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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

7UFG

Cryo-EM structure of PAPP-A in complex with IGFBP5

Functional Information from GO Data
ChainGOidnamespacecontents
A0004175molecular_functionendopeptidase activity
A0004222molecular_functionmetalloendopeptidase activity
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0006508biological_processproteolysis
A0007166biological_processcell surface receptor signaling pathway
A0007565biological_processfemale pregnancy
A0008233molecular_functionpeptidase activity
A0008237molecular_functionmetallopeptidase activity
A0008270molecular_functionzinc ion binding
A0016787molecular_functionhydrolase activity
A0046872molecular_functionmetal ion binding
B0004175molecular_functionendopeptidase activity
B0004222molecular_functionmetalloendopeptidase activity
B0005515molecular_functionprotein binding
B0005576cellular_componentextracellular region
B0005615cellular_componentextracellular space
B0006508biological_processproteolysis
B0007166biological_processcell surface receptor signaling pathway
B0007565biological_processfemale pregnancy
B0008233molecular_functionpeptidase activity
B0008237molecular_functionmetallopeptidase activity
B0008270molecular_functionzinc ion binding
B0016787molecular_functionhydrolase activity
B0046872molecular_functionmetal ion binding
C0001649biological_processosteoblast differentiation
C0001968molecular_functionfibronectin binding
C0005515molecular_functionprotein binding
C0005520molecular_functioninsulin-like growth factor binding
C0005576cellular_componentextracellular region
C0005615cellular_componentextracellular space
C0005634cellular_componentnucleus
C0005737cellular_componentcytoplasm
C0005788cellular_componentendoplasmic reticulum lumen
C0007165biological_processsignal transduction
C0007565biological_processfemale pregnancy
C0008283biological_processcell population proliferation
C0014912biological_processnegative regulation of smooth muscle cell migration
C0016942cellular_componentinsulin-like growth factor binding protein complex
C0017148biological_processnegative regulation of translation
C0019838molecular_functiongrowth factor binding
C0030336biological_processnegative regulation of cell migration
C0031994molecular_functioninsulin-like growth factor I binding
C0031995molecular_functioninsulin-like growth factor II binding
C0035556biological_processintracellular signal transduction
C0042567cellular_componentinsulin-like growth factor ternary complex
C0043567biological_processregulation of insulin-like growth factor receptor signaling pathway
C0043569biological_processnegative regulation of insulin-like growth factor receptor signaling pathway
C0045926biological_processnegative regulation of growth
C0048018molecular_functionreceptor ligand activity
C0048286biological_processlung alveolus development
C0048662biological_processnegative regulation of smooth muscle cell proliferation
C0060416biological_processresponse to growth hormone
C0071320biological_processcellular response to cAMP
C1901862biological_processnegative regulation of muscle tissue development
C1904205biological_processnegative regulation of skeletal muscle hypertrophy
C1904707biological_processpositive regulation of vascular associated smooth muscle cell proliferation
C1904754biological_processpositive regulation of vascular associated smooth muscle cell migration
D0001649biological_processosteoblast differentiation
D0001968molecular_functionfibronectin binding
D0005515molecular_functionprotein binding
D0005520molecular_functioninsulin-like growth factor binding
D0005576cellular_componentextracellular region
D0005615cellular_componentextracellular space
D0005634cellular_componentnucleus
D0005737cellular_componentcytoplasm
D0005788cellular_componentendoplasmic reticulum lumen
D0007165biological_processsignal transduction
D0007565biological_processfemale pregnancy
D0008283biological_processcell population proliferation
D0014912biological_processnegative regulation of smooth muscle cell migration
D0016942cellular_componentinsulin-like growth factor binding protein complex
D0017148biological_processnegative regulation of translation
D0019838molecular_functiongrowth factor binding
D0030336biological_processnegative regulation of cell migration
D0031994molecular_functioninsulin-like growth factor I binding
D0031995molecular_functioninsulin-like growth factor II binding
D0035556biological_processintracellular signal transduction
D0042567cellular_componentinsulin-like growth factor ternary complex
D0043567biological_processregulation of insulin-like growth factor receptor signaling pathway
D0043569biological_processnegative regulation of insulin-like growth factor receptor signaling pathway
D0045926biological_processnegative regulation of growth
D0048018molecular_functionreceptor ligand activity
D0048286biological_processlung alveolus development
D0048662biological_processnegative regulation of smooth muscle cell proliferation
D0060416biological_processresponse to growth hormone
D0071320biological_processcellular response to cAMP
D1901862biological_processnegative regulation of muscle tissue development
D1904205biological_processnegative regulation of skeletal muscle hypertrophy
D1904707biological_processpositive regulation of vascular associated smooth muscle cell proliferation
D1904754biological_processpositive regulation of vascular associated smooth muscle cell migration
Functional Information from PROSITE/UniProt
site_idPS00222
Number of Residues16
DetailsIGFBP_N_1 Insulin-like growth factor-binding protein (IGFBP) N-terminal domain signature. GCGCCmtCAlaegqsC
ChainResidueDetails
DGLY32-CYS47
site_idPS00484
Number of Residues34
DetailsTHYROGLOBULIN_1_1 Thyroglobulin type-1 repeat signature. YlpnCdrk.GfYkrkQckpsrgrkrgicWCVdky.G
ChainResidueDetails
DTYR195-GLY228
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues69
DetailsDomain: {"description":"Sushi 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00302","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues122
DetailsDomain: {"description":"Sushi 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00302","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues42
DetailsRegion: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues24
DetailsCompositional bias: {"description":"Basic and acidic residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues2
DetailsActive site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU10095","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU10095","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues6
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues15
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"12421832","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

247947

PDB entries from 2026-01-21

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