ID   PPIB_NEUCR              Reviewed;         285 AA.
AC   Q7S7Z6; A7UWE9; A7UWF0; Q8X0S3; V5IM99; V5IP42;
DT   18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 3.
DT   25-MAY-2022, entry version 118.
DE   RecName: Full=Peptidyl-prolyl cis-trans isomerase B;
DE            Short=PPIase B;
DE            EC=5.2.1.8;
DE   AltName: Full=Rotamase B;
DE   Flags: Precursor;
GN   Name=cpr2; ORFNames=18F11.170, NCU01200;
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 [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12655011; DOI=10.1093/nar/gkg293;
RA   Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V., Hoheisel J.D.,
RA   Fartmann B., Nyakatura G., Kempken F., Maier J., Schulte U.;
RT   "What's in the genome of a filamentous fungus? Analysis of the Neurospora
RT   genome sequence.";
RL   Nucleic Acids Res. 31:1944-1954(2003).
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).
RN   [3]
RP   REVISION OF GENE MODEL.
RA   Pemberton T.J.;
RL   Submitted (FEB-2006) to UniProtKB.
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 cyclosporin A (CsA). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: [Isoform Long]: Membrane {ECO:0000305}; Single-
CC       pass membrane protein {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: [Isoform Short]: Endoplasmic reticulum lumen
CC       {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=Long;
CC         IsoId=Q7S7Z6-1; Sequence=Displayed;
CC       Name=Short;
CC         IsoId=Q7S7Z6-2; Sequence=VSP_029975;
CC   -!- MISCELLANEOUS: [Isoform Short]: Lacks the C-terminal transmembrane
CC       domain, but has an ER retention motif at its extreme C-terminus.
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family. PPIase B
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AL670011; CAD21421.1; -; Genomic_DNA.
DR   EMBL; CM002240; ESA42515.1; -; Genomic_DNA.
DR   EMBL; CM002240; ESA42516.1; -; Genomic_DNA.
DR   RefSeq; XP_011394481.1; XM_011396179.1. [Q7S7Z6-2]
DR   RefSeq; XP_011394482.1; XM_011396180.1. [Q7S7Z6-1]
DR   AlphaFoldDB; Q7S7Z6; -.
DR   SMR; Q7S7Z6; -.
DR   IntAct; Q7S7Z6; 4.
DR   MINT; Q7S7Z6; -.
DR   STRING; 5141.EFNCRP00000004282; -.
DR   EnsemblFungi; ESA42515; ESA42515; NCU01200. [Q7S7Z6-1]
DR   EnsemblFungi; ESA42516; ESA42516; NCU01200. [Q7S7Z6-2]
DR   GeneID; 5847555; -.
DR   KEGG; ncr:NCU01200; -.
DR   VEuPathDB; FungiDB:NCU01200; -.
DR   HOGENOM; CLU_012062_4_1_1; -.
DR   InParanoid; Q7S7Z6; -.
DR   OMA; GEGYPGS; -.
DR   Proteomes; UP000001805; Chromosome 2, Linkage Group V.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR   GO; GO:0016018; F:cyclosporin A binding; IBA:GO_Central.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IBA:GO_Central.
DR   GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR   GO; GO:0000413; P:protein peptidyl-prolyl isomerization; IBA:GO_Central.
DR   Gene3D; 2.40.100.10; -; 1.
DR   InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR   InterPro; IPR020892; Cyclophilin-type_PPIase_CS.
DR   InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
DR   Pfam; PF00160; Pro_isomerase; 1.
DR   PRINTS; PR00153; CSAPPISMRASE.
DR   SUPFAM; SSF50891; SSF50891; 1.
DR   PROSITE; PS00170; CSA_PPIASE_1; 1.
DR   PROSITE; PS50072; CSA_PPIASE_2; 1.
PE   3: Inferred from homology;
KW   Alternative splicing; Endoplasmic reticulum; Glycoprotein; Isomerase;
KW   Membrane; Reference proteome; Rotamase; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000255"
FT   CHAIN           28..285
FT                   /note="Peptidyl-prolyl cis-trans isomerase B"
FT                   /id="PRO_0000233049"
FT   TRANSMEM        250..270
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          38..195
FT                   /note="PPIase cyclophilin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
FT   REGION          217..243
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        139
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         203..285
FT                   /note="LEGQSEWASPAYANEDEKPAAPVPVTDAKPPAHDSIPAATADDDDTGAPLFA
FT                   KVLFFGVLVLGLVLYIRLRRAPKGTYGKGME -> IHVEL (in isoform
FT                   Short)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_029975"
SQ   SEQUENCE   285 AA;  30743 MW;  C8C6DD66836DBB6F CRC64;
     MFSLRRLLLA ATLFLGAMLL FAQSAEAAKG PKITHKVYFD IEQGDKPLGR IVMGLYGKTV
     PKTAENFRAL ATGEKGFGYE GSTFHRVIKQ FMIQGGDFTK GDGTGGKSIY GDKFPDENFK
     LKHSKKGLLS MANAGKDTNG SQFFITTVIT SWLDGKHVVF GEVLEGYDVV EKIENTKTGP
     RDAPAEPIKI AKSGELEVPP EGLEGQSEWA SPAYANEDEK PAAPVPVTDA KPPAHDSIPA
     ATADDDDTGA PLFAKVLFFG VLVLGLVLYI RLRRAPKGTY GKGME