ID PPIB_NEUCR STANDARD; PRT; 207 AA. AC Q7S7Z6; Q8X0S3; DT 18-APR-2006, integrated into UniProtKB/Swiss-Prot. DT 18-APR-2006, sequence version 2. DT 18-APR-2006, entry version 20. DE Peptidyl-prolyl cis-trans isomerase B precursor (EC 5.2.1.8) (PPIase DE B) (Rotamase B). GN Name=cpr-2; ORFNames=18F11.170, NCU01200; OS Neurospora crassa. OC Eukaryota; Fungi; Ascomycota; Pezizomycotina; Sordariomycetes; OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora. OX NCBI_TaxID=5141; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=74-OR23-1A / FGSC 987; RX MEDLINE=22542210; 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=74-OR23-1A / FGSC 987; RX MEDLINE=22598136; 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., 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., 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 Swiss-Prot. 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). CC -!- CATALYTIC ACTIVITY: Peptidylproline (omega=180) = peptidylproline CC (omega=0). CC -!- ENZYME REGULATION: Inhibited by cyclosporin A (CsA) (By CC similarity). CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum; endoplasmic reticulum CC lumen (By similarity). CC -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family. PPIase CC B subfamily. CC -!- SIMILARITY: Contains 1 PPIase cyclophilin-type domain. CC -!- CAUTION: Ref.2 sequence differs from that shown due to erroneous CC gene model prediction. 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; AABX01000267; EAA32330.1; ALT_SEQ; Genomic_DNA. DR HSSP; P23284; 1CYN. DR SMR; Q7S7Z6; 30-198. DR InterPro; IPR002130; CSA_PPIase. DR Pfam; PF00160; Pro_isomerase; 1. DR PRINTS; PR00153; CSAPPISMRASE. DR PROSITE; PS00170; CSA_PPIASE_1; 1. DR PROSITE; PS50072; CSA_PPIASE_2; 1. KW Cyclosporin; Endoplasmic reticulum; Glycoprotein; Isomerase; Rotamase; KW Signal. FT SIGNAL 1 27 Potential. FT CHAIN 28 207 Peptidyl-prolyl cis-trans isomerase B. FT /FTId=PRO_0000233049. FT DOMAIN 38 195 PPIase cyclophilin-type. FT MOTIF 204 207 Prevents secretion from ER. FT CARBOHYD 139 139 N-linked (GlcNAc...) (Potential). SQ SEQUENCE 207 AA; 22557 MW; AA0B42D3A8D9E931 CRC64; MFSLRRLLLA ATLFLGAMLL FAQSAEAAKG PKITHKVYFD IEQGDKPLGR IVMGLYGKTV PKTAENFRAL ATGEKGFGYE GSTFHRVIKQ FMIQGGDFTK GDGTGGKSIY GDKFPDENFK LKHSKKGLLS MANAGKDTNG SQFFITTVIT SWLDGKHVVF GEVLEGYDVV EKIENTKTGP RDAPAEPIKI AKSGELEVPP EGIHVEL //