PPIB_DICDI
ID PPIB_DICDI Reviewed; 197 AA.
AC Q9TW32; Q55DC3;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 131.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase B;
DE Short=PPIase B;
DE EC=5.2.1.8;
DE AltName: Full=Cyclophilin B;
DE AltName: Full=Rotamase B;
DE Flags: Precursor;
GN Name=cypB; Synonyms=cyp2; ORFNames=DDB_G0269120;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 23-31, SUBCELLULAR
RP LOCATION, AND DEVELOPMENTAL STAGE.
RC STRAIN=AX2;
RX PubMed=10575348; DOI=10.1016/s0300-9084(99)00225-4;
RA Tapparo A., Kieffer S., Cretin F., Satre M., Klein G.;
RT "The multigene immunophilin family of Dictyostelium discoideum.
RT Characterization of microsomal and mitochondrial cyclophilin isoforms.";
RL Biochimie 81:943-954(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
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: Binds cyclosporin A (CsA). CsA mediates some of
CC its effects via an inhibitory action on PPIase (Probable).
CC {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Microsome {ECO:0000269|PubMed:10575348}.
CC -!- DEVELOPMENTAL STAGE: Strongly expressed in vegetative cells with
CC expression levels steadily decreasing during differentiation. After 12
CC hours of differentiation mRNA expression levels are very. slightly
CC expressed. {ECO:0000269|PubMed:10575348}.
CC -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family.
CC {ECO:0000305}.
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DR EMBL; AF053068; AAD48893.1; -; Genomic_DNA.
DR EMBL; AF123597; AAD48910.1; -; mRNA.
DR EMBL; AAFI02000005; EAL71910.1; -; Genomic_DNA.
DR RefSeq; XP_646208.1; XM_641116.1.
DR AlphaFoldDB; Q9TW32; -.
DR SMR; Q9TW32; -.
DR STRING; 44689.DDB0191497; -.
DR PaxDb; Q9TW32; -.
DR EnsemblProtists; EAL71910; EAL71910; DDB_G0269120.
DR GeneID; 8617162; -.
DR KEGG; ddi:DDB_G0269120; -.
DR dictyBase; DDB_G0269120; cypB.
DR eggNOG; KOG0865; Eukaryota.
DR HOGENOM; CLU_012062_4_2_1; -.
DR InParanoid; Q9TW32; -.
DR OMA; VESMGSN; -.
DR PhylomeDB; Q9TW32; -.
DR PRO; PR:Q9TW32; -.
DR Proteomes; UP000002195; Chromosome 1.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:dictyBase.
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; IPR024936; Cyclophilin-type_PPIase.
DR InterPro; IPR020892; Cyclophilin-type_PPIase_CS.
DR InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
DR Pfam; PF00160; Pro_isomerase; 1.
DR PIRSF; PIRSF001467; Peptidylpro_ismrse; 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 Direct protein sequencing; Endoplasmic reticulum; Isomerase; Microsome;
KW Reference proteome; Rotamase; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000269|PubMed:10575348"
FT CHAIN 23..197
FT /note="Peptidyl-prolyl cis-trans isomerase B"
FT /id="PRO_0000386633"
FT DOMAIN 33..196
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
SQ SEQUENCE 197 AA; 21399 MW; 372156AA0111D9A7 CRC64;
MKVIFVVLAI VLVTLWAMPS EAGKDPKITN KVFFDIEIDN KPAGRIVFGL YGKTVPKTVE
NFRALCTGEK GLGTSGKPLH YKDSKFHRII PNFMIQGGDF TRGDGTGGES IYGKKFNDEN
FKIKHSKPGL LSMANAGPNT NGSQFFITTV VTSWLDGRHT VFGEVIEGMD IVKLLESIGS
QSGTPSKIAK ISNSGEL
