ID   PPIB_ASPNG              Reviewed;         212 AA.
AC   Q8X166;
DT   18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Peptidyl-prolyl cis-trans isomerase B;
DE            Short=PPIase B;
DE            EC=5.2.1.8 {ECO:0000269|PubMed:11810224};
DE   AltName: Full=Rotamase B;
DE   Flags: Precursor;
GN   Name=cypB;
OS   Aspergillus niger.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=5061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=11810224; DOI=10.1007/s004380100587;
RA   Derkx P.M.F., Madrid S.M.;
RT   "The foldase CYPB is a component of the secretory pathway of Aspergillus
RT   niger and contains the endoplasmic reticulum retention signal HEEL.";
RL   Mol. Gen. Genet. 266:537-545(2001).
CC   -!- FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the
CC       cis-trans isomerization of proline imidic peptide bonds in
CC       oligopeptides. {ECO:0000269|PubMed:11810224}.
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         Evidence={ECO:0000269|PubMed:11810224};
CC   -!- ACTIVITY REGULATION: Inhibited by cyclosporin A (CsA). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000255|PROSITE-
CC       ProRule:PRU10138}.
CC   -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family. PPIase B
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AY005867; AAF98447.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8X166; -.
DR   SMR; Q8X166; -.
DR   STRING; 5061.CADANGAP00003825; -.
DR   PRIDE; Q8X166; -.
DR   VEuPathDB; FungiDB:An04g02020; -.
DR   VEuPathDB; FungiDB:ASPNIDRAFT2_1126047; -.
DR   VEuPathDB; FungiDB:ATCC64974_78060; -.
DR   VEuPathDB; FungiDB:M747DRAFT_330957; -.
DR   eggNOG; KOG0880; Eukaryota.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IDA:AspGD.
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.
DR   PROSITE; PS00014; ER_TARGET; 1.
PE   1: Evidence at protein level;
KW   Endoplasmic reticulum; Glycoprotein; Isomerase; Rotamase; Signal.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..212
FT                   /note="Peptidyl-prolyl cis-trans isomerase B"
FT                   /id="PRO_0000233044"
FT   DOMAIN          38..195
FT                   /note="PPIase cyclophilin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
FT   REGION          181..212
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           209..212
FT                   /note="Prevents secretion from ER"
FT   CARBOHYD        139
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   212 AA;  23302 MW;  FA00BA7D1E50019C CRC64;
     MNFKNIFLSF FFVLAVGLAL VHAEDAQPRG PKITSKVFFD IEHGDKPLGR VVLGLYGKTV
     PKTAENFRAL ATGEKGFGYE GSTFHRVIKD FMIQGGDFTR GDGTGGKSIY GEKFADENFK
     LRHTRKGLLS MANAGKDTNG SQFFITTVPT PWLDGRHVVF GEVLEGYEIV AQIENVPKGR
     SDRPVETVKI VKSGELESED KAGEKGSSHE EL