FKBP2_CRYNB
ID FKBP2_CRYNB Reviewed; 141 AA.
AC P0CP97; Q55SE5; Q5KGT9;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 36.
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; OrderedLocusNames=CNBE2370;
OS Cryptococcus neoformans var. neoformans serotype D (strain B-3501A)
OS (Filobasidiella neoformans).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus;
OC Cryptococcus neoformans species complex.
OX NCBI_TaxID=283643;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B-3501A;
RX PubMed=15653466; DOI=10.1126/science.1103773;
RA Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D.,
RA Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E.,
RA Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A.,
RA Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C.,
RA Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I., Kwon-Chung K.J.,
RA Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A.,
RA Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E.,
RA Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A.,
RA Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W.,
RA Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
RT "The genome of the basidiomycetous yeast and human pathogen Cryptococcus
RT neoformans.";
RL Science 307:1321-1324(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:0000250}.
CC -!- SIMILARITY: Belongs to the FKBP-type PPIase family. FKBP2 subfamily.
CC {ECO:0000305}.
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DR EMBL; AAEY01000024; EAL20876.1; -; Genomic_DNA.
DR RefSeq; XP_775523.1; XM_770430.1.
DR AlphaFoldDB; P0CP97; -.
DR SMR; P0CP97; -.
DR EnsemblFungi; EAL20876; EAL20876; CNBE2370.
DR GeneID; 4936247; -.
DR KEGG; cnb:CNBE2370; -.
DR VEuPathDB; FungiDB:CNBE2370; -.
DR HOGENOM; CLU_013615_8_2_1; -.
DR Proteomes; UP000001435; Chromosome 5.
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; PS50059; FKBP_PPIASE; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum; Isomerase; Rotamase; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..141
FT /note="FK506-binding protein 2"
FT /id="PRO_0000410208"
FT DOMAIN 45..134
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00277"
SQ SEQUENCE 141 AA; 15727 MW; 2E3801791393A56F CRC64;
MYHPKALIIA LLFTLSLILA AKSAEQLQIG VKYVPEECPV KSRKGDRLSM HYTGTLAKDG
SKFDSSLDRN RPFEFTLGAG QVIKGWDQGL LDMCISEKRK LTIPSHLAYG ERGHPPVIPP
QSTLVFEVEL LGIKNRHVDE L
