PPIB_MOUSE
ID PPIB_MOUSE Reviewed; 216 AA.
AC P24369;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 2.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase B;
DE Short=PPIase B;
DE EC=5.2.1.8 {ECO:0000250|UniProtKB:P23284};
DE AltName: Full=CYP-S1;
DE AltName: Full=Cyclophilin B;
DE AltName: Full=Rotamase B;
DE AltName: Full=S-cyclophilin;
DE Short=SCYLP;
DE Flags: Precursor;
GN Name=Ppib;
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 [MRNA].
RX PubMed=1710767; DOI=10.1128/mcb.11.7.3484-3491.1991;
RA Hasel K.W., Glass J.R., Godbout M., Sutcliffe J.G.;
RT "An endoplasmic reticulum-specific cyclophilin.";
RL Mol. Cell. Biol. 11:3484-3491(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J;
RX PubMed=1756174; DOI=10.1016/0167-4781(91)90207-3;
RA Schumacher A., Schroeter H., Multhaup G., Nordheim A.;
RT "Murine cyclophilin-S1: a variant peptidyl-prolyl isomerase with a putative
RT signal sequence expressed in differentiating F9 cells.";
RL Biochim. Biophys. Acta 1129:13-22(1991).
RN [3]
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 [4]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-209, SUCCINYLATION [LARGE SCALE
RP ANALYSIS] AT LYS-209, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Embryonic fibroblast, and Liver;
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).
RN [5]
RP TISSUE SPECIFICITY.
RX PubMed=25967121; DOI=10.1681/asn.2014070728;
RA Borschewski A., Himmerkus N., Boldt C., Blankenstein K.I., McCormick J.A.,
RA Lazelle R., Willnow T.E., Jankowski V., Plain A., Bleich M., Ellison D.H.,
RA Bachmann S., Mutig K.;
RT "Calcineurin and sorting-related receptor with A-type repeats interact to
RT regulate the renal Na(+)-K(+)-2Cl(-) cotransporter.";
RL J. Am. Soc. Nephrol. 27:107-119(2016).
CC -!- FUNCTION: PPIase that catalyzes the cis-trans isomerization of proline
CC imidic peptide bonds in oligopeptides and may therefore assist protein
CC folding. {ECO:0000250|UniProtKB:P23284}.
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:P23284};
CC -!- ACTIVITY REGULATION: Inhibited by cyclosporin A (CsA).
CC {ECO:0000250|UniProtKB:P23284}.
CC -!- SUBUNIT: Interacts with DYM. Interacts with CALR, CLGN and CANX. Part
CC of a large chaperone multiprotein complex comprising DNAJB11, HSP90B1,
CC HSPA5, HYOU, PDIA2, PDIA4, PDIA6, PPIB, SDF2L1, UGGT1 and very small
CC amounts of ERP29, but not, or at very low levels, CALR nor CANX.
CC {ECO:0000250|UniProtKB:P23284}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
CC {ECO:0000250|UniProtKB:P23284}. Melanosome
CC {ECO:0000250|UniProtKB:P23284}.
CC -!- TISSUE SPECIFICITY: Expressed in the kidney thick ascending limb (at
CC protein level). {ECO:0000269|PubMed:25967121}.
CC -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family. PPIase B
CC subfamily. {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-9 is the initiator.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA37498.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAA41736.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; M60456; AAA37498.1; ALT_INIT; mRNA.
DR EMBL; X58990; CAA41736.1; ALT_INIT; mRNA.
DR CCDS; CCDS23301.1; -.
DR RefSeq; NP_035279.2; NM_011149.2.
DR AlphaFoldDB; P24369; -.
DR SMR; P24369; -.
DR BioGRID; 202328; 25.
DR CORUM; P24369; -.
DR IntAct; P24369; 6.
DR MINT; P24369; -.
DR STRING; 10090.ENSMUSP00000034947; -.
DR iPTMnet; P24369; -.
DR PhosphoSitePlus; P24369; -.
DR EPD; P24369; -.
DR jPOST; P24369; -.
DR PaxDb; P24369; -.
DR PeptideAtlas; P24369; -.
DR PRIDE; P24369; -.
DR ProteomicsDB; 289377; -.
DR TopDownProteomics; P24369; -.
DR Antibodypedia; 2584; 501 antibodies from 33 providers.
DR DNASU; 19035; -.
DR Ensembl; ENSMUST00000034947; ENSMUSP00000034947; ENSMUSG00000032383.
DR GeneID; 19035; -.
DR KEGG; mmu:19035; -.
DR UCSC; uc009qei.1; mouse.
DR CTD; 5479; -.
DR MGI; MGI:97750; Ppib.
DR VEuPathDB; HostDB:ENSMUSG00000032383; -.
DR eggNOG; KOG0880; Eukaryota.
DR GeneTree; ENSGT00940000158007; -.
DR HOGENOM; CLU_012062_4_2_1; -.
DR InParanoid; P24369; -.
DR OMA; GEGYPGS; -.
DR OrthoDB; 1403619at2759; -.
DR PhylomeDB; P24369; -.
DR TreeFam; TF354259; -.
DR Reactome; R-MMU-1650814; Collagen biosynthesis and modifying enzymes.
DR BioGRID-ORCS; 19035; 4 hits in 73 CRISPR screens.
DR ChiTaRS; Ppib; mouse.
DR PRO; PR:P24369; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; P24369; protein.
DR Bgee; ENSMUSG00000032383; Expressed in external carotid artery and 264 other tissues.
DR ExpressionAtlas; P24369; baseline and differential.
DR Genevisible; P24369; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0034663; C:endoplasmic reticulum chaperone complex; IDA:ParkinsonsUK-UCL.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISS:CAFA.
DR GO; GO:0005790; C:smooth endoplasmic reticulum; ISO:MGI.
DR GO; GO:0016018; F:cyclosporin A binding; ISS:UniProtKB.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; ISS:UniProtKB.
DR GO; GO:0070063; F:RNA polymerase binding; ISO:MGI.
DR GO; GO:0060348; P:bone development; ISO:MGI.
DR GO; GO:0061077; P:chaperone-mediated protein folding; ISS:CAFA.
DR GO; GO:0030593; P:neutrophil chemotaxis; ISO:MGI.
DR GO; GO:0044829; P:positive regulation by host of viral genome replication; ISO:MGI.
DR GO; GO:0044794; P:positive regulation by host of viral process; ISO:MGI.
DR GO; GO:0040018; P:positive regulation of multicellular organism growth; ISO:MGI.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR GO; GO:0000413; P:protein peptidyl-prolyl isomerization; ISS:UniProtKB.
DR GO; GO:0050821; P:protein stabilization; ISO:MGI.
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 1: Evidence at protein level;
KW Acetylation; Endoplasmic reticulum; Isomerase; Reference proteome;
KW Rotamase; Signal.
FT SIGNAL 1..33
FT /evidence="ECO:0000250"
FT CHAIN 34..216
FT /note="Peptidyl-prolyl cis-trans isomerase B"
FT /id="PRO_0000025480"
FT DOMAIN 47..204
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
FT MOTIF 213..216
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000250"
FT MOD_RES 84
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99KR7"
FT MOD_RES 165
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99KR7"
FT MOD_RES 209
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 209
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
SQ SEQUENCE 216 AA; 23713 MW; CE9DAD1544AE72FE CRC64;
MLRLSERNMK VLFAAALIVG SVVFLLLPGP SVANDKKKGP KVTVKVYFDL QIGDESVGRV
VFGLFGKTVP KTVDNFVALA TGEKGFGYKN SKFHRVIKDF MIQGGDFTRG DGTGGKSIYG
ERFPDENFKL KHYGPGWVSM ANAGKDTNGS QFFITTVKTS WLDGKHVVFG KVLEGMDVVR
KVESTKTDSR DKPLKDVIIV DSGKIEVEKP FAIAKE
