ID   FKB70_PINPS             Reviewed;          15 AA.
AC   P81104;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1998, sequence version 1.
DT   25-MAY-2022, entry version 55.
DE   RecName: Full=70 kDa peptidyl-prolyl isomerase;
DE            EC=5.2.1.8;
DE   AltName: Full=Cyclophilin;
DE   AltName: Full=PPIase;
DE   AltName: Full=Peptidyl-prolyl cis-trans isomerase;
DE   AltName: Full=S1205-06;
DE   Flags: Fragment;
OS   Pinus pinaster (Maritime pine).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Pinopsida; Pinidae; Conifers I; Pinales; Pinaceae; Pinus;
OC   Pinus subgen. Pinus.
OX   NCBI_TaxID=71647;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   TISSUE=Needle;
RA   Plomion C., Costa P., Bahrman N., Frigerio J.-M.;
RT   "Genetic analysis of needle proteins in maritime pine. 1. Mapping dominant
RT   and codominant protein markers assayed on diploid tissue, in a haploid-
RT   based genetic map.";
RL   Silvae Genet. 46:161-165(1997).
RN   [2]
RP   PROTEIN SEQUENCE.
RC   TISSUE=Needle;
RX   PubMed=10344291;
RX   DOI=10.1002/(sici)1522-2683(19990101)20:4/5<1098::aid-elps1098>3.0.co;2-z;
RA   Costa P., Pionneau C., Bauw G., Dubos C., Bahrman N., Kremer A.,
RA   Frigerio J.-M., Plomion C.;
RT   "Separation and characterization of needle and xylem maritime pine
RT   proteins.";
RL   Electrophoresis 20:1098-1108(1999).
CC   -!- FUNCTION: PPIases accelerate the folding of proteins during protein
CC       synthesis.
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   -!- SUBUNIT: This PPIase probably binds calmodulin. {ECO:0000250}.
CC   -!- MISCELLANEOUS: On the 2D-gel the determined pI of this protein is: 5.3,
CC       its MW is: 72 kDa.
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DR   GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Calmodulin-binding; Direct protein sequencing; Isomerase; Repeat; Rotamase.
FT   CHAIN           <1..>15
FT                   /note="70 kDa peptidyl-prolyl isomerase"
FT                   /id="PRO_0000075334"
FT   NON_TER         1
FT   NON_TER         15
SQ   SEQUENCE   15 AA;  1676 MW;  2B53999722277F3F CRC64;
     XGESWETPET GDEVE