PPID_MOUSE
ID PPID_MOUSE Reviewed; 370 AA.
AC Q9CR16; Q543G1;
DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase D {ECO:0000250|UniProtKB:Q08752};
DE Short=PPIase D {ECO:0000250|UniProtKB:Q08752};
DE EC=5.2.1.8 {ECO:0000250|UniProtKB:Q08752};
DE AltName: Full=40 kDa peptidyl-prolyl cis-trans isomerase;
DE AltName: Full=Cyclophilin-40 {ECO:0000250|UniProtKB:Q08752};
DE Short=CYP-40 {ECO:0000250|UniProtKB:Q08752};
DE AltName: Full=Rotamase D {ECO:0000250|UniProtKB:Q08752};
GN Name=Ppid {ECO:0000312|MGI:MGI:1914988};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo, Embryonic head, and Spinal ganglion;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PROTEIN SEQUENCE OF 18-28; 32-43 AND 219-227, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=C57BL/6J, and OF1; TISSUE=Brain, and Hippocampus;
RA Lubec G., Yang J.W., Zigmond M., Kang S.U., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [4]
RP IDENTIFICATION IN A COMPLEX WITH HSP90AA1 AND NR3C1.
RX PubMed=9195923; DOI=10.1074/jbc.272.26.16224;
RA Silverstein A.M., Galigniana M.D., Chen M.S., Owens-Grillo J.K.,
RA Chinkers M., Pratt W.B.;
RT "Protein phosphatase 5 is a major component of glucocorticoid
RT receptor.hsp90 complexes with properties of an FK506-binding
RT immunophilin.";
RL J. Biol. Chem. 272:16224-16230(1997).
RN [5]
RP FUNCTION.
RX PubMed=18771283; DOI=10.1021/bi8011862;
RA Banerjee A., Periyasamy S., Wolf I.M., Hinds T.D. Jr., Yong W., Shou W.,
RA Sanchez E.R.;
RT "Control of glucocorticoid and progesterone receptor subcellular
RT localization by the ligand-binding domain is mediated by distinct
RT interactions with tetratricopeptide repeat proteins.";
RL Biochemistry 47:10471-10480(2008).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-171, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
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 region. Involved in regulation of UV radiation-induced apoptosis.
CC {ECO:0000250|UniProtKB:Q08752, ECO:0000269|PubMed:18771283}.
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:Q08752};
CC -!- ACTIVITY REGULATION: Less sensitive to inhibition by cyclosporin A than
CC is CYP-18. {ECO:0000250|UniProtKB:Q08752}.
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:9195923}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q08752}.
CC Nucleus, nucleolus {ECO:0000250|UniProtKB:Q08752}. Nucleus, nucleoplasm
CC {ECO:0000250|UniProtKB:Q08752}.
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; AK003402; BAB22767.1; -; mRNA.
DR EMBL; AK013919; BAB29056.1; -; mRNA.
DR EMBL; AK051597; BAC34686.1; -; mRNA.
DR EMBL; BC011499; AAH11499.1; -; mRNA.
DR EMBL; BC019778; AAH19778.1; -; mRNA.
DR CCDS; CCDS17417.1; -.
DR RefSeq; NP_080628.1; NM_026352.3.
DR AlphaFoldDB; Q9CR16; -.
DR SMR; Q9CR16; -.
DR BioGRID; 212408; 18.
DR IntAct; Q9CR16; 3.
DR STRING; 10090.ENSMUSP00000029382; -.
DR iPTMnet; Q9CR16; -.
DR PhosphoSitePlus; Q9CR16; -.
DR SwissPalm; Q9CR16; -.
DR REPRODUCTION-2DPAGE; Q9CR16; -.
DR EPD; Q9CR16; -.
DR jPOST; Q9CR16; -.
DR MaxQB; Q9CR16; -.
DR PaxDb; Q9CR16; -.
DR PeptideAtlas; Q9CR16; -.
DR PRIDE; Q9CR16; -.
DR ProteomicsDB; 291832; -.
DR Antibodypedia; 16935; 371 antibodies from 37 providers.
DR DNASU; 67738; -.
DR Ensembl; ENSMUST00000029382; ENSMUSP00000029382; ENSMUSG00000027804.
DR GeneID; 67738; -.
DR KEGG; mmu:67738; -.
DR UCSC; uc008pnp.1; mouse.
DR CTD; 5481; -.
DR MGI; MGI:1914988; Ppid.
DR VEuPathDB; HostDB:ENSMUSG00000027804; -.
DR eggNOG; KOG0546; Eukaryota.
DR GeneTree; ENSGT00940000154672; -.
DR HOGENOM; CLU_012062_37_1_1; -.
DR InParanoid; Q9CR16; -.
DR OMA; CKDFGNK; -.
DR OrthoDB; 1403619at2759; -.
DR PhylomeDB; Q9CR16; -.
DR TreeFam; TF324493; -.
DR Reactome; R-MMU-8939211; ESR-mediated signaling.
DR BioGRID-ORCS; 67738; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Ppid; mouse.
DR PRO; PR:Q9CR16; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q9CR16; protein.
DR Bgee; ENSMUSG00000027804; Expressed in embryonic post-anal tail and 122 other tissues.
DR ExpressionAtlas; Q9CR16; baseline and differential.
DR Genevisible; Q9CR16; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0016018; F:cyclosporin A binding; ISS:UniProtKB.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0005528; F:FK506 binding; TAS:MGI.
DR GO; GO:0031072; F:heat shock protein binding; ISO:MGI.
DR GO; GO:0030544; F:Hsp70 protein binding; ISS:UniProtKB.
DR GO; GO:0051879; F:Hsp90 protein binding; ISS:UniProtKB.
DR GO; GO:0030331; F:nuclear estrogen receptor binding; ISS: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:0043066; P:negative regulation of apoptotic process; ISO:MGI.
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; ISO:MGI.
DR GO; GO:0045070; P:positive regulation of viral genome replication; ISO:MGI.
DR GO; GO:0006457; P:protein folding; ISS: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 GO; GO:0051881; P:regulation of mitochondrial membrane potential; ISO:MGI.
DR GO; GO:0006979; P:response to oxidative stress; ISO:MGI.
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 Acetylation; Apoptosis; Chaperone; Cytoplasm; Direct protein sequencing;
KW Isomerase; Nucleus; Phosphoprotein; Protein transport; Reference proteome;
KW Repeat; Rotamase; TPR repeat; Transport.
FT CHAIN 1..370
FT /note="Peptidyl-prolyl cis-trans isomerase D"
FT /id="PRO_0000064154"
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 /evidence="ECO:0000250"
FT REGION 214..370
FT /note="Interaction with HSP90AB1"
FT /evidence="ECO:0000250"
FT MOD_RES 5
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q08752"
FT MOD_RES 171
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 198
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q08752"
SQ SEQUENCE 370 AA; 40743 MW; 32891716E9113438 CRC64;
MSHASPAAKP SNSKNPRVFF DVDIGGERVG RIVLELFADI VPKTAENFRA LCTGEKGTGS
TTGKPLHFKG CPFHRIIKKF MIQGGDFSNQ NGTGGESIYG EKFEDENFHY KHDREGLLSM
ANAGPNTNGS QFFITTVPTP HLDGKHVVFG QVIKGLGVAR TLENVEVNGE KPAKLCVIAE
CGELKEGDDW GIFPKDGSGD SHPDFPEDAD IDLKDVDKIL LISEDLKNIG NTFFKSQNWE
MAIKKYAKVL RYVDSSKAVI EKADRSRLQP IALSCVLNIG ACKLKMSNWQ GAIDSCLEAL
EMDPSNTKAL YRKAQGWQGL KEYDQALADL KKAQEIAPGD KAIQAELLKV KQMIKAQKDK
EKAVYAKMFA
