ID H0YSQ7_TAEGU Unreviewed; 301 AA.
AC H0YSQ7;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 2.
DT 27-MAR-2024, entry version 80.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase E {ECO:0000256|ARBA:ARBA00021137, ECO:0000256|PIRNR:PIRNR001475};
DE Short=PPIase E {ECO:0000256|PIRNR:PIRNR001475};
DE EC=5.2.1.8 {ECO:0000256|ARBA:ARBA00013194, ECO:0000256|PIRNR:PIRNR001475};
GN Name=PPIE {ECO:0000313|Ensembl:ENSTGUP00000001318.2};
OS Taeniopygia guttata (Zebra finch) (Poephila guttata).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; Estrildidae;
OC Estrildinae; Taeniopygia.
OX NCBI_TaxID=59729 {ECO:0000313|Ensembl:ENSTGUP00000001318.2, ECO:0000313|Proteomes:UP000007754};
RN [1] {ECO:0000313|Ensembl:ENSTGUP00000001318.2, ECO:0000313|Proteomes:UP000007754}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20360741; DOI=10.1038/nature08819;
RA Warren W.C., Clayton D.F., Ellegren H., Arnold A.P., Hillier L.W.,
RA Kunstner A., Searle S., White S., Vilella A.J., Fairley S., Heger A.,
RA Kong L., Ponting C.P., Jarvis E.D., Mello C.V., Minx P., Lovell P.,
RA Velho T.A., Ferris M., Balakrishnan C.N., Sinha S., Blatti C., London S.E.,
RA Li Y., Lin Y.C., George J., Sweedler J., Southey B., Gunaratne P.,
RA Watson M., Nam K., Backstrom N., Smeds L., Nabholz B., Itoh Y., Whitney O.,
RA Pfenning A.R., Howard J., Volker M., Skinner B.M., Griffin D.K., Ye L.,
RA McLaren W.M., Flicek P., Quesada V., Velasco G., Lopez-Otin C.,
RA Puente X.S., Olender T., Lancet D., Smit A.F., Hubley R., Konkel M.K.,
RA Walker J.A., Batzer M.A., Gu W., Pollock D.D., Chen L., Cheng Z.,
RA Eichler E.E., Stapley J., Slate J., Ekblom R., Birkhead T., Burke T.,
RA Burt D., Scharff C., Adam I., Richard H., Sultan M., Soldatov A.,
RA Lehrach H., Edwards S.V., Yang S.P., Li X., Graves T., Fulton L.,
RA Nelson J., Chinwalla A., Hou S., Mardis E.R., Wilson R.K.;
RT "The genome of a songbird.";
RL Nature 464:757-762(2010).
RN [2] {ECO:0000313|Ensembl:ENSTGUP00000001318.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Catalyzes the cis-trans isomerization of proline imidic
CC peptide bonds in proteins. {ECO:0000256|PIRNR:PIRNR001475}.
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:0000256|ARBA:ARBA00000971,
CC ECO:0000256|PIRNR:PIRNR001475};
CC -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family. PPIase E
CC subfamily. {ECO:0000256|ARBA:ARBA00009483,
CC ECO:0000256|PIRNR:PIRNR001475}.
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DR AlphaFoldDB; H0YSQ7; -.
DR STRING; 59729.ENSTGUP00000001318; -.
DR Ensembl; ENSTGUT00000001331.2; ENSTGUP00000001318.2; ENSTGUG00000001276.2.
DR GeneTree; ENSGT00940000158790; -.
DR HOGENOM; CLU_012062_27_0_1; -.
DR InParanoid; H0YSQ7; -.
DR OrthoDB; 339082at2759; -.
DR TreeFam; TF313817; -.
DR Proteomes; UP000007754; Chromosome 23.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0016607; C:nuclear speck; IEA:Ensembl.
DR GO; GO:0071007; C:U2-type catalytic step 2 spliceosome; IEA:Ensembl.
DR GO; GO:0016018; F:cyclosporin A binding; IEA:Ensembl.
DR GO; GO:0003729; F:mRNA binding; IEA:Ensembl.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0008143; F:poly(A) binding; IEA:Ensembl.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IEA:Ensembl.
DR GO; GO:0045070; P:positive regulation of viral genome replication; IEA:Ensembl.
DR GO; GO:0006457; P:protein folding; IEA:InterPro.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:Ensembl.
DR CDD; cd01926; cyclophilin_ABH_like; 1.
DR CDD; cd12347; RRM_PPIE; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR Gene3D; 2.40.100.10; Cyclophilin-like; 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 PANTHER; PTHR11071; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE; 1.
DR PANTHER; PTHR11071:SF561; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE H; 1.
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; Cyclophilin-like; 1.
DR SUPFAM; SSF54928; RNA-binding domain, RBD; 1.
DR PROSITE; PS00170; CSA_PPIASE_1; 1.
DR PROSITE; PS50072; CSA_PPIASE_2; 1.
DR PROSITE; PS50102; RRM; 1.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|PIRNR:PIRNR001475};
KW Reference proteome {ECO:0000313|Proteomes:UP000007754};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW ProRule:PRU00176};
KW Rotamase {ECO:0000256|ARBA:ARBA00023110, ECO:0000256|PIRNR:PIRNR001475}.
FT DOMAIN 6..84
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT DOMAIN 143..299
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000259|PROSITE:PS50072"
FT REGION 111..138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 111..135
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 301 AA; 33344 MW; B2AC153D39C759DF CRC64;
MAATKRVLYV GGLAEEVDEK VLHAAFIPFG DITDIQIPLD YETEKHRGFA FVEFELAEDA
AAAIDNMNES ELFGRTIRVN LAKPMRIKEG SSRPVWSDDE WLKKFSGKTL EENKEEGGAE
APKAEAQEEE PPAKKSRVNP QVYMDIKIGN KPAGRLRILL RSDVVPMTAE NFRCLCTHEK
GFGFKGSSFH RIIPQFMCQA GDFTNHNGTG GKSIYGKKFD DENFILKHTG PGMVSMANSG
PNTNGSQFFI TCDKTDWLDG KHVVFGEVTE GMDVVREIEA QGTKDGKPKQ KVIISDCGEC
A
//
