PIN1_THEAN
ID PIN1_THEAN Reviewed; 142 AA.
AC Q4UG71;
DT 01-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 25-MAY-2022, entry version 70.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 {ECO:0000305};
DE Short=TaPIN1 {ECO:0000303|PubMed:25624101};
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; ORFNames=TA18945 {ECO:0000312|EMBL:CAI73918.1};
OS Theileria annulata.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Piroplasmida;
OC Theileriidae; Theileria.
OX NCBI_TaxID=5874;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ankara {ECO:0000312|Proteomes:UP000001950};
RX PubMed=15994557; DOI=10.1126/science.1110418;
RA Pain A., Renauld H., Berriman M., Murphy L., Yeats C.A., Weir W.,
RA Kerhornou A., Aslett M., Bishop R., Bouchier C., Cochet M., Coulson R.M.R.,
RA Cronin A., de Villiers E.P., Fraser A., Fosker N., Gardner M., Goble A.,
RA Griffiths-Jones S., Harris D.E., Katzer F., Larke N., Lord A., Maser P.,
RA McKellar S., Mooney P., Morton F., Nene V., O'Neil S., Price C.,
RA Quail M.A., Rabbinowitsch E., Rawlings N.D., Rutter S., Saunders D.,
RA Seeger K., Shah T., Squares R., Squares S., Tivey A., Walker A.R.,
RA Woodward J., Dobbelaere D.A.E., Langsley G., Rajandream M.A., McKeever D.,
RA Shiels B., Tait A., Barrell B.G., Hall N.;
RT "Genome of the host-cell transforming parasite Theileria annulata compared
RT with T. parva.";
RL Science 309:131-133(2005).
RN [2]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH HOST FBXW7, CATALYTIC
RP ACTIVITY, ACTIVITY REGULATION, AND MUTAGENESIS OF LYS-38 AND CYS-92.
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:0000269|PubMed:25624101}.
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 buparvaquone and juglone
CC anti-parasite drugs. Inhibited at lesser degree by the non-quinone
CC inhibitor dipentamethylene thiuram monosulphide (DTM).
CC {ECO:0000269|PubMed:25624101}.
CC -!- SUBUNIT: Interacts with host FBXW7; leading to FBXW7 autoubiquitination
CC and subsequent degradation. {ECO:0000269|PubMed:25624101}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:25624101}. Host
CC cytoplasm {ECO:0000269|PubMed:25624101}. Host nucleus
CC {ECO:0000269|PubMed:25624101}.
CC -!- MISCELLANEOUS: PIN1 harbors a single amino acid variation in a strain
CC resistant to buparvaquone (AC P0DMT5). {ECO:0000269|PubMed:25624101}.
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DR EMBL; CR940347; CAI73918.1; -; Genomic_DNA.
DR RefSeq; XP_954595.1; XM_949502.1.
DR AlphaFoldDB; Q4UG71; -.
DR SMR; Q4UG71; -.
DR DIP; DIP-61527N; -.
DR IntAct; Q4UG71; 3.
DR STRING; 5874.XP_954595.1; -.
DR GeneID; 3863623; -.
DR KEGG; tan:TA18945; -.
DR VEuPathDB; PiroplasmaDB:TA18945; -.
DR eggNOG; KOG3259; Eukaryota.
DR InParanoid; Q4UG71; -.
DR OMA; DEVQCLH; -.
DR OrthoDB; 1437969at2759; -.
DR Proteomes; UP000001950; Chromosome 1 part 1.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0030430; C:host cell cytoplasm; IDA:UniProtKB.
DR GO; GO:0042025; C:host cell nucleus; IDA:UniProtKB.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IDA:UniProtKB.
DR GO; GO:0044003; P:modulation by symbiont of host process; IDA:UniProtKB.
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; Oncogene; Reference proteome;
KW Rotamase; Secreted; Signal; Virulence.
FT SIGNAL 1..32
FT /evidence="ECO:0000255"
FT CHAIN 33..142
FT /note="Peptidyl-prolyl cis-trans isomerase NIMA-interacting
FT 1"
FT /evidence="ECO:0000255"
FT /id="PRO_0000432706"
FT DOMAIN 34..142
FT /note="PpiC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00278"
FT MUTAGEN 38
FT /note="K->A: Loss of peptidyl-prolyl cis/trans isomerase
FT activity."
FT /evidence="ECO:0000269|PubMed:25624101"
FT MUTAGEN 92
FT /note="C->A: Loss of peptidyl-prolyl cis/trans isomerase
FT activity."
FT /evidence="ECO:0000269|PubMed:25624101"
SQ SEQUENCE 142 AA; 16308 MW; 9E158179219E097C CRC64;
MIRNFLNFLW NNTSLRFLII NTIIFAMDKV RCAHLLLKHT GSRNPVNRNT GMAVTRTKEE
AVSEMKGYLE MLRKSDNLDQ EFRRLATAKS ECSSARKGGD LGFFDRNTMQ KPFTEASFKL
EVNEISDLVE TDSGVHLIYR IA
