PIN1B_THEAN
ID PIN1B_THEAN Reviewed; 142 AA.
AC P0DMT5;
DT 01-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-2015, sequence version 1.
DT 25-MAY-2022, entry version 17.
DE RecName: Full=Buparvaquone-resistant peptidyl-prolyl cis-trans isomerase NIMA-interacting 1;
DE EC=5.2.1.8 {ECO:0000269|PubMed:25624101};
DE AltName: Full=Peptidyl-prolyl cis-trans isomerase Pin1;
DE Short=PPIase Pin1;
DE AltName: Full=Rotamase Pin1;
DE Flags: Precursor;
GN Name=PIN1;
OS Theileria annulata.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Piroplasmida;
OC Theileriidae; Theileria.
OX NCBI_TaxID=5874;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], CATALYTIC ACTIVITY, AND ACTIVITY
RP REGULATION.
RX PubMed=25624101; DOI=10.1038/nature14044;
RA Marsolier J., Perichon M., DeBarry J.D., Villoutreix B.O., Chluba J.,
RA Lopez T., Garrido C., Zhou X.Z., Lu K.P., Fritsch L., Ait-Si-Ali S.,
RA Mhadhbi M., Medjkane S., Weitzman J.B.;
RT "Theileria parasites secrete a prolyl isomerase to maintain host leukocyte
RT transformation.";
RL Nature 520:378-382(2015).
CC -!- FUNCTION: Peptidyl-prolyl cis/trans isomerase (PPIase) that acts as a
CC key virulence factor by promoting host leukocyte transformation. Binds
CC to and isomerizes specific phosphorylated Ser/Thr-Pro (pSer/Thr-Pro)
CC motifs in a subset of proteins, resulting in conformational changes in
CC the proteins. Promotes host leukocyte transformation by binding to
CC phosphorylated host FBXW7, disrupting dimerization and promoting FBXW7
CC autoubiquitination and subsequent degradation. Degradation of host
CC FBXW7, leads to stabilization of JUN, which promotes cell
CC transformation. {ECO:0000250|UniProtKB:Q4UG71}.
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:0000269|PubMed:25624101};
CC -!- ACTIVITY REGULATION: Directly inhibited by juglone anti-parasite drug.
CC Not inhibited by buparvaquone anti-parasite drug.
CC {ECO:0000269|PubMed:25624101}.
CC -!- SUBUNIT: Interacts with host FBXW7; leading to FBXW7 autoubiquitination
CC and subsequent degradation. {ECO:0000250|UniProtKB:Q4UG71}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q4UG71}. Host
CC cytoplasm {ECO:0000250|UniProtKB:Q4UG71}. Host nucleus
CC {ECO:0000250|UniProtKB:Q4UG71}.
CC -!- MISCELLANEOUS: PIN1 harbors a single amino acid variation in strains
CC sensitive to buparvaquone (AC Q4UG71). {ECO:0000250|UniProtKB:Q4UG71}.
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DR AlphaFoldDB; P0DMT5; -.
DR SMR; P0DMT5; -.
DR PRIDE; P0DMT5; -.
DR VEuPathDB; PiroplasmaDB:TA18945; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.10.50.40; -; 1.
DR InterPro; IPR046357; PPIase_dom_sf.
DR InterPro; IPR000297; PPIase_PpiC.
DR Pfam; PF00639; Rotamase; 1.
DR PROSITE; PS50198; PPIC_PPIASE_2; 1.
PE 1: Evidence at protein level;
KW Host cytoplasm; Host nucleus; Isomerase; Rotamase; Secreted; Signal;
KW Virulence.
FT SIGNAL 1..32
FT /evidence="ECO:0000255"
FT CHAIN 33..142
FT /note="Buparvaquone-resistant peptidyl-prolyl cis-trans
FT isomerase NIMA-interacting 1"
FT /evidence="ECO:0000255"
FT /id="PRO_0000432707"
FT DOMAIN 34..142
FT /note="PpiC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00278"
SQ SEQUENCE 142 AA; 16334 MW; 9E058069309F197D CRC64;
MIRNFLNFLW NNTSLRFLII NTIIFAMDKV RCAHLLLKHT GSRNPVNRNT GMPVTRTKEE
AVSEMKGYLE MLRKSDNLDQ EFRRLATAKS ECSSARKGGD LGFFDRNTMQ KPFTEASFKL
EVNEISDLVE TDSGVHLIYR IA
