PPIC_MOUSE
ID PPIC_MOUSE Reviewed; 212 AA.
AC P30412;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase C {ECO:0000305};
DE Short=PPIase C {ECO:0000305};
DE EC=5.2.1.8 {ECO:0000269|PubMed:1652374};
DE AltName: Full=Cyclophilin C {ECO:0000303|PubMed:1652374};
DE AltName: Full=Rotamase C;
GN Name=Ppic {ECO:0000312|MGI:MGI:97751};
GN Synonyms=Cypc {ECO:0000303|PubMed:1652374};
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], FUNCTION, CATALYTIC ACTIVITY, ACTIVITY
RP REGULATION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=1652374; DOI=10.1016/0092-8674(91)90123-g;
RA Friedman J., Weissman I.L.;
RT "Two cytoplasmic candidates for immunophilin action are revealed by
RT affinity for a new cyclophilin: one in the presence and one in the absence
RT of CsA.";
RL Cell 66:799-806(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Mammary gland;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen,
RC 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 X-RAY CRYSTALLOGRAPHY (1.64 ANGSTROMS) IN COMPLEX WITH CYCLOSPORIN A.
RX PubMed=8265636; DOI=10.1073/pnas.90.24.11850;
RA Ke H., Zhao Y., Luo F., Weissman I.L., Friedman J.;
RT "Crystal structure of murine cyclophilin C complexed with immunosuppressive
RT drug cyclosporin A.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:11850-11854(1993).
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:0000269|PubMed:1652374}.
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; Evidence={ECO:0000269|PubMed:1652374};
CC -!- ACTIVITY REGULATION: Inhibited by cyclosporin A (CsA).
CC {ECO:0000269|PubMed:1652374}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:1652374}.
CC -!- TISSUE SPECIFICITY: Specifically expressed in kidney.
CC {ECO:0000269|PubMed:1652374}.
CC -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family.
CC {ECO:0000305}.
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DR EMBL; M74227; AAA37511.1; -; mRNA.
DR EMBL; BC025861; AAH25861.1; -; mRNA.
DR CCDS; CCDS29252.1; -.
DR PIR; A40047; A40047.
DR RefSeq; NP_032934.1; NM_008908.4.
DR PDB; 2RMC; X-ray; 1.64 A; A/C/E/G=31-212.
DR PDBsum; 2RMC; -.
DR AlphaFoldDB; P30412; -.
DR SMR; P30412; -.
DR BioGRID; 202329; 1.
DR STRING; 10090.ENSMUSP00000025419; -.
DR PhosphoSitePlus; P30412; -.
DR REPRODUCTION-2DPAGE; IPI00130240; -.
DR EPD; P30412; -.
DR jPOST; P30412; -.
DR PaxDb; P30412; -.
DR PeptideAtlas; P30412; -.
DR PRIDE; P30412; -.
DR ProteomicsDB; 289804; -.
DR Antibodypedia; 25658; 254 antibodies from 27 providers.
DR DNASU; 19038; -.
DR Ensembl; ENSMUST00000025419; ENSMUSP00000025419; ENSMUSG00000024538.
DR GeneID; 19038; -.
DR KEGG; mmu:19038; -.
DR UCSC; uc008exu.1; mouse.
DR CTD; 5480; -.
DR MGI; MGI:97751; Ppic.
DR VEuPathDB; HostDB:ENSMUSG00000024538; -.
DR eggNOG; KOG0880; Eukaryota.
DR GeneTree; ENSGT00940000159786; -.
DR HOGENOM; CLU_012062_4_2_1; -.
DR InParanoid; P30412; -.
DR OMA; CSIINSG; -.
DR OrthoDB; 1403619at2759; -.
DR PhylomeDB; P30412; -.
DR TreeFam; TF354259; -.
DR BioGRID-ORCS; 19038; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Ppic; mouse.
DR EvolutionaryTrace; P30412; -.
DR PRO; PR:P30412; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; P30412; protein.
DR Bgee; ENSMUSG00000024538; Expressed in molar tooth and 207 other tissues.
DR ExpressionAtlas; P30412; baseline and differential.
DR Genevisible; P30412; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0016018; F:cyclosporin A binding; ISS:UniProtKB.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IDA:UniProtKB.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR GO; GO:0000413; P:protein peptidyl-prolyl isomerization; IDA:UniProtKB.
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 3D-structure; Cytoplasm; Isomerase; Reference proteome; Rotamase.
FT CHAIN 1..212
FT /note="Peptidyl-prolyl cis-trans isomerase C"
FT /id="PRO_0000064148"
FT DOMAIN 41..198
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
FT STRAND 35..46
FT /evidence="ECO:0007829|PDB:2RMC"
FT STRAND 49..58
FT /evidence="ECO:0007829|PDB:2RMC"
FT TURN 60..62
FT /evidence="ECO:0007829|PDB:2RMC"
FT HELIX 64..75
FT /evidence="ECO:0007829|PDB:2RMC"
FT TURN 76..78
FT /evidence="ECO:0007829|PDB:2RMC"
FT STRAND 86..91
FT /evidence="ECO:0007829|PDB:2RMC"
FT TURN 92..94
FT /evidence="ECO:0007829|PDB:2RMC"
FT STRAND 95..98
FT /evidence="ECO:0007829|PDB:2RMC"
FT STRAND 102..107
FT /evidence="ECO:0007829|PDB:2RMC"
FT STRAND 131..134
FT /evidence="ECO:0007829|PDB:2RMC"
FT STRAND 136..138
FT /evidence="ECO:0007829|PDB:2RMC"
FT STRAND 146..151
FT /evidence="ECO:0007829|PDB:2RMC"
FT HELIX 154..156
FT /evidence="ECO:0007829|PDB:2RMC"
FT TURN 157..159
FT /evidence="ECO:0007829|PDB:2RMC"
FT STRAND 162..168
FT /evidence="ECO:0007829|PDB:2RMC"
FT HELIX 170..177
FT /evidence="ECO:0007829|PDB:2RMC"
FT STRAND 187..189
FT /evidence="ECO:0007829|PDB:2RMC"
FT STRAND 191..206
FT /evidence="ECO:0007829|PDB:2RMC"
SQ SEQUENCE 212 AA; 22794 MW; C99E7AA5D0FA04B6 CRC64;
MSPGPRLLLP AVLCLGLGAL VSSSGSSGVR KRGPSVTDKV FFDVRIGDKD VGRIVIGLFG
NVVPKTVENF VALATGEKGY GYKGSIFHRV IKDFMIQGGD FTARDGTGGM SIYGETFPDE
NFKLKHYGIG WVSMANAGPD TNGSQFFITL TKPTWLDGKH VVFGKVLDGM TVVHSIELQA
TDGHDRPLTD CTIVNSGKID VKTPFVVEVP DW
