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 11-NOV-2015, entry version 87. 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 OS 1257 / FGSC 987). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; OC Sordariomycetes; Sordariomycetidae; Sordariales; Sordariaceae; OC 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., RA Hoheisel J.D., Fartmann B., Nyakatura G., Kempken F., Maier J., RA Schulte U.; RT "What's in the genome of a filamentous fungus? Analysis of the RT Neurospora 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., RA Werner-Washburne M., Selitrennikoff C.P., Kinsey J.A., Braun E.L., RA Zelter A., Schulte U., Kothe G.O., Jedd G., Mewes H.-W., Staben C., RA Marcotte E., Greenberg D., Roy A., Foley K., Naylor J., RA Stange-Thomann N., Barrett R., Gnerre S., Kamal M., Kamvysselis M., RA Mauceli E.W., Bielke C., Rudd S., Frishman D., Krystofova S., RA Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S., Cogoni C., RA 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., RA Paulsen I., 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 CC the cis-trans isomerization of proline imidic peptide bonds in CC oligopeptides (By similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Peptidylproline (omega=180) = peptidylproline CC (omega=0). CC -!- ENZYME REGULATION: Inhibited by cyclosporin A (CsA). CC {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Isoform Long: Membrane {ECO:0000305}; CC Single-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 Note=Lacks the C-terminal transmembrane domain, but has an ER CC retention motif at its extreme C-terminus.; CC -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family. PPIase CC B subfamily. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 PPIase cyclophilin-type domain. CC {ECO:0000255|PROSITE-ProRule:PRU00156}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 SMR; Q7S7Z6; 30-198. DR IntAct; Q7S7Z6; 4. DR MINT; MINT-4653739; -. DR PRIDE; Q7S7Z6; -. DR EnsemblFungi; EFNCRT00000004282; EFNCRP00000004282; EFNCRG00000004277. [Q7S7Z6-1] DR EnsemblFungi; EFNCRT00000004283; EFNCRP00000004283; EFNCRG00000004277. [Q7S7Z6-2] DR GeneID; 5847555; -. DR KEGG; ncr:NCU01200; -. DR HOGENOM; HOG000065981; -. DR InParanoid; Q7S7Z6; -. DR KO; K03768; -. DR OMA; SPAYANE; -. DR OrthoDB; EOG757D7G; -. DR Proteomes; UP000001805; Chromosome 2, Linkage Group V. DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell. DR GO; GO:0005794; C:Golgi apparatus; IEA:EnsemblFungi. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042277; F:peptide binding; IEA:UniProtKB-KW. DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW. DR GO; GO:0006457; P:protein folding; IEA:InterPro. DR Gene3D; 2.40.100.10; -; 1. DR InterPro; IPR029000; Cyclophilin-like_dom. DR InterPro; IPR024936; Cyclophilin-type_PPIase. DR InterPro; IPR020892; Cyclophilin-type_PPIase_CS. DR InterPro; IPR002130; Cyclophilin-type_PPIase_dom. DR PANTHER; PTHR11071; PTHR11071; 1. 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; Complete proteome; Cyclosporin; KW Endoplasmic reticulum; Glycoprotein; Isomerase; Membrane; KW Reference proteome; Rotamase; Signal; Transmembrane; KW Transmembrane helix. FT SIGNAL 1 27 {ECO:0000255}. FT CHAIN 28 285 Peptidyl-prolyl cis-trans isomerase B. FT /FTId=PRO_0000233049. FT TRANSMEM 250 270 Helical. {ECO:0000255}. FT DOMAIN 38 195 PPIase cyclophilin-type. FT {ECO:0000255|PROSITE-ProRule:PRU00156}. FT CARBOHYD 139 139 N-linked (GlcNAc...). {ECO:0000255}. FT VAR_SEQ 203 285 LEGQSEWASPAYANEDEKPAAPVPVTDAKPPAHDSIPAATA FT DDDDTGAPLFAKVLFFGVLVLGLVLYIRLRRAPKGTYGKGM FT E -> IHVEL (in isoform Short). FT {ECO:0000305}. FT /FTId=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 //