ID   PPIL3_CHICK             Reviewed;         161 AA.
AC   Q5ZLV2;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=Peptidyl-prolyl cis-trans isomerase-like 3;
DE            Short=PPIase;
DE            EC=5.2.1.8;
DE   AltName: Full=Cyclophilin-like protein PPIL3;
DE   AltName: Full=Rotamase PPIL3;
GN   Name=PPIL3; ORFNames=RCJMB04_4l15;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=CB; TISSUE=Bursa of Fabricius;
RX   PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA   Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA   Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA   Hayashizaki Y., Buerstedde J.-M.;
RT   "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT   function analysis.";
RL   Genome Biol. 6:R6.1-R6.9(2005).
CC   -!- FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the
CC       cis-trans isomerization of proline imidic peptide bonds in
CC       oligopeptides.
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   -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family. PPIL3
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AJ719632; CAG31291.1; -; mRNA.
DR   RefSeq; NP_001008475.1; NM_001008475.1.
DR   AlphaFoldDB; Q5ZLV2; -.
DR   SMR; Q5ZLV2; -.
DR   STRING; 9031.ENSGALP00000013375; -.
DR   PaxDb; Q5ZLV2; -.
DR   Ensembl; ENSGALT00000013390; ENSGALP00000013375; ENSGALG00000008228.
DR   Ensembl; ENSGALT00000103811; ENSGALP00000070689; ENSGALG00000008228.
DR   GeneID; 424075; -.
DR   KEGG; gga:424075; -.
DR   CTD; 53938; -.
DR   VEuPathDB; HostDB:geneid_424075; -.
DR   eggNOG; KOG0884; Eukaryota.
DR   GeneTree; ENSGT00940000153189; -.
DR   HOGENOM; CLU_012062_16_3_1; -.
DR   InParanoid; Q5ZLV2; -.
DR   OMA; VPFHRVM; -.
DR   OrthoDB; 1392223at2759; -.
DR   PhylomeDB; Q5ZLV2; -.
DR   TreeFam; TF352224; -.
DR   Reactome; R-GGA-72163; mRNA Splicing - Major Pathway.
DR   PRO; PR:Q5ZLV2; -.
DR   Proteomes; UP000000539; Chromosome 7.
DR   Bgee; ENSGALG00000008228; Expressed in lung and 13 other tissues.
DR   GO; GO:0071013; C:catalytic step 2 spliceosome; IBA:GO_Central.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IBA:GO_Central.
DR   GO; GO:0006457; P:protein folding; IEA:InterPro.
DR   GO; GO:0000413; P:protein peptidyl-prolyl isomerization; IBA:GO_Central.
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; Reference proteome; Rotamase.
FT   CHAIN           1..161
FT                   /note="Peptidyl-prolyl cis-trans isomerase-like 3"
FT                   /id="PRO_0000064169"
FT   DOMAIN          1..154
FT                   /note="PPIase cyclophilin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
SQ   SEQUENCE   161 AA;  18052 MW;  19115ED5EA3ABA21 CRC64;
     MAVTLHTDVG DIKIELFCER TPKTCENFLA LCASNYYNGC VFHRNIKGFM VQTGDPLGTG
     KGGTSIWGKK FEDEFSEYLK HSVRGVVSMA NNGPNTNGSQ FFITYGKQPH LDMKYTVFGK
     VIDGLETLDE LEKLPVNEKT YRPLNDVHIK DITIHANPFA L