PPIL3

Peptidyl-prolyl cis-trans isomerase-like 3 is an enzyme that in humans is encoded by the PPIL3 gene.^[5][6]

PPIL3
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1XYH, 2OJU, 2OK3
Identifiers
Aliases	PPIL3, CYPJ, peptidylprolyl isomerase like 3
External IDs	OMIM: 615811; MGI: 1917475; HomoloGene: 41717; GeneCards: PPIL3; OMA:PPIL3 - orthologs
Gene location (Human) Chr. Chromosome 2 (human)[1] Band 2q33.1 Start 200,870,907 bp[1] End 200,889,303 bp[1]
Gene location (Mouse) Chr. Chromosome 1 (mouse)[2] Band 1|1 C1.3 Start 58,470,153 bp[2] End 58,484,645 bp[2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in mucosa of ileum pancreatic epithelial cell ganglionic eminence myocardium of left ventricle ventricular zone secondary oocyte right uterine tube tibialis anterior muscle germinal epithelium tibia Top expressed in facial motor nucleus endothelial cell of lymphatic vessel hand primitive streak primary oocyte otolith organ utricle superior cervical ganglion medullary collecting duct condyle More reference expression data BioGPS n/a
Gene ontology Molecular function isomerase activity protein binding peptidyl-prolyl cis-trans isomerase activity Cellular component catalytic step 2 spliceosome spliceosomal complex Biological process mRNA splicing, via spliceosome mRNA processing protein folding RNA splicing protein peptidyl-prolyl isomerization Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 53938 70225 Ensembl ENSG00000240344 ENSMUSG00000026035 UniProt Q9H2H8 Q9D6L8 RefSeq (mRNA) NM_032472 NM_130906 NM_131916 NM_001285826 NM_001285827 NM_027351 NM_027374 RefSeq (protein) NP_115861 NP_570981 NP_001272755 NP_001272756 NP_081627 NP_081650 Location (UCSC) Chr 2: 200.87 – 200.89 Mb Chr 1: 58.47 – 58.48 Mb PubMed search [3] [4]
Wikidata
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Function

This gene encodes a member of the cyclophilin family. Cyclophilins catalyze the cis-trans isomerization of peptidylprolyl imide bonds in oligopeptides. They have been proposed to act either as catalysts or as molecular chaperones in protein-folding events. Transcript variants derived from alternative splicing and/or alternative polyadenylation exist; some of these variants encode different isoforms.^[6]