PPIE_BOVIN
ID PPIE_BOVIN Reviewed; 301 AA.
AC A4FV72;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 17-APR-2007, sequence version 1.
DT 25-MAY-2022, entry version 81.
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=Rotamase E;
GN Name=PPIE;
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].
RC STRAIN=Hereford; TISSUE=Thalamus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
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; BC123818; AAI23819.1; -; mRNA.
DR RefSeq; NP_001091630.1; NM_001098161.1.
DR AlphaFoldDB; A4FV72; -.
DR BMRB; A4FV72; -.
DR SMR; A4FV72; -.
DR STRING; 9913.ENSBTAP00000055082; -.
DR PaxDb; A4FV72; -.
DR PeptideAtlas; A4FV72; -.
DR PRIDE; A4FV72; -.
DR GeneID; 787681; -.
DR KEGG; bta:787681; -.
DR CTD; 10450; -.
DR eggNOG; KOG0111; Eukaryota.
DR InParanoid; A4FV72; -.
DR OrthoDB; 1484092at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005737; C:cytoplasm; 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: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:0006457; P:protein folding; IBA:GO_Central.
DR GO; GO:0000413; P:protein peptidyl-prolyl isomerization; ISS:UniProtKB.
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 2: Evidence at transcript 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_0000327215"
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 107..137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 107..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 MOD_RES 119
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UNP9"
SQ SEQUENCE 301 AA; 33461 MW; C5A7F4E844F2DBC2 CRC64;
MATTKRVLYV GGLAEEVDDK VLHAAFIPFG DITDIQIPLD YETEKHRGFA FVEFELAEDA
AAAIDNMNES ELFGRTIRVN LAKPMRIKEG SSRPVWSDDD WLKKFSGKTL EENKEEEGSE
PPKVETQEGE PAVKKARSNP QVYMDIKIGN KPAGRIQMLL RSDVVPMTAE NFRCLCTHEK
GFGFKGSSFH RIIPQFMCQG GDFTNHNGTG GKSIYGKKFD DENFILKHTG PGLLSMANSG
PNTNGSQFFL TCDKTDWLDG KHVVFGEITD GLDVLRQIEA QGSKDGKPKQ KVIISDCGEY
V
