Summary for peptidase A01.007: renin

Summary Gene structure Alignment Tree Sequences Sequence features Distribution Structure Literature Human EST Mouse EST Substrates Inhibitors Pharma

 

Names
MEROPS Namerenin
Other namesangiotensin-forming enzyme, angiotensinogenase, Ren1 g.p. (Mus musculus)
Domain architecture
MEROPS Classification
Classification Clan AA >> Subclan (none) >> Family A1 >> Subfamily A >> A01.007
Holotyperenin (Homo sapiens), Uniprot accession P00797 (peptidase unit: 73-406), MERNUM MER0000917
History Identifier created: Handbook of Proteolytic Enzymes (1998) Academic Press, London.
Activity
Catalytic typeAspartic
PeplistIncluded in the Peplist with identifier PL00005
NC-IUBMBSubclass 3.4 (Peptidases) >> Sub-subclass 3.4.23 (Aspartic endopeptidases) >> Peptidase 3.4.23.15
EnzymologyBRENDA database
ActivityCleaves near the N-terminus of the protein angiotensinogen to release angiotensin I.
Proteolytic eventsCutDB database (2 cleavages)
Activity statushuman: active (Suzuki et al., 2004)
mouse: active (Hansen et al., 2004)
InhibitorsNot trapped by alpha-2-macroglobulin (Barrett 1981).
PhysiologyLiberated from kidney into the plasma, renin plays a central role in controlling blood pressure as it catalyzes the first step in the production of angiotensin II, release of angiotensin I from angiotensinogen (Fuchs et al., 2002). Angiotensin I is subsequently converted to the hypertensive peptide angiotensin II by the action of angiotensin-converting enzyme (XM02-001).
KnockoutA variety of transgenic models have been used in the investigation of the functions of renin (Lavoie & Sigmund, 2003).
Pharmaceutical relevanceInhibitors of renin lower blood pressure in some forms of hypertension, and are being studied for their potential as drugs in the management of high blood pressure (Leckie, 2005). A drug in a late stage of development is aliskiren.
Pathways KEGGRenin-angiotensin system
Other databases WIKIPEDIAhttp://en.wikipedia.org/wiki/Renin
Cleavage site specificity Explanations of how to interpret the following cleavage site sequence logo and specificity matrix can be found here.
Cleavage patternP/F/H/LScissile bondLvk/viy/Yhg/Sn (based on 10 cleavages)
weblogo
Specificity matrix
 
Amino acid P4 P3 P2 P1 P1' P2' P3' P4'
Gly 0 0 0 0 0 0 1 0
Pro 10 0 0 0 0 0 0 0
Ala 0 0 0 0 0 0 0 0
Val 0 0 0 0 2 5 0 0
Leu 0 0 0 10 7 0 0 0
Ile 0 0 1 0 0 2 0 0
Met 0 0 0 0 0 0 0 0
Phe 0 9 0 0 0 0 0 0
Tyr 0 1 0 0 0 2 5 0
Trp 0 0 0 0 0 0 0 0
Ser 0 0 0 0 0 0 0 6
Thr 0 0 0 0 0 0 0 0
Cys 0 0 0 0 0 0 0 0
Asn 0 0 0 0 0 0 0 2
Gln 0 0 0 0 0 0 0 0
Asp 0 0 0 0 0 0 0 0
Glu 0 0 0 0 0 0 0 0
Lys 0 0 0 0 1 0 0 0
Arg 0 0 0 0 0 1 0 0
His 0 0 9 0 0 0 4 0
Human genetics
Gene symbol Locus Megabases Ensembl Entrez gene Gene Cards OMIM
REN 1q32 ENSG00000143839 5972 REN 179820