ID   FKB15_VICFA             Reviewed;         151 AA.
AC   Q41649;
DT   19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   16-JUN-2009, entry version 52.
DE   RecName: Full=FK506-binding protein 2;
DE            EC=5.2.1.8;
DE   AltName: Full=Peptidyl-prolyl cis-trans isomerase;
DE            Short=PPIase;
DE            Short=Rotamase;
DE   AltName: Full=15 kDa FKBP;
DE   AltName: Full=FKBP-15;
DE   Flags: Precursor;
GN   Name=FKBP15;
OS   Vicia faba (Broad bean).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC   rosids; eurosids I; Fabales; Fabaceae; Papilionoideae; Fabeae; Vicia.
OX   NCBI_TaxID=3906;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 23-56, AND
RP   CHARACTERIZATION.
RX   MEDLINE=96293457; PubMed=8692927; DOI=10.1073/pnas.93.14.6964;
RA   Luan S., Kudla J., Gruissem W., Schreiber S.L.;
RT   "Molecular characterization of a FKBP-type immunophilin from higher
RT   plants.";
RL   Proc. Natl. Acad. Sci. U.S.A. 93:6964-6969(1996).
CC   -!- FUNCTION: PPIases accelerate the folding of proteins. It catalyzes
CC       the cis-trans isomerization of proline imidic peptide bonds in
CC       oligopeptides.
CC   -!- CATALYTIC ACTIVITY: Peptidylproline (omega=180) = peptidylproline
CC       (omega=0).
CC   -!- ENZYME REGULATION: Inhibited by both FK506 and rapamycin.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen (Potential).
CC   -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC   -!- INDUCTION: By heat shock.
CC   -!- SIMILARITY: Belongs to the FKBP-type PPIase family. FKBP2
CC       subfamily.
CC   -!- SIMILARITY: Contains 1 PPIase FKBP-type domain.
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DR   EMBL; U52045; AAC49392.1; -; mRNA.
DR   PIR; T12090; T12090.
DR   HSSP; Q13451; 1KT0.
DR   BRENDA; 5.2.1.8; 30.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006457; P:protein folding; IEA:UniProtKB-KW.
DR   GO; GO:0006950; P:response to stress; IEA:UniProtKB-KW.
DR   InterPro; IPR001179; PPIase_FKBP.
DR   PANTHER; PTHR10516; PPIase_FKBP; 1.
DR   Pfam; PF00254; FKBP_C; 1.
DR   PROSITE; PS50059; FKBP_PPIASE; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Endoplasmic reticulum; Isomerase; Rotamase;
KW   Signal; Stress response.
FT   SIGNAL        1     22
FT   CHAIN        23    151       FK506-binding protein 2.
FT                                /FTId=PRO_0000025510.
FT   DOMAIN       49    137       PPIase FKBP-type.
FT   MOTIF       148    151       Prevents secretion from ER (Potential).
SQ   SEQUENCE   151 AA;  16224 MW;  0363CB99B20C5D19 CRC64;
     MKLFSIFLIF TIFIIASALV AAKSAADVTE LQIGVKYKPA SCEVQAHKGD KVKVHYRGKL
     TDGTVFDSSF ERNSPIDFEL GGGQVIKGWD QGLLGMCLGE KRKLKIPAKL GYGEQGSPPT
     IPGGATLIFD TELVGVNDKS LSEEKSTSSE L
//