ID   FKBP2_NEUCR             Reviewed;         217 AA.
AC   O60046; Q7S451;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 119.
DE   RecName: Full=FK506-binding protein 2;
DE            Short=FKBP2;
DE            EC=5.2.1.8;
DE   AltName: Full=FK506-resistance protein 5;
DE   AltName: Full=NcFKBP22;
DE   AltName: Full=Peptidyl-prolyl cis-trans isomerase fkr-5;
DE            Short=PPIase fkr-5;
DE   Flags: Precursor;
GN   Name=fkr-5; ORFNames=NCU02455;
OS   Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS   FGSC 987).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=367110;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 21-55, AND CATALYTIC
RP   ACTIVITY.
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=11034311; DOI=10.1016/s0014-5793(00)01901-3;
RA   Solscheid B., Tropschug M.;
RT   "A novel type of FKBP in the secretory pathway of Neurospora crassa.";
RL   FEBS Lett. 480:118-122(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12712197; DOI=10.1038/nature01554;
RA   Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA   Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA   Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA   Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA   Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA   Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA   Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA   Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA   Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA   Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA   DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA   Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA   Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA   Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT   "The genome sequence of the filamentous fungus Neurospora crassa.";
RL   Nature 422:859-868(2003).
CC   -!- FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the
CC       cis-trans isomerization of proline imidic peptide bonds in
CC       oligopeptides.
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         Evidence={ECO:0000269|PubMed:11034311};
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000255|PROSITE-
CC       ProRule:PRU10138}.
CC   -!- SIMILARITY: Belongs to the FKBP-type PPIase family. {ECO:0000305}.
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DR   EMBL; AJ006297; CAA06962.1; -; mRNA.
DR   EMBL; CM002242; EAA30274.3; -; Genomic_DNA.
DR   RefSeq; XP_959510.3; XM_954417.3.
DR   AlphaFoldDB; O60046; -.
DR   SMR; O60046; -.
DR   IntAct; O60046; 5.
DR   MINT; O60046; -.
DR   STRING; 367110.O60046; -.
DR   EnsemblFungi; EAA30274; EAA30274; NCU02455.
DR   GeneID; 3875657; -.
DR   KEGG; ncr:NCU02455; -.
DR   VEuPathDB; FungiDB:NCU02455; -.
DR   HOGENOM; CLU_013615_8_1_1; -.
DR   InParanoid; O60046; -.
DR   Proteomes; UP000001805; Chromosome 7, Linkage Group VII.
DR   GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IBA:GO_Central.
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   1: Evidence at protein level;
KW   Direct protein sequencing; Endoplasmic reticulum; Isomerase;
KW   Reference proteome; Rotamase; Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000269|PubMed:11034311"
FT   CHAIN           21..217
FT                   /note="FK506-binding protein 2"
FT                   /id="PRO_0000025511"
FT   DOMAIN          41..129
FT                   /note="PPIase FKBP-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00277"
FT   MOTIF           214..217
FT                   /note="Prevents secretion from ER"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
SQ   SEQUENCE   217 AA;  22915 MW;  72313067521BCDAF CRC64;
     MKSIFLSLSL LASATVGVLA AEELGIDVTV PVECDRKTRK GDKINVHYRG TLQSNGQQFD
     ASYDRGTPFS FKLGGGQVIK GWDEGLVDMC IGEKRTLTVP PSYGYGQRSI GPIPAGSTLI
     FETELIGIDG VPKPESIVYK QAAEKAEEAA SAVEEKVAEA TDKAGGKIAD ATKKVEEKAE
     EASANVVEKV ASVVSGAAEA VKTVVADTDD VQEHNEL