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   03-AUG-2022, entry version 100.
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}.
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DR   EMBL; AY662332; AAT74864.2; -; mRNA.
DR   RefSeq; NP_001028088.1; NM_001032916.1.
DR   AlphaFoldDB; Q6DLW5; -.
DR   SMR; Q6DLW5; -.
DR   STRING; 9544.ENSMMUP00000011102; -.
DR   BindingDB; Q6DLW5; -.
DR   ChEMBL; CHEMBL1287631; -.
DR   MEROPS; A01.007; -.
DR   GeneID; 574299; -.
DR   KEGG; mcc:574299; -.
DR   CTD; 5972; -.
DR   eggNOG; KOG1339; Eukaryota.
DR   InParanoid; Q6DLW5; -.
DR   OrthoDB; 1619495at2759; -.
DR   Proteomes; UP000006718; Unplaced.
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   GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR   CDD; cd05487; renin_like; 1.
DR   Gene3D; 2.40.70.10; -; 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; PTHR47966; 1.
DR   Pfam; PF07966; A1_Propeptide; 1.
DR   Pfam; PF00026; Asp; 1.
DR   PRINTS; PR00792; PEPSIN.
DR   SUPFAM; SSF50630; SSF50630; 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