Page last updated: 2024-08-07 12:57:58

Acrosin

An acrosin that is encoded in the genome of human. [PRO:DNx, UniProtKB:P10323]

Synonyms

EC 3.4.21.10

Research

Bioassay Publications (4)

TimeframeStudies on this Protein(%)All Drugs %
pre-19901 (25.00)18.7374
1990's0 (0.00)18.2507
2000's0 (0.00)29.6817
2010's3 (75.00)24.3611
2020's0 (0.00)2.80

Compounds (2)

Drugs with Inhibition Measurements

DrugTaxonomyMeasurementAverage (mM)Bioassay(s)Publication(s)
2'-carbomethoxyphenyl 4-guanidinobenzoateHomo sapiens (human)IC500.012911
tosyllysine chloromethyl ketoneHomo sapiens (human)IC50142,600.000033

Enables

This protein enables 10 target(s):

TargetCategoryDefinition
protease bindingmolecular functionBinding to a protease or a peptidase. [GOC:hjd]
DNA bindingmolecular functionAny molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid). [GOC:dph, GOC:jl, GOC:tb, GOC:vw]
amidase activitymolecular functionCatalysis of the reaction: a monocarboxylic acid amide + H2O = a monocarboxylate + NH3. [EC:3.5.1.4]
serine-type endopeptidase activitymolecular functionCatalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain by a catalytic mechanism that involves a catalytic triad consisting of a serine nucleophile that is activated by a proton relay involving an acidic residue (e.g. aspartate or glutamate) and a basic residue (usually histidine). [GOC:mah, https://www.ebi.ac.uk/merops/about/glossary.shtml#CATTYPE]
copper ion bindingmolecular functionBinding to a copper (Cu) ion. [GOC:ai]
protein bindingmolecular functionBinding to a protein. [GOC:go_curators]
mannose bindingmolecular functionBinding to mannose, a monosaccharide hexose, stereoisomeric with glucose, that occurs naturally only in polymerized forms called mannans. [GOC:jl, ISBN:0192800981]
serine-type peptidase activitymolecular functionCatalysis of the hydrolysis of peptide bonds in a polypeptide chain by a catalytic mechanism that involves a catalytic triad consisting of a serine nucleophile that is activated by a proton relay involving an acidic residue (e.g. aspartate or glutamate) and a basic residue (usually histidine). [https://www.ebi.ac.uk/merops/about/glossary.shtml#CATTYPE]
zinc ion bindingmolecular functionBinding to a zinc ion (Zn). [GOC:ai]
fucose bindingmolecular functionBinding to fucose, the pentose 6-deoxygalactose. [ISBN:0582227089]

Located In

This protein is located in 4 target(s):

TargetCategoryDefinition
extracellular regioncellular componentThe space external to the outermost structure of a cell. For cells without external protective or external encapsulating structures this refers to space outside of the plasma membrane. This term covers the host cell environment outside an intracellular parasite. [GOC:go_curators]
nucleuscellular componentA membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent. [GOC:go_curators]
Golgi-associated vesiclecellular componentAny vesicle associated with the Golgi complex and involved in mediating transport within the Golgi or between the Golgi and other parts of the cell. [GOC:mah]
acrosomal matrixcellular componentA structural framework, or 'dense core' at the interior of an acrosome. May regulate the distribution of hydrolases within the acrosome and their release during the acrosome reaction. [GOC:jl, PMID:8949900, PMID:9139729]

Part Of

This protein is part of 1 target(s):

TargetCategoryDefinition
protein-containing complexcellular componentA stable assembly of two or more macromolecules, i.e. proteins, nucleic acids, carbohydrates or lipids, in which at least one component is a protein and the constituent parts function together. [GOC:dos, GOC:mah]

Involved In

This protein is involved in 7 target(s):

TargetCategoryDefinition
acrosome matrix dispersalbiological processThe proteolytic digestion of components in the acrosomal matrix that occurs as part of the acrosome reaction. The process can occur either in the cumulus oophorous facilitating the penetration of it by the sperm, or at the zona pellucida allowing the sperm to reach the plasma membrane of the egg where the inner acrosomal membrane of the sperm can interact with the egg plasma membrane. [GOC:dph, PMID:3886029]
activation of adenylate cyclase activitybiological processAny process that initiates the activity of the inactive enzyme adenylate cyclase. [GOC:ai]
single fertilizationbiological processThe union of male and female gametes to form a zygote. [GOC:ems, GOC:mtg_sensu]
binding of sperm to zona pellucidabiological processThe process in which the sperm binds to the zona pellucida glycoprotein layer of the egg. The process begins with the attachment of the sperm plasma membrane to the zona pellucida and includes attachment of the acrosome inner membrane to the zona pellucida after the acrosomal reaction takes place. [GOC:dph, ISBN:0878932437]
acrosome reactionbiological processThe discharge, by sperm, of a single, anterior secretory granule following the sperm's attachment to the zona pellucida of the oocyte. The process begins with the fusion of the outer acrosomal membrane with the sperm plasma membrane and ends with the exocytosis of the acrosomal contents into the zona pellucida. [GOC:dph, PMID:11175768, PMID:21042299, PMID:3886029]
penetration of zona pellucidabiological processThe infiltration by sperm of the zona pellucida to reach the oocyte. The process involves digestive enzymes from a modified lysosome called the acrosome, situated at the head of the sperm. [GOC:jl, http://arbl.cvmbs.colostate.edu/hbooks/pathphys/reprod/fert/fert.html]
response to steroid hormonebiological processAny process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a steroid hormone stimulus. [GOC:go_curators]