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Peptidyl-prolyl cis-trans isomerase FKBP12 (PPIase FKBP12) (EC 5.2.1.8) (12 kDa FK506-binding protein) (12 kDa FKBP) (FK506-binding protein 12) (VfFKBP12) (FKBP-12) (Immunophilin FKBP12) (Rotamase)

 FKB12_VICFA             Reviewed;         112 AA.
O04287;
30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
01-JUL-1997, sequence version 1.
15-MAR-2017, entry version 67.
RecName: Full=Peptidyl-prolyl cis-trans isomerase FKBP12;
Short=PPIase FKBP12;
EC=5.2.1.8;
AltName: Full=12 kDa FK506-binding protein;
Short=12 kDa FKBP;
AltName: Full=FK506-binding protein 12;
Short=VfFKBP12;
AltName: Full=FKBP-12;
AltName: Full=Immunophilin FKBP12;
AltName: Full=Rotamase;
Name=FKBP12;
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], DISULFIDE BOND, AND INTERACTION WITH
FK506.
PubMed=9753776; DOI=10.1046/j.1365-313X.1998.00232.x;
Xu Q., Liang S., Kudla J., Luan S.;
"Molecular characterization of a plant FKBP12 that does not mediate
action of FK506 and rapamycin.";
Plant J. 15:511-519(1998).
-!- FUNCTION: PPIases accelerate the folding of proteins. It catalyzes
the cis-trans isomerization of proline imidic peptide bonds in
oligopeptides (By similarity). {ECO:0000250}.
-!- CATALYTIC ACTIVITY: Peptidylproline (omega=180) = peptidylproline
(omega=0).
-!- SUBUNIT: Interacts with FK506. {ECO:0000269|PubMed:9753776}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
-!- SIMILARITY: Belongs to the FKBP-type PPIase family. {ECO:0000305}.
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EMBL; U96925; AAB57848.1; -; mRNA.
PIR; T12197; T12197.
ProteinModelPortal; O04287; -.
SMR; O04287; -.
PRIDE; O04287; -.
GO; GO:0005737; C:cytoplasm; 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;
Cytoplasm; Disulfide bond; Isomerase; Rotamase.
CHAIN 1 112 Peptidyl-prolyl cis-trans isomerase
FKBP12.
/FTId=PRO_0000075301.
DOMAIN 19 112 PPIase FKBP-type. {ECO:0000255|PROSITE-
ProRule:PRU00277}.
DISULFID 26 80 {ECO:0000269|PubMed:9753776}.
SEQUENCE 112 AA; 12101 MW; 7B1311F74FD3DA7B CRC64;
MGVEKQIIRA GTGPNPSRGQ NVTVHCTGYG KNGDLSQKFW STKDPGQNPF TFKIGQGSVI
KGWDEGVLGM QLGEVARLRC SPDYAYGAGG FPAWGIQPNS VLEFEIEVLR AQ


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