5MKT

Crystal structure of mouse prorenin

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0001822	biological_process	kidney development
A	0001823	biological_process	mesonephros development
A	0002003	biological_process	angiotensin maturation
A	0002016	biological_process	regulation of blood volume by renin-angiotensin
A	0002018	biological_process	renin-angiotensin regulation of aldosterone production
A	0002034	biological_process	maintenance of blood vessel diameter homeostasis by renin-angiotensin
A	0004175	molecular_function	endopeptidase activity
A	0004190	molecular_function	aspartic-type endopeptidase activity
A	0005102	molecular_function	signaling receptor binding
A	0005159	molecular_function	insulin-like growth factor receptor binding
A	0005576	cellular_component	extracellular region
A	0005615	cellular_component	extracellular space
A	0006508	biological_process	proteolysis
A	0008217	biological_process	regulation of blood pressure
A	0008233	molecular_function	peptidase activity
A	0008584	biological_process	male gonad development
A	0009410	biological_process	response to xenobiotic stimulus
A	0009755	biological_process	hormone-mediated signaling pathway
A	0010467	biological_process	gene expression
A	0016020	cellular_component	membrane
A	0016787	molecular_function	hydrolase activity
A	0032496	biological_process	response to lipopolysaccharide
A	0035902	biological_process	response to immobilization stress
A	0038166	biological_process	angiotensin-activated signaling pathway
A	0042756	biological_process	drinking behavior
A	0043408	biological_process	regulation of MAPK cascade
A	0045177	cellular_component	apical part of cell
A	0048469	biological_process	cell maturation
A	0051591	biological_process	response to cAMP
A	0070305	biological_process	response to cGMP
A	0071466	biological_process	cellular response to xenobiotic stimulus
A	0072051	biological_process	juxtaglomerular apparatus development

Functional Information from PROSITE/UniProt

site_id	PS00141
Number of Residues	12
Details	ASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. VIFDTGSANLWV

Chain	Residue	Details
A	VAL78-VAL89
A	VAL263-ALA274

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	Active site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU10094","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	2
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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