PPIC_HUMAN
ID PPIC_HUMAN Reviewed; 212 AA.
AC P45877; A4LBB5;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 181.
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:20676357};
DE AltName: Full=Cyclophilin C {ECO:0000303|PubMed:8031755};
DE AltName: Full=Rotamase C;
GN Name=PPIC {ECO:0000312|HGNC:HGNC:9256}; Synonyms=CYPC;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=8031755; DOI=10.1021/bi00193a007;
RA Schneider H., Charara N., Schmitz R., Wehrli S., Mikol V., Zurini M.G.,
RA Quesniaux V.F., Movva N.R.;
RT "Human cyclophilin C: primary structure, tissue distribution, and
RT determination of binding specificity for cyclosporins.";
RL Biochemistry 33:8218-8224(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ARG-86; LEU-160 AND
RP SER-190.
RG NIEHS SNPs program;
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Uterus;
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 [5] {ECO:0007744|PDB:2ESL}
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 24-212 IN COMPLEX WITH
RP CYCLOSPORIN A, FUNCTION, CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
RX PubMed=20676357; DOI=10.1371/journal.pbio.1000439;
RA Davis T.L., Walker J.R., Campagna-Slater V., Finerty P.J., Paramanathan R.,
RA Bernstein G., MacKenzie F., Tempel W., Ouyang H., Lee W.H.,
RA Eisenmesser E.Z., Dhe-Paganon S.;
RT "Structural and biochemical characterization of the human cyclophilin
RT family of peptidyl-prolyl isomerases.";
RL PLoS Biol. 8:E1000439-E1000439(2010).
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:20676357}.
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:0000269|PubMed:20676357};
CC -!- ACTIVITY REGULATION: Inhibited by cyclosporin A (CsA).
CC {ECO:0000305|PubMed:20676357}.
CC -!- INTERACTION:
CC P45877; Q8N9N5: BANP; NbExp=3; IntAct=EBI-953909, EBI-744695;
CC P45877; Q8N9N5-2: BANP; NbExp=3; IntAct=EBI-953909, EBI-11524452;
CC P45877; Q96L46: CAPNS2; NbExp=3; IntAct=EBI-953909, EBI-12188723;
CC P45877; B3EWG5: FAM25C; NbExp=3; IntAct=EBI-953909, EBI-14240149;
CC P45877; O43765: SGTA; NbExp=6; IntAct=EBI-953909, EBI-347996;
CC P45877; Q96EQ0: SGTB; NbExp=3; IntAct=EBI-953909, EBI-744081;
CC P45877; Q9NZ09: UBAP1; NbExp=3; IntAct=EBI-953909, EBI-9641159;
CC P45877; Q9UMX0: UBQLN1; NbExp=3; IntAct=EBI-953909, EBI-741480;
CC P45877; Q9UMX0-2: UBQLN1; NbExp=3; IntAct=EBI-953909, EBI-10173939;
CC P45877; Q9UHD9: UBQLN2; NbExp=5; IntAct=EBI-953909, EBI-947187;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P30412}.
CC -!- TISSUE SPECIFICITY: Expressed in kidney, skeletal muscle, pancreas,
CC heart, lung, liver and to a lower extent in brain.
CC {ECO:0000269|PubMed:8031755}.
CC -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/ppic/";
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DR EMBL; S71018; AAB31350.1; -; mRNA.
DR EMBL; EF506885; ABO43038.1; -; Genomic_DNA.
DR EMBL; CH471086; EAW48878.1; -; Genomic_DNA.
DR EMBL; BC002678; AAH02678.1; -; mRNA.
DR CCDS; CCDS4133.1; -.
DR PIR; A54204; A54204.
DR RefSeq; NP_000934.1; NM_000943.4.
DR PDB; 2ESL; X-ray; 1.90 A; A/B/C/D/E/F=24-212.
DR PDBsum; 2ESL; -.
DR AlphaFoldDB; P45877; -.
DR BMRB; P45877; -.
DR SMR; P45877; -.
DR BioGRID; 111476; 23.
DR IntAct; P45877; 13.
DR STRING; 9606.ENSP00000303057; -.
DR BindingDB; P45877; -.
DR ChEMBL; CHEMBL2424505; -.
DR DrugBank; DB00172; Proline.
DR GlyConnect; 1596; 3 N-Linked glycans (1 site).
DR GlyGen; P45877; 1 site, 3 N-linked glycans (1 site).
DR iPTMnet; P45877; -.
DR PhosphoSitePlus; P45877; -.
DR BioMuta; PPIC; -.
DR DMDM; 1169178; -.
DR EPD; P45877; -.
DR jPOST; P45877; -.
DR MassIVE; P45877; -.
DR MaxQB; P45877; -.
DR PaxDb; P45877; -.
DR PeptideAtlas; P45877; -.
DR PRIDE; P45877; -.
DR ProteomicsDB; 55686; -.
DR Antibodypedia; 25658; 254 antibodies from 27 providers.
DR DNASU; 5480; -.
DR Ensembl; ENST00000306442.5; ENSP00000303057.4; ENSG00000168938.6.
DR GeneID; 5480; -.
DR KEGG; hsa:5480; -.
DR MANE-Select; ENST00000306442.5; ENSP00000303057.4; NM_000943.5; NP_000934.1.
DR UCSC; uc003kth.4; human.
DR CTD; 5480; -.
DR DisGeNET; 5480; -.
DR GeneCards; PPIC; -.
DR HGNC; HGNC:9256; PPIC.
DR HPA; ENSG00000168938; Low tissue specificity.
DR MIM; 123842; gene.
DR neXtProt; NX_P45877; -.
DR OpenTargets; ENSG00000168938; -.
DR PharmGKB; PA33581; -.
DR VEuPathDB; HostDB:ENSG00000168938; -.
DR eggNOG; KOG0880; Eukaryota.
DR GeneTree; ENSGT00940000159786; -.
DR HOGENOM; CLU_012062_4_2_1; -.
DR InParanoid; P45877; -.
DR OMA; CSIINSG; -.
DR OrthoDB; 1403619at2759; -.
DR PhylomeDB; P45877; -.
DR TreeFam; TF354259; -.
DR BRENDA; 5.2.1.8; 2681.
DR PathwayCommons; P45877; -.
DR SignaLink; P45877; -.
DR BioGRID-ORCS; 5480; 17 hits in 1081 CRISPR screens.
DR ChiTaRS; PPIC; human.
DR EvolutionaryTrace; P45877; -.
DR GeneWiki; PPIC; -.
DR GenomeRNAi; 5480; -.
DR Pharos; P45877; Tbio.
DR PRO; PR:P45877; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; P45877; protein.
DR Bgee; ENSG00000168938; Expressed in tibia and 194 other tissues.
DR Genevisible; P45877; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0016018; F:cyclosporin A binding; IDA: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_0000064147"
FT DOMAIN 41..198
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
FT VARIANT 86
FT /note="K -> R (in dbSNP:rs34341374)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_051770"
FT VARIANT 160
FT /note="H -> L (in dbSNP:rs45560036)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_060712"
FT VARIANT 190
FT /note="N -> S (in dbSNP:rs451195)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_024319"
FT STRAND 35..46
FT /evidence="ECO:0007829|PDB:2ESL"
FT STRAND 49..58
FT /evidence="ECO:0007829|PDB:2ESL"
FT TURN 60..62
FT /evidence="ECO:0007829|PDB:2ESL"
FT HELIX 64..75
FT /evidence="ECO:0007829|PDB:2ESL"
FT TURN 76..78
FT /evidence="ECO:0007829|PDB:2ESL"
FT STRAND 89..91
FT /evidence="ECO:0007829|PDB:2ESL"
FT TURN 92..94
FT /evidence="ECO:0007829|PDB:2ESL"
FT STRAND 95..98
FT /evidence="ECO:0007829|PDB:2ESL"
FT STRAND 102..107
FT /evidence="ECO:0007829|PDB:2ESL"
FT STRAND 131..134
FT /evidence="ECO:0007829|PDB:2ESL"
FT STRAND 136..138
FT /evidence="ECO:0007829|PDB:2ESL"
FT STRAND 146..151
FT /evidence="ECO:0007829|PDB:2ESL"
FT HELIX 154..156
FT /evidence="ECO:0007829|PDB:2ESL"
FT TURN 157..159
FT /evidence="ECO:0007829|PDB:2ESL"
FT STRAND 162..168
FT /evidence="ECO:0007829|PDB:2ESL"
FT HELIX 170..177
FT /evidence="ECO:0007829|PDB:2ESL"
FT STRAND 187..189
FT /evidence="ECO:0007829|PDB:2ESL"
FT STRAND 191..206
FT /evidence="ECO:0007829|PDB:2ESL"
SQ SEQUENCE 212 AA; 22763 MW; 6F3DB547A2AE581B CRC64;
MGPGPRLLLP LVLCVGLGAL VFSSGAEGFR KRGPSVTAKV FFDVRIGDKD VGRIVIGLFG
KVVPKTVENF VALATGEKGY GYKGSKFHRV IKDFMIQGGD ITTGDGTGGV SIYGETFPDE
NFKLKHYGIG WVSMANAGPD TNGSQFFITL TKPTWLDGKH VVFGKVIDGM TVVHSIELQA
TDGHDRPLTN CSIINSGKID VKTPFVVEIA DW
