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   16-JUN-2009, entry version 62.
DE   RecName: Full=Renin;
DE            EC=3.4.23.15;
DE   AltName: Full=Angiotensinogenase;
DE   Flags: Precursor;
GN   Name=REN;
OS   Ovis aries (Sheep).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
OC   Pecora; Bovidae; Caprinae; Ovis.
OX   NCBI_TaxID=9940;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Merino; TISSUE=Kidney;
RX   MEDLINE=92181567; PubMed=1543532;
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
CC       known function is to generate angiotensin I from angiotensinogen
CC       in the plasma, initiating a cascade of reactions that produce an
CC       elevation of blood pressure and increased sodium retention by the
CC       kidney.
CC   -!- CATALYTIC ACTIVITY: Cleavage of Leu-|-Xaa bond in angiotensinogen
CC       to generate angiotensin I.
CC   -!- ENZYME REGULATION: Interaction with ATP6AP2 results in a 5-fold
CC       increased efficiency in angiotensinogen processing (By
CC       similarity).
CC   -!- SUBUNIT: Interacts with ATP6AP2 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Secreted (By similarity). Membrane (By
CC       similarity). Note=Associated to membranes via binding to ATP6AP2
CC       (By similarity).
CC   -!- TISSUE SPECIFICITY: Kidney.
CC   -!- SIMILARITY: Belongs to the peptidase A1 family.
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DR   EMBL; L43524; AAA69809.1; -; mRNA.
DR   PIR; I47099; I47099.
DR   RefSeq; NP_001009299.1; -.
DR   UniGene; Oar.403; -.
DR   HSSP; P00796; 1SMR.
DR   SMR; P52115; 63-400.
DR   MEROPS; A01.007; -.
DR   GeneID; 443310; -.
DR   HOVERGEN; P52115; -.
DR   BRENDA; 3.4.23.15; 271.
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:InterPro.
DR   InterPro; IPR001461; Peptidase_A1.
DR   InterPro; IPR001969; Peptidase_aspartic_AS.
DR   InterPro; IPR009007; Peptidase_aspartic_catalytic.
DR   InterPro; IPR012848; Propep_A1.
DR   Gene3D; G3DSA:2.40.70.10; Pept_Aspartc_cat; 1.
DR   PANTHER; PTHR13683; Peptidase_A1; 1.
DR   Pfam; PF07966; A1_Propeptide; 1.
DR   Pfam; PF00026; Asp; 1.
DR   PRINTS; PR00792; PEPSIN.
DR   PROSITE; PS00141; ASP_PROTEASE; 2.
PE   2: Evidence at transcript level;
KW   Aspartyl protease; Disulfide bond; Glycoprotein; Hydrolase; Membrane;
KW   Protease; Secreted; Signal; Zymogen.
FT   SIGNAL        1     17       Potential.
FT   PROPEP       18     59       Activation peptide (Potential).
FT                                /FTId=PRO_0000026093.
FT   CHAIN        60    400       Renin.
FT                                /FTId=PRO_0000026094.
FT   ACT_SITE     98     98       By similarity.
FT   ACT_SITE    286    286       By similarity.
FT   CARBOHYD     65     65       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    135    135       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    353    353       N-linked (GlcNAc...) (Potential).
FT   DISULFID    111    118       By similarity.
FT   DISULFID    277    281       By similarity.
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
//