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FK506-binding protein 2 (EC 5.2.1.8) (15 kDa FKBP) (FKBP-15) (Peptidyl-prolyl cis-trans isomerase) (PPIase) (Rotamase)

 FKB15_VICFA             Reviewed;         151 AA.
Q41649;
19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
15-MAR-2017, entry version 77.
RecName: Full=FK506-binding protein 2;
EC=5.2.1.8;
AltName: Full=15 kDa FKBP;
AltName: Full=FKBP-15;
AltName: Full=Peptidyl-prolyl cis-trans isomerase;
Short=PPIase;
AltName: Full=Rotamase;
Flags: Precursor;
Name=FKBP15;
Vicia faba (Broad bean) (Faba vulgaris).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; fabids; Fabales; Fabaceae; Papilionoideae;
Fabeae; Vicia.
NCBI_TaxID=3906;
[1]
NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 23-56, AND
CHARACTERIZATION.
PubMed=8692927; DOI=10.1073/pnas.93.14.6964;
Luan S., Kudla J., Gruissem W., Schreiber S.L.;
"Molecular characterization of a FKBP-type immunophilin from higher
plants.";
Proc. Natl. Acad. Sci. U.S.A. 93:6964-6969(1996).
-!- FUNCTION: PPIases accelerate the folding of proteins. It catalyzes
the cis-trans isomerization of proline imidic peptide bonds in
oligopeptides.
-!- CATALYTIC ACTIVITY: Peptidylproline (omega=180) = peptidylproline
(omega=0).
-!- ENZYME REGULATION: Inhibited by both FK506 and rapamycin.
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000305}.
-!- TISSUE SPECIFICITY: Ubiquitously expressed.
-!- INDUCTION: By heat shock.
-!- SIMILARITY: Belongs to the FKBP-type PPIase family. FKBP2
subfamily. {ECO:0000305}.
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EMBL; U52045; AAC49392.1; -; mRNA.
PIR; T12090; T12090.
ProteinModelPortal; Q41649; -.
SMR; Q41649; -.
PRIDE; Q41649; -.
GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
InterPro; IPR023566; PPIase_FKBP.
InterPro; IPR001179; PPIase_FKBP_dom.
PANTHER; PTHR10516; PTHR10516; 1.
Pfam; PF00254; FKBP_C; 1.
PROSITE; PS50059; FKBP_PPIASE; 1.
1: Evidence at protein level;
Direct protein sequencing; Endoplasmic reticulum; Isomerase; Rotamase;
Signal; Stress response.
SIGNAL 1 22 {ECO:0000269|PubMed:8692927}.
CHAIN 23 151 FK506-binding protein 2.
/FTId=PRO_0000025510.
DOMAIN 49 137 PPIase FKBP-type. {ECO:0000255|PROSITE-
ProRule:PRU00277}.
MOTIF 148 151 Prevents secretion from ER.
{ECO:0000255}.
SEQUENCE 151 AA; 16224 MW; 0363CB99B20C5D19 CRC64;
MKLFSIFLIF TIFIIASALV AAKSAADVTE LQIGVKYKPA SCEVQAHKGD KVKVHYRGKL
TDGTVFDSSF ERNSPIDFEL GGGQVIKGWD QGLLGMCLGE KRKLKIPAKL GYGEQGSPPT
IPGGATLIFD TELVGVNDKS LSEEKSTSSE L


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