ppig peptidylprolyl isomerase G (cyclophilin G) [Danio rerio (zebrafish)] - Gene

Summary

Official Symbol: ppigprovided by ZNC
Official Full Name: peptidylprolyl isomerase G (cyclophilin G)provided by ZNC
Primary source: ZFIN:ZDB-GENE-040426-2822
See related: Ensembl:ENSDARG00000044431 AllianceGenome:ZFIN:ZDB-GENE-040426-2822
Gene type: protein coding
RefSeq status: PROVISIONAL
Organism: Danio rerio
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes; Danionidae; Danioninae; Danio
Also known as: zgc:55535; wu:fb33a06; wu:fi37a09
Summary: Predicted to enable cyclosporin A binding activity and peptidyl-prolyl cis-trans isomerase activity. Predicted to be involved in protein folding. Predicted to act upstream of or within protein peptidyl-prolyl isomerization. Predicted to be active in cytoplasm and nucleus. Orthologous to human PPIG (peptidylprolyl isomerase G). [provided by Alliance of Genome Resources, Jan 2025]
Orthologs: human mouse all
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Genomic context

Location:: chromosome: 6

Exon count:: 13

Annotation release	Status	Assembly	Chr	Location
RS_2024_08	current	GRCz11 (GCF_000002035.6)	6	NC_007117.7 (3693441..3708388)
105	previous assembly	GRCz10 (GCF_000002035.5)	6	NC_007117.6 (3532621..3547568)

Chromosome 6 - NC_007117.7 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: Sequencing the Zebrafish transcriptome from a range of tissues and developmental stages
Description: Sequencing the Zebrafish transcriptome from a range of tissues and developmental stages
BioProject: PRJEB1986
Analysis date: Fri Dec 8 19:48:10 2017

Bibliography

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GeneRIFs: Gene References Into Functions

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General gene information

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Markers

fi37a09.x1 (e-PCR)
- UniSTS:197396

fb33a06 (e-PCR)
- UniSTS:187076

Gene Ontology Provided by ZFIN

Function	Evidence Code	Pubs
enables cyclosporin A binding	IBA Inferred from Biological aspect of Ancestor more info
enables isomerase activity	IEA Inferred from Electronic Annotation 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

Process	Evidence Code	Pubs
involved_in protein folding	IBA Inferred from Biological aspect of Ancestor more info
acts_upstream_of_or_within protein folding	IEA Inferred from Electronic Annotation more info
acts_upstream_of_or_within protein peptidyl-prolyl isomerization	IEA Inferred from Electronic Annotation more info

Component	Evidence Code	Pubs
is_active_in cytoplasm	IBA Inferred from Biological aspect of Ancestor more info
is_active_in nucleus	IBA Inferred from Biological aspect of Ancestor more info

General protein information

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Preferred Names: peptidyl-prolyl cis-trans isomerase G

Names: peptidyl-prolyl isomerase G (cyclophilin G)

NP_998629.1

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_213464.1 → NP_998629.1 peptidyl-prolyl cis-trans isomerase G

See identical proteins and their annotated locations for NP_998629.1

Status: PROVISIONAL

Source sequence(s)

BC044189

UniProtKB/TrEMBL

Q7ZYY1

Related

ENSDARP00000065255.3, ENSDART00000065256.4

Conserved Domains (1) summary

cl00197
Location:8 → 175

cyclophilin; cyclophilin: cyclophilin-type peptidylprolyl cis- trans isomerases. This family contains eukaryotic, bacterial and archeal proteins which exhibit a peptidylprolyl cis- trans isomerases activity (PPIase, Rotamase) and in addition bind the ...