PPIL1_BOVIN
ID PPIL1_BOVIN Reviewed; 166 AA.
AC Q5E992;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 118.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in pre-mRNA splicing as component of the
CC spliceosome. PPIases accelerate the folding of proteins. It catalyzes
CC the cis-trans isomerization of proline imidic peptide bonds in
CC oligopeptides. Catalyzes prolyl peptide bond isomerization in
CC CDC40/PRP17. Plays an important role in embryonic brain development;
CC this function is independent of its isomerase activity.
CC {ECO:0000250|UniProtKB:Q9Y3C6}.
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 -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family. PPIL1
CC subfamily. {ECO:0000305}.
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DR EMBL; BT021028; AAX09045.1; -; mRNA.
DR EMBL; BC102396; AAI02397.1; -; mRNA.
DR RefSeq; NP_001014869.1; NM_001014869.1.
DR AlphaFoldDB; Q5E992; -.
DR BMRB; Q5E992; -.
DR SMR; Q5E992; -.
DR STRING; 9913.ENSBTAP00000003071; -.
DR PaxDb; Q5E992; -.
DR PeptideAtlas; Q5E992; -.
DR PRIDE; Q5E992; -.
DR Ensembl; ENSBTAT00000003071; ENSBTAP00000003071; ENSBTAG00000002376.
DR GeneID; 508179; -.
DR KEGG; bta:508179; -.
DR CTD; 51645; -.
DR VEuPathDB; HostDB:ENSBTAG00000002376; -.
DR VGNC; VGNC:33201; PPIL1.
DR eggNOG; KOG0881; Eukaryota.
DR GeneTree; ENSGT00940000153189; -.
DR HOGENOM; CLU_012062_16_3_1; -.
DR InParanoid; Q5E992; -.
DR OMA; ELYNDHA; -.
DR OrthoDB; 1392223at2759; -.
DR TreeFam; TF300200; -.
DR Proteomes; UP000009136; Chromosome 23.
DR Bgee; ENSBTAG00000002376; Expressed in diaphragm and 104 other tissues.
DR ExpressionAtlas; Q5E992; baseline.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; IBA:GO_Central.
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: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 2: Evidence at transcript 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_0000247935"
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"
SQ SEQUENCE 166 AA; 18237 MW; 2872DC3336CD05E4 CRC64;
MAAIPPDSWQ PPNVYLETSM GIIVLELYWK HAPKTCKNFA ELARRGYYNG TKFHRIIKDF
MIQGGDPTGT GRGGASIYGK QFEDELHPDL KFTGAGILAM ANAGPDTNGS QFFVTLAPTQ
WLDGKHTIFG RVCQGIGMVN RVGMVETNSQ DRPVDDVKII KAYPSG
