PPID_BOVIN
ID PPID_BOVIN Reviewed; 370 AA.
AC P26882; Q28077; Q2HJ45;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 6.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase D {ECO:0000305};
DE Short=PPIase D {ECO:0000305};
DE EC=5.2.1.8 {ECO:0000250|UniProtKB:Q9CR16};
DE AltName: Full=40 kDa peptidyl-prolyl cis-trans isomerase {ECO:0000303|PubMed:1544925};
DE AltName: Full=Cyclophilin-40 {ECO:0000303|PubMed:8509368};
DE Short=CYP-40 {ECO:0000303|PubMed:8509368};
DE AltName: Full=Cyclophilin-related protein {ECO:0000303|PubMed:8514757};
DE AltName: Full=Estrogen receptor-binding cyclophilin {ECO:0000303|PubMed:8514757};
DE AltName: Full=Rotamase D;
GN Name=PPID {ECO:0000250|UniProtKB:Q08752}; Synonyms=CYPD;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, IDENTIFICATION IN AN
RP ESR1 STEROID RECEPTOR-CHAPERONE COMPLEX, AND TISSUE SPECIFICITY.
RX PubMed=8514757; DOI=10.1016/s0021-9258(19)38636-3;
RA Ratajczak T., Carrello A., Mark P.J., Warner B.J., Simpson R.J.,
RA Moritz R.L., House A.K.;
RT "The cyclophilin component of the unactivated estrogen receptor contains a
RT tetratricopeptide repeat domain and shares identity with p59 (FKBP59).";
RL J. Biol. Chem. 268:13187-13192(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Uterus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 37-345.
RC TISSUE=Brain;
RX PubMed=8509368; DOI=10.1016/s0021-9258(18)31389-9;
RA Kieffer L.J., Seng T.W., Li W., Osterman D.G., Handschumacher R.E.,
RA Bayney R.M.;
RT "Cyclophilin-40, a protein with homology to the P59 component of the
RT steroid receptor complex. Cloning of the cDNA and further
RT characterization.";
RL J. Biol. Chem. 268:12303-12310(1993).
RN [4]
RP PROTEIN SEQUENCE OF 18-42; 147-154; 199-219; 228-235 AND 309-312, AND
RP FUNCTION.
RC TISSUE=Brain;
RX PubMed=1544925; DOI=10.1016/s0021-9258(18)42795-0;
RA Kieffer L.J., Thalhammer T., Handschumacher R.E.;
RT "Isolation and characterization of a 40-kDa cyclophilin-related protein.";
RL J. Biol. Chem. 267:5503-5507(1992).
RN [5]
RP INTERACTION WITH HSP90AB1.
RX PubMed=8621687; DOI=10.1074/jbc.271.6.2961;
RA Ratajczak T., Carrello A.;
RT "Cyclophilin 40 (CyP-40), mapping of its hsp90 binding domain and evidence
RT that FKBP52 competes with CyP-40 for hsp90 binding.";
RL J. Biol. Chem. 271:2961-2965(1996).
RN [6]
RP INTERACTION WITH HSP90AA1 AND HSP90AB1.
RX PubMed=9915798; DOI=10.1074/jbc.274.5.2682;
RA Carrello A., Ingley E., Minchin R.F., Tsai S., Ratajczak T.;
RT "The common tetratricopeptide repeat acceptor site for steroid receptor-
RT associated immunophilins and hop is located in the dimerization domain of
RT Hsp90.";
RL J. Biol. Chem. 274:2682-2689(1999).
RN [7]
RP INTERACTION WITH HSPA8.
RX PubMed=15497503; DOI=10.1379/csc-26r.1;
RA Carrello A., Allan R.K., Morgan S.L., Owen B.A., Mok D., Ward B.K.,
RA Minchin R.F., Toft D.O., Ratajczak T.;
RT "Interaction of the Hsp90 cochaperone cyclophilin 40 with Hsc70.";
RL Cell Stress Chaperones 9:167-181(2004).
RN [8]
RP FUNCTION, AND INTERACTION WITH HSP90AB1.
RX PubMed=16650407; DOI=10.1016/j.febslet.2006.04.039;
RA Mok D., Allan R.K., Carrello A., Wangoo K., Walkinshaw M.D., Ratajczak T.;
RT "The chaperone function of cyclophilin 40 maps to a cleft between the
RT prolyl isomerase and tetratricopeptide repeat domains.";
RL FEBS Lett. 580:2761-2768(2006).
RN [9]
RP INTERACTION WITH S100A1; S100A2 AND S100A6.
RX PubMed=20188096; DOI=10.1016/j.febslet.2010.02.055;
RA Shimamoto S., Kubota Y., Tokumitsu H., Kobayashi R.;
RT "S100 proteins regulate the interaction of Hsp90 with cyclophilin 40 and
RT FKBP52 through their tetratricopeptide repeats.";
RL FEBS Lett. 584:1119-1125(2010).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
RX PubMed=11377203; DOI=10.1016/s0969-2126(01)00603-7;
RA Taylor P., Dornan J., Carrello A., Minchin R.F., Ratajczak T.,
RA Walkinshaw M.D.;
RT "Two structures of cyclophilin 40: folding and fidelity in the TPR
RT domains.";
RL Structure 9:431-438(2001).
CC -!- FUNCTION: PPIase that catalyzes the cis-trans isomerization of proline
CC imidic peptide bonds in oligopeptides and may therefore assist protein
CC folding. Proposed to act as a co-chaperone in HSP90 complexes such as
CC in unligated steroid receptors heterocomplexes. Different co-chaperones
CC seem to compete for association with HSP90 thus establishing distinct
CC HSP90-co-chaperone-receptor complexes with the potential to exert
CC tissue-specific receptor activity control. May have a preference for
CC estrogen receptor complexes and is not found in glucocorticoid receptor
CC complexes. May be involved in cytoplasmic dynein-dependent movement of
CC the receptor from the cytoplasm to the nucleus. May regulate MYB by
CC inhibiting its DNA-binding activity. Involved in regulation of AHR
CC signaling by promoting the formation of the AHR:ARNT dimer; the
CC function is independent of HSP90 but requires the chaperone activity.
CC Involved in regulation of UV radiation-induced apoptosis.
CC {ECO:0000250|UniProtKB:Q9CR16, ECO:0000269|PubMed:1544925,
CC ECO:0000269|PubMed:16650407}.
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:0000250|UniProtKB:Q9CR16};
CC -!- ACTIVITY REGULATION: Less sensitive to inhibition by cyclosporin A than
CC is CYP-18. {ECO:0000250|UniProtKB:Q9CR16}.
CC -!- SUBUNIT: Identified in ESR1 or NR3C1/GCR steroid receptor-chaperone
CC complexes. Found in HSP90 chaperone complexes with kinase clients LCK
CC or EIF2AK1. Two monomers associate with one HSP90 homodimer. Interacts
CC with HSP90AA1. Interacts with HSP90AB1; PPID and FKBP4 compete for
CC binding to HSP90AB1 and the interaction is mutually exclusive with the
CC PPID:HSPA8 interaction. Interacts with HSPA8; PPID and STIP1 but not
CC FKBP4 compete for binding to HSPA8 and the interaction is mutually
CC exclusive with the PPID:HSP90AB1 interaction. Interacts with S100A1 and
CC S100A2; the interactions dissociate the PPID:HSP90AA1 interaction.
CC Interacts with S100A6. Interacts with MYB, ILF2, XRCC6, RACK1 and RPS3.
CC Interacts with cytoplasmic dynein 1 intermediate chain (DYNC1I1 or
CC DYNC1I2). {ECO:0000269|PubMed:15497503, ECO:0000269|PubMed:16650407,
CC ECO:0000269|PubMed:20188096, ECO:0000269|PubMed:8514757,
CC ECO:0000269|PubMed:8621687, ECO:0000269|PubMed:9915798}.
CC -!- INTERACTION:
CC P26882; P02639: S100A1; NbExp=2; IntAct=EBI-6477155, EBI-6477285;
CC P26882; P07900: HSP90AA1; Xeno; NbExp=4; IntAct=EBI-6477155, EBI-296047;
CC P26882; P35467: S100a1; Xeno; NbExp=7; IntAct=EBI-6477155, EBI-6477109;
CC P26882; P29034: S100A2; Xeno; NbExp=3; IntAct=EBI-6477155, EBI-752230;
CC P26882; P06703: S100A6; Xeno; NbExp=3; IntAct=EBI-6477155, EBI-352877;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q08752}.
CC Nucleus, nucleolus {ECO:0000250|UniProtKB:Q08752}. Nucleus, nucleoplasm
CC {ECO:0000250|UniProtKB:Q08752}.
CC -!- TISSUE SPECIFICITY: Detected in heart, thymis and brain.
CC {ECO:0000269|PubMed:8514757}.
CC -!- PTM: The N-terminus is blocked.
CC -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family. PPIase D
CC subfamily. {ECO:0000305}.
CC -!- CAUTION: This protein should not be confused with mitochondrial
CC peptidyl-prolyl cis-trans isomerase F (PPIF) which is often referred to
CC as cyclophilin D or CypD. {ECO:0000305}.
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DR EMBL; D14074; BAA03159.1; -; mRNA.
DR EMBL; BC113318; AAI13319.1; -; mRNA.
DR EMBL; L11668; AAA30484.1; -; mRNA.
DR PIR; A46579; A46579.
DR RefSeq; NP_776578.1; NM_174153.3.
DR PDB; 1IHG; X-ray; 1.80 A; A=1-370.
DR PDB; 1IIP; X-ray; 2.00 A; A=1-370.
DR PDBsum; 1IHG; -.
DR PDBsum; 1IIP; -.
DR AlphaFoldDB; P26882; -.
DR SMR; P26882; -.
DR BioGRID; 158751; 1.
DR IntAct; P26882; 6.
DR MINT; P26882; -.
DR STRING; 9913.ENSBTAP00000022180; -.
DR PaxDb; P26882; -.
DR PRIDE; P26882; -.
DR Ensembl; ENSBTAT00000022180; ENSBTAP00000022180; ENSBTAG00000016680.
DR GeneID; 281420; -.
DR KEGG; bta:281420; -.
DR CTD; 5481; -.
DR VEuPathDB; HostDB:ENSBTAG00000016680; -.
DR VGNC; VGNC:33197; PPID.
DR eggNOG; KOG0546; Eukaryota.
DR GeneTree; ENSGT00940000154672; -.
DR HOGENOM; CLU_012062_37_1_1; -.
DR InParanoid; P26882; -.
DR OMA; EMEQNCN; -.
DR OrthoDB; 1403619at2759; -.
DR TreeFam; TF324493; -.
DR Reactome; R-BTA-8939211; ESR-mediated signaling.
DR EvolutionaryTrace; P26882; -.
DR Proteomes; UP000009136; Chromosome 17.
DR Bgee; ENSBTAG00000016680; Expressed in oocyte and 104 other tissues.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0016018; F:cyclosporin A binding; ISS:UniProtKB.
DR GO; GO:0030544; F:Hsp70 protein binding; IDA:UniProtKB.
DR GO; GO:0051879; F:Hsp90 protein binding; ISS:UniProtKB.
DR GO; GO:0030331; F:nuclear estrogen receptor binding; IDA:UniProtKB.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; ISS:UniProtKB.
DR GO; GO:0008134; F:transcription factor binding; ISS:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0071492; P:cellular response to UV-A; ISS:UniProtKB.
DR GO; GO:0061077; P:chaperone-mediated protein folding; ISS:UniProtKB.
DR GO; GO:0034389; P:lipid droplet organization; ISS:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0050714; P:positive regulation of protein secretion; IEA:Ensembl.
DR GO; GO:0045070; P:positive regulation of viral genome replication; IEA:Ensembl.
DR GO; GO:0006457; P:protein folding; IDA:UniProtKB.
DR GO; GO:0000413; P:protein peptidyl-prolyl isomerization; ISS:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0065003; P:protein-containing complex assembly; ISS:UniProtKB.
DR Gene3D; 1.25.40.10; -; 1.
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 InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR Pfam; PF00160; Pro_isomerase; 1.
DR Pfam; PF13176; TPR_7; 1.
DR PRINTS; PR00153; CSAPPISMRASE.
DR SMART; SM00028; TPR; 3.
DR SUPFAM; SSF48452; SSF48452; 1.
DR SUPFAM; SSF50891; SSF50891; 1.
DR PROSITE; PS00170; CSA_PPIASE_1; 1.
DR PROSITE; PS50072; CSA_PPIASE_2; 1.
DR PROSITE; PS50005; TPR; 3.
DR PROSITE; PS50293; TPR_REGION; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Apoptosis; Chaperone; Cytoplasm;
KW Direct protein sequencing; Isomerase; Nucleus; Phosphoprotein;
KW Protein transport; Reference proteome; Repeat; Rotamase; TPR repeat;
KW Transport.
FT CHAIN 1..370
FT /note="Peptidyl-prolyl cis-trans isomerase D"
FT /id="PRO_0000064152"
FT DOMAIN 19..183
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
FT REPEAT 223..256
FT /note="TPR 1"
FT REPEAT 273..306
FT /note="TPR 2"
FT REPEAT 307..340
FT /note="TPR 3"
FT REGION 185..215
FT /note="Chaperone activity"
FT REGION 214..370
FT /note="Interaction with HSP90AB1"
FT MOD_RES 5
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q08752"
FT MOD_RES 171
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9CR16"
FT MOD_RES 198
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q08752"
FT STRAND 8..11
FT /evidence="ECO:0007829|PDB:1IHG"
FT STRAND 17..24
FT /evidence="ECO:0007829|PDB:1IHG"
FT STRAND 27..36
FT /evidence="ECO:0007829|PDB:1IHG"
FT TURN 38..40
FT /evidence="ECO:0007829|PDB:1IHG"
FT HELIX 42..53
FT /evidence="ECO:0007829|PDB:1IHG"
FT TURN 60..62
FT /evidence="ECO:0007829|PDB:1IHG"
FT STRAND 63..66
FT /evidence="ECO:0007829|PDB:1IHG"
FT STRAND 72..77
FT /evidence="ECO:0007829|PDB:1IHG"
FT TURN 78..80
FT /evidence="ECO:0007829|PDB:1IHG"
FT STRAND 81..84
FT /evidence="ECO:0007829|PDB:1IHG"
FT TURN 87..89
FT /evidence="ECO:0007829|PDB:1IHG"
FT STRAND 90..93
FT /evidence="ECO:0007829|PDB:1IHG"
FT STRAND 98..101
FT /evidence="ECO:0007829|PDB:1IIP"
FT STRAND 117..120
FT /evidence="ECO:0007829|PDB:1IHG"
FT STRAND 132..137
FT /evidence="ECO:0007829|PDB:1IHG"
FT HELIX 140..142
FT /evidence="ECO:0007829|PDB:1IHG"
FT TURN 143..145
FT /evidence="ECO:0007829|PDB:1IHG"
FT STRAND 148..154
FT /evidence="ECO:0007829|PDB:1IHG"
FT HELIX 156..163
FT /evidence="ECO:0007829|PDB:1IHG"
FT STRAND 171..174
FT /evidence="ECO:0007829|PDB:1IHG"
FT STRAND 176..184
FT /evidence="ECO:0007829|PDB:1IHG"
FT STRAND 196..198
FT /evidence="ECO:0007829|PDB:1IHG"
FT HELIX 206..208
FT /evidence="ECO:0007829|PDB:1IHG"
FT STRAND 209..211
FT /evidence="ECO:0007829|PDB:1IHG"
FT HELIX 216..235
FT /evidence="ECO:0007829|PDB:1IHG"
FT HELIX 239..259
FT /evidence="ECO:0007829|PDB:1IHG"
FT HELIX 262..265
FT /evidence="ECO:0007829|PDB:1IHG"
FT HELIX 266..268
FT /evidence="ECO:0007829|PDB:1IHG"
FT HELIX 269..285
FT /evidence="ECO:0007829|PDB:1IHG"
FT HELIX 289..300
FT /evidence="ECO:0007829|PDB:1IHG"
FT HELIX 307..319
FT /evidence="ECO:0007829|PDB:1IHG"
FT HELIX 323..336
FT /evidence="ECO:0007829|PDB:1IHG"
FT HELIX 341..362
FT /evidence="ECO:0007829|PDB:1IHG"
SQ SEQUENCE 370 AA; 40620 MW; F278FDE1B9494241 CRC64;
MSHPSPQAKP SNPSNPRVFF DVDIGGERVG RIVLELFADI VPKTAENFRA LCTGEKGIGP
TTGKPLHFKG CPFHRIIKKF MIQGGDFSNQ NGTGGESIYG EKFEDENFHY KHDKEGLLSM
ANAGSNTNGS QFFITTVPTP HLDGKHVVFG QVIKGMGVAK ILENVEVKGE KPAKLCVIAE
CGELKEGDDW GIFPKDGSGD SHPDFPEDAD VDLKDVDKIL LISEDLKNIG NTFFKSQNWE
MAIKKYTKVL RYVEGSRAAA EDADGAKLQP VALSCVLNIG ACKLKMSDWQ GAVDSCLEAL
EIDPSNTKAL YRRAQGWQGL KEYDQALADL KKAQEIAPED KAIQAELLKV KQKIKAQKDK
EKAAYAKMFA
