ID   RENI_CANLF              Reviewed;         403 AA.
AC   Q6DYE7;
DT   29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 113.
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   Canis lupus familiaris (Dog) (Canis familiaris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX   NCBI_TaxID=9615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Zecher M., Wu Z., Scott B., McGeehan G., Harrison R.;
RT   "The cloning and characterization of canine renin.";
RL   Submitted (MAY-2004) 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; AY630442; AAT68959.1; -; mRNA.
DR   RefSeq; NP_001003194.1; NM_001003194.2.
DR   AlphaFoldDB; Q6DYE7; -.
DR   SMR; Q6DYE7; -.
DR   STRING; 9612.ENSCAFP00000014146; -.
DR   MEROPS; A01.008; -.
DR   PaxDb; Q6DYE7; -.
DR   Ensembl; ENSCAFT00030022244; ENSCAFP00030019403; ENSCAFG00030011832.
DR   Ensembl; ENSCAFT00040025395; ENSCAFP00040022078; ENSCAFG00040013534.
DR   GeneID; 403838; -.
DR   KEGG; cfa:403838; -.
DR   CTD; 5972; -.
DR   eggNOG; KOG1339; Eukaryota.
DR   HOGENOM; CLU_013253_3_3_1; -.
DR   InParanoid; Q6DYE7; -.
DR   OMA; SWQITMK; -.
DR   OrthoDB; 1619495at2759; -.
DR   TreeFam; TF314990; -.
DR   BRENDA; 3.4.23.15; 1153.
DR   Reactome; R-CFA-2022377; Metabolism of Angiotensinogen to Angiotensins.
DR   Proteomes; UP000002254; Unplaced.
DR   Bgee; ENSCAFG00000009623; Expressed in metanephros cortex and 10 other tissues.
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..22
FT                   /evidence="ECO:0000250|UniProtKB:P00797"
FT   PROPEP          23..65
FT                   /note="Activation peptide"
FT                   /evidence="ECO:0000250|UniProtKB:P00797"
FT                   /id="PRO_0000026079"
FT   CHAIN           66..403
FT                   /note="Renin"
FT                   /id="PRO_0000026080"
FT   DOMAIN          85..400
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT   ACT_SITE        103
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT   ACT_SITE        288
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT   CARBOHYD        70
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        140
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        116..123
FT                   /evidence="ECO:0000250|UniProtKB:P00797"
FT   DISULFID        279..283
FT                   /evidence="ECO:0000250|UniProtKB:P00797"
FT   DISULFID        322..359
FT                   /evidence="ECO:0000250|UniProtKB:P00797"
SQ   SEQUENCE   403 AA;  44099 MW;  B63101337155AE44 CRC64;
     MARCRMPRWG LLLVLWGSCT FGLPADTGAF RRIFLKKMPS IRESLKERGV DVAGLGAEWN
     QFTKRLSSGN STSPVVLTNY LDTQYYGEIG IGTPPQTFKV VFDTGSANLW VPSTRCSPLY
     TACEIHCLYD SSESSSYMEN GTTFTIRYGS GKVKGFLSQD MVTVGGITVT QTFGEVTELP
     LIPFMLAKFD GVLGMGFPAQ AVGGVTPVFD HILSQGVLKE EVFSVYYSRN SHLLGGEVVL
     GGSDPQYYQG NFHYVSISKT GSWQIKMKGV SVRSATLVCE EGCMVVVDTG ASYISGPTSS
     LRLLMDTLGA QELSTNEYVV NCNQVPTLPD ISFHLGGRAY TLTSKDYVLQ DPYGNEDLCT
     LALHGLDVPP PTGPVWVLGA SFIRKFYTEF DRHNNRIGFA LAR