PPIL3_MOUSE
ID PPIL3_MOUSE Reviewed; 161 AA.
AC Q9D6L8; Q812D2; Q9CY23;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase-like 3;
DE Short=PPIase;
DE EC=5.2.1.8;
DE AltName: Full=CYP10L;
DE AltName: Full=Cyclophilin-like protein PPIL3;
DE AltName: Full=Rotamase PPIL3;
GN Name=Ppil3; Synonyms=Cyp10l;
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 [MRNA] (ISOFORM 1).
RA Yu L.;
RL Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Liver, and Tongue;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=129; TISSUE=Brain, and Mammary tumor;
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Liver, 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 [5]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-61, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the
CC cis-trans isomerization of proline imidic peptide bonds in
CC oligopeptides. May be involved in pre-mRNA splicing (By similarity).
CC {ECO:0000250}.
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 -!- SUBUNIT: Identified in the spliceosome C complex. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9D6L8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9D6L8-2; Sequence=VSP_015469;
CC -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family. PPIL3
CC subfamily. {ECO:0000305}.
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DR EMBL; AF315803; AAO32944.1; -; mRNA.
DR EMBL; AK010207; BAB26768.1; -; mRNA.
DR EMBL; AK011000; BAB27319.1; -; mRNA.
DR EMBL; BC060993; AAH60993.1; -; mRNA.
DR EMBL; BC061645; AAH61645.1; -; mRNA.
DR CCDS; CCDS35579.1; -. [Q9D6L8-1]
DR CCDS; CCDS35580.1; -. [Q9D6L8-2]
DR RefSeq; NP_001272755.1; NM_001285826.1. [Q9D6L8-1]
DR RefSeq; NP_001272756.1; NM_001285827.1. [Q9D6L8-1]
DR RefSeq; NP_081627.1; NM_027351.3. [Q9D6L8-1]
DR RefSeq; NP_081650.2; NM_027374.3. [Q9D6L8-2]
DR AlphaFoldDB; Q9D6L8; -.
DR SMR; Q9D6L8; -.
DR BioGRID; 213923; 26.
DR IntAct; Q9D6L8; 1.
DR STRING; 10090.ENSMUSP00000080378; -.
DR iPTMnet; Q9D6L8; -.
DR PhosphoSitePlus; Q9D6L8; -.
DR EPD; Q9D6L8; -.
DR MaxQB; Q9D6L8; -.
DR PaxDb; Q9D6L8; -.
DR PeptideAtlas; Q9D6L8; -.
DR PRIDE; Q9D6L8; -.
DR ProteomicsDB; 291784; -. [Q9D6L8-1]
DR ProteomicsDB; 291785; -. [Q9D6L8-2]
DR Antibodypedia; 34922; 238 antibodies from 24 providers.
DR DNASU; 70225; -.
DR Ensembl; ENSMUST00000081677; ENSMUSP00000080378; ENSMUSG00000026035. [Q9D6L8-1]
DR Ensembl; ENSMUST00000114345; ENSMUSP00000109984; ENSMUSG00000026035. [Q9D6L8-2]
DR Ensembl; ENSMUST00000114348; ENSMUSP00000109988; ENSMUSG00000026035. [Q9D6L8-1]
DR Ensembl; ENSMUST00000117069; ENSMUSP00000112947; ENSMUSG00000026035. [Q9D6L8-1]
DR GeneID; 70225; -.
DR KEGG; mmu:70225; -.
DR UCSC; uc007bbv.2; mouse. [Q9D6L8-1]
DR CTD; 53938; -.
DR MGI; MGI:1917475; Ppil3.
DR VEuPathDB; HostDB:ENSMUSG00000026035; -.
DR eggNOG; KOG0884; Eukaryota.
DR GeneTree; ENSGT00940000153189; -.
DR HOGENOM; CLU_012062_16_3_1; -.
DR InParanoid; Q9D6L8; -.
DR OMA; VPFHRVM; -.
DR OrthoDB; 1392223at2759; -.
DR PhylomeDB; Q9D6L8; -.
DR TreeFam; TF352224; -.
DR Reactome; R-MMU-72163; mRNA Splicing - Major Pathway.
DR BioGRID-ORCS; 70225; 3 hits in 74 CRISPR screens.
DR ChiTaRS; Ppil3; mouse.
DR PRO; PR:Q9D6L8; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q9D6L8; protein.
DR Bgee; ENSMUSG00000026035; Expressed in facial nucleus and 220 other tissues.
DR ExpressionAtlas; Q9D6L8; baseline and differential.
DR Genevisible; Q9D6L8; MM.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; ISO:MGI.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IBA:GO_Central.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0006457; P:protein folding; IEA:InterPro.
DR GO; GO:0000413; P:protein peptidyl-prolyl isomerization; IBA:GO_Central.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
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 Acetylation; Alternative splicing; Isomerase; Methylation; mRNA processing;
KW mRNA splicing; Reference proteome; Rotamase; Spliceosome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9H2H8"
FT CHAIN 2..161
FT /note="Peptidyl-prolyl cis-trans isomerase-like 3"
FT /id="PRO_0000064167"
FT DOMAIN 2..154
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H2H8"
FT MOD_RES 61
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT VAR_SEQ 121..161
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_015469"
FT CONFLICT 23
FT /note="K -> R (in Ref. 1; AAO32944)"
FT /evidence="ECO:0000305"
FT CONFLICT 103
FT /note="I -> V (in Ref. 2; BAB27319)"
FT /evidence="ECO:0000305"
FT CONFLICT 144
FT /note="L -> F (in Ref. 1; AAO32944)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 161 AA; 18128 MW; 913ED4C8CB839E2C CRC64;
MSVTLHTDVG DIKIEVFCER TPKTCENFLA LCASNYYNGC VFHRNIKGFM VQTGDPTGTG
RGGSSIWAKK FEDEYSEYLK HNVRGVVSMA NNGPNTNGSQ FFITYGKQPH LDMKYTVFGK
VIDGLETLDE LEKLPVNEKT YRPLNDVHIK DITIHANPFA Q
