Peptidyl-prolyl cis-trans isomerase-like 1 (PPIL1)

The protein contains 166 amino acids for an estimated molecular weight of 18237 Da.

 

Involved in pre-mRNA splicing as component of the spliceosome (PubMed:11991638, PubMed:28502770, PubMed:28076346). PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (PubMed:16595688). (updated: March 28, 2018)

Protein identification was indicated in the following studies:

  1. Goodman and co-workers. (2013) The proteomics and interactomics of human erythrocytes. Exp Biol Med (Maywood) 238(5), 509-518.
  2. Hegedűs and co-workers. (2015) Inconsistencies in the red blood cell membrane proteome analysis: generation of a database for research and diagnostic applications. Database (Oxford) 1-8.
  3. Bryk and co-workers. (2017) Quantitative Analysis of Human Red Blood Cell Proteome. J Proteome Res. 16(8), 2752-2761.
  4. D'Alessandro and co-workers. (2017) Red blood cell proteomics update: is there more to discover? Blood Transfus. 15(2), 182-187.

Methods

The following articles were analysed to gather the proteome content of erythrocytes.

The gene or protein list provided in the studies were processed using the ID mapping API of Uniprot in September 2018. The number of proteins identified and mapped without ambiguity in these studies is indicated below.
Only Swiss-Prot entries (reviewed) were considered for protein evidence assignation.

PublicationIdentification 1Uniprot mapping 2Not mapped /
Obsolete
TrEMBLSwiss-Prot
Goodman (2013)2289 (gene list)227853205992269
Lange (2014)123412347281224
Hegedus (2015)2638262202352387
Wilson (2016)165815281702911068
d'Alessandro (2017)18261817201815
Bryk (2017)20902060101081942
Chu (2018)18531804553621387

1 as available in the article and/or in supplementary material
2 uniprot mapping returns all protein isoforms as one entry

The compilation of older studies can be retrieved from the Red Blood Cell Collection database.

The data and differentiation stages presented below come from the proteomic study and analysis performed by our partners of the GReX consortium, more details are available in their published work.

No sequence conservation computed yet.

Interpro domains
Total structural coverage: 100%
Model score: 100
No model available.

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VariantDescription
dbSNP:rs12194408

The reference OMIM entry for this protein is 601301

Peptidyl-prolyl isomerase-like 1; ppil1
Cyclophilin-related gene 1; cypl1

Cyclophilin (see 123840), first identified as a protein with high binding affinity for the immunosuppressive agent cyclosporin A, is one of the most effective therapeutic agents for prevention of graft rejection after organ transplantation.

CLONING

Ozaki et al. (1996) isolated a human cDNA clone encoding a protein homologous to cyclophilins and showed that it is conserved in species ranging from human to prokaryotes. This cDNA contained an open reading frame of 498 nucleotides encoding a polypeptide of 166 amino acids. The predicted amino acid sequence had 41.6% homology to the human cyclophilins. Northern blot analysis indicated ubiquitous expression in adult human tissues, with the most abundant expression in heart and skeletal muscle.

MAPPING

Ozaki et al. (1996) localized the PPIL1 gene to 2p23.3-p23.1 by FISH. However, Mann et al. (1998) assigned the PPIL1 gene to 6p21.1 by FISH and radiation hybrid mapping. ... More on the omim web site

Subscribe to this protein entry history

April 12, 2018: Protein entry updated
Automatic update: Entry updated from uniprot information.

Feb. 2, 2018: Protein entry updated
Automatic update: Uniprot description updated

Dec. 19, 2017: Protein entry updated
Automatic update: Uniprot description updated

Nov. 23, 2017: Protein entry updated
Automatic update: Uniprot description updated

March 16, 2016: Protein entry updated
Automatic update: OMIM entry 601301 was added.

Jan. 28, 2016: Protein entry updated
Automatic update: model status changed

Jan. 25, 2016: Protein entry updated
Automatic update: model status changed