P00797 (RENI_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Renin
EC=3.4.23.15

Alternative name(s):
Angiotensinogenase

Gene names

Name:

REN

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	406 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Renin is a highly specific endopeptidase, whose only known function is to generate angiotensin I from angiotensinogen in the plasma, initiating a cascade of reactions that produce an elevation of blood pressure and increased sodium retention by the kidney.
Catalytic activity	Cleavage of Leu-|-Xaa bond in angiotensinogen to generate angiotensin I.
Enzyme regulation	Interaction with ATP6AP2 results in a 5-fold increased efficiency in angiotensinogen processing.
Subunit structure	Interacts with ATP6AP2. Ref.14
Subcellular location	Secreted. Membrane. Note: Associated to membranes via binding to ATP6AP2.
Involvement in disease	Renal tubular dysgenesis (RTD) [MIM:267430]: Autosomal recessive severe disorder of renal tubular development characterized by persistent fetal anuria and perinatal death, probably due to pulmonary hypoplasia from early-onset oligohydramnios (the Potter phenotype). Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.18 Familial juvenile hyperuricemic nephropathy 2 (HNFJ2) [MIM:613092]: A renal disease characterized by juvenile onset of hyperuricemia, slowly progressive renal failure and anemia. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.19
Sequence similarities	Belongs to the peptidase A1 family.
Biophysicochemical properties	Kinetic parameters: KM=1 µM for angiotensinogen (in absence of ATP6AP2) KM=0.15 µM for angiotensinogen (in presence of membrane-bound ATP6AP2)

Ontologies

Keywords
Cellular component	Membrane Secreted
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Disease mutation
Domain	Signal
Molecular function	Aspartyl protease Hydrolase Protease
PTM	Cleavage on pair of basic residues Disulfide bond Glycoprotein Zymogen
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	angiotensin maturation Inferred from direct assay Ref.14. Source: HGNC beta-amyloid metabolic process Inferred from electronic annotation. Source: Compara cell maturation Inferred from electronic annotation. Source: Compara cellular response to drug Inferred from electronic annotation. Source: Compara drinking behavior Inferred from electronic annotation. Source: Compara hormone-mediated signaling pathway Inferred from electronic annotation. Source: Compara kidney development Inferred from mutant phenotype Ref.18. Source: BHF-UCL male gonad development Inferred from electronic annotation. Source: Compara mesonephros development Inferred from electronic annotation. Source: Compara proteolysis Inferred from direct assay Ref.14. Source: HGNC regulation of MAPK cascade Inferred from direct assay Ref.14. Source: HGNC renin-angiotensin regulation of aldosterone production Inferred from electronic annotation. Source: Compara response to cAMP Inferred from electronic annotation. Source: Compara response to cGMP Inferred from electronic annotation. Source: Compara response to lipopolysaccharide Inferred from electronic annotation. Source: Compara response to stress Inferred from electronic annotation. Source: Compara
Cellular_component	cytoplasmic part Inferred from electronic annotation. Source: Compara extracellular space Inferred from direct assay Ref.14. Source: HGNC membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	aspartic-type endopeptidase activity Inferred from direct assay Ref.14. Source: HGNC
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P00797-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: P00797-2)

The sequence of this isoform differs from the canonical sequence as follows:
     231-233: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 23

23

Ref.13

Propeptide

24 – 66

43

Activation peptide

PRO_0000026081

Chain

67 – 406

340

Renin

PRO_0000026082

Sites

Active site

104

1

Active site

292

1

Amino acid modifications

Glycosylation

71

1

N-linked (GlcNAc...)

Glycosylation

141

1

N-linked (GlcNAc...)

Disulfide bond

117 ↔ 124

Ref.17

Disulfide bond

283 ↔ 287

Ref.17

Disulfide bond

325 ↔ 362

Ref.17

Natural variations

Alternative sequence

231 – 233

3

Missing in isoform 2.

VSP_012899

Natural variant

16

1

L → R in HNFJ2; affects ER translocation and processing of nascent preprorenin, resulting in abolished prorenin and renin biosynthesis and secretion. Ref.19

VAR_063770

Natural variant

33

1

R → W.
Corresponds to variant rs11571098 [ dbSNP | Ensembl ].

VAR_020375

Natural variant

104

1

D → N in RTD. Ref.18

VAR_035088

Natural variant

160

1

Q → K.
Corresponds to variant rs11571083 [ dbSNP | Ensembl ].

VAR_029171

Natural variant

217

1

G → R.
Corresponds to variant rs11571117 [ dbSNP | Ensembl ].

VAR_020376

Natural variant

230

1

R → K in RTD. Ref.18

VAR_035087

Experimental info

Sequence conflict

55

1

R → S in AAA60364. Ref.2

Sequence conflict

189

1

E → Q in AAA60364. Ref.2

Sequence conflict

304

1

S → C in AAA60364. Ref.2

Sequence conflict

351

1

V → I Ref.9

Secondary structure

1

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406

Helix Strand Turn

Details...

Beta strand

74 – 81

8

Turn

82 – 84

3

Beta strand

85 – 92

8

Turn

93 – 96

4

Beta strand

97 – 104

8

Beta strand

110 – 114

5

Beta strand

119 – 121

3

Helix

122 – 125

4

Helix

132 – 134

3

Beta strand

139 – 149

11

Beta strand

152 – 165

14

Beta strand

168 – 179

12

Helix

182 – 185

4

Beta strand

189 – 195

7

Helix

199 – 201

3

Helix

203 – 205

3

Helix

209 – 215

7

Beta strand

219 – 228

10

Beta strand

233 – 236

4

Beta strand

240 – 246

7

Helix

249 – 251

3

Beta strand

252 – 260

9

Beta strand

262 – 266

5

Beta strand

268 – 271

4

Beta strand

274 – 276

3

Beta strand

279 – 282

4

Turn

284 – 286

3

Beta strand

287 – 291

5

Beta strand

296 – 300

5

Helix

302 – 312

11

Beta strand

315 – 317

3

Beta strand

318 – 320

3

Beta strand

321 – 324

4

Helix

325 – 330

6

Beta strand

334 – 338

5

Beta strand

341 – 345

5

Helix

347 – 350

4

Beta strand

360 – 368

9

Turn

373 – 375

3

Beta strand

379 – 381

3

Helix

383 – 386

4

Beta strand

389 – 394

6

Turn

395 – 398

4

Beta strand

399 – 405

7

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified January 1, 1988. Version 1. Checksum: 5AFDF8E973B21EDA	FASTA	406	45,057
	10 20 30 40 50 60 MDGWRRMPRW GLLLLLWGSC TFGLPTDTTT FKRIFLKRMP SIRESLKERG VDMARLGPEW 70 80 90 100 110 120 SQPMKRLTLG NTTSSVILTN YMDTQYYGEI GIGTPPQTFK VVFDTGSSNV WVPSSKCSRL 130 140 150 160 170 180 YTACVYHKLF DASDSSSYKH NGTELTLRYS TGTVSGFLSQ DIITVGGITV TQMFGEVTEM 190 200 210 220 230 240 PALPFMLAEF DGVVGMGFIE QAIGRVTPIF DNIISQGVLK EDVFSFYYNR DSENSQSLGG 250 260 270 280 290 300 QIVLGGSDPQ HYEGNFHYIN LIKTGVWQIQ MKGVSVGSST LLCEDGCLAL VDTGASYISG 310 320 330 340 350 360 STSSIEKLME ALGAKKRLFD YVVKCNEGPT LPDISFHLGG KEYTLTSADY VFQESYSSKK 370 380 390 400 LCTLAIHAMD IPPPTGPTWA LGATFIRKFY TEFDRRNNRI GFALAR
	Isoform 2 [UniParc]. Checksum: 4DEF0016D9EF5854	FASTA	403	44,726
	10 20 30 40 50 60 MDGWRRMPRW GLLLLLWGSC TFGLPTDTTT FKRIFLKRMP SIRESLKERG VDMARLGPEW 70 80 90 100 110 120 SQPMKRLTLG NTTSSVILTN YMDTQYYGEI GIGTPPQTFK VVFDTGSSNV WVPSSKCSRL 130 140 150 160 170 180 YTACVYHKLF DASDSSSYKH NGTELTLRYS TGTVSGFLSQ DIITVGGITV TQMFGEVTEM 190 200 210 220 230 240 PALPFMLAEF DGVVGMGFIE QAIGRVTPIF DNIISQGVLK EDVFSFYYNR NSQSLGGQIV 250 260 270 280 290 300 LGGSDPQHYE GNFHYINLIK TGVWQIQMKG VSVGSSTLLC EDGCLALVDT GASYISGSTS 310 320 330 340 350 360 SIEKLMEALG AKKRLFDYVV KCNEGPTLPD ISFHLGGKEY TLTSADYVFQ ESYSSKKLCT 370 380 390 400 LAIHAMDIPP PTGPTWALGA TFIRKFYTEF DRRNNRIGFA LAR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and sequence analysis of cDNA for human renin precursor." Imai T., Miyazaki H., Hirose S., Hori H., Hayashi T., Kageyama R., Ohkubo H., Nakanishi S., Murakami K. Proc. Natl. Acad. Sci. U.S.A. 80:7405-7409(1983) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
[2]	"New possibilities for intracellular renin and inactive renin now that the structure of the human renin gene has been elucidated." Morris B.J. Clin. Sci. 71:345-355(1986) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 2).
[3]	"Primary structure of the human renin gene." Hardman J.A., Hort Y.J., Catanzaro D.F., Tellam J.T., Baxter J.D., Morris B.J., Shine J. DNA 3:457-468(1984) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Tissue: Fetal liver.
[4]	Rieder M.J., da Ponte S.H., Kuldanek S.A., Rajkumar N., Smith J.D., Toth E.J., Krauss R.M., Nickerson D.A. Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]	"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)." Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B. Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[6]	NIEHS SNPs program Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[7]	"The DNA sequence and biological annotation of human chromosome 1." Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R. Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Colon and Ovary.
[9]	"Molecular cloning and nucleotide sequence of a human renin cDNA fragment." Soubrier F., Panthier J.-J., Corvol P., Rougeon F. Nucleic Acids Res. 11:7181-7190(1983) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 108-406 (ISOFORM 1).
[10]	"Human renin gene of renin-secreting tumor." Fukamizu A., Nishi K., Nishimatsu S., Miyazaki H., Hirose S., Murakami K. Gene 49:139-145(1986) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-33.
[11]	"Identification of negative and positive regulatory elements in the human renin gene." Burt D.W., Nakamura N., Kelley P., Dzau V.J. J. Biol. Chem. 264:7357-7362(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-33.
[12]	"Segmental homology between the promoter region of the human renin gene and the mouse ren1 and ren2 promoter regions." Soubrier F., Panthier J.J., Houot A.-M., Rougeon F., Corvol P. Gene 41:85-92(1986) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-33.
[13]	"Isolation and characterization of recombinant human prorenin in Chinese hamster ovary cells." Ishizuka Y., Shoda A., Yoshida S., Kawamura Y., Haraguchi K., Murakami K. J. Biochem. 109:30-35(1991) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 24-42 AND 67-86.
[14]	"Pivotal role of the renin/prorenin receptor in angiotensin II production and cellular responses to renin." Nguyen G., Delarue F., Burckle C., Bouzhir L., Giller T., Sraer J.-D. J. Clin. Invest. 109:1417-1427(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH ATP6AP2, CHARACTERIZATION.
[15]	"Structure of recombinant human renin, a target for cardiovascular-active drugs, at 2.5-A resolution." Sielecki A.R., Hayakawa K., Fujinaga M., Murphy M.E.P., Fraser M., Muir A.K., Carilli C.T., Lewicki J.A., Baxter J.D., James M.N.G. Science 243:1346-1351(1989) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
[16]	"X-ray analyses of peptide-inhibitor complexes define the structural basis of specificity for human and mouse renins." Dhanaraj V., Dealwis C.G., Frazao C., Badasso M., Sibanda B.L., Tickle I.J., Cooper J.B., Driessen H.P.C., Newman M., Aguilar C., Wood S.P., Blundell T.L., Hobart P.M., Geoghegan K.F., Ammirati M.J., Danley D.E., O'Connor B.A., Hoover D.J. Nature 357:466-472(1992) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
[17]	"A redox switch in angiotensinogen modulates angiotensin release." Zhou A., Carrell R.W., Murphy M.P., Wei Z., Yan Y., Stanley P.L., Stein P.E., Broughton Pipkin F., Read R.J. Nature 468:108-111(2010) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (4.33 ANGSTROMS) OF 24-406 OF MUTANT ALA-292 IN COMPLEX WITH ANGIOTENSINOGEN, DISULFIDE BONDS.
[18]	"Mutations in genes in the renin-angiotensin system are associated with autosomal recessive renal tubular dysgenesis." Gribouval O., Gonzales M., Neuhaus T., Aziza J., Bieth E., Laurent N., Bouton J.M., Feuillet F., Makni S., Ben Amar H., Laube G., Delezoide A.-L., Bouvier R., Dijoud F., Ollagnon-Roman E., Roume J., Joubert M., Antignac C., Gubler M.-C. Nat. Genet. 37:964-968(2005) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS RTD ASN-104 AND LYS-230.
[19]	"Dominant renin gene mutations associated with early-onset hyperuricemia, anemia, and chronic kidney failure." Zivna M., Hulkova H., Matignon M., Hodanova K., Vylet'al P., Kalbacova M., Baresova V., Sikora J., Blazkova H., Zivny J., Ivanek R., Stranecky V., Sovova J., Claes K., Lerut E., Fryns J.P., Hart P.S., Hart T.C. , Adams J.N., Pawtowski A., Clemessy M., Gasc J.M., Guebler M.C., Antignac C., Elleder M., Kapp K., Grimbert P., Bleyer A.J., Kmoch S. Am. J. Hum. Genet. 85:204-213(2009) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT HNFJ2 ARG-16, CHARACTERIZATION OF VARIANT HNFJ2 ARG-16.
+	Additional computationally mapped references.

Web resources

Wikipedia

Renin entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

L00073 , L00064, L00065, L00066, L00067, L00068, L00069, L00070, L00071, L00072 Genomic DNA. Translation: AAA60363.1.
M26901, M26899, M26900 Genomic DNA. Translation: AAA60364.1.
M10152 , M10030, M10128, M10150, M10151 Genomic DNA. Translation: AAD03461.1.
AY436324 Genomic DNA. Translation: AAR03502.1.
CR536498 mRNA. Translation: CAG38737.1.
EU332871 Genomic DNA. Translation: ABY87560.1.
AL592114, AL592146 Genomic DNA. Translation: CAH71224.1.
AL592146, AL592114 Genomic DNA. Translation: CAI16594.1.
BC033474 mRNA. Translation: AAH33474.1.
BC047752 mRNA. Translation: AAH47752.1.
M15410 Genomic DNA. Translation: AAA60263.1.
M26440 Genomic DNA. Translation: AAA60365.1.
M13253 Genomic DNA. Translation: AAA60262.1.

IPI

IPI00019644.
IPI00552207.

PIR

REHUK. A21454.

RefSeq

NP_000528.1. NM_000537.3.

UniGene

Hs.3210.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1BBS	X-ray	2.80	A/B	67-406	[»]
1BIL	X-ray	2.40	A/B	70-406	[»]
1BIM	X-ray	2.80	A/B	70-406	[»]
1HRN	X-ray	1.80	A/B	70-406	[»]
1RNE	X-ray	2.40	A	67-406	[»]
2BKS	X-ray	2.20	A/B	67-406	[»]
2BKT	X-ray	2.30	A/B	67-406	[»]
2FS4	X-ray	2.20	A/B	74-406	[»]
2G1N	X-ray	2.90	A/B	74-406	[»]
2G1O	X-ray	2.70	A/B	74-406	[»]
2G1R	X-ray	2.42	A/B	74-406	[»]
2G1S	X-ray	2.50	A/B	74-406	[»]
2G1Y	X-ray	2.50	A/B	74-406	[»]
2G20	X-ray	2.40	A/B	74-406	[»]
2G21	X-ray	2.20	A/B	74-406	[»]
2G22	X-ray	2.50	A/B	74-406	[»]
2G24	X-ray	1.90	A/B	74-406	[»]
2G26	X-ray	2.10	A/B	74-406	[»]
2G27	X-ray	2.90	A/B	74-406	[»]
2I4Q	X-ray	2.30	A/B	73-406	[»]
2IKO	X-ray	1.90	A/B	67-406	[»]
2IKU	X-ray	2.60	A/B	67-406	[»]
2IL2	X-ray	2.24	A/B	67-406	[»]
2REN	X-ray	2.50	A	67-406	[»]
2V0Z	X-ray	2.20	C/O	67-406	[»]
2V10	X-ray	3.10	C/O	67-406	[»]
2V11	X-ray	3.10	C/O	67-406	[»]
2V12	X-ray	3.20	C/O	67-406	[»]
2V13	X-ray	2.80	A	67-406	[»]
2V16	X-ray	2.80	C/O	67-406	[»]
2X0B	X-ray	4.33	A/C/E/G	24-406	[»]
3D91	X-ray	2.20	A/B	67-406	[»]
3G6Z	X-ray	2.00	A/B	67-406	[»]
3G70	X-ray	2.00	A/B	67-406	[»]
3G72	X-ray	1.90	A/B	67-406	[»]
3GW5	X-ray	2.00	A/B	70-406	[»]
3K1W	X-ray	1.50	A/B	67-406	[»]
3KM4	X-ray	1.90	A/B	70-406	[»]
3O9L	X-ray	2.40	A/C	67-232	[»]
			B/D	237-406	[»]
3OAD	X-ray	2.17	A/C	67-232	[»]
			B/D	237-406	[»]
3OAG	X-ray	2.30	A/C	67-232	[»]
			B/D	237-406	[»]
3OOT	X-ray	2.55	A/B	67-406	[»]
3OQF	X-ray	2.78	A/B	67-406	[»]
3OQK	X-ray	2.90	A/B	67-406	[»]
3OWN	X-ray	2.00	A/B	67-406	[»]
3Q3T	X-ray	2.60	A/B	67-406	[»]
3Q4B	X-ray	2.19	A/B	67-406	[»]
3Q5H	X-ray	2.16	A/B	67-406	[»]
3SFC	X-ray	2.10	A/B	67-406	[»]
3VCM	X-ray	2.93	A/B	67-406	[»]
			P/Q	24-66	[»]
3VSW	X-ray	3.00	A/B	67-406	[»]
3VSX	X-ray	2.80	A/B	67-406	[»]
3VYD	X-ray	2.81	A/B	67-406	[»]
3VYE	X-ray	2.70	A/B	67-406	[»]
3VYF	X-ray	2.80	A/B	67-406	[»]
4GJ5	X-ray	2.40	A/B	67-406	[»]
4GJ6	X-ray	2.58	A/B	67-406	[»]
4GJ7	X-ray	2.80	A/B	67-406	[»]
4GJ8	X-ray	2.50	A/B	67-406	[»]
4GJ9	X-ray	2.60	A/B	67-406	[»]
4GJA	X-ray	2.60	A/B	67-406	[»]
4GJB	X-ray	2.75	A/B	67-406	[»]
4GJC	X-ray	2.40	A/B	67-406	[»]
4GJD	X-ray	2.65	A/B	67-406	[»]

ProteinModelPortal

P00797.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-59219N.

IntAct

P00797. 1 interaction.

MINT

MINT-1381167.

STRING

9606.ENSP00000272190.

Protein family/group databases

MEROPS

A01.007.

PTM databases

GlycoSuiteDB

P00797.

PhosphoSite

P00797.

Polymorphism databases

DMDM

132326.

Proteomic databases

PaxDb

P00797.

PRIDE

P00797.

Protocols and materials databases

DNASU

5972.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000272190; ENSP00000272190; ENSG00000143839.
ENST00000367195; ENSP00000356163; ENSG00000143839.

GeneID

5972.

KEGG

hsa:5972.

UCSC

uc001haq.2. human.

Organism-specific databases

CTD

5972.

GeneCards

GC01M204123.

HGNC

HGNC:9958. REN.

HPA

CAB025903.
HPA005131.

MIM

179820. gene.
267430. phenotype.
613092. phenotype.

neXtProt

NX_P00797.

Orphanet

217330. Hyperuricemia - anemia - renal failure.
97369. Renal tubular dysgenesis of genetic origin.

PharmGKB

PA297.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG248684.

HOGENOM

HOG000197681.

HOVERGEN

HBG000482.

KO

K01380.

OMA

SFHLGGK.

OrthoDB

EOG4W3SN8.

Enzyme and pathway databases

Reactome

REACT_17015. Metabolism of proteins.

Gene expression databases

ArrayExpress

P00797.

Bgee

P00797.

CleanEx

HS_REN.

Genevestigator

P00797.

GermOnline

ENSG00000143839. Homo sapiens.

Family and domain databases

Gene3D

2.40.70.10. 2 hits.

InterPro

IPR001461. Peptidase_A1.
IPR021109. Peptidase_aspartic.
IPR001969. Peptidase_aspartic_AS.
IPR012848. Propep_A1.
[Graphical view]

PANTHER

PTHR13683. PTHR13683. 1 hit.

Pfam

PF07966. A1_Propeptide. 1 hit.
PF00026. Asp. 1 hit.
[Graphical view]

PRINTS

PR00792. PEPSIN.

SUPFAM

SSF50630. Pept_Aspartic. 1 hit.

PROSITE

PS00141. ASP_PROTEASE. 2 hits.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P00797.

ChEMBL

CHEMBL286.

DrugBank

DB01258. Aliskiren.
DB00212. Remikiren.

EvolutionaryTrace

P00797.

GenomeRNAi

5972.

NextBio

23249.

PMAP-CutDB

P00797.

SOURCE

Search...

Entry information

Entry name

RENI_HUMAN

Accession

Primary (citable) accession number: P00797
Secondary accession number(s): Q6FI38, Q6T5C2

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	January 1, 1988
Last modified:	May 1, 2013
This is version 166 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.