ID RENI_RAT Reviewed; 402 AA. AC P08424; Q63497; DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 2. DT 24-JAN-2024, entry version 189. DE RecName: Full=Renin {ECO:0000303|PubMed:3287330}; DE EC=3.4.23.15 {ECO:0000250|UniProtKB:P00797}; DE AltName: Full=Angiotensinogenase; DE Flags: Precursor; GN Name=Ren1; Synonyms=Ren; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=Sprague-Dawley; RX PubMed=3287330; DOI=10.1093/nar/16.8.3576; RA Tada M., Fukamizu A., Seo M.S., Takahashi S., Murakami K.; RT "Nucleotide sequence of rat renin cDNA."; RL Nucleic Acids Res. 16:3576-3576(1988). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=3039496; DOI=10.1073/pnas.84.16.5605; RA Burnham C.E., Hawelu-Johnson C.L., Frank B.M., Lynch K.R.; RT "Molecular cloning of rat renin cDNA and its gene."; RL Proc. Natl. Acad. Sci. U.S.A. 84:5605-5609(1987). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=Sprague-Dawley; RX PubMed=3047403; DOI=10.1016/0022-2836(88)90151-9; RA Fukamizu A., Nishi K., Cho T., Saitoh M., Nakayama K., Ohkubo H., RA Nakanishi S., Murakami K.; RT "Structure of the rat renin gene."; RL J. Mol. Biol. 201:443-450(1988). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=8490598; DOI=10.3109/10641969309041632; RA Alam K.Y., Wang Y., Dene H., Rapp J.P.; RT "Renin gene nucleotide sequence of coding and regulatory regions in Dahl RT rats."; RL Clin. Exp. Hypertens. 15:599-614(1993). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Kidney; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). 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; X07033; CAA30082.1; -; mRNA. DR EMBL; J02941; AAA42030.1; -; mRNA. DR EMBL; M37278; AAA42031.1; ALT_SEQ; Genomic_DNA. DR EMBL; S60054; AAP13916.1; -; mRNA. DR EMBL; BC078878; AAH78878.1; -; mRNA. DR PIR; A29991; RERTK. DR RefSeq; NP_036774.4; NM_012642.4. DR PDB; 5MLG; X-ray; 2.60 A; A=22-402. DR PDBsum; 5MLG; -. DR AlphaFoldDB; P08424; -. DR SMR; P08424; -. DR BioGRID; 246843; 1. DR STRING; 10116.ENSRNOP00000003951; -. DR BindingDB; P08424; -. DR ChEMBL; CHEMBL2322; -. DR DrugCentral; P08424; -. DR MEROPS; A01.008; -. DR GlyCosmos; P08424; 3 sites, No reported glycans. DR GlyGen; P08424; 3 sites. DR PhosphoSitePlus; P08424; -. DR PaxDb; 10116-ENSRNOP00000003951; -. DR DNASU; 24715; -. DR Ensembl; ENSRNOT00000003951.5; ENSRNOP00000003951.2; ENSRNOG00000002937.5. DR Ensembl; ENSRNOT00055036484; ENSRNOP00055029659; ENSRNOG00055021334. DR Ensembl; ENSRNOT00060028921; ENSRNOP00060023284; ENSRNOG00060016874. DR Ensembl; ENSRNOT00065034664; ENSRNOP00065027808; ENSRNOG00065020497. DR GeneID; 24715; -. DR KEGG; rno:24715; -. DR UCSC; RGD:3554; rat. DR AGR; RGD:3554; -. DR CTD; 5972; -. DR RGD; 3554; Ren1. DR eggNOG; KOG1339; Eukaryota. DR GeneTree; ENSGT00940000157898; -. DR HOGENOM; CLU_013253_3_3_1; -. DR InParanoid; P08424; -. DR OMA; KMPSIRD; -. DR OrthoDB; 1120702at2759; -. DR PhylomeDB; P08424; -. DR TreeFam; TF314990; -. DR Reactome; R-RNO-2022377; Metabolism of Angiotensinogen to Angiotensins. DR PRO; PR:P08424; -. DR Proteomes; UP000002494; Chromosome 13. DR Bgee; ENSRNOG00000002937; Expressed in kidney and 9 other cell types or tissues. DR ExpressionAtlas; P08424; baseline and differential. DR GO; GO:0045177; C:apical part of cell; ISO:RGD. DR GO; GO:0005615; C:extracellular space; IDA:RGD. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell. DR GO; GO:0004190; F:aspartic-type endopeptidase activity; ISO:RGD. DR GO; GO:0004175; F:endopeptidase activity; IDA:RGD. DR GO; GO:0005159; F:insulin-like growth factor receptor binding; IDA:RGD. DR GO; GO:0008233; F:peptidase activity; ISO:RGD. DR GO; GO:0005102; F:signaling receptor binding; IPI:RGD. DR GO; GO:0050435; P:amyloid-beta metabolic process; IEP:RGD. DR GO; GO:0002003; P:angiotensin maturation; IDA:RGD. DR GO; GO:0048469; P:cell maturation; ISO:RGD. DR GO; GO:0071466; P:cellular response to xenobiotic stimulus; IEP:RGD. DR GO; GO:0042756; P:drinking behavior; ISO:RGD. DR GO; GO:0009755; P:hormone-mediated signaling pathway; ISO:RGD. DR GO; GO:0072051; P:juxtaglomerular apparatus development; IEP:RGD. DR GO; GO:0001822; P:kidney development; ISO:RGD. DR GO; GO:0008584; P:male gonad development; ISO:RGD. DR GO; GO:0001823; P:mesonephros development; ISO:RGD. DR GO; GO:0006508; P:proteolysis; ISO:RGD. DR GO; GO:0008217; P:regulation of blood pressure; IMP:RGD. DR GO; GO:0002016; P:regulation of blood volume by renin-angiotensin; ISO:RGD. DR GO; GO:0043408; P:regulation of MAPK cascade; ISO:RGD. DR GO; GO:0002018; P:renin-angiotensin regulation of aldosterone production; ISO:RGD. DR GO; GO:0051591; P:response to cAMP; IDA:RGD. DR GO; GO:0070305; P:response to cGMP; IDA:RGD. DR GO; GO:0035902; P:response to immobilization stress; IEP:RGD. DR GO; GO:0032496; P:response to lipopolysaccharide; IEP:RGD. DR GO; GO:0010033; P:response to organic substance; ISO:RGD. DR GO; GO:0009410; P:response to xenobiotic stimulus; IDA:RGD. 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; 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; 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. DR Genevisible; P08424; RN. PE 1: Evidence at protein level; KW 3D-structure; Aspartyl protease; Cleavage on pair of basic residues; KW Disulfide bond; Glycoprotein; Hydrolase; Membrane; Protease; KW Reference proteome; Secreted; Signal; Zymogen. FT SIGNAL 1..26 FT /evidence="ECO:0000305" FT PROPEP 27..64 FT /note="Activation peptide" FT /id="PRO_0000026091" FT CHAIN 65..402 FT /note="Renin" FT /id="PRO_0000026092" FT DOMAIN 84..399 FT /note="Peptidase A1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01103" FT ACT_SITE 102 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10094" FT ACT_SITE 287 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10094" FT CARBOHYD 69 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 139 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 320 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 115..122 FT /evidence="ECO:0000250|UniProtKB:P00797" FT DISULFID 278..282 FT /evidence="ECO:0000250|UniProtKB:P00797" FT DISULFID 321..358 FT /evidence="ECO:0000250|UniProtKB:P00797" FT CONFLICT 200 FT /note="A -> V (in Ref. 1; CAA30082)" FT /evidence="ECO:0000305" FT CONFLICT 214..215 FT /note="QR -> HE (in Ref. 2; AAA42030)" FT /evidence="ECO:0000305" FT CONFLICT 271 FT /note="V -> L (in Ref. 1; CAA30082)" FT /evidence="ECO:0000305" FT STRAND 30..36 FT /evidence="ECO:0007829|PDB:5MLG" FT HELIX 40..46 FT /evidence="ECO:0007829|PDB:5MLG" FT HELIX 51..58 FT /evidence="ECO:0007829|PDB:5MLG" FT STRAND 79..81 FT /evidence="ECO:0007829|PDB:5MLG" FT STRAND 84..90 FT /evidence="ECO:0007829|PDB:5MLG" FT TURN 91..94 FT /evidence="ECO:0007829|PDB:5MLG" FT STRAND 95..102 FT /evidence="ECO:0007829|PDB:5MLG" FT STRAND 108..112 FT /evidence="ECO:0007829|PDB:5MLG" FT HELIX 120..124 FT /evidence="ECO:0007829|PDB:5MLG" FT HELIX 130..132 FT /evidence="ECO:0007829|PDB:5MLG" FT STRAND 137..146 FT /evidence="ECO:0007829|PDB:5MLG" FT STRAND 151..163 FT /evidence="ECO:0007829|PDB:5MLG" FT STRAND 166..177 FT /evidence="ECO:0007829|PDB:5MLG" FT HELIX 180..183 FT /evidence="ECO:0007829|PDB:5MLG" FT STRAND 190..193 FT /evidence="ECO:0007829|PDB:5MLG" FT HELIX 197..199 FT /evidence="ECO:0007829|PDB:5MLG" FT HELIX 201..203 FT /evidence="ECO:0007829|PDB:5MLG" FT HELIX 207..213 FT /evidence="ECO:0007829|PDB:5MLG" FT STRAND 217..226 FT /evidence="ECO:0007829|PDB:5MLG" FT STRAND 235..241 FT /evidence="ECO:0007829|PDB:5MLG" FT HELIX 244..246 FT /evidence="ECO:0007829|PDB:5MLG" FT STRAND 247..255 FT /evidence="ECO:0007829|PDB:5MLG" FT STRAND 261..271 FT /evidence="ECO:0007829|PDB:5MLG" FT STRAND 274..277 FT /evidence="ECO:0007829|PDB:5MLG" FT STRAND 282..286 FT /evidence="ECO:0007829|PDB:5MLG" FT STRAND 292..295 FT /evidence="ECO:0007829|PDB:5MLG" FT HELIX 297..307 FT /evidence="ECO:0007829|PDB:5MLG" FT STRAND 316..318 FT /evidence="ECO:0007829|PDB:5MLG" FT HELIX 321..323 FT /evidence="ECO:0007829|PDB:5MLG" FT STRAND 330..334 FT /evidence="ECO:0007829|PDB:5MLG" FT STRAND 337..341 FT /evidence="ECO:0007829|PDB:5MLG" FT TURN 343..345 FT /evidence="ECO:0007829|PDB:5MLG" FT STRAND 346..348 FT /evidence="ECO:0007829|PDB:5MLG" FT STRAND 359..364 FT /evidence="ECO:0007829|PDB:5MLG" FT TURN 369..371 FT /evidence="ECO:0007829|PDB:5MLG" FT STRAND 373..377 FT /evidence="ECO:0007829|PDB:5MLG" FT HELIX 379..384 FT /evidence="ECO:0007829|PDB:5MLG" FT STRAND 385..390 FT /evidence="ECO:0007829|PDB:5MLG" FT TURN 391..394 FT /evidence="ECO:0007829|PDB:5MLG" FT STRAND 395..401 FT /evidence="ECO:0007829|PDB:5MLG" SQ SEQUENCE 402 AA; 44276 MW; E4E22CEE449EAC3F CRC64; MGGRRMPLWA LLLLWTSCSF SLPTDTASFG RILLKKMPSV REILEERGVD MTRISAEWGE FIKKSSFTNV TSPVVLTNYL DTQYYGEIGI GTPSQTFKVI FDTGSANLWV PSTKCGPLYT ACEIHNLYDS SESSSYMENG TEFTIHYGSG KVKGFLSQDV VTVGGIIVTQ TFGEVTELPL IPFMLAKFDG VLGMGFPAQA VDGVIPVFDH ILSQRVLKEE VFSVYYSRES HLLGGEVVLG GSDPQHYQGN FHYVSISKAG SWQITMKGVS VGPATLLCEE GCMAVVDTGT SYISGPTSSL QLIMQALGVK EKRANNYVVN CSQVPTLPDI SFYLGGRTYT LSNMDYVQKN PFRNDDLCIL ALQGLDIPPP TGPVWVLGAT FIRKFYTEFD RHNNRIGFAL AR //