ID   MIP_TRYCR               Reviewed;         196 AA.
AC   Q09734;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   25-MAY-2022, entry version 98.
DE   RecName: Full=Macrophage infectivity potentiator;
DE            EC=5.2.1.8;
DE   AltName: Full=Peptidyl-prolyl cis-trans isomerase;
DE            Short=PPIase;
DE   AltName: Full=Rotamase;
DE   Flags: Precursor;
GN   Name=MIP;
OS   Trypanosoma cruzi.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Trypanosoma; Schizotrypanum.
OX   NCBI_TaxID=5693;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Y;
RX   PubMed=7540135; DOI=10.1002/j.1460-2075.1995.tb07245.x;
RA   Moro A., Ruiz-Cabello F., Fernandez-Cano A., Stock R.P., Gonzalez A.;
RT   "Secretion by Trypanosoma cruzi of a peptidyl-prolyl cis-trans isomerase
RT   involved in cell infection.";
RL   EMBO J. 14:2483-2490(1995).
CC   -!- FUNCTION: Essential virulence factor associated with macrophage
CC       infectivity. Exhibits PPIase activity.
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   -!- ACTIVITY REGULATION: Strongly inhibited by FK506 and L-685,818.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space.
CC   -!- SIMILARITY: Belongs to the FKBP-type PPIase family. {ECO:0000305}.
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DR   EMBL; X69655; CAA49346.1; -; Genomic_DNA.
DR   PIR; S55332; S55332.
DR   PDB; 1JVW; X-ray; 1.70 A; A=30-196.
DR   PDBsum; 1JVW; -.
DR   AlphaFoldDB; Q09734; -.
DR   SMR; Q09734; -.
DR   VEuPathDB; TriTrypDB:BCY84_18529; -.
DR   VEuPathDB; TriTrypDB:C3747_2g288; -.
DR   VEuPathDB; TriTrypDB:C4B63_4g508; -.
DR   VEuPathDB; TriTrypDB:TcBrA4_0086400; -.
DR   VEuPathDB; TriTrypDB:TcCL_NonESM01613; -.
DR   VEuPathDB; TriTrypDB:TcCLB.508323.84; -.
DR   VEuPathDB; TriTrypDB:TcCLB.508897.110; -.
DR   VEuPathDB; TriTrypDB:TcG_00148; -.
DR   VEuPathDB; TriTrypDB:TcYC6_0113560; -.
DR   EvolutionaryTrace; Q09734; -.
DR   GO; GO:0005615; C:extracellular space; 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; IPR001179; PPIase_FKBP_dom.
DR   Pfam; PF00254; FKBP_C; 1.
DR   PROSITE; PS50059; FKBP_PPIASE; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Isomerase; Rotamase; Secreted; Signal; Virulence.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000255"
FT   CHAIN           30..196
FT                   /note="Macrophage infectivity potentiator"
FT                   /id="PRO_0000025535"
FT   DOMAIN          85..171
FT                   /note="PPIase FKBP-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00277"
FT   HELIX           36..57
FT                   /evidence="ECO:0007829|PDB:1JVW"
FT   STRAND          61..63
FT                   /evidence="ECO:0007829|PDB:1JVW"
FT   STRAND          69..74
FT                   /evidence="ECO:0007829|PDB:1JVW"
FT   STRAND          88..95
FT                   /evidence="ECO:0007829|PDB:1JVW"
FT   STRAND          101..104
FT                   /evidence="ECO:0007829|PDB:1JVW"
FT   HELIX           105..108
FT                   /evidence="ECO:0007829|PDB:1JVW"
FT   STRAND          112..114
FT                   /evidence="ECO:0007829|PDB:1JVW"
FT   HELIX           116..118
FT                   /evidence="ECO:0007829|PDB:1JVW"
FT   HELIX           121..127
FT                   /evidence="ECO:0007829|PDB:1JVW"
FT   STRAND          135..140
FT                   /evidence="ECO:0007829|PDB:1JVW"
FT   HELIX           142..144
FT                   /evidence="ECO:0007829|PDB:1JVW"
FT   TURN            145..149
FT                   /evidence="ECO:0007829|PDB:1JVW"
FT   STRAND          151..155
FT                   /evidence="ECO:0007829|PDB:1JVW"
FT   STRAND          161..170
FT                   /evidence="ECO:0007829|PDB:1JVW"
FT   HELIX           171..173
FT                   /evidence="ECO:0007829|PDB:1JVW"
FT   HELIX           179..191
FT                   /evidence="ECO:0007829|PDB:1JVW"
SQ   SEQUENCE   196 AA;  22136 MW;  40ACD50B2ED4AFA3 CRC64;
     MHRENYFSKI AFCLLGVLFL SCITSVQTVS GDAASHEERM NNYRKRVGRL FMEQKAAQPD
     AVKLPSGLVF QRIARGSGKR APAIDDKCEV HYTGRLRDGT VFDSSRERGK PTTFRPNEVI
     KGWTEALQLM REGDRWRLFI PYDLAYGVTG GGGMIPPYSP LEFDVELISI KDGGKGRTAE
     EVDEILRKAE EDREDM