P85064 · SPI_SCHGR

Function

function

Serine protease inhibitor (PubMed:16839309, PubMed:23075397).
Inhibits porcine pancreatic elastase with a Ki of 58.3 nM, human neutrophil elastase with a Ki of 3.6 nM, cathepsin G with a Ki of 153.5 nM, chymotrypsin with a Ki of 26.7 nM and subtilisin with a Ki of 0.68 nM. Does not inhibit neutrophil protease 3 or pancreatic trypsin (PubMed:16839309).

pH Dependence

No decrease in activity observed after incubating at pH 2.5, pH 7.4 and at pH 11.0 for 1 hour to overnight (PubMed:16839309, PubMed:23075397).

Temperature Dependence

Thermostable (PubMed:16839309, PubMed:23075397).
No decrease in activity was observed after heating for 1 hour at up to 95 degrees Celsius (PubMed:16839309, PubMed:23075397).

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Molecular Functionserine-type endopeptidase inhibitor activity
Biological Processnegative regulation of peptidase activity

Keywords

Protein family/group databases

Names & Taxonomy

Protein names

  • Recommended name
    Greglin

Organism names

Accessions

  • Primary accession
    P85064

PTM/Processing

Features

Showing features for chain, modified residue, disulfide bond.

Type
IDPosition(s)Description
ChainPRO_00002714081-83Greglin
Modified residue8Phosphoserine
Modified residue11Phosphoserine
Modified residue15Phosphoserine
Disulfide bond21↔55
Disulfide bond25↔48
Disulfide bond33↔69
Disulfide bond53↔76

Keywords

PTM databases

Interaction

Protein-protein interaction databases

Family & Domains

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    83
  • Mass (Da)
    9,195
  • Last updated
    2015-04-29 v3
  • Checksum
    CFEAA69ABDCC39EF
SEDDGSASPESQEMSYTELPCPSICPLIYAPVCVEDSNQDFYLFVNECEVRKCGCEAGFVYTFVPREMCKATTSLCPMQTKSS

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict7in Ref. 1; AA sequence
Sequence conflict17-25in Ref. 1; AA sequence
Sequence conflict39in Ref. 1; AA sequence

Mass Spectrometry

Molecular mass is 9,661.13 Da. Determined by Electrospray.
Molecular mass is 9,733.08 Da. Determined by Electrospray. Mono-phosphorylated form.
Molecular mass is 9,813.06 Da. Determined by Electrospray. Di-phosphorylated form.
Molecular mass is 9,893.04 Da. Determined by Electrospray. Tri-phosphorylated form.

Keywords

Genome annotation databases

Similar Proteins

Disclaimer

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