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7P2Q

Human Signal Peptidase Complex Paralog C (SPC-C)

Functional Information from GO Data
ChainGOidnamespacecontents
A0004252molecular_functionserine-type endopeptidase activity
A0005515molecular_functionprotein binding
A0005783cellular_componentendoplasmic reticulum
A0005787cellular_componentsignal peptidase complex
A0005789cellular_componentendoplasmic reticulum membrane
A0006465biological_processsignal peptide processing
A0006508biological_processproteolysis
A0008233molecular_functionpeptidase activity
A0016020cellular_componentmembrane
B0005515molecular_functionprotein binding
B0005783cellular_componentendoplasmic reticulum
B0005787cellular_componentsignal peptidase complex
B0005789cellular_componentendoplasmic reticulum membrane
B0006465biological_processsignal peptide processing
B0006508biological_processproteolysis
B0016020cellular_componentmembrane
B0019082biological_processviral protein processing
B0045047biological_processprotein targeting to ER
C0005515molecular_functionprotein binding
C0005783cellular_componentendoplasmic reticulum
C0005787cellular_componentsignal peptidase complex
C0005789cellular_componentendoplasmic reticulum membrane
C0006465biological_processsignal peptide processing
C0016020cellular_componentmembrane
C0045047biological_processprotein targeting to ER
D0003674molecular_functionmolecular_function
D0005515molecular_functionprotein binding
D0005783cellular_componentendoplasmic reticulum
D0005787cellular_componentsignal peptidase complex
D0005789cellular_componentendoplasmic reticulum membrane
D0006465biological_processsignal peptide processing
D0006508biological_processproteolysis
D0016020cellular_componentmembrane
D0019068biological_processvirion assembly
D0019082biological_processviral protein processing
D0045047biological_processprotein targeting to ER
Functional Information from PROSITE/UniProt
site_idPS00430
Number of Residues22
DetailsTONB_DEPENDENT_REC_1 TonB-dependent receptor (TBDR) proteins signature 1. pmntvlsranslfa.....................................................................................................FSLSVMAA
ChainResidueDetails
BPRO0-ALA21

site_idPS00501
Number of Residues8
DetailsSPASE_I_1 Signal peptidases I serine active site. SGSMEPAF
ChainResidueDetails
ASER66-PHE73

site_idPS00761
Number of Residues14
DetailsSPASE_I_3 Signal peptidases I signature 3. FLTKGDNNevDdrG
ChainResidueDetails
APHE123-GLY136

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues177
DetailsTOPO_DOM: Cytoplasmic => ECO:0000250|UniProtKB:Q28250
ChainResidueDetails
CALA2-THR86
CSER133-LYS226

site_idSWS_FT_FI2
Number of Residues40
DetailsTRANSMEM: Helical => ECO:0000255
ChainResidueDetails
CILE87-PHE107
CPRO112-THR132

site_idSWS_FT_FI3
Number of Residues3
DetailsTOPO_DOM: Lumenal => ECO:0000250|UniProtKB:Q28250
ChainResidueDetails
CPRO108-LYS111

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: N-acetylalanine => ECO:0000269|PubMed:34388369, ECO:0000269|Ref.4, ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22814378, ECO:0007744|PubMed:25944712
ChainResidueDetails
CALA2
AHIS108
AASP134

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
CLYS169
CLYS191

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PDB entries from 2024-07-17

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