CYPH_NEUCR
ID CYPH_NEUCR Reviewed; 223 AA.
AC P10255; A7UVW7; A7UVW8; Q7RV39; V5IRD0;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase, mitochondrial;
DE Short=PPIase;
DE EC=5.2.1.8;
DE AltName: Full=Cyclophilin;
DE Short=CPH;
DE AltName: Full=Cyclosporin A-binding protein;
DE AltName: Full=Rotamase;
DE Flags: Precursor;
GN Name=csr-1; Synonyms=cyp; ORFNames=NCU00726;
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] (ISOFORMS CYTOSOLIC AND MITOCHONDRIAL), PARTIAL
RP PROTEIN SEQUENCE, AND ALTERNATIVE INITIATION.
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=2971658; DOI=10.1016/s0021-9258(18)68238-9;
RA Tropschug M., Nicholson D.W., Hartl F.-U., Kohler H., Pfanner N.,
RA Wachter E., Neupert W.;
RT "Cyclosporin A-binding protein (cyclophilin) of Neurospora crassa. One gene
RT codes for both the cytosolic and mitochondrial forms.";
RL J. Biol. Chem. 263:14433-14440(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2137907; DOI=10.1093/nar/18.1.190;
RA Tropschug M.;
RT "Nucleotide sequence of the gene coding for cyclophilin/peptidyl-prolyl
RT cis-trans isomerase of Neurospora crassa.";
RL Nucleic Acids Res. 18:190-190(1990).
RN [3]
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 -!- ACTIVITY REGULATION: Binds cyclosporin A (CsA). CsA mediates some of
CC its effects via an inhibitory action on PPIase.
CC -!- SUBCELLULAR LOCATION: Mitochondrion. Cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing, Alternative initiation; Named isoforms=3;
CC Name=Mitochondrial;
CC IsoId=P10255-1; Sequence=Displayed;
CC Name=Cytosolic;
CC IsoId=P10255-2; Sequence=VSP_018863;
CC Name=Short;
CC IsoId=P10255-3; Sequence=VSP_029976;
CC -!- MISCELLANEOUS: [Isoform Cytosolic]: Produced by alternative initiation.
CC {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform Short]: Produced by alternative splicing. This
CC isoform is found in the cell following 22 hours growth in dark.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family.
CC {ECO:0000305}.
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; J03963; AAA33584.1; -; mRNA.
DR EMBL; X17692; CAA35681.1; -; Genomic_DNA.
DR EMBL; X17692; CAA35682.1; -; Genomic_DNA.
DR EMBL; CM002236; ESA44269.1; -; Genomic_DNA.
DR PIR; B30809; CSNCM.
DR RefSeq; XP_011392822.1; XM_011394520.1. [P10255-1]
DR AlphaFoldDB; P10255; -.
DR SMR; P10255; -.
DR STRING; 5141.EFNCRP00000000880; -.
DR PRIDE; P10255; -.
DR EnsemblFungi; ESA44269; ESA44269; NCU00726. [P10255-1]
DR GeneID; 5847832; -.
DR KEGG; ncr:NCU00726; -.
DR VEuPathDB; FungiDB:NCU00726; -.
DR HOGENOM; CLU_012062_4_3_1; -.
DR InParanoid; P10255; -.
DR Proteomes; UP000001805; Chromosome 1, Linkage Group I.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
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 1: Evidence at protein level;
KW Alternative initiation; Alternative splicing; Cytoplasm;
KW Direct protein sequencing; Isomerase; Mitochondrion; Reference proteome;
KW Rotamase; Transit peptide.
FT TRANSIT 1..44
FT /note="Mitochondrion"
FT CHAIN 45..223
FT /note="Peptidyl-prolyl cis-trans isomerase, mitochondrial"
FT /id="PRO_0000025475"
FT DOMAIN 62..222
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
FT VAR_SEQ 1..43
FT /note="Missing (in isoform Cytosolic)"
FT /evidence="ECO:0000303|PubMed:2971658"
FT /id="VSP_018863"
FT VAR_SEQ 119..223
FT /note="GGDFTRGNGTGGKSIYGEKFADENFAKKHVRPGLLSMANAGPNTNGSQFFVT
FT TVPTSWLDGRHVVFGEVADDESMKVVKALEATGSSSGAIRYSKKPTIVDCGAL -> AA
FT VLFVTPRSPPLSTAALSKFPCGHCRGF (in isoform Short)"
FT /evidence="ECO:0000305"
FT /id="VSP_029976"
SQ SEQUENCE 223 AA; 24064 MW; D494AB77F9768AE0 CRC64;
MFGPRHFSVL KTTGSLVSST FSSSLKPTAT FSCARAFSQT SSIMSKVFFD LEWEGPVLGP
NNKPTSEIKA QSGRINFTLY DDVVPKTARN FKELCTGQNG FGYKGSSFHR IIPEFMLQGG
DFTRGNGTGG KSIYGEKFAD ENFAKKHVRP GLLSMANAGP NTNGSQFFVT TVPTSWLDGR
HVVFGEVADD ESMKVVKALE ATGSSSGAIR YSKKPTIVDC GAL
