PPIL1_MOUSE
ID PPIL1_MOUSE Reviewed; 166 AA.
AC Q9D0W5; Q3UA03;
DT 16-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase-like 1;
DE Short=PPIase;
DE EC=5.2.1.8 {ECO:0000250|UniProtKB:Q9Y3C6};
DE AltName: Full=Rotamase PPIL1;
GN Name=Ppil1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Bone marrow, and Embryo;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Liver, Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [4]
RP FUNCTION, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
RP ARG-55.
RX PubMed=33220177; DOI=10.1016/j.neuron.2020.10.035;
RA Chai G., Webb A., Li C., Antaki D., Lee S., Breuss M.W., Lang N.,
RA Stanley V., Anzenberg P., Yang X., Marshall T., Gaffney P., Wierenga K.J.,
RA Chung B.H., Tsang M.H., Pais L.S., Lovgren A.K., VanNoy G.E., Rehm H.L.,
RA Mirzaa G., Leon E., Diaz J., Neumann A., Kalverda A.P., Manfield I.W.,
RA Parry D.A., Logan C.V., Johnson C.A., Bonthron D.T., Valleley E.M.A.,
RA Issa M.Y., Abdel-Ghafar S.F., Abdel-Hamid M.S., Jennings P., Zaki M.S.,
RA Sheridan E., Gleeson J.G.;
RT "Mutations in Spliceosomal Genes PPIL1 and PRP17 Cause Neurodegenerative
RT Pontocerebellar Hypoplasia with Microcephaly.";
RL Neuron 109:241-256(2021).
CC -!- FUNCTION: Involved in pre-mRNA splicing as component of the spliceosome
CC (PubMed:33220177). PPIases accelerate the folding of proteins. It
CC catalyzes the cis-trans isomerization of proline imidic peptide bonds
CC in oligopeptides (By similarity). Catalyzes prolyl peptide bond
CC isomerization in CDC40/PRP17 (By similarity). Plays an important role
CC in embryonic brain development; this function is independent of its
CC isomerase activity (PubMed:33220177). {ECO:0000250|UniProtKB:Q9Y3C6,
CC ECO:0000269|PubMed:33220177}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[protein]-peptidylproline (omega=180) = [protein]-
CC peptidylproline (omega=0); Xref=Rhea:RHEA:16237, Rhea:RHEA-
CC COMP:10747, Rhea:RHEA-COMP:10748, ChEBI:CHEBI:83833,
CC ChEBI:CHEBI:83834; EC=5.2.1.8;
CC Evidence={ECO:0000250|UniProtKB:Q9Y3C6};
CC -!- ACTIVITY REGULATION: Inhibited by Cyclosporin A.
CC {ECO:0000250|UniProtKB:Q9Y3C6}.
CC -!- SUBUNIT: Identified in the spliceosome C complex. Interacts with
CC SNW1/SKIP. Interacts with CDC40/PRP17; this interaction leads to CDC40
CC isomerization. Interacts with RBM22. {ECO:0000250|UniProtKB:Q9Y3C6}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9Y3C6}.
CC -!- DEVELOPMENTAL STAGE: Widely expressed in the developing cortex at 14.5
CC dpc. {ECO:0000269|PubMed:33220177}.
CC -!- DISRUPTION PHENOTYPE: Mutant mice, in which PPIL1 is truncated at
CC position 102, die before 12.5 dpc. {ECO:0000269|PubMed:33220177}.
CC -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family. PPIL1
CC subfamily. {ECO:0000305}.
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DR EMBL; AK004331; BAB23265.1; -; mRNA.
DR EMBL; AK150643; BAE29731.1; -; mRNA.
DR EMBL; AK151572; BAE30513.1; -; mRNA.
DR EMBL; BC058369; AAH58369.1; -; mRNA.
DR CCDS; CCDS28593.1; -.
DR RefSeq; NP_081121.1; NM_026845.4.
DR AlphaFoldDB; Q9D0W5; -.
DR BMRB; Q9D0W5; -.
DR SMR; Q9D0W5; -.
DR BioGRID; 213066; 18.
DR STRING; 10090.ENSMUSP00000024802; -.
DR iPTMnet; Q9D0W5; -.
DR PhosphoSitePlus; Q9D0W5; -.
DR EPD; Q9D0W5; -.
DR MaxQB; Q9D0W5; -.
DR PaxDb; Q9D0W5; -.
DR PRIDE; Q9D0W5; -.
DR ProteomicsDB; 291806; -.
DR Antibodypedia; 29729; 278 antibodies from 29 providers.
DR DNASU; 68816; -.
DR Ensembl; ENSMUST00000024802; ENSMUSP00000024802; ENSMUSG00000024007.
DR GeneID; 68816; -.
DR KEGG; mmu:68816; -.
DR UCSC; uc008bsm.1; mouse.
DR CTD; 51645; -.
DR MGI; MGI:1916066; Ppil1.
DR VEuPathDB; HostDB:ENSMUSG00000024007; -.
DR eggNOG; KOG0881; Eukaryota.
DR GeneTree; ENSGT00940000153189; -.
DR HOGENOM; CLU_012062_16_3_1; -.
DR InParanoid; Q9D0W5; -.
DR OMA; ELYNDHA; -.
DR OrthoDB; 1392223at2759; -.
DR PhylomeDB; Q9D0W5; -.
DR TreeFam; TF300200; -.
DR Reactome; R-MMU-72163; mRNA Splicing - Major Pathway.
DR BioGRID-ORCS; 68816; 27 hits in 77 CRISPR screens.
DR ChiTaRS; Ppil1; mouse.
DR PRO; PR:Q9D0W5; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q9D0W5; protein.
DR Bgee; ENSMUSG00000024007; Expressed in dorsal pancreas and 242 other tissues.
DR ExpressionAtlas; Q9D0W5; baseline and differential.
DR Genevisible; Q9D0W5; MM.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0071007; C:U2-type catalytic step 2 spliceosome; ISS:UniProtKB.
DR GO; GO:0016018; F:cyclosporin A binding; ISS:UniProtKB.
DR GO; GO:0097718; F:disordered domain specific binding; ISO:MGI.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; ISS:UniProtKB.
DR GO; GO:1990403; P:embryonic brain development; ISS:UniProtKB.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; ISS:UniProtKB.
DR GO; GO:0006457; P:protein folding; IEA:InterPro.
DR GO; GO:0000413; P:protein peptidyl-prolyl isomerization; ISS:UniProtKB.
DR Gene3D; 2.40.100.10; -; 1.
DR InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR InterPro; IPR024936; Cyclophilin-type_PPIase.
DR InterPro; IPR020892; Cyclophilin-type_PPIase_CS.
DR InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
DR InterPro; IPR044666; Cyclophilin_A-like.
DR PANTHER; PTHR45625; PTHR45625; 1.
DR Pfam; PF00160; Pro_isomerase; 1.
DR PIRSF; PIRSF001467; Peptidylpro_ismrse; 1.
DR PRINTS; PR00153; CSAPPISMRASE.
DR SUPFAM; SSF50891; SSF50891; 1.
DR PROSITE; PS00170; CSA_PPIASE_1; 1.
DR PROSITE; PS50072; CSA_PPIASE_2; 1.
PE 1: Evidence at protein level;
KW Isomerase; mRNA processing; mRNA splicing; Nucleus; Phosphoprotein;
KW Reference proteome; Rotamase; Spliceosome.
FT CHAIN 1..166
FT /note="Peptidyl-prolyl cis-trans isomerase-like 1"
FT /id="PRO_0000064165"
FT DOMAIN 10..164
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
FT BINDING 54..65
FT /ligand="cyclosporin A"
FT /ligand_id="ChEBI:CHEBI:4031"
FT /evidence="ECO:0000250"
FT BINDING 70..71
FT /ligand="cyclosporin A"
FT /ligand_id="ChEBI:CHEBI:4031"
FT /evidence="ECO:0000250"
FT BINDING 99..104
FT /ligand="cyclosporin A"
FT /ligand_id="ChEBI:CHEBI:4031"
FT /evidence="ECO:0000250"
FT BINDING 109..113
FT /ligand="cyclosporin A"
FT /ligand_id="ChEBI:CHEBI:4031"
FT /evidence="ECO:0000250"
FT BINDING 119
FT /ligand="cyclosporin A"
FT /ligand_id="ChEBI:CHEBI:4031"
FT /evidence="ECO:0000250"
FT BINDING 125
FT /ligand="cyclosporin A"
FT /ligand_id="ChEBI:CHEBI:4031"
FT /evidence="ECO:0000250"
FT MOD_RES 149
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y3C6"
FT MUTAGEN 55
FT /note="R->A: Loss of isomerase activity. No phenotype when
FT introduced in mice, animals are viable and fertile with no
FT microcephaly or defective cortical lamination; no splicing
FT defect."
FT /evidence="ECO:0000269|PubMed:33220177"
SQ SEQUENCE 166 AA; 18237 MW; A5C5B04FE29C52C9 CRC64;
MAAIPPDTWQ PPNVYLETSM GVIVLELYWK HAPKTCKNFA ELARRGYYNG TKFHRIIKDF
MIQGGDPTGT GRGGASIYGK QFEDELHPDL KFTGAGILAM ANAGPDTNGS QFFVTLAPTQ
WLDGKHTIFG RVCQGIGMVN RVGMVETNSQ DRPVDDVKIL KAYPSG
