PPIE_MOUSE
ID PPIE_MOUSE Reviewed; 301 AA.
AC Q9QZH3; Q9D8C0;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 26-SEP-2003, sequence version 2.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase E;
DE Short=PPIase E;
DE EC=5.2.1.8 {ECO:0000250|UniProtKB:Q9UNP9};
DE AltName: Full=Cyclophilin E;
DE AltName: Full=Cyclophilin-33;
DE AltName: Full=Rotamase E;
GN Name=Ppie; Synonyms=Cyp33 {ECO:0000303|Ref.3};
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=Small intestine;
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 TISSUE=Eye;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 4-301.
RA Anderson M.S., Diaz M.O.;
RT "Cyp33: a new family of cyclophilins.";
RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart, Liver, Lung, Pancreas, 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).
CC -!- FUNCTION: Involved in pre-mRNA splicing as component of the
CC spliceosome. Combines RNA-binding and PPIase activities. Binds mRNA and
CC has a preference for single-stranded RNA molecules with poly-A and
CC poly-U stretches, suggesting it binds to the poly(A)-region in the 3'-
CC UTR of mRNA molecules. Catalyzes the cis-trans isomerization of proline
CC imidic peptide bonds in proteins. Inhibits KMT2A activity; this
CC requires proline isomerase activity. {ECO:0000250|UniProtKB:Q9UNP9}.
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:Q9UNP9};
CC -!- SUBUNIT: Identified in the spliceosome C complex. Component of the XAB2
CC complex, a multimeric protein complex composed of XAB2, PRPF19, AQR,
CC ZNF830, ISY1, and PPIE. Identified in a pentameric intron-binding (IB)
CC complex composed of AQR, XAB2, ISY1, ZNF830 and PPIE that is
CC incorporated into the spliceosome as a preassembled complex. The IB
CC complex does not contain PRPF19. Interacts (via RNA-binding domain)
CC with KMT2A (via the third PHD-type zinc-finger).
CC {ECO:0000250|UniProtKB:Q9UNP9}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9UNP9}.
CC -!- DOMAIN: The RRM domain mediates both interaction with RNA and with
CC KMT2A (via the third PHD-type zinc-finger), but has much higher
CC affinity for the KMT2A PHD-type zinc-finger.
CC {ECO:0000250|UniProtKB:Q9UNP9}.
CC -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family. PPIase E
CC subfamily. {ECO:0000305}.
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DR EMBL; AK008177; BAB25512.1; -; mRNA.
DR EMBL; BC045154; AAH45154.1; -; mRNA.
DR EMBL; AF182825; AAF01030.1; -; mRNA.
DR CCDS; CCDS18610.1; -.
DR RefSeq; NP_062362.1; NM_019489.5.
DR AlphaFoldDB; Q9QZH3; -.
DR BMRB; Q9QZH3; -.
DR SMR; Q9QZH3; -.
DR BioGRID; 207784; 19.
DR STRING; 10090.ENSMUSP00000030404; -.
DR iPTMnet; Q9QZH3; -.
DR PhosphoSitePlus; Q9QZH3; -.
DR REPRODUCTION-2DPAGE; IPI00111343; -.
DR EPD; Q9QZH3; -.
DR MaxQB; Q9QZH3; -.
DR PaxDb; Q9QZH3; -.
DR PeptideAtlas; Q9QZH3; -.
DR PRIDE; Q9QZH3; -.
DR ProteomicsDB; 289378; -.
DR Antibodypedia; 17854; 275 antibodies from 30 providers.
DR DNASU; 56031; -.
DR Ensembl; ENSMUST00000030404; ENSMUSP00000030404; ENSMUSG00000028651.
DR GeneID; 56031; -.
DR KEGG; mmu:56031; -.
DR UCSC; uc008uow.1; mouse.
DR CTD; 10450; -.
DR MGI; MGI:1917118; Ppie.
DR VEuPathDB; HostDB:ENSMUSG00000028651; -.
DR eggNOG; KOG0111; Eukaryota.
DR GeneTree; ENSGT00940000158790; -.
DR HOGENOM; CLU_012062_27_0_1; -.
DR InParanoid; Q9QZH3; -.
DR OMA; KIVIYAC; -.
DR OrthoDB; 1484092at2759; -.
DR PhylomeDB; Q9QZH3; -.
DR TreeFam; TF313817; -.
DR Reactome; R-MMU-6781823; Formation of TC-NER Pre-Incision Complex.
DR Reactome; R-MMU-6782135; Dual incision in TC-NER.
DR Reactome; R-MMU-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR Reactome; R-MMU-72163; mRNA Splicing - Major Pathway.
DR BioGRID-ORCS; 56031; 23 hits in 76 CRISPR screens.
DR ChiTaRS; Ppie; mouse.
DR PRO; PR:Q9QZH3; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q9QZH3; protein.
DR Bgee; ENSMUSG00000028651; Expressed in ventricular zone and 216 other tissues.
DR Genevisible; Q9QZH3; MM.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0016607; C:nuclear speck; 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:0003729; F:mRNA binding; ISS:UniProtKB.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; ISS:UniProtKB.
DR GO; GO:0008143; F:poly(A) binding; ISS:UniProtKB.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; ISS:UniProtKB.
DR GO; GO:0045070; P:positive regulation of viral genome replication; ISO:MGI.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR GO; GO:0000413; P:protein peptidyl-prolyl isomerization; ISS:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISO:MGI.
DR CDD; cd12347; RRM_PPIE; 1.
DR Gene3D; 2.40.100.10; -; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR InterPro; IPR020892; Cyclophilin-type_PPIase_CS.
DR InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR016304; PPIE.
DR InterPro; IPR034168; PPIE_RRM.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR Pfam; PF00160; Pro_isomerase; 1.
DR Pfam; PF00076; RRM_1; 1.
DR PIRSF; PIRSF001475; PPI_cyclophilin_E; 1.
DR PRINTS; PR00153; CSAPPISMRASE.
DR SMART; SM00360; RRM; 1.
DR SUPFAM; SSF50891; SSF50891; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS00170; CSA_PPIASE_1; 1.
DR PROSITE; PS50072; CSA_PPIASE_2; 1.
DR PROSITE; PS50102; RRM; 1.
PE 1: Evidence at protein level;
KW Isomerase; mRNA processing; mRNA splicing; Nucleus; Phosphoprotein;
KW Reference proteome; RNA-binding; Rotamase; Spliceosome.
FT CHAIN 1..301
FT /note="Peptidyl-prolyl cis-trans isomerase E"
FT /id="PRO_0000064158"
FT DOMAIN 5..83
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 143..299
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
FT REGION 110..141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 110..132
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 91
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UNP9"
FT MOD_RES 97
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UNP9"
FT CONFLICT 62
FT /note="A -> P (in Ref. 3; AAF01030)"
FT /evidence="ECO:0000305"
FT CONFLICT 241
FT /note="P -> S (in Ref. 3; AAF01030)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 301 AA; 33449 MW; 856F7AE7F721B219 CRC64;
MATTKRVLYV GGLAEEVDDK VLHAAFIPFG DITDIQIPLD YETEKHRGFA FVEFELAEDA
AAAIDNMNES ELFGRTIRVN LAKPMRIKEG SSRPVWSDDD WLKKFSGKTL EENKEEEGPE
PPKAEAQEGE PTAKKARSNP QVYMDIKIGN KPAGRIQMLL RSDVVPMTAE NFRCLCTHEK
GFGFKGSSFH RIIPQFMCQG GDFTNHNGTG GKSIYGKKFD DENFILKHTG PGLLSMANSG
PNTNGSQFFL TCDKTDWLDG KHVVFGEVTE GLDVLRQIEA QGSKDGKPKQ KVMIADCGEY
M
