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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

1MIR

RAT PROCATHEPSIN B

Functional Information from GO Data
ChainGOidnamespacecontents
A0004175molecular_functionendopeptidase activity
A0004197molecular_functioncysteine-type endopeptidase activity
A0005515molecular_functionprotein binding
A0005518molecular_functioncollagen binding
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0005764cellular_componentlysosome
A0005901cellular_componentcaveola
A0006508biological_processproteolysis
A0006590biological_processthyroid hormone generation
A0006914biological_processautophagy
A0007283biological_processspermatogenesis
A0007519biological_processskeletal muscle tissue development
A0008233molecular_functionpeptidase activity
A0008234molecular_functioncysteine-type peptidase activity
A0009612biological_processresponse to mechanical stimulus
A0009749biological_processresponse to glucose
A0009897cellular_componentexternal side of plasma membrane
A0009986cellular_componentcell surface
A0014075biological_processresponse to amine
A0016324cellular_componentapical plasma membrane
A0016787molecular_functionhydrolase activity
A0030163biological_processprotein catabolic process
A0030574biological_processcollagen catabolic process
A0030855biological_processepithelial cell differentiation
A0030984molecular_functionkininogen binding
A0034097biological_processresponse to cytokine
A0042277molecular_functionpeptide binding
A0042383cellular_componentsarcolemma
A0042470cellular_componentmelanosome
A0042802molecular_functionidentical protein binding
A0043394molecular_functionproteoglycan binding
A0043434biological_processresponse to peptide hormone
A0044877molecular_functionprotein-containing complex binding
A0045471biological_processresponse to ethanol
A0046697biological_processdecidualization
A0046718biological_processsymbiont entry into host cell
A0048471cellular_componentperinuclear region of cytoplasm
A0050790biological_processregulation of catalytic activity
A0051402biological_processneuron apoptotic process
A0051603biological_processproteolysis involved in protein catabolic process
A0070670biological_processresponse to interleukin-4
A0071260biological_processcellular response to mechanical stimulus
A0071548biological_processresponse to dexamethasone
A0097067biological_processcellular response to thyroid hormone stimulus
A1904090cellular_componentpeptidase inhibitor complex
A1904373biological_processresponse to kainic acid
B0004175molecular_functionendopeptidase activity
B0004197molecular_functioncysteine-type endopeptidase activity
B0005515molecular_functionprotein binding
B0005518molecular_functioncollagen binding
B0005576cellular_componentextracellular region
B0005615cellular_componentextracellular space
B0005764cellular_componentlysosome
B0005901cellular_componentcaveola
B0006508biological_processproteolysis
B0006590biological_processthyroid hormone generation
B0006914biological_processautophagy
B0007283biological_processspermatogenesis
B0007519biological_processskeletal muscle tissue development
B0008233molecular_functionpeptidase activity
B0008234molecular_functioncysteine-type peptidase activity
B0009612biological_processresponse to mechanical stimulus
B0009749biological_processresponse to glucose
B0009897cellular_componentexternal side of plasma membrane
B0009986cellular_componentcell surface
B0014075biological_processresponse to amine
B0016324cellular_componentapical plasma membrane
B0016787molecular_functionhydrolase activity
B0030163biological_processprotein catabolic process
B0030574biological_processcollagen catabolic process
B0030855biological_processepithelial cell differentiation
B0030984molecular_functionkininogen binding
B0034097biological_processresponse to cytokine
B0042277molecular_functionpeptide binding
B0042383cellular_componentsarcolemma
B0042470cellular_componentmelanosome
B0042802molecular_functionidentical protein binding
B0043394molecular_functionproteoglycan binding
B0043434biological_processresponse to peptide hormone
B0044877molecular_functionprotein-containing complex binding
B0045471biological_processresponse to ethanol
B0046697biological_processdecidualization
B0046718biological_processsymbiont entry into host cell
B0048471cellular_componentperinuclear region of cytoplasm
B0050790biological_processregulation of catalytic activity
B0051402biological_processneuron apoptotic process
B0051603biological_processproteolysis involved in protein catabolic process
B0070670biological_processresponse to interleukin-4
B0071260biological_processcellular response to mechanical stimulus
B0071548biological_processresponse to dexamethasone
B0097067biological_processcellular response to thyroid hormone stimulus
B1904090cellular_componentpeptidase inhibitor complex
B1904373biological_processresponse to kainic acid
Functional Information from PDB Data
site_idCYA
Number of Residues3
DetailsACTIVE SITE WITH CYS 29 MUTATED TO SER.
ChainResidue
ASER29
AHIS199
AASN219
site_idCYB
Number of Residues3
DetailsACTIVE SITE WITH CYS 29 MUTATED TO SER.
ChainResidue
BSER29
BHIS199
BASN219
Functional Information from PROSITE/UniProt
site_idPS00435
Number of Residues11
DetailsPEROXIDASE_1 Peroxidases proximal heme-ligand signature. EAGDVMGGHAI
ChainResidueDetails
AGLU191-ILE201
site_idPS00639
Number of Residues11
DetailsTHIOL_PROTEASE_HIS Eukaryotic thiol (cysteine) proteases histidine active site. GGHAIRILGWG
ChainResidueDetails
AGLY197-GLY207
site_idPS00640
Number of Residues20
DetailsTHIOL_PROTEASE_ASN Eukaryotic thiol (cysteine) proteases asparagine active site. YWLvANSWnadWGdnGFFkI
ChainResidueDetails
ATYR214-ILE233
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues10
DetailsPropeptide: {"featureId":"PRO_0000026157","evidences":[{"source":"UniProtKB","id":"P07858","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues2
DetailsActive site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU10088","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"7890671","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8740363","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues2
DetailsActive site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU10089","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"7890671","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8740363","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues2
DetailsActive site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU10090","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"7890671","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8740363","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P10605","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"6574504","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 9pap
ChainResidueDetails
AHIS199
AASN219
AGLN23
site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 9pap
ChainResidueDetails
BHIS199
BASN219
BGLN23
site_idCSA3
Number of Residues4
DetailsAnnotated By Reference To The Literature 9pap
ChainResidueDetails
AHIS199
AASN219
AGLN23
ASER29
site_idCSA4
Number of Residues4
DetailsAnnotated By Reference To The Literature 9pap
ChainResidueDetails
BHIS199
BASN219
BGLN23
BSER29

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PDB entries from 2025-12-24

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