ID   FKBP2_ASPOR             Reviewed;         134 AA.
AC   Q2UPT7;
DT   18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   03-AUG-2022, entry version 83.
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=fpr2; ORFNames=AO090005001515;
OS   Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=510516;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 42149 / RIB 40;
RX   PubMed=16372010; DOI=10.1038/nature04300;
RA   Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA   Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA   Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA   Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA   Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA   Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA   Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA   Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA   Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA   Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA   Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA   Kikuchi H.;
RT   "Genome sequencing and analysis of Aspergillus oryzae.";
RL   Nature 438:1157-1161(2005).
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; AP007151; BAE56428.1; -; Genomic_DNA.
DR   RefSeq; XP_001818430.1; XM_001818378.2.
DR   AlphaFoldDB; Q2UPT7; -.
DR   SMR; Q2UPT7; -.
DR   STRING; 510516.Q2UPT7; -.
DR   EnsemblFungi; BAE56428; BAE56428; AO090005001515.
DR   GeneID; 5990375; -.
DR   KEGG; aor:AO090005001515; -.
DR   VEuPathDB; FungiDB:AO090005001515; -.
DR   HOGENOM; CLU_013615_8_1_1; -.
DR   OMA; WAYGSRG; -.
DR   Proteomes; UP000006564; Chromosome 1.
DR   GO; GO:0005783; C:endoplasmic reticulum; 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; 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..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..134
FT                   /note="FK506-binding protein 2"
FT                   /id="PRO_0000233064"
FT   DOMAIN          39..127
FT                   /note="PPIase FKBP-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00277"
FT   MOTIF           131..134
FT                   /note="Prevents secretion from ER"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
SQ   SEQUENCE   134 AA;  14524 MW;  033183381DFD9825 CRC64;
     MRFSIFSTLL VSLATLSTAA ELGIEKTHEV ECTRKTVKGD TVQMHYKGTL QSDGSEFDSS
     YKRNSPLKFK VGSGMVIKGW DEGLLDMCIG EKRTLTIPPE YGYGSRGVGP IPGGATLIFE
     TELVGIDGVS KDEL