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   03-AUG-2022, entry version 86.
DE   RecName: Full=FK506-binding protein 2;
DE            EC=5.2.1.8;
DE   AltName: Full=15 kDa FKBP;
DE   AltName: Full=FKBP-15;
DE   AltName: Full=Peptidyl-prolyl cis-trans isomerase;
DE            Short=PPIase;
DE   AltName: Full=Rotamase;
DE   Flags: Precursor;
GN   Name=FKBP15;
OS   Vicia faba (Broad bean) (Faba vulgaris).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; IRL clade; Fabeae; Vicia.
OX   NCBI_TaxID=3906;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 23-56, AND
RP   CHARACTERIZATION.
RX   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 the
CC       cis-trans isomerization of proline imidic peptide bonds in
CC       oligopeptides.
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: Inhibited by both FK506 and rapamycin.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC   -!- INDUCTION: By heat shock.
CC   -!- SIMILARITY: Belongs to the FKBP-type PPIase family. FKBP2 subfamily.
CC       {ECO:0000305}.
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DR   EMBL; U52045; AAC49392.1; -; mRNA.
DR   PIR; T12090; T12090.
DR   AlphaFoldDB; Q41649; -.
DR   SMR; Q41649; -.
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:0061077; P:chaperone-mediated protein folding; IEA:InterPro.
DR   GO; GO:0000413; P:protein peptidyl-prolyl isomerization; IEA:InterPro.
DR   Gene3D; 3.10.50.40; -; 1.
DR   InterPro; IPR044609; FKBP2/11.
DR   InterPro; IPR046357; PPIase_dom_sf.
DR   InterPro; IPR001179; PPIase_FKBP_dom.
DR   PANTHER; PTHR45779; PTHR45779; 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                   /evidence="ECO:0000269|PubMed:8692927"
FT   CHAIN           23..151
FT                   /note="FK506-binding protein 2"
FT                   /id="PRO_0000025510"
FT   DOMAIN          49..137
FT                   /note="PPIase FKBP-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00277"
FT   MOTIF           148..151
FT                   /note="Prevents secretion from ER"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   151 AA;  16224 MW;  0363CB99B20C5D19 CRC64;
     MKLFSIFLIF TIFIIASALV AAKSAADVTE LQIGVKYKPA SCEVQAHKGD KVKVHYRGKL
     TDGTVFDSSF ERNSPIDFEL GGGQVIKGWD QGLLGMCLGE KRKLKIPAKL GYGEQGSPPT
     IPGGATLIFD TELVGVNDKS LSEEKSTSSE L