ID RENI_MACMU Reviewed; 406 AA.
AC Q6DLW5;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 2.
DT 27-MAR-2024, entry version 106.
DE RecName: Full=Renin {ECO:0000303|Ref.1};
DE EC=3.4.23.15 {ECO:0000250|UniProtKB:P00797};
DE AltName: Full=Angiotensinogenase;
DE Flags: Precursor;
GN Name=REN;
OS Macaca mulatta (Rhesus macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9544;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Atkins C.L., Lucas B.J., Lewis S.D., Yuan J., Hershey J.C.,
RA Feuerstein G.Z.;
RT "Cloning and biochemical characterization of the rhesus renin precursor
RT protein.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Renin is a highly specific endopeptidase, whose only known
CC function is to generate angiotensin I from angiotensinogen in the
CC plasma, initiating a cascade of reactions that produce an elevation of
CC blood pressure and increased sodium retention by the kidney.
CC {ECO:0000250|UniProtKB:P00797}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Cleavage of Leu-|-Xaa bond in angiotensinogen to generate
CC angiotensin I.; EC=3.4.23.15;
CC Evidence={ECO:0000250|UniProtKB:P00797};
CC -!- ACTIVITY REGULATION: Interaction with ATP6AP2 results in a 5-fold
CC increased efficiency in angiotensinogen processing.
CC {ECO:0000250|UniProtKB:P00797}.
CC -!- SUBUNIT: Interacts with ATP6AP2. {ECO:0000250|UniProtKB:P00797}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P00797}. Membrane
CC {ECO:0000250|UniProtKB:P00797}. Note=Associated to membranes via
CC binding to ATP6AP2. {ECO:0000250|UniProtKB:P00797}.
CC -!- SIMILARITY: Belongs to the peptidase A1 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY662332; AAT74864.2; -; mRNA.
DR RefSeq; NP_001028088.1; NM_001032916.1.
DR AlphaFoldDB; Q6DLW5; -.
DR SMR; Q6DLW5; -.
DR STRING; 9544.ENSMMUP00000011105; -.
DR BindingDB; Q6DLW5; -.
DR ChEMBL; CHEMBL1287631; -.
DR MEROPS; A01.007; -.
DR GlyCosmos; Q6DLW5; 2 sites, No reported glycans.
DR PaxDb; 9544-ENSMMUP00000011102; -.
DR GeneID; 574299; -.
DR KEGG; mcc:574299; -.
DR CTD; 5972; -.
DR eggNOG; KOG1339; Eukaryota.
DR InParanoid; Q6DLW5; -.
DR OrthoDB; 1120702at2759; -.
DR Proteomes; UP000006718; Unassembled WGS sequence.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0002003; P:angiotensin maturation; IBA:GO_Central.
DR CDD; cd05487; renin_like; 1.
DR Gene3D; 2.40.70.10; Acid Proteases; 2.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
DR InterPro; IPR001969; Aspartic_peptidase_AS.
DR InterPro; IPR012848; Aspartic_peptidase_N.
DR InterPro; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR InterPro; IPR034135; Renin-like_dom.
DR PANTHER; PTHR47966; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR PANTHER; PTHR47966:SF24; RENIN; 1.
DR Pfam; PF07966; A1_Propeptide; 1.
DR Pfam; PF00026; Asp; 1.
DR PRINTS; PR00792; PEPSIN.
DR SUPFAM; SSF50630; Acid proteases; 1.
DR PROSITE; PS00141; ASP_PROTEASE; 2.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 2: Evidence at transcript level;
KW Aspartyl protease; Cleavage on pair of basic residues; Disulfide bond;
KW Glycoprotein; Hydrolase; Membrane; Protease; Reference proteome; Secreted;
KW Signal; Zymogen.
FT SIGNAL 1..23
FT /evidence="ECO:0000250|UniProtKB:P00797"
FT PROPEP 24..66
FT /note="Activation peptide"
FT /evidence="ECO:0000250|UniProtKB:P00797"
FT /id="PRO_0000026085"
FT CHAIN 67..406
FT /note="Renin"
FT /id="PRO_0000026086"
FT DOMAIN 86..403
FT /note="Peptidase A1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT ACT_SITE 104
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT ACT_SITE 292
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT CARBOHYD 71
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 141
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 117..124
FT /evidence="ECO:0000250|UniProtKB:P00797"
FT DISULFID 283..287
FT /evidence="ECO:0000250|UniProtKB:P00797"
FT DISULFID 325..362
FT /evidence="ECO:0000250|UniProtKB:P00797"
SQ SEQUENCE 406 AA; 44961 MW; BFAC82495AD57220 CRC64;
MDGWRRMPRW GLLLLLWGSC TFGLPTDTTT FKRIFLKRMP SIRESLKERG VDMARLGPEW
SQPMKRLALG NTTSSVILTN YMDTQYYGEI GIGTPPQTFK VVFDTGSSNV WVPSSKCSRL
YTACVYHKLF DASDSSSYKH NGTELTLRYS TGTVSGFLSQ DIITVGGITV TQMFGEVTEM
PALPFMLAEF DGVVGMGFIE QAIGRVTPIF DNILSQGVLK EDVFSFYYNR DSENAQSLGG
QIVLGGSDPQ HYEGNFHYIN LIKTGVWQIP MKGVSVGSST LLCEDGCLAL VDTGASYISG
STSSIEKLME ALGAKKRLFD YVVKCNEGPT LPDISFHLGG KEYTLTSADY VFQESYSSKK
LCTLAIHAMD IPPPTGPTWA LGATFIRKFY TEFDRRNNRI GFALAH
//
