Peptidyl-prolyl cis-trans isomerase C

NamePeptidyl-prolyl cis-trans isomerase C
Synonyms
  • 5.2.1.8
  • Cyclophilin C
  • CYPC
  • PPIase C
  • Rotamase C
Gene NamePPIC
OrganismHuman
Amino acid sequence
>lcl|BSEQ0011678|Peptidyl-prolyl cis-trans isomerase C
MGPGPRLLLPLVLCVGLGALVFSSGAEGFRKRGPSVTAKVFFDVRIGDKDVGRIVIGLFG
KVVPKTVENFVALATGEKGYGYKGSKFHRVIKDFMIQGGDITTGDGTGGVSIYGETFPDE
NFKLKHYGIGWVSMANAGPDTNGSQFFITLTKPTWLDGKHVVFGKVIDGMTVVHSIELQA
TDGHDRPLTNCSIINSGKIDVKTPFVVEIADW
Number of residues212
Molecular Weight22763.165
Theoretical pI8.69
GO Classification
Functions
  • peptidyl-prolyl cis-trans isomerase activity
  • cyclosporin A binding
Processes
  • protein folding
  • protein peptidyl-prolyl isomerization
Components
  • cytoplasm
  • extracellular exosome
General FunctionPeptidyl-prolyl cis-trans isomerase activity
Specific FunctionPPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
Pfam Domain Function
Transmembrane RegionsNot Available
GenBank Protein ID547304
UniProtKB IDP45877
UniProtKB Entry NamePPIC_HUMAN
Cellular LocationCytoplasm
Gene sequence
>lcl|BSEQ0011679|Peptidyl-prolyl cis-trans isomerase C (PPIC)
ATGGGCCCGGGTCCTCGGCTGCTGCTACCTCTCGTGCTTTGCGTGGGGCTCGGCGCACTT
GTGTTTTCTTCGGGGGCCGAGGGCTTCCGCAAGCGAGGCCCCTCGGTGACGGCCAAGGTC
TTCTTTGATGTGAGGATTGGAGACAAAGATGTTGGCAGAATTGTGATTGGCCTCTTTGGA
AAAGTTGTGCCCAAGACAGTGGAAAATTTTGTTGCTCTAGCAACAGGAGAGAAAGGATAT
GGATATAAAGGAAGCAAGTTTCATCGTGTCATCAAGGATTTCATGATTCAAGGAGGTGAC
ATCACCACTGGAGATGGCACTGGGGGTGTGAGCATCTATGGTGAGACATTTCCAGATGAG
AACTTCAAGCTGAAGCACTATGGCATTGGGTGGGTCAGCATGGCCAACGCTGGGCCTGAC
ACCAATGGCTCTCAGTTCTTTATCACCTTGACCAAGCCCACCTGGTTGGACGGCAAACAT
GTGGTGTTTGGAAAAGTCATTGATGGGATGACAGTGGTGCACTCCATAGAGCTCCAAGCA
ACTGATGGGCATGACCGTCCACTCACCAACTGCTCGATCATCAACAGTGGCAAGATAGAC
GTGAAAACGCCTTTTGTGGTTGAGATCGCTGATTGGTGA
GenBank Gene IDS71018
GeneCard IDNot Available
GenAtlas IDPPIC
HGNC IDHGNC:9256
Chromosome Location5
Locus5q23.2
References
  1. Schneider H, Charara N, Schmitz R, Wehrli S, Mikol V, Zurini MG, Quesniaux VF, Movva NR: Human cyclophilin C: primary structure, tissue distribution, and determination of binding specificity for cyclosporins. Biochemistry. 1994 Jul 12;33(27):8218-24. 8031755
  2. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. 15489334