Peptidyl-prolyl cis-trans isomerase C

Details

Name
Peptidyl-prolyl cis-trans isomerase C
Synonyms
  • 5.2.1.8
  • Cyclophilin C
  • CYPC
  • PPIase C
  • Rotamase C
Gene Name
PPIC
Organism
Humans
Amino acid sequence
>lcl|BSEQ0011678|Peptidyl-prolyl cis-trans isomerase C
MGPGPRLLLPLVLCVGLGALVFSSGAEGFRKRGPSVTAKVFFDVRIGDKDVGRIVIGLFG
KVVPKTVENFVALATGEKGYGYKGSKFHRVIKDFMIQGGDITTGDGTGGVSIYGETFPDE
NFKLKHYGIGWVSMANAGPDTNGSQFFITLTKPTWLDGKHVVFGKVIDGMTVVHSIELQA
TDGHDRPLTNCSIINSGKIDVKTPFVVEIADW
Number of residues
212
Molecular Weight
22763.165
Theoretical pI
8.69
GO Classification
Functions
cyclosporin A binding / peptidyl-prolyl cis-trans isomerase activity
Processes
protein folding / protein peptidyl-prolyl isomerization
Components
cytoplasm / extracellular exosome
General Function
Peptidyl-prolyl cis-trans isomerase activity
Specific Function
PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Cytoplasm
Gene sequence
>lcl|BSEQ0011679|Peptidyl-prolyl cis-trans isomerase C (PPIC)
ATGGGCCCGGGTCCTCGGCTGCTGCTACCTCTCGTGCTTTGCGTGGGGCTCGGCGCACTT
GTGTTTTCTTCGGGGGCCGAGGGCTTCCGCAAGCGAGGCCCCTCGGTGACGGCCAAGGTC
TTCTTTGATGTGAGGATTGGAGACAAAGATGTTGGCAGAATTGTGATTGGCCTCTTTGGA
AAAGTTGTGCCCAAGACAGTGGAAAATTTTGTTGCTCTAGCAACAGGAGAGAAAGGATAT
GGATATAAAGGAAGCAAGTTTCATCGTGTCATCAAGGATTTCATGATTCAAGGAGGTGAC
ATCACCACTGGAGATGGCACTGGGGGTGTGAGCATCTATGGTGAGACATTTCCAGATGAG
AACTTCAAGCTGAAGCACTATGGCATTGGGTGGGTCAGCATGGCCAACGCTGGGCCTGAC
ACCAATGGCTCTCAGTTCTTTATCACCTTGACCAAGCCCACCTGGTTGGACGGCAAACAT
GTGGTGTTTGGAAAAGTCATTGATGGGATGACAGTGGTGCACTCCATAGAGCTCCAAGCA
ACTGATGGGCATGACCGTCCACTCACCAACTGCTCGATCATCAACAGTGGCAAGATAGAC
GTGAAAACGCCTTTTGTGGTTGAGATCGCTGATTGGTGA
Chromosome Location
5
Locus
5q23.2
External Identifiers
ResourceLink
UniProtKB IDP45877
UniProtKB Entry NamePPIC_HUMAN
GenBank Protein ID547304
GenBank Gene IDS71018
GenAtlas IDPPIC
HGNC IDHGNC:9256
General 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. [Article]
  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. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB00172ProlinenutraceuticalunknownDetails