viral genome replication	ISO Inferred from Sequence Orthology more info
involved_in positive regulation by host of viral process	ISO Inferred from Sequence Orthology more info
involved_in positive regulation of multicellular organism growth	IEA Inferred from Electronic Annotation more info
involved_in positive regulation of multicellular organism growth	ISO Inferred from Sequence Orthology more info
involved_in protein folding	IBA Inferred from Biological aspect of Ancestor more info
involved_in protein peptidyl-prolyl isomerization	ISO Inferred from Sequence Orthology more info
involved_in protein peptidyl-prolyl isomerization	ISS Inferred from Sequence or Structural Similarity more info
involved_in protein stabilization	IEA Inferred from Electronic Annotation more info
involved_in protein stabilization	ISO Inferred from Sequence Orthology more info

Component	Evidence Code	Pubs
is_active_in cytoplasm	IBA Inferred from Biological aspect of Ancestor more info
located_in endoplasmic reticulum	ISO Inferred from Sequence Orthology more info
part_of endoplasmic reticulum chaperone complex	IDA Inferred from Direct Assay more info	PubMed
located_in endoplasmic reticulum lumen	IEA Inferred from Electronic Annotation more info
is_active_in intracellular membrane-bounded organelle	IBA Inferred from Biological aspect of Ancestor more info
located_in melanosome	IEA Inferred from Electronic Annotation more info
located_in nucleoplasm	IEA Inferred from Electronic Annotation more info
located_in nucleoplasm	ISO Inferred from Sequence Orthology more info
located_in perinuclear region of cytoplasm	IEA Inferred from Electronic Annotation more info
located_in perinuclear region of cytoplasm	ISO Inferred from Sequence Orthology more info
part_of protein-containing complex	ISS Inferred from Sequence or Structural Similarity more info
located_in smooth endoplasmic reticulum	IEA Inferred from Electronic Annotation more info
located_in smooth endoplasmic reticulum	ISO Inferred from Sequence Orthology more info

General protein information

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Preferred Names: peptidyl-prolyl cis-trans isomerase B

Names: CYP-S1; PPIase B; S-cyclophilin; SCYLP; cyclophilin B; rotamase B

NP_035279.2

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_011149.2 → NP_035279.2 peptidyl-prolyl cis-trans isomerase B precursor

See identical proteins and their annotated locations for NP_035279.2

Status: VALIDATED

Source sequence(s)

AK002357, AL363449, CA321924

Consensus CDS

CCDS23301.1

UniProtKB/Swiss-Prot

P24369

UniProtKB/TrEMBL

Q9DCY1

Related

ENSMUSP00000034947.6, ENSMUST00000034947.7

Conserved Domains (1) summary

cd01926
Location:45 → 203

cyclophilin_ABH_like; cyclophilin_ABH_like: Cyclophilin A, B and H-like cyclophilin-type peptidylprolyl cis- trans isomerase (PPIase) domain. This family represents the archetypal cystolic cyclophilin similar to human cyclophilins A, B and H. PPIase is an enzyme which ...