PPIL1

PPIL1
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	1XWN, 2K7N, 2X7K
Identifiers
Aliases	PPIL1 , CYPL1, PPIase, hCyPX, CGI-124, peptidylprolyl isomerase like 1, PCH14
External IDs	OMIM: 601301 MGI: 1916066 HomoloGene: 9367 GeneCards: PPIL1
Gene location (Human)
Chr.	Chromosome 6 (human)
End	36,874,803 bp
Gene location (Mouse)
Chr.	Chromosome 17 (mouse)
End	29,483,160 bp
RNA expression pattern
	Top expressed in
	right ventricle; ; oocyte; ; secondary oocyte; ; Left adrenal gland; ; islet of Langerhans; ; ganglionic eminence; ; prefrontal cortex; ; sperm; ; nucleus accumbens; ; metanephros;
	Top expressed in
	superior cervical ganglion; ; morula; ; neural tube; ; yolk sac; ; renal corpuscle; ; hand; ; endocardial cushion; ; interventricular septum; ; primitive streak; ; abdominal wall;
	More reference expression data
	More reference expression data
Gene ontology
Molecular function	isomerase activity ; protein binding ; disordered domain specific binding ; peptidyl-prolyl cis-trans isomerase activity ; cyclosporin A binding ;
Cellular component	catalytic step 2 spliceosome ; spliceosomal complex ; nucleoplasm ; nucleus ; U2-type catalytic step 2 spliceosome ;
Biological process	mRNA processing ; protein folding ; RNA splicing ; mRNA splicing, via spliceosome ; protein peptidyl-prolyl isomerization ;
	Sources:Amigo / QuickGO
Orthologs
	51645
	68816
	ENSG00000137168
	ENSMUSG00000024007
	Q9Y3C6
	Q9D0W5
	NM_016059
	NM_026845
	NP_057143
	NP_081121
	Wikidata
View/Edit Human	View/Edit Mouse

Last updated March 04, 2023

Peptidyl-prolyl cis-trans isomerase-like 1 is an enzyme that in humans is encoded by the PPIL1 gene.^[5]^[6]^[7]

This gene is a member of the cyclophilin family of peptidylprolyl isomerases (PPIases). The cyclophilins are a highly conserved, ubiquitous family, members of which play an important role in protein folding, immunosuppression by cyclosporin A, and infection of HIV-1 virions.

Based on similarity to other PPIases, this protein could accelerate the folding of proteins and might catalyze the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.^[7]

Related Research Articles

Cyclophilins (CYPs) are a family of proteins named after their ability to bind to ciclosporin, an immunosuppressant which is usually used to suppress rejection after internal organ transplants. They are found in all domains of life. These proteins have peptidyl prolyl isomerase activity, which catalyzes the isomerization of peptide bonds from trans form to cis form at proline residues and facilitates protein folding.

Peptidylprolyl isomerase A (PPIA), also known as cyclophilin A (CypA) or rotamase A is an enzyme that in humans is encoded by the PPIA gene on chromosome 7. As a member of the peptidyl-prolyl cis-trans isomerase (PPIase) family, this protein catalyzes the cis-trans isomerization of proline imidic peptide bonds, which allows it to regulate many biological processes, including intracellular signaling, transcription, inflammation, and apoptosis. Due to its various functions, PPIA has been implicated in a broad range of inflammatory diseases, including atherosclerosis and arthritis, and viral infections.

Peptidyl-prolyl cis-trans isomerase B is an enzyme that is encoded by the PPIB gene. As a member of the peptidyl-prolyl cis-trans isomerase (PPIase) family, this protein catalyzes the cis-trans isomerization of proline imidic peptide bonds, which allows it to regulate protein folding of type I collagen. Generally, PPIases are found in all eubacteria and eukaryotes, as well as in a few archaebacteria, and thus are highly conserved.

Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 is an enzyme that in humans is encoded by the PIN1 gene.

Peptidylprolyl isomerase D (cyclophilin D), also known as PPID, is an enzyme which in humans is encoded by the PPID gene on chromosome 4. As a member of the peptidyl-prolyl cis-trans isomerase (PPIase) family, this protein catalyzes the cis-trans isomerization of proline imidic peptide bonds, which allows it to facilitate folding or repair of proteins. In addition, PPID participates in many biological processes, including mitochondrial metabolism, apoptosis, redox, and inflammation, as well as in related diseases and conditions, such as ischemic reperfusion injury, AIDS, and cancer.

Peroxisomal 3,2-trans-enoyl-CoA isomerase is an enzyme that in humans is encoded by the PECI gene.

DnaJ homolog subfamily B member 9 is a protein that in humans is encoded by the DNAJB9 gene.

Peptidyl-prolyl cis-trans isomerase, mitochondrial (PPIF) is an enzyme that in humans is encoded by the PPIF gene. It has also been referred to as, but should not be confused with, cyclophilin D (CypD), which is encoded by the PPID gene. As a member of the peptidyl-prolyl cis-trans isomerase (PPIase) family, this protein catalyzes the cis-trans isomerization of proline imidic peptide bonds, which allows it to facilitate folding or repair of proteins. PPIF is a major component of the mitochondrial permeability transition pore (MPTP) and, thus, highly involved in mitochondrial metabolism and apoptosis, as well as in mitochondrial diseases and related conditions, including cardiac diseases, neurodegenerative diseases, and muscular dystrophy. In addition, PPIF participates in inflammation, as well as in ischemic reperfusion injury, AIDS, and cancer.

Peptidyl-prolyl cis-trans isomerase NIMA-interacting 4 is an enzyme that in humans is encoded by the PIN4 gene.

Peptidyl-prolyl cis-trans isomerase H is an enzyme that in humans is encoded by the PPIH gene.

Peptidyl-prolyl cis-trans isomerase C (PPIC) is an enzyme that in humans is encoded by the PPIC gene on chromosome 5. As a member of the peptidyl-prolyl cis-trans isomerase (PPIase) family, this protein catalyzes the cis-trans isomerization of proline imidic peptide bonds, which allows it to facilitate folding or repair of proteins. In addition, PPIC participates in many biological processes, including mitochondrial metabolism, apoptosis, redox, and inflammation, as well as in related diseases and conditions, such as ischemic reperfusion injury, AIDS, and cancer.

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

Peptidyl-prolyl cis-trans isomerase G is an enzyme that in humans is encoded by the PPIG gene.

Kinesin-like protein KIF20B is a protein that in humans is encoded by the KIF20B gene.

Peptidylprolyl isomerase E (cyclophilin E), also known as PPIE, is an enzyme which in humans is encoded by the PPIE gene on chromosome 1. As a member of the peptidyl-prolyl cis-trans isomerase (PPIase) family, this protein catalyzes the cis-trans isomerization of proline imidic peptide bonds, which allows it to facilitate folding or repair of proteins. In addition, PPIE participates in many biological processes, including mitochondrial metabolism, apoptosis, and inflammation, as well as related diseases and conditions, such as ischemic reperfusion injury, AIDS, influenza, and cancer.

Peptidyl-prolyl cis-trans isomerase-like 2 is an enzyme that in humans is encoded by the PPIL2 gene.

NK-tumor recognition protein is a protein that in humans is encoded by the NKTR gene.

FK506-binding protein 10 is a protein that in humans is encoded by the FKBP10 gene.

Peptidyl-prolyl cis-trans isomerase-like 4 is an enzyme that in humans is encoded by the PPIL4 gene.

Prolyl 3-hydroxylase 3 is an enzyme that in humans is encoded by the LEPREL2 gene.

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000137168 - Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000024007 - Ensembl, May 2017
↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ Mann SS, Pettenati MJ, von Kap-herr C, Hart TC (Mar 1999). "Reassignment of peptidyl prolyl isomerase-like 1 gene (PPIL1) to human chromosome region 6p21.1 by radiation hybrid mapping and fluorescence in situ hybridization". Cytogenet Cell Genet. 83 (3–4): 228–9. doi:10.1159/000015186. PMID 10072585. S2CID 85413695.
↑ Ozaki K, Fujiwara T, Kawai A, Shimizu F, Takami S, Okuno S, Takeda S, Shimada Y, Nagata M, Watanabe T, Takaichi A, Takahashi E, Nakamura Y, Shin S (Jan 1997). "Cloning, expression and chromosomal mapping of a novel cyclophilin-related gene (PPIL1) from human fetal brain". Cytogenet Cell Genet. 72 (2–3): 242–5. doi:10.1159/000134199. PMID 8978786.
1 2 "Entrez Gene: PPIL1 peptidylprolyl isomerase (cyclophilin)-like 1".

Tripodis N, Mason R, Humphray SJ, et al. (1999). "Physical map of human 6p21.2-6p21.3: region flanking the centromeric end of the major histocompatibility complex". Genome Res. 8 (6): 631–43. doi:10.1101/gr.8.6.631. PMC 310739 . PMID 9647638.
Lai CH, Chou CY, Ch'ang LY, et al. (2000). "Identification of novel human genes evolutionarily conserved in Caenorhabditis elegans by comparative proteomics". Genome Res. 10 (5): 703–13. doi:10.1101/gr.10.5.703. PMC 310876 . PMID 10810093.
Jurica MS, Licklider LJ, Gygi SR, et al. (2002). "Purification and characterization of native spliceosomes suitable for three-dimensional structural analysis". RNA. 8 (4): 426–39. doi:10.1017/S1355838202021088. PMC 1370266 . PMID 11991638.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi: 10.1073/pnas.242603899 . PMC 139241 . PMID 12477932.
Clark HF, Gurney AL, Abaya E, et al. (2003). "The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment". Genome Res. 13 (10): 2265–70. doi:10.1101/gr.1293003. PMC 403697 . PMID 12975309.
Mungall AJ, Palmer SA, Sims SK, et al. (2003). "The DNA sequence and analysis of human chromosome 6". Nature. 425 (6960): 805–11. Bibcode:2003Natur.425..805M. doi: 10.1038/nature02055 . PMID 14574404.
Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928 . PMID 15489334.
Xu C, Xu Y, Tang Y, et al. (2005). "Backbone and side chain assignments of human Peptidylprolyl Isomerase Like 1 (hPPIL1)". J. Biomol. NMR. 31 (2): 179–80. doi:10.1007/s10858-004-8238-0. PMID 15772761. S2CID 30456850.
Xu C, Zhang J, Huang X, et al. (2006). "Solution structure of human peptidyl prolyl isomerase-like protein 1 and insights into its interaction with SKIP". J. Biol. Chem. 281 (23): 15900–8. doi: 10.1074/jbc.M511155200 . PMID 16595688.

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[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000137168 - Ensembl, May 2017

[refGRCm38Ensembl-2] 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000024007 - Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid10072585-5] Mann SS, Pettenati MJ, von Kap-herr C, Hart TC (Mar 1999). "Reassignment of peptidyl prolyl isomerase-like 1 gene (PPIL1) to human chromosome region 6p21.1 by radiation hybrid mapping and fluorescence in situ hybridization". Cytogenet Cell Genet. 83 (3–4): 228–9. doi:10.1159/000015186. PMID 10072585. S2CID 85413695.

[pmid8978786-6] Ozaki K, Fujiwara T, Kawai A, Shimizu F, Takami S, Okuno S, Takeda S, Shimada Y, Nagata M, Watanabe T, Takaichi A, Takahashi E, Nakamura Y, Shin S (Jan 1997). "Cloning, expression and chromosomal mapping of a novel cyclophilin-related gene (PPIL1) from human fetal brain". Cytogenet Cell Genet. 72 (2–3): 242–5. doi:10.1159/000134199. PMID 8978786.

[entrez-7] 1 2 "Entrez Gene: PPIL1 peptidylprolyl isomerase (cyclophilin)-like 1".

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PPIL1

Related Research Articles

References

Further reading