FKB12_VICFA
ID FKB12_VICFA Reviewed; 112 AA.
AC O04287;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 25-MAY-2022, entry version 76.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase FKBP12;
DE Short=PPIase FKBP12;
DE EC=5.2.1.8;
DE AltName: Full=12 kDa FK506-binding protein;
DE Short=12 kDa FKBP;
DE AltName: Full=FK506-binding protein 12;
DE Short=VfFKBP12;
DE AltName: Full=FKBP-12;
DE AltName: Full=Immunophilin FKBP12;
DE AltName: Full=Rotamase;
GN Name=FKBP12;
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], DISULFIDE BOND, AND INTERACTION WITH FK506.
RX PubMed=9753776; DOI=10.1046/j.1365-313x.1998.00232.x;
RA Xu Q., Liang S., Kudla J., Luan S.;
RT "Molecular characterization of a plant FKBP12 that does not mediate action
RT of FK506 and rapamycin.";
RL Plant J. 15:511-519(1998).
CC -!- FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the
CC cis-trans isomerization of proline imidic peptide bonds in
CC oligopeptides (By similarity). {ECO:0000250}.
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: Interacts with FK506. {ECO:0000269|PubMed:9753776}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the FKBP-type PPIase family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U96925; AAB57848.1; -; mRNA.
DR PIR; T12197; T12197.
DR AlphaFoldDB; O04287; -.
DR SMR; O04287; -.
DR PRIDE; O04287; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.10.50.40; -; 1.
DR InterPro; IPR046357; PPIase_dom_sf.
DR InterPro; IPR001179; PPIase_FKBP_dom.
DR Pfam; PF00254; FKBP_C; 1.
DR PROSITE; PS50059; FKBP_PPIASE; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Disulfide bond; Isomerase; Rotamase.
FT CHAIN 1..112
FT /note="Peptidyl-prolyl cis-trans isomerase FKBP12"
FT /id="PRO_0000075301"
FT DOMAIN 19..112
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00277"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 26..80
FT /evidence="ECO:0000269|PubMed:9753776"
SQ SEQUENCE 112 AA; 12101 MW; 7B1311F74FD3DA7B CRC64;
MGVEKQIIRA GTGPNPSRGQ NVTVHCTGYG KNGDLSQKFW STKDPGQNPF TFKIGQGSVI
KGWDEGVLGM QLGEVARLRC SPDYAYGAGG FPAWGIQPNS VLEFEIEVLR AQ
