KEGG   PATHWAY: cho04141
Entry
cho04141                    Pathway                                
Name
Protein processing in endoplasmic reticulum - Cryptosporidium hominis
Description
The endoplasmic reticulum (ER) is a subcellular organelle where proteins are folded with the help of lumenal chaperones. Newly synthesized peptides enter the ER via the sec61 pore and are glycosylated. Correctly folded proteins are packaged into transport vesicles that shuttle them to the Golgi complex. Misfolded proteins are retained within the ER lumen in complex with molecular chaperones. Proteins that are terminally misfolded bind to BiP and are directed toward degradation through the proteasome in a process called ER-associated degradation (ERAD). Accumulation of misfolded proteins in the ER causes ER stress and activates a signaling pathway called the unfolded protein response (UPR). In certain severe situations, however, the protective mechanisms activated by the UPR are not sufficient to restore normal ER function and cells die by apoptosis.
Class
Genetic Information Processing; Folding, sorting and degradation
Pathway map
cho04141  Protein processing in endoplasmic reticulum
cho04141

Other DBs
GO: 0030433 0034976
Organism
Cryptosporidium hominis [GN:cho]
Gene
Chro.70118  Pfsec61 [KO:K10956]
Chro.50257  hypothetical protein [KO:K12275]
Chro.70433  DNAJ-like Sec63 [KO:K09540]
Chro.60585  ribophorin i [KO:K12666]
Chro.70567  hypothetical protein [KO:K12667]
Chro.50149  defender against cell death protein [KO:K12668]
Chro.20179  dolichyl-di-phosphooligosaccharide-protein glycotransferase (oligosaccharyltransferase)-related [KO:K12670]
Chro.60239  oligosaccharyl transferase stt3 protein [KO:K07151] [EC:2.4.99.18]
Chro.80596  hypothetical protein [KO:K19478]
Chro.20349  HSP protein [KO:K09486]
Chro.70049  heat shock protein 70 precursor [KO:K09490] [EC:3.6.4.10]
Chro.70265  small GTP-binding protein sar1 [KO:K07953] [EC:3.6.5.-]
Chro.80472  hypothetical protein [KO:K14004]
Chro.40040  hypothetical protein [KO:K14005]
Chro.30216  transport protein [KO:K14006]
Chro.80148  SEC24 [KO:K14007]
Chro.80513  hypothetical protein [KO:K14007]
Chro.60023  protein disulphide isomerase [KO:K09580] [EC:5.3.4.1]
Chro.10099  hypothetical protein [KO:K09580] [EC:5.3.4.1]
Chro.70569  protein disulfide isomerase precursor (PDI) [KO:K09580] [EC:5.3.4.1]
Chro.60110  transmembrane, thioredoxin domain protein [KO:K09580] [EC:5.3.4.1]
Chro.70453  protein disulfide isomerase-related protein (provisional) [KO:K09584] [EC:5.3.4.1]
Chro.80371  hypothetical protein [KO:K10950] [EC:1.8.4.-]
Chro.50040  hypothetical protein [KO:K13989]
Chro.60413  multi-pass transmembrane protein [KO:K13989]
Chro.10043  cell division cycle protein 48 [KO:K13525]
Chro.70227  hypothetical protein [KO:K14015]
Chro.40141  hypothetical protein [KO:K14016]
Chro.20010  heat shock protein [KO:K03283]
Chro.80434  DNAJ domain protein [KO:K09503]
Chro.50028  CG3061-PA [KO:K09518]
Chro.30427  heat shock protein 83 [KO:K04079]
Chro.20225  hypothetical protein [KO:K09562]
Chro.40262  At3g18860/MCB22_3 [KO:K14018]
Chro.70524  RAD 23B protein [KO:K10839]
Chro.40266  required with RAD23 for duplication of the spindle pole body; Dsk2p [KO:K04523]
Chro.70562  suppressor of NosA [KO:K04523]
Chro.10044  hypothetical protein [KO:K11863] [EC:3.4.22.-]
Chro.30281  hypothetical protein [KO:K10597] [EC:2.3.2.27]
Chro.70587  eukaryotic translation initiation factor 2 alpha subunit [KO:K03237]
Chro.80443  hypothetical protein [KO:K10578] [EC:2.3.2.23]
Chro.10052  ubiquitin conjugating enzyme E2 [KO:K10575] [EC:2.3.2.23]
Chro.80300  hypothetical protein [KO:K10601] [EC:2.3.2.27]
Chro.80112  ring-box 1; RING box protein 1; regulator of cullins 1; RING finger protein; ZYP protein [KO:K03868] [EC:2.3.2.32]
Compound
C00076  Calcium cation
G00009   
G00010   
G00011   
G00012   
G10694   
Reference
  Authors
Naidoo N
  Title
ER and aging-Protein folding and the ER stress response.
  Journal
Ageing Res Rev 8:150-9 (2009)
DOI:10.1016/j.arr.2009.03.001
Reference
  Authors
Malhotra JD, Kaufman RJ
  Title
The endoplasmic reticulum and the unfolded protein response.
  Journal
Semin Cell Dev Biol 18:716-31 (2007)
DOI:10.1016/j.semcdb.2007.09.003
Reference
  Authors
Maattanen P, Gehring K, Bergeron JJ, Thomas DY
  Title
Protein quality control in the ER: the recognition of misfolded proteins.
  Journal
Semin Cell Dev Biol 21:500-11 (2010)
DOI:10.1016/j.semcdb.2010.03.006
Reference
  Authors
Stolz A, Wolf DH
  Title
Endoplasmic reticulum associated protein degradation: a chaperone assisted journey to hell.
  Journal
Biochim Biophys Acta 1803:694-705 (2010)
DOI:10.1016/j.bbamcr.2010.02.005
Reference
  Authors
Dejgaard K, Theberge JF, Heath-Engel H, Chevet E, Tremblay ML, Thomas DY
  Title
Organization of the Sec61 translocon, studied by high resolution native electrophoresis.
  Journal
J Proteome Res 9:1763-71 (2010)
DOI:10.1021/pr900900x
Related
pathway
cho00510  N-Glycan biosynthesis
cho03050  Proteasome
cho03060  Protein export
KO pathway
ko04141   

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