PPIB1_RHIO9
ID PPIB1_RHIO9 Reviewed; 209 AA.
AC P0C1H9; I1CT30;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 27-JUN-2006, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase B1;
DE Short=PPIase B1;
DE EC=5.2.1.8;
DE AltName: Full=Cyclophilin B1;
DE AltName: Full=Rotamase B1;
DE Flags: Precursor;
GN Name=cyp8; ORFNames=RO3G_16321;
OS Rhizopus delemar (strain RA 99-880 / ATCC MYA-4621 / FGSC 9543 / NRRL
OS 43880) (Mucormycosis agent) (Rhizopus arrhizus var. delemar).
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Mucorineae; Rhizopodaceae; Rhizopus.
OX NCBI_TaxID=246409;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RA 99-880 / ATCC MYA-4621 / FGSC 9543 / NRRL 43880;
RX PubMed=19578406; DOI=10.1371/journal.pgen.1000549;
RA Ma L.-J., Ibrahim A.S., Skory C., Grabherr M.G., Burger G., Butler M.,
RA Elias M., Idnurm A., Lang B.F., Sone T., Abe A., Calvo S.E.,
RA Corrochano L.M., Engels R., Fu J., Hansberg W., Kim J.-M., Kodira C.D.,
RA Koehrsen M.J., Liu B., Miranda-Saavedra D., O'Leary S.,
RA Ortiz-Castellanos L., Poulter R., Rodriguez-Romero J., Ruiz-Herrera J.,
RA Shen Y.-Q., Zeng Q., Galagan J., Birren B.W., Cuomo C.A., Wickes B.L.;
RT "Genomic analysis of the basal lineage fungus Rhizopus oryzae reveals a
RT whole-genome duplication.";
RL PLoS Genet. 5:E1000549-E1000549(2009).
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: Endoplasmic reticulum lumen {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family. PPIase B
CC subfamily. {ECO:0000305}.
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DR EMBL; CH476750; EIE91610.1; -; Genomic_DNA.
DR AlphaFoldDB; P0C1H9; -.
DR SMR; P0C1H9; -.
DR STRING; 936053.P0C1H9; -.
DR PRIDE; P0C1H9; -.
DR EnsemblFungi; EIE91610; EIE91610; RO3G_16321.
DR VEuPathDB; FungiDB:RO3G_16321; -.
DR eggNOG; KOG0880; Eukaryota.
DR InParanoid; P0C1H9; -.
DR OMA; VMKMQSF; -.
DR OrthoDB; 1403619at2759; -.
DR Proteomes; UP000009138; Unassembled WGS sequence.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
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 Endoplasmic reticulum; Glycoprotein; Isomerase; Reference proteome;
KW Rotamase; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..209
FT /note="Peptidyl-prolyl cis-trans isomerase B1"
FT /id="PRO_0000244712"
FT DOMAIN 37..194
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
FT MOTIF 206..209
FT /note="Prevents secretion from ER"
FT CARBOHYD 138
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 209 AA; 22698 MW; FFC6C6B133E910FC CRC64;
MARFNLATLL VTLFLAVCTF SFVSAEGRGP VITDKIYFDI KQGDESLGRI VLGLYGKTVP
KTAENFKQLA TGENGYGYKG STFHRVIKKF MIQGGDFTNH DGTGGKSIYG NRFADENFKL
RHSTPGLLSM ANAGRDTNGS QFFITTVVTP WLDGKHVVFG RVLEGMDVVT KIENTPTGSR
SKPSVDVVIA DCGLLPDEPA KEAAEHAEL