Ppib peptidylprolyl isomerase B [Rattus norvegicus (Norway rat)] - Gene

Summary

Official Symbol: Ppibprovided by RGD
Official Full Name: peptidylprolyl isomerase Bprovided by RGD
Primary source: RGD:620312
See related: Ensembl:ENSRNOG00000016781 AllianceGenome:RGD:620312
Gene type: protein coding
RefSeq status: PROVISIONAL
Organism: Rattus norvegicus
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Rattus
Also known as: CypB; Scylp
Summary: Predicted to enable RNA polymerase binding activity; cyclosporin A binding activity; and peptidyl-prolyl cis-trans isomerase activity. Predicted to be involved in several processes, including neutrophil chemotaxis; positive regulation by host of viral genome replication; and protein stabilization. Located in smooth endoplasmic reticulum. 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, Apr 2022]
Expression: Biased expression in Liver (RPKM 1849.0), Kidney (RPKM 1309.9) and 9 other tissues See more
Orthologs: human mouse all
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Genomic context

Location:: 8q24

Exon count:: 5

Annotation release	Status	Assembly	Chr	Location
RS_2024_02	current	GRCr8 (GCF_036323735.1)	8	NC_086026.1 (75498966..75504823)
RS_2023_06	previous assembly	mRatBN7.2 (GCF_015227675.2)	8	NC_051343.1 (66603877..66609734)
106	previous assembly	Rnor_6.0 (GCF_000001895.5)	8	NC_005107.4 (71719681..71725538)

Chromosome 8 - NC_086026.1 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: A rat RNA-Seq transcriptomic BodyMap across 11 organs and 4 developmental stages
Description: 320 RNA samples isolated from 11 organs (adrenal gland, brain, heart, kidney, liver, lung, muscle, spleen, thymus, and testes or uterus) from both sexes of Fischer 344 rats across four developmental stages (2-, 6-, 21-, and 104-weeks-old)
BioProject: PRJNA238328
Publication: PMID 24510058
Analysis date: Mon Jun 6 17:44:12 2016

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

CypB-CD147 Signaling Is Involved in Crosstalk between Cartilage and FLS in Collagen-Induced Arthritis.
Title: CypB-CD147 Signaling Is Involved in Crosstalk between Cartilage and FLS in Collagen-Induced Arthritis.
Cyclophilin B in the hepatocyte proliferation.TMUB1 interfered with the binding of CAML to cyclophilin B in hepatocytes.
Title: TMUB1 Inhibits BRL-3A Hepatocyte Proliferation by Interfering with the Binding of CAML to Cyclophilin B through its TM1 Hydrophobic Domain.
neuroprotective effects against amyloid-beta-induced neurotoxicity in PC12 cells
Title: Neuroprotective effects of overexpressed cyclophilin B against Aβ-induced neurotoxicity in PC12 cells.
NIM811 attenuates liver fibrosis in a CCl(4)-induced rat liver fibrosis model, which may be related to binding with cyclophilin B and D.
Title: N-methyl-4-isoleucine cyclosporine attenuates CCl -induced liver fibrosis in rats by interacting with cyclophilin B and D.
CypB performs a crucial function in protecting cells against ER stress via its PPIase activity
Title: Overexpressed cyclophilin B suppresses apoptosis associated with ROS and Ca2+ homeostasis after ER stress.

Submit: New GeneRIF Correction

Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Markers

RH127700 (e-PCR)
- UniSTS:211010

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

RH132751 (e-PCR)
- UniSTS:216034

Gene Ontology Provided by RGD

Function	Evidence Code	Pubs
enables RNA polymerase binding	ISO Inferred from Sequence Orthology 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 cyclosporin A binding	ISS Inferred from Sequence or Structural Similarity 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	IEA Inferred from Electronic Annotation 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

Process	Evidence Code	Pubs
involved_in bone development	ISO Inferred from Sequence Orthology more info
NOT involved_in chaperone-mediated protein folding	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	ISO Inferred from Sequence Orthology more info
involved_in nuclear transport	TAS Traceable Author Statement more info	PubMed
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	ISO Inferred from Sequence Orthology more info
involved_in protein folding	IBA Inferred from Biological aspect of Ancestor more info
involved_in protein folding	IEA Inferred from Electronic Annotation more info
involved_in protein peptidyl-prolyl isomerization	IBA Inferred from Biological aspect of Ancestor more info
involved_in protein stabilization	ISO Inferred from Sequence Orthology more info
NOT involved_in regulation of post-translational protein modification	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	ISO Inferred from Sequence Orthology more info
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	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	IDA Inferred from Direct Assay more info	PubMed

General protein information

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Preferred Names: peptidyl-prolyl cis-trans isomerase B

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

NP_071981.1

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_022536.2 → NP_071981.1 peptidyl-prolyl cis-trans isomerase B precursor

See identical proteins and their annotated locations for NP_071981.1

Status: PROVISIONAL

Source sequence(s)

AF071225

UniProtKB/TrEMBL

A0A8I6GG55

Related

ENSRNOP00000022828.5, ENSRNOT00000022828.8

Conserved Domains (1) summary

cd01926
Location:37 → 195

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 accelerates protein folding ...