ID RENI_HUMAN Reviewed; 406 AA. AC P00797; Q6FI38; Q6T5C2; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1988, sequence version 1. DT 13-FEB-2019, entry version 220. DE RecName: Full=Renin; DE EC=3.4.23.15; DE AltName: Full=Angiotensinogenase; DE Flags: Precursor; GN Name=REN; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1). RX PubMed=6324167; DOI=10.1073/pnas.80.24.7405; RA Imai T., Miyazaki H., Hirose S., Hori H., Hayashi T., Kageyama R., RA Ohkubo H., Nakanishi S., Murakami K.; RT "Cloning and sequence analysis of cDNA for human renin precursor."; RL Proc. Natl. Acad. Sci. U.S.A. 80:7405-7409(1983). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 2). RX PubMed=3530608; DOI=10.1042/cs0710345; RA Morris B.J.; RT "New possibilities for intracellular renin and inactive renin now that RT the structure of the human renin gene has been elucidated."; RL Clin. Sci. 71:345-355(1986). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC TISSUE=Fetal liver; RX PubMed=6391881; DOI=10.1089/dna.1.1984.3.457; RA Hardman J.A., Hort Y.J., Catanzaro D.F., Tellam J.T., Baxter J.D., RA Morris B.J., Shine J.; RT "Primary structure of the human renin gene."; RL DNA 3:457-468(1984). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Rieder M.J., da Ponte S.H., Kuldanek S.A., Rajkumar N., Smith J.D., RA Toth E.J., Krauss R.M., Nickerson D.A.; RL Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RG NIEHS SNPs program; RL Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C., RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., RA Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Colon, and Ovary; 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [9] RP NUCLEOTIDE SEQUENCE [MRNA] OF 108-406 (ISOFORM 1). RX PubMed=6138751; DOI=10.1093/nar/11.20.7181; RA Soubrier F., Panthier J.-J., Corvol P., Rougeon F.; RT "Molecular cloning and nucleotide sequence of a human renin cDNA RT fragment."; RL Nucleic Acids Res. 11:7181-7190(1983). RN [10] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-33. RX PubMed=3032746; DOI=10.1016/0378-1119(86)90393-8; RA Fukamizu A., Nishi K., Nishimatsu S., Miyazaki H., Hirose S., RA Murakami K.; RT "Human renin gene of renin-secreting tumor."; RL Gene 49:139-145(1986). RN [11] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-33. RX PubMed=2540188; RA Burt D.W., Nakamura N., Kelley P., Dzau V.J.; RT "Identification of negative and positive regulatory elements in the RT human renin gene."; RL J. Biol. Chem. 264:7357-7362(1989). RN [12] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-33. RX PubMed=3516796; DOI=10.1016/0378-1119(86)90270-2; RA Soubrier F., Panthier J.J., Houot A.-M., Rougeon F., Corvol P.; RT "Segmental homology between the promoter region of the human renin RT gene and the mouse ren1 and ren2 promoter regions."; RL Gene 41:85-92(1986). RN [13] RP PROTEIN SEQUENCE OF 24-42 AND 67-86. RX PubMed=2016271; DOI=10.1093/oxfordjournals.jbchem.a123347; RA Ishizuka Y., Shoda A., Yoshida S., Kawamura Y., Haraguchi K., RA Murakami K.; RT "Isolation and characterization of recombinant human prorenin in RT Chinese hamster ovary cells."; RL J. Biochem. 109:30-35(1991). RN [14] RP INTERACTION WITH ATP6AP2, AND CHARACTERIZATION. RX PubMed=12045255; DOI=10.1172/JCI0214276; RA Nguyen G., Delarue F., Burckle C., Bouzhir L., Giller T., Sraer J.-D.; RT "Pivotal role of the renin/prorenin receptor in angiotensin II RT production and cellular responses to renin."; RL J. Clin. Invest. 109:1417-1427(2002). RN [15] RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS). RX PubMed=2493678; DOI=10.1126/science.2493678; RA Sielecki A.R., Hayakawa K., Fujinaga M., Murphy M.E.P., Fraser M., RA Muir A.K., Carilli C.T., Lewicki J.A., Baxter J.D., James M.N.G.; RT "Structure of recombinant human renin, a target for cardiovascular- RT active drugs, at 2.5-A resolution."; RL Science 243:1346-1351(1989). RN [16] RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS). RX PubMed=1608447; DOI=10.1038/357466a0; RA Dhanaraj V., Dealwis C.G., Frazao C., Badasso M., Sibanda B.L., RA Tickle I.J., Cooper J.B., Driessen H.P.C., Newman M., Aguilar C., RA Wood S.P., Blundell T.L., Hobart P.M., Geoghegan K.F., Ammirati M.J., RA Danley D.E., O'Connor B.A., Hoover D.J.; RT "X-ray analyses of peptide-inhibitor complexes define the structural RT basis of specificity for human and mouse renins."; RL Nature 357:466-472(1992). RN [17] RP X-RAY CRYSTALLOGRAPHY (4.33 ANGSTROMS) OF 24-406 OF MUTANT ALA-292 IN RP COMPLEX WITH ANGIOTENSINOGEN, AND DISULFIDE BONDS. RX PubMed=20927107; DOI=10.1038/nature09505; RA Zhou A., Carrell R.W., Murphy M.P., Wei Z., Yan Y., Stanley P.L., RA Stein P.E., Broughton Pipkin F., Read R.J.; RT "A redox switch in angiotensinogen modulates angiotensin release."; RL Nature 468:108-111(2010). RN [18] RP VARIANTS RTD ASN-104 AND LYS-230. RX PubMed=16116425; DOI=10.1038/ng1623; RA Gribouval O., Gonzales M., Neuhaus T., Aziza J., Bieth E., Laurent N., RA Bouton J.M., Feuillet F., Makni S., Ben Amar H., Laube G., RA Delezoide A.-L., Bouvier R., Dijoud F., Ollagnon-Roman E., Roume J., RA Joubert M., Antignac C., Gubler M.-C.; RT "Mutations in genes in the renin-angiotensin system are associated RT with autosomal recessive renal tubular dysgenesis."; RL Nat. Genet. 37:964-968(2005). RN [19] RP VARIANT HNFJ2 ARG-16, AND CHARACTERIZATION OF VARIANT HNFJ2 ARG-16. RX PubMed=19664745; DOI=10.1016/j.ajhg.2009.07.010; RA Zivna M., Hulkova H., Matignon M., Hodanova K., Vylet'al P., RA Kalbacova M., Baresova V., Sikora J., Blazkova H., Zivny J., RA Ivanek R., Stranecky V., Sovova J., Claes K., Lerut E., Fryns J.P., RA Hart P.S., Hart T.C., Adams J.N., Pawtowski A., Clemessy M., RA Gasc J.M., Guebler M.C., Antignac C., Elleder M., Kapp K., RA Grimbert P., Bleyer A.J., Kmoch S.; RT "Dominant renin gene mutations associated with early-onset RT hyperuricemia, anemia, and chronic kidney failure."; RL Am. J. Hum. Genet. 85:204-213(2009). 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: CC Reaction=Cleavage of Leu-|-Xaa bond in angiotensinogen to generate CC angiotensin I.; EC=3.4.23.15; CC -!- ACTIVITY REGULATION: Interaction with ATP6AP2 results in a 5-fold CC increased efficiency in angiotensinogen processing. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=1 uM for angiotensinogen (in absence of ATP6AP2); CC KM=0.15 uM for angiotensinogen (in presence of membrane-bound CC ATP6AP2); CC -!- SUBUNIT: Interacts with ATP6AP2. {ECO:0000269|PubMed:12045255, CC ECO:0000269|PubMed:20927107}. CC -!- INTERACTION: CC P01019:AGT; NbExp=2; IntAct=EBI-715794, EBI-751728; CC -!- SUBCELLULAR LOCATION: Secreted. Membrane. Note=Associated to CC membranes via binding to ATP6AP2. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P00797-1; Sequence=Displayed; CC Name=2; CC IsoId=P00797-2; Sequence=VSP_012899; CC -!- DISEASE: Renal tubular dysgenesis (RTD) [MIM:267430]: Autosomal CC recessive severe disorder of renal tubular development CC characterized by persistent fetal anuria and perinatal death, CC probably due to pulmonary hypoplasia from early-onset CC oligohydramnios (the Potter phenotype). CC {ECO:0000269|PubMed:16116425}. Note=The disease is caused by CC mutations affecting the gene represented in this entry. CC -!- DISEASE: Familial juvenile hyperuricemic nephropathy 2 (HNFJ2) CC [MIM:613092]: A renal disease characterized by juvenile onset of CC hyperuricemia, slowly progressive renal failure and anemia. CC {ECO:0000269|PubMed:19664745}. Note=The disease is caused by CC mutations affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the peptidase A1 family. {ECO:0000305}. CC -!- WEB RESOURCE: Name=Wikipedia; Note=Renin entry; CC URL="https://en.wikipedia.org/wiki/Renin"; 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; L00073; AAA60363.1; -; Genomic_DNA. DR EMBL; L00064; AAA60363.1; JOINED; Genomic_DNA. DR EMBL; L00065; AAA60363.1; JOINED; Genomic_DNA. DR EMBL; L00066; AAA60363.1; JOINED; Genomic_DNA. DR EMBL; L00067; AAA60363.1; JOINED; Genomic_DNA. DR EMBL; L00068; AAA60363.1; JOINED; Genomic_DNA. DR EMBL; L00069; AAA60363.1; JOINED; Genomic_DNA. DR EMBL; L00070; AAA60363.1; JOINED; Genomic_DNA. DR EMBL; L00071; AAA60363.1; JOINED; Genomic_DNA. DR EMBL; L00072; AAA60363.1; JOINED; Genomic_DNA. DR EMBL; M26901; AAA60364.1; -; Genomic_DNA. DR EMBL; M26899; AAA60364.1; JOINED; Genomic_DNA. DR EMBL; M26900; AAA60364.1; JOINED; Genomic_DNA. DR EMBL; M10152; AAD03461.1; -; Genomic_DNA. DR EMBL; M10030; AAD03461.1; JOINED; Genomic_DNA. DR EMBL; M10128; AAD03461.1; JOINED; Genomic_DNA. DR EMBL; M10150; AAD03461.1; JOINED; Genomic_DNA. DR EMBL; M10151; AAD03461.1; JOINED; Genomic_DNA. DR EMBL; AY436324; AAR03502.1; -; Genomic_DNA. DR EMBL; CR536498; CAG38737.1; -; mRNA. DR EMBL; EU332871; ABY87560.1; -; Genomic_DNA. DR EMBL; AL592114; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL592146; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC033474; AAH33474.1; -; mRNA. DR EMBL; BC047752; AAH47752.1; -; mRNA. DR EMBL; M15410; AAA60263.1; -; Genomic_DNA. DR EMBL; M26440; AAA60365.1; -; Genomic_DNA. DR EMBL; M13253; AAA60262.1; -; Genomic_DNA. DR CCDS; CCDS30981.1; -. [P00797-1] DR PIR; A21454; REHUK. DR RefSeq; NP_000528.1; NM_000537.3. [P00797-1] DR UniGene; Hs.3210; -. DR PDB; 1BBS; X-ray; 2.80 A; A/B=67-406. DR PDB; 1BIL; X-ray; 2.40 A; A/B=70-406. DR PDB; 1BIM; X-ray; 2.80 A; A/B=70-406. DR PDB; 1HRN; X-ray; 1.80 A; A/B=70-406. DR PDB; 1RNE; X-ray; 2.40 A; A=67-406. DR PDB; 2BKS; X-ray; 2.20 A; A/B=67-406. DR PDB; 2BKT; X-ray; 2.30 A; A/B=67-406. DR PDB; 2FS4; X-ray; 2.20 A; A/B=74-406. DR PDB; 2G1N; X-ray; 2.90 A; A/B=74-406. DR PDB; 2G1O; X-ray; 2.70 A; A/B=74-406. DR PDB; 2G1R; X-ray; 2.42 A; A/B=74-406. DR PDB; 2G1S; X-ray; 2.50 A; A/B=74-406. DR PDB; 2G1Y; X-ray; 2.50 A; A/B=74-406. DR PDB; 2G20; X-ray; 2.40 A; A/B=74-406. DR PDB; 2G21; X-ray; 2.20 A; A/B=74-406. DR PDB; 2G22; X-ray; 2.50 A; A/B=74-406. DR PDB; 2G24; X-ray; 1.90 A; A/B=74-406. DR PDB; 2G26; X-ray; 2.10 A; A/B=74-406. DR PDB; 2G27; X-ray; 2.90 A; A/B=74-406. DR PDB; 2I4Q; X-ray; 2.30 A; A/B=73-406. DR PDB; 2IKO; X-ray; 1.90 A; A/B=67-406. DR PDB; 2IKU; X-ray; 2.60 A; A/B=67-406. DR PDB; 2IL2; X-ray; 2.24 A; A/B=67-406. DR PDB; 2REN; X-ray; 2.50 A; A=67-406. DR PDB; 2V0Z; X-ray; 2.20 A; C/O=67-406. DR PDB; 2V10; X-ray; 3.10 A; C/O=67-406. DR PDB; 2V11; X-ray; 3.10 A; C/O=67-406. DR PDB; 2V12; X-ray; 3.20 A; C/O=67-406. DR PDB; 2V13; X-ray; 2.80 A; A=67-406. DR PDB; 2V16; X-ray; 2.80 A; C/O=67-406. DR PDB; 2X0B; X-ray; 4.33 A; A/C/E/G=24-406. DR PDB; 3D91; X-ray; 2.20 A; A/B=67-406. DR PDB; 3G6Z; X-ray; 2.00 A; A/B=67-406. DR PDB; 3G70; X-ray; 2.00 A; A/B=67-406. DR PDB; 3G72; X-ray; 1.90 A; A/B=67-406. DR PDB; 3GW5; X-ray; 2.00 A; A/B=70-406. DR PDB; 3K1W; X-ray; 1.50 A; A/B=67-406. DR PDB; 3KM4; X-ray; 1.90 A; A/B=70-406. DR PDB; 3O9L; X-ray; 2.40 A; A/C=67-232, B/D=237-406. DR PDB; 3OAD; X-ray; 2.17 A; A/C=67-232, B/D=237-406. DR PDB; 3OAG; X-ray; 2.30 A; A/C=67-232, B/D=237-406. DR PDB; 3OOT; X-ray; 2.55 A; A/B=67-406. DR PDB; 3OQF; X-ray; 2.78 A; A/B=67-406. DR PDB; 3OQK; X-ray; 2.90 A; A/B=67-406. DR PDB; 3OWN; X-ray; 2.00 A; A/B=67-406. DR PDB; 3Q3T; X-ray; 2.60 A; A/B=67-406. DR PDB; 3Q4B; X-ray; 2.19 A; A/B=67-406. DR PDB; 3Q5H; X-ray; 2.16 A; A/B=67-406. DR PDB; 3SFC; X-ray; 2.10 A; A/B=67-406. DR PDB; 3VCM; X-ray; 2.93 A; A/B=67-406, P/Q=24-66. DR PDB; 3VSW; X-ray; 3.00 A; A/B=67-406. DR PDB; 3VSX; X-ray; 2.80 A; A/B=67-406. DR PDB; 3VUC; X-ray; 2.60 A; A/B=67-406. DR PDB; 3VYD; X-ray; 2.81 A; A/B=67-406. DR PDB; 3VYE; X-ray; 2.70 A; A/B=67-406. DR PDB; 3VYF; X-ray; 2.80 A; A/B=67-406. DR PDB; 4AMT; X-ray; 2.60 A; A=24-406. DR PDB; 4GJ5; X-ray; 2.40 A; A/B=67-406. DR PDB; 4GJ6; X-ray; 2.58 A; A/B=67-406. DR PDB; 4GJ7; X-ray; 2.80 A; A/B=67-406. DR PDB; 4GJ8; X-ray; 2.50 A; A/B=67-406. DR PDB; 4GJ9; X-ray; 2.60 A; A/B=67-406. DR PDB; 4GJA; X-ray; 2.60 A; A/B=67-406. DR PDB; 4GJB; X-ray; 2.75 A; A/B=67-406. DR PDB; 4GJC; X-ray; 2.40 A; A/B=67-406. DR PDB; 4GJD; X-ray; 2.65 A; A/B=67-406. DR PDB; 4PYV; X-ray; 2.65 A; A/B=67-406. DR PDB; 4Q1N; X-ray; 2.09 A; A/B=67-406. DR PDB; 4RYC; X-ray; 2.45 A; A/B=67-406. DR PDB; 4RYG; X-ray; 2.65 A; A/B=67-406. DR PDB; 4RZ1; X-ray; 2.60 A; A/B=67-406. DR PDB; 4S1G; X-ray; 2.10 A; A/B=67-406. DR PDB; 4XX3; X-ray; 2.40 A; A/B=67-406. DR PDB; 4XX4; X-ray; 2.40 A; A/B=67-406. DR PDB; 5KOQ; X-ray; 2.70 A; A/B=70-406. DR PDB; 5KOS; X-ray; 2.41 A; A/B=70-406. DR PDB; 5KOT; X-ray; 2.10 A; A/B=70-406. DR PDB; 5SXN; X-ray; 2.10 A; A/B=68-406. DR PDB; 5SY2; X-ray; 2.25 A; A/B=67-406. DR PDB; 5SY3; X-ray; 2.30 A; A/B=68-406. DR PDB; 5SZ9; X-ray; 2.85 A; A/B=68-406. DR PDB; 5T4S; X-ray; 2.64 A; A/B=68-406. DR PDB; 5TMG; X-ray; 2.20 A; A/B=70-406. DR PDB; 5TMK; X-ray; 2.65 A; A/B=70-406. DR PDB; 5V8V; X-ray; 2.60 A; A/B=70-406. DR PDB; 5VPM; X-ray; 2.90 A; A/B=70-406. DR PDB; 5VRP; X-ray; 3.22 A; A/B=70-406. DR PDB; 6I3F; X-ray; 2.55 A; B=67-406. DR PDBsum; 1BBS; -. DR PDBsum; 1BIL; -. DR PDBsum; 1BIM; -. DR PDBsum; 1HRN; -. DR PDBsum; 1RNE; -. DR PDBsum; 2BKS; -. DR PDBsum; 2BKT; -. DR PDBsum; 2FS4; -. DR PDBsum; 2G1N; -. DR PDBsum; 2G1O; -. DR PDBsum; 2G1R; -. DR PDBsum; 2G1S; -. DR PDBsum; 2G1Y; -. DR PDBsum; 2G20; -. DR PDBsum; 2G21; -. DR PDBsum; 2G22; -. DR PDBsum; 2G24; -. DR PDBsum; 2G26; -. DR PDBsum; 2G27; -. DR PDBsum; 2I4Q; -. DR PDBsum; 2IKO; -. DR PDBsum; 2IKU; -. DR PDBsum; 2IL2; -. DR PDBsum; 2REN; -. DR PDBsum; 2V0Z; -. DR PDBsum; 2V10; -. DR PDBsum; 2V11; -. DR PDBsum; 2V12; -. DR PDBsum; 2V13; -. DR PDBsum; 2V16; -. DR PDBsum; 2X0B; -. DR PDBsum; 3D91; -. DR PDBsum; 3G6Z; -. DR PDBsum; 3G70; -. DR PDBsum; 3G72; -. DR PDBsum; 3GW5; -. DR PDBsum; 3K1W; -. DR PDBsum; 3KM4; -. DR PDBsum; 3O9L; -. DR PDBsum; 3OAD; -. DR PDBsum; 3OAG; -. DR PDBsum; 3OOT; -. DR PDBsum; 3OQF; -. DR PDBsum; 3OQK; -. DR PDBsum; 3OWN; -. DR PDBsum; 3Q3T; -. DR PDBsum; 3Q4B; -. DR PDBsum; 3Q5H; -. DR PDBsum; 3SFC; -. DR PDBsum; 3VCM; -. DR PDBsum; 3VSW; -. DR PDBsum; 3VSX; -. DR PDBsum; 3VUC; -. DR PDBsum; 3VYD; -. DR PDBsum; 3VYE; -. DR PDBsum; 3VYF; -. DR PDBsum; 4AMT; -. DR PDBsum; 4GJ5; -. DR PDBsum; 4GJ6; -. DR PDBsum; 4GJ7; -. DR PDBsum; 4GJ8; -. DR PDBsum; 4GJ9; -. DR PDBsum; 4GJA; -. DR PDBsum; 4GJB; -. DR PDBsum; 4GJC; -. DR PDBsum; 4GJD; -. DR PDBsum; 4PYV; -. DR PDBsum; 4Q1N; -. DR PDBsum; 4RYC; -. DR PDBsum; 4RYG; -. DR PDBsum; 4RZ1; -. DR PDBsum; 4S1G; -. DR PDBsum; 4XX3; -. DR PDBsum; 4XX4; -. DR PDBsum; 5KOQ; -. DR PDBsum; 5KOS; -. DR PDBsum; 5KOT; -. DR PDBsum; 5SXN; -. DR PDBsum; 5SY2; -. DR PDBsum; 5SY3; -. DR PDBsum; 5SZ9; -. DR PDBsum; 5T4S; -. DR PDBsum; 5TMG; -. DR PDBsum; 5TMK; -. DR PDBsum; 5V8V; -. DR PDBsum; 5VPM; -. DR PDBsum; 5VRP; -. DR PDBsum; 6I3F; -. DR ProteinModelPortal; P00797; -. DR SMR; P00797; -. DR BioGrid; 111904; 9. DR DIP; DIP-59219N; -. DR ELM; P00797; -. DR IntAct; P00797; 3. DR STRING; 9606.ENSP00000272190; -. DR BindingDB; P00797; -. DR ChEMBL; CHEMBL286; -. DR DrugBank; DB04387; 1-Hydroxy-2-Amino-3-Cyclohexylpropane. DR DrugBank; DB02296; 1-Hydroxy-3-Methylbutane. DR DrugBank; DB03736; 2-Cyclopropylmethylenepropanal. DR DrugBank; DB03024; 2-Methyl-3-(2-Aminothiazolo)Propanal. DR DrugBank; DB09026; Aliskiren. DR DrugBank; DB01844; Dimethylformamide. DR DrugBank; DB03395; Enalkiren. DR DrugBank; DB04379; N-Methyl-N-(Methylbenzyl)Formamide. DR DrugBank; DB00212; Remikiren. DR DrugBank; DB05203; SPP1148. DR GuidetoPHARMACOLOGY; 2413; -. DR MEROPS; A01.007; -. DR GlyConnect; 513; -. DR iPTMnet; P00797; -. DR PhosphoSitePlus; P00797; -. DR UniCarbKB; P00797; -. DR BioMuta; REN; -. DR DMDM; 132326; -. DR PaxDb; P00797; -. DR PeptideAtlas; P00797; -. DR PRIDE; P00797; -. DR ProteomicsDB; 51287; -. DR ProteomicsDB; 51288; -. [P00797-2] DR DNASU; 5972; -. DR Ensembl; ENST00000272190; ENSP00000272190; ENSG00000143839. [P00797-1] DR GeneID; 5972; -. DR KEGG; hsa:5972; -. DR UCSC; uc001haq.3; human. [P00797-1] DR CTD; 5972; -. DR DisGeNET; 5972; -. DR EuPathDB; HostDB:ENSG00000143839.13; -. DR GeneCards; REN; -. DR GeneReviews; REN; -. DR HGNC; HGNC:9958; REN. DR HPA; CAB025903; -. DR HPA; HPA005131; -. DR MalaCards; REN; -. DR MIM; 179820; gene. DR MIM; 267430; phenotype. DR MIM; 613092; phenotype. DR neXtProt; NX_P00797; -. DR OpenTargets; ENSG00000143839; -. DR Orphanet; 217330; REN-related autosomal dominant tubulointerstitial kidney disease. DR Orphanet; 97369; Renal tubular dysgenesis of genetic origin. DR PharmGKB; PA297; -. DR eggNOG; KOG1339; Eukaryota. DR eggNOG; ENOG410XNV7; LUCA. DR GeneTree; ENSGT00940000157898; -. DR HOGENOM; HOG000197681; -. DR HOVERGEN; HBG000482; -. DR InParanoid; P00797; -. DR KO; K01380; -. DR OMA; LGKYYTE; -. DR OrthoDB; 1619495at2759; -. DR PhylomeDB; P00797; -. DR TreeFam; TF314990; -. DR BRENDA; 3.4.23.15; 2681. DR Reactome; R-HSA-2022377; Metabolism of Angiotensinogen to Angiotensins. DR SIGNOR; P00797; -. DR EvolutionaryTrace; P00797; -. DR GeneWiki; Renin; -. DR GenomeRNAi; 5972; -. DR PMAP-CutDB; P00797; -. DR PRO; PR:P00797; -. DR Proteomes; UP000005640; Chromosome 1. DR Bgee; ENSG00000143839; Expressed in 69 organ(s), highest expression level in kidney. DR ExpressionAtlas; P00797; baseline and differential. DR Genevisible; P00797; HS. DR GO; GO:0045177; C:apical part of cell; IDA:BHF-UCL. DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl. DR GO; GO:0005576; C:extracellular region; TAS:Reactome. DR GO; GO:0005615; C:extracellular space; IDA:HGNC. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IDA:HGNC. DR GO; GO:0005159; F:insulin-like growth factor receptor binding; IEA:Ensembl. DR GO; GO:0008233; F:peptidase activity; IDA:HGNC. DR GO; GO:0005102; F:signaling receptor binding; IPI:HGNC. DR GO; GO:0050435; P:amyloid-beta metabolic process; IEA:Ensembl. DR GO; GO:0002003; P:angiotensin maturation; IDA:HGNC. DR GO; GO:0048469; P:cell maturation; IEA:Ensembl. DR GO; GO:0035690; P:cellular response to drug; IEA:Ensembl. DR GO; GO:0042756; P:drinking behavior; IEA:Ensembl. DR GO; GO:0009755; P:hormone-mediated signaling pathway; IEA:Ensembl. DR GO; GO:0001822; P:kidney development; IMP:BHF-UCL. DR GO; GO:0008584; P:male gonad development; IEA:Ensembl. DR GO; GO:0001823; P:mesonephros development; IEA:Ensembl. DR GO; GO:0006508; P:proteolysis; IDA:HGNC. DR GO; GO:0008217; P:regulation of blood pressure; TAS:ProtInc. DR GO; GO:0043408; P:regulation of MAPK cascade; IDA:HGNC. DR GO; GO:0002018; P:renin-angiotensin regulation of aldosterone production; IEA:Ensembl. DR GO; GO:0051591; P:response to cAMP; IEA:Ensembl. DR GO; GO:0070305; P:response to cGMP; IEA:Ensembl. DR GO; GO:0035902; P:response to immobilization stress; IEA:Ensembl. DR GO; GO:0032496; P:response to lipopolysaccharide; IEA:Ensembl. 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; PTHR13683; PTHR13683; 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 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Aspartyl protease; KW Cleavage on pair of basic residues; Complete proteome; KW Direct protein sequencing; Disease mutation; Disulfide bond; KW Glycoprotein; Hydrolase; Membrane; Polymorphism; Protease; KW Reference proteome; Secreted; Signal; Zymogen. FT SIGNAL 1 23 {ECO:0000269|PubMed:2016271}. FT PROPEP 24 66 Activation peptide. FT {ECO:0000269|PubMed:2016271}. FT /FTId=PRO_0000026081. FT CHAIN 67 406 Renin. FT /FTId=PRO_0000026082. FT DOMAIN 86 403 Peptidase A1. {ECO:0000255|PROSITE- FT ProRule:PRU01103}. FT ACT_SITE 104 104 FT ACT_SITE 292 292 FT CARBOHYD 71 71 N-linked (GlcNAc...) asparagine. FT CARBOHYD 141 141 N-linked (GlcNAc...) asparagine. FT DISULFID 117 124 {ECO:0000269|PubMed:20927107}. FT DISULFID 283 287 {ECO:0000269|PubMed:20927107}. FT DISULFID 325 362 {ECO:0000269|PubMed:20927107}. FT VAR_SEQ 231 233 Missing (in isoform 2). {ECO:0000305}. FT /FTId=VSP_012899. FT VARIANT 16 16 L -> R (in HNFJ2; affects ER FT translocation and processing of nascent FT preprorenin, resulting in abolished FT prorenin and renin biosynthesis and FT secretion; dbSNP:rs121917743). FT {ECO:0000269|PubMed:19664745}. FT /FTId=VAR_063770. FT VARIANT 33 33 R -> W (in dbSNP:rs11571098). FT /FTId=VAR_020375. FT VARIANT 104 104 D -> N (in RTD; dbSNP:rs868694193). FT {ECO:0000269|PubMed:16116425}. FT /FTId=VAR_035088. FT VARIANT 160 160 Q -> K (in dbSNP:rs11571083). FT /FTId=VAR_029171. FT VARIANT 217 217 G -> R (in dbSNP:rs11571117). FT /FTId=VAR_020376. FT VARIANT 230 230 R -> K (in RTD; dbSNP:rs121917742). FT {ECO:0000269|PubMed:16116425}. FT /FTId=VAR_035087. FT CONFLICT 55 55 R -> S (in Ref. 2; AAA60364). FT {ECO:0000305}. FT CONFLICT 189 189 E -> Q (in Ref. 2; AAA60364). FT {ECO:0000305}. FT CONFLICT 304 304 S -> C (in Ref. 2; AAA60364). FT {ECO:0000305}. FT CONFLICT 351 351 V -> I (in Ref. 9). {ECO:0000305}. FT STRAND 33 35 {ECO:0000244|PDB:4AMT}. FT HELIX 42 49 {ECO:0000244|PDB:4AMT}. FT HELIX 53 56 {ECO:0000244|PDB:3VCM}. FT STRAND 59 61 {ECO:0000244|PDB:3VCM}. FT STRAND 74 81 {ECO:0000244|PDB:3K1W}. FT TURN 82 84 {ECO:0000244|PDB:3K1W}. FT STRAND 85 92 {ECO:0000244|PDB:3K1W}. FT TURN 93 96 {ECO:0000244|PDB:3K1W}. FT STRAND 97 104 {ECO:0000244|PDB:3K1W}. FT STRAND 110 114 {ECO:0000244|PDB:3K1W}. FT HELIX 119 121 {ECO:0000244|PDB:4AMT}. FT HELIX 122 125 {ECO:0000244|PDB:3K1W}. FT HELIX 132 134 {ECO:0000244|PDB:3K1W}. FT STRAND 139 149 {ECO:0000244|PDB:3K1W}. FT STRAND 152 165 {ECO:0000244|PDB:3K1W}. FT STRAND 168 179 {ECO:0000244|PDB:3K1W}. FT HELIX 182 185 {ECO:0000244|PDB:3K1W}. FT STRAND 189 195 {ECO:0000244|PDB:3K1W}. FT HELIX 199 201 {ECO:0000244|PDB:3K1W}. FT HELIX 203 205 {ECO:0000244|PDB:3K1W}. FT HELIX 209 215 {ECO:0000244|PDB:3K1W}. FT STRAND 219 228 {ECO:0000244|PDB:3K1W}. FT STRAND 233 236 {ECO:0000244|PDB:3GW5}. FT STRAND 240 246 {ECO:0000244|PDB:3K1W}. FT HELIX 249 251 {ECO:0000244|PDB:3K1W}. FT STRAND 252 260 {ECO:0000244|PDB:3K1W}. FT STRAND 262 266 {ECO:0000244|PDB:1BBS}. FT STRAND 268 271 {ECO:0000244|PDB:3K1W}. FT STRAND 274 276 {ECO:0000244|PDB:3K1W}. FT STRAND 279 282 {ECO:0000244|PDB:3K1W}. FT TURN 284 286 {ECO:0000244|PDB:2G27}. FT STRAND 287 291 {ECO:0000244|PDB:3K1W}. FT STRAND 296 300 {ECO:0000244|PDB:3K1W}. FT HELIX 302 312 {ECO:0000244|PDB:3K1W}. FT STRAND 315 317 {ECO:0000244|PDB:3SFC}. FT STRAND 318 320 {ECO:0000244|PDB:2G27}. FT STRAND 321 324 {ECO:0000244|PDB:3K1W}. FT HELIX 325 330 {ECO:0000244|PDB:3K1W}. FT STRAND 334 338 {ECO:0000244|PDB:3K1W}. FT STRAND 341 345 {ECO:0000244|PDB:3K1W}. FT HELIX 347 350 {ECO:0000244|PDB:3K1W}. FT STRAND 360 368 {ECO:0000244|PDB:3K1W}. FT TURN 373 375 {ECO:0000244|PDB:3K1W}. FT STRAND 379 381 {ECO:0000244|PDB:3K1W}. FT HELIX 383 386 {ECO:0000244|PDB:3K1W}. FT STRAND 389 394 {ECO:0000244|PDB:3K1W}. FT TURN 395 398 {ECO:0000244|PDB:3K1W}. FT STRAND 399 405 {ECO:0000244|PDB:3K1W}. SQ SEQUENCE 406 AA; 45057 MW; 5AFDF8E973B21EDA CRC64; MDGWRRMPRW GLLLLLWGSC TFGLPTDTTT FKRIFLKRMP SIRESLKERG VDMARLGPEW SQPMKRLTLG NTTSSVILTN YMDTQYYGEI GIGTPPQTFK VVFDTGSSNV WVPSSKCSRL YTACVYHKLF DASDSSSYKH NGTELTLRYS TGTVSGFLSQ DIITVGGITV TQMFGEVTEM PALPFMLAEF DGVVGMGFIE QAIGRVTPIF DNIISQGVLK EDVFSFYYNR DSENSQSLGG QIVLGGSDPQ HYEGNFHYIN LIKTGVWQIQ MKGVSVGSST LLCEDGCLAL VDTGASYISG STSSIEKLME ALGAKKRLFD YVVKCNEGPT LPDISFHLGG KEYTLTSADY VFQESYSSKK LCTLAIHAMD IPPPTGPTWA LGATFIRKFY TEFDRRNNRI GFALAR //