FKBP2_EMENI
ID FKBP2_EMENI Reviewed; 135 AA.
AC Q5ATN7; C8VE36; Q3HV69;
DT 18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 96.
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 AltName: Full=Rotamase;
DE Flags: Precursor;
GN Name=fkbB; ORFNames=AN8343;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Cha M.-J., Kwon N.-J., Chae S.-K.;
RT "Rapamycin resistant mutations in fkbA encoding a FK506-binding protein of
RT Aspergillus nidulans.";
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
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 -!- ACTIVITY REGULATION: Inhibited by both FK506 and rapamycin.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000255|PROSITE-
CC ProRule:PRU10138}.
CC -!- SIMILARITY: Belongs to the FKBP-type PPIase family. FKBP2 subfamily.
CC {ECO:0000305}.
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DR EMBL; DQ192016; ABA39173.1; -; Genomic_DNA.
DR EMBL; AACD01000151; EAA66905.1; -; Genomic_DNA.
DR EMBL; BN001305; CBF80348.1; -; Genomic_DNA.
DR RefSeq; XP_681612.1; XM_676520.1.
DR AlphaFoldDB; Q5ATN7; -.
DR SMR; Q5ATN7; -.
DR STRING; 162425.CADANIAP00002809; -.
DR EnsemblFungi; CBF80348; CBF80348; ANIA_08343.
DR EnsemblFungi; EAA66905; EAA66905; AN8343.2.
DR GeneID; 2868823; -.
DR KEGG; ani:AN8343.2; -.
DR VEuPathDB; FungiDB:AN8343; -.
DR eggNOG; KOG0549; Eukaryota.
DR HOGENOM; CLU_013615_8_1_1; -.
DR InParanoid; Q5ATN7; -.
DR OMA; WAYGSRG; -.
DR OrthoDB; 1507309at2759; -.
DR Proteomes; UP000000560; Chromosome V.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IBA:GO_Central.
DR GO; GO:0097308; P:cellular response to farnesol; IEP:AspGD.
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; PS00014; ER_TARGET; 1.
DR PROSITE; PS50059; FKBP_PPIASE; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum; Isomerase; Reference proteome; Rotamase; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..135
FT /note="FK506-binding protein 2"
FT /id="PRO_0000233068"
FT DOMAIN 40..128
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00277"
FT MOTIF 132..135
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
SQ SEQUENCE 135 AA; 14572 MW; 594AC6EFC3A8DCF6 CRC64;
MRVPIITTLL TLALTGLSQA ASLGVETTHG VECNRKTTKG DTVKMHYRGT LAEDGSQFDA
SYDRGTPFKF KLGAGRVIKG WDEGLLDMCV GEKRTLTIPP EYGYGDRGIG PIPGGATLIF
QTELLEIEGV PKDEL
