PPIB_GIBZE
ID PPIB_GIBZE Reviewed; 248 AA.
AC Q4I5R9; A0A0E0SD09; I1RTD6; V6RHL0;
DT 18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2012, sequence version 2.
DT 03-AUG-2022, entry version 95.
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=FGRRES_07439, FGSG_07439;
OS Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084
OS / PH-1) (Wheat head blight fungus) (Fusarium graminearum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=229533;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=17823352; DOI=10.1126/science.1143708;
RA Cuomo C.A., Gueldener U., Xu J.-R., Trail F., Turgeon B.G., Di Pietro A.,
RA Walton J.D., Ma L.-J., Baker S.E., Rep M., Adam G., Antoniw J., Baldwin T.,
RA Calvo S.E., Chang Y.-L., DeCaprio D., Gale L.R., Gnerre S., Goswami R.S.,
RA Hammond-Kosack K., Harris L.J., Hilburn K., Kennell J.C., Kroken S.,
RA Magnuson J.K., Mannhaupt G., Mauceli E.W., Mewes H.-W., Mitterbauer R.,
RA Muehlbauer G., Muensterkoetter M., Nelson D., O'Donnell K., Ouellet T.,
RA Qi W., Quesneville H., Roncero M.I.G., Seong K.-Y., Tetko I.V., Urban M.,
RA Waalwijk C., Ward T.J., Yao J., Birren B.W., Kistler H.C.;
RT "The Fusarium graminearum genome reveals a link between localized
RT polymorphism and pathogen specialization.";
RL Science 317:1400-1402(2007).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=20237561; DOI=10.1038/nature08850;
RA Ma L.-J., van der Does H.C., Borkovich K.A., Coleman J.J., Daboussi M.-J.,
RA Di Pietro A., Dufresne M., Freitag M., Grabherr M., Henrissat B.,
RA Houterman P.M., Kang S., Shim W.-B., Woloshuk C., Xie X., Xu J.-R.,
RA Antoniw J., Baker S.E., Bluhm B.H., Breakspear A., Brown D.W.,
RA Butchko R.A.E., Chapman S., Coulson R., Coutinho P.M., Danchin E.G.J.,
RA Diener A., Gale L.R., Gardiner D.M., Goff S., Hammond-Kosack K.E.,
RA Hilburn K., Hua-Van A., Jonkers W., Kazan K., Kodira C.D., Koehrsen M.,
RA Kumar L., Lee Y.-H., Li L., Manners J.M., Miranda-Saavedra D.,
RA Mukherjee M., Park G., Park J., Park S.-Y., Proctor R.H., Regev A.,
RA Ruiz-Roldan M.C., Sain D., Sakthikumar S., Sykes S., Schwartz D.C.,
RA Turgeon B.G., Wapinski I., Yoder O., Young S., Zeng Q., Zhou S.,
RA Galagan J., Cuomo C.A., Kistler H.C., Rep M.;
RT "Comparative genomics reveals mobile pathogenicity chromosomes in
RT Fusarium.";
RL Nature 464:367-373(2010).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=26198851; DOI=10.1186/s12864-015-1756-1;
RA King R., Urban M., Hammond-Kosack M.C.U., Hassani-Pak K.,
RA Hammond-Kosack K.E.;
RT "The completed genome sequence of the pathogenic ascomycete fungus Fusarium
RT graminearum.";
RL BMC Genomics 16:544-544(2015).
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=Q4I5R9-1; Sequence=Displayed;
CC Name=Short;
CC IsoId=Q4I5R9-2; Sequence=VSP_044415;
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; DS231666; ESU13704.1; -; Genomic_DNA.
DR EMBL; HG970335; CEF84322.1; -; Genomic_DNA.
DR RefSeq; XP_011327211.1; XM_011328909.1. [Q4I5R9-1]
DR AlphaFoldDB; Q4I5R9; -.
DR SMR; Q4I5R9; -.
DR STRING; 5518.FGSG_07439P0; -.
DR EnsemblFungi; ESU13704; ESU13704; FGSG_07439. [Q4I5R9-1]
DR GeneID; 23554516; -.
DR KEGG; fgr:FGSG_07439; -.
DR VEuPathDB; FungiDB:FGRAMPH1_01G24825; -.
DR eggNOG; KOG0880; Eukaryota.
DR HOGENOM; CLU_012062_4_1_1; -.
DR InParanoid; Q4I5R9; -.
DR Proteomes; UP000070720; Chromosome 4.
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:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0006457; P:protein folding; IEA:InterPro.
DR GO; GO:0000413; P:protein peptidyl-prolyl isomerization; IEA:InterPro.
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..248
FT /note="Peptidyl-prolyl cis-trans isomerase B"
FT /id="PRO_0000233048"
FT TRANSMEM 219..239
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 38..195
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
FT CARBOHYD 139
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 203..248
FT /note="LVGTSEFAAEEVASAGWSPMQKAGLFAIFAGVLFVGLRSARQHSRF -> IH
FT VEL (in isoform Short)"
FT /evidence="ECO:0000305"
FT /id="VSP_044415"
SQ SEQUENCE 248 AA; 26883 MW; AC502CA79D19EFAA CRC64;
MFNLRRLFAS ALFLGLGLLF LAQTAEAAKG PKITHKVYFD ITQGDQPLGR VVMGLYGKTV
PETTENFRAL ATGEKGFGYE GSAFHRVIKN FMIQGGDFTK GDGTGGKSIY GDRFKDENFK
LKHTKKGLLS MANAGRDTNG SQFFITTVVT SWLDGKHVVF GEVLEGYEII EKIENSKTGA
ADRPVEAVKI AKSGELDVPP EGLVGTSEFA AEEVASAGWS PMQKAGLFAI FAGVLFVGLR
SARQHSRF
