ID   RENI_SHEEP              Reviewed;         400 AA.
AC   P52115;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=Renin {ECO:0000303|PubMed:1543532};
DE            EC=3.4.23.15 {ECO:0000250|UniProtKB:P00797};
DE   AltName: Full=Angiotensinogenase;
DE   Flags: Precursor;
GN   Name=REN;
OS   Ovis aries (Sheep).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Caprinae; Ovis.
OX   NCBI_TaxID=9940;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Merino; TISSUE=Kidney;
RX   PubMed=1543532; DOI=10.1677/jme.0.0080003;
RA   Aldred G.P., Fu P., Crawford R.J., Fernley R.T.;
RT   "The sequence and tissue expression of ovine renin.";
RL   J. Mol. Endocrinol. 8:3-11(1992).
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   -!- TISSUE SPECIFICITY: Kidney. {ECO:0000269|PubMed:1543532}.
CC   -!- SIMILARITY: Belongs to the peptidase A1 family. {ECO:0000305}.
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DR   EMBL; L43524; AAA69809.1; -; mRNA.
DR   PIR; I47099; I47099.
DR   RefSeq; NP_001009299.1; NM_001009299.1.
DR   AlphaFoldDB; P52115; -.
DR   SMR; P52115; -.
DR   STRING; 9940.ENSOARP00000002426; -.
DR   MEROPS; A01.008; -.
DR   GeneID; 443310; -.
DR   KEGG; oas:443310; -.
DR   CTD; 5972; -.
DR   eggNOG; KOG1339; Eukaryota.
DR   OrthoDB; 1619495at2759; -.
DR   Proteomes; UP000002356; Unplaced.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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; Disulfide bond; Glycoprotein; Hydrolase; Membrane;
KW   Protease; Reference proteome; Secreted; Signal; Zymogen.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000255"
FT   PROPEP          18..59
FT                   /note="Activation peptide"
FT                   /evidence="ECO:0000250|UniProtKB:P00797"
FT                   /id="PRO_0000026093"
FT   CHAIN           60..400
FT                   /note="Renin"
FT                   /id="PRO_0000026094"
FT   DOMAIN          80..397
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT   ACT_SITE        98
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT   ACT_SITE        286
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT   CARBOHYD        65
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        135
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        353
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        111..118
FT                   /evidence="ECO:0000250|UniProtKB:P00797"
FT   DISULFID        277..281
FT                   /evidence="ECO:0000250|UniProtKB:P00797"
FT   DISULFID        320..356
FT                   /evidence="ECO:0000250|UniProtKB:P00797"
SQ   SEQUENCE   400 AA;  44016 MW;  95ED40716565FE25 CRC64;
     MPLWGLLLAL WGCSTFSLPA DTAAFRRIFL KKMPSVRESL KERGVDMAQL GAEWSQLTKT
     LSFGNRTSPV VLTNYLDTQY YGEIGIGTPP QTFKVIFDTG SANLWVPSTK CSPLYTACEI
     HSLYDSLESS SYVENGTEFT IYYGSGKVKG FLSQDLVTVG GITVTQTFGE VTELPLRPFM
     LAKFDGVLGM GFPAQAVGGV TPVFDHILAQ RVLTEDVFSV YYSRDSKNSH LLGGEIVLGG
     SDPQYYQENF HYVSISKPGS WQIRMKGVSV RSTTLLCEEG CMVVVDTGAS YISGPTSSLR
     LLMEALGAKE LSIDEYVVNC NQMPTLPDIS FHLGGKAYTL TSADYVLQDP YNNISCTLAL
     HGMDIPPPTG PVWVLGATFI RKFYTEFDRR NNRIGFALAR