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P00797 (RENI_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 179. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Renin

EC=3.4.23.15
Alternative name(s):
Angiotensinogenase
Gene names
Name:REN
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length406 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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 componentMembrane
Secreted
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
   DomainSignal
   Molecular functionAspartyl protease
Hydrolase
Protease
   PTMCleavage on pair of basic residues
Disulfide bond
Glycoprotein
Zymogen
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processangiotensin maturation

Inferred from direct assay Ref.14. Source: HGNC

beta-amyloid metabolic process

Inferred from electronic annotation. Source: Ensembl

cell maturation

Inferred from electronic annotation. Source: Ensembl

cellular protein metabolic process

Traceable author statement. Source: Reactome

cellular response to drug

Inferred from electronic annotation. Source: Ensembl

drinking behavior

Inferred from electronic annotation. Source: Ensembl

hormone-mediated signaling pathway

Inferred from electronic annotation. Source: Ensembl

kidney development

Inferred from mutant phenotype Ref.18. Source: BHF-UCL

male gonad development

Inferred from electronic annotation. Source: Ensembl

mesonephros development

Inferred from electronic annotation. Source: Ensembl

proteolysis

Inferred from direct assay Ref.14. Source: HGNC

regulation of MAPK cascade

Inferred from direct assay Ref.14. Source: HGNC

regulation of blood pressure

Traceable author statement PubMed 7584914. Source: ProtInc

renin-angiotensin regulation of aldosterone production

Inferred from electronic annotation. Source: Ensembl

response to cAMP

Inferred from electronic annotation. Source: Ensembl

response to cGMP

Inferred from electronic annotation. Source: Ensembl

response to lipopolysaccharide

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentextracellular region

Traceable author statement. Source: Reactome

extracellular space

Inferred from direct assay Ref.14. Source: HGNC

intracellular

Inferred from electronic annotation. Source: Ensembl

plasma membrane

Traceable author statement. Source: Reactome

   Molecular_functionaspartic-type endopeptidase activity

Inferred from direct assay Ref.14. Source: HGNC

peptidase activity

Inferred from direct assay Ref.14. Source: HGNC

receptor binding

Inferred from physical interaction 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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323 Ref.13
Propeptide24 – 6643Activation peptide
PRO_0000026081
Chain67 – 406340Renin
PRO_0000026082

Sites

Active site1041
Active site2921

Amino acid modifications

Glycosylation711N-linked (GlcNAc...)
Glycosylation1411N-linked (GlcNAc...)
Disulfide bond117 ↔ 124 Ref.17
Disulfide bond283 ↔ 287 Ref.17
Disulfide bond325 ↔ 362 Ref.17

Natural variations

Alternative sequence231 – 2333Missing in isoform 2.
VSP_012899
Natural variant161L → 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 variant331R → W.
Corresponds to variant rs11571098 [ dbSNP | Ensembl ].
VAR_020375
Natural variant1041D → N in RTD. Ref.18
VAR_035088
Natural variant1601Q → K.
Corresponds to variant rs11571083 [ dbSNP | Ensembl ].
VAR_029171
Natural variant2171G → R.
Corresponds to variant rs11571117 [ dbSNP | Ensembl ].
VAR_020376
Natural variant2301R → K in RTD. Ref.18
VAR_035087

Experimental info

Sequence conflict551R → S in AAA60364. Ref.2
Sequence conflict1891E → Q in AAA60364. Ref.2
Sequence conflict3041S → C in AAA60364. Ref.2
Sequence conflict3511V → I Ref.9

Secondary structure

..................................................................................... 406
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 1, 1988. Version 1.
Checksum: 5AFDF8E973B21EDA

FASTA40645,057
        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 

« Hide

Isoform 2 [UniParc].

Checksum: 4DEF0016D9EF5854
Show »

FASTA40344,726

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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 expand/collapse EMBL AC list , L00064, L00065, L00066, L00067, L00068, L00069, L00070, L00071, L00072 Genomic DNA. Translation: AAA60363.1.
M26901, M26899, M26900 Genomic DNA. Translation: AAA60364.1.
M10152 expand/collapse EMBL AC list , 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.
CCDSCCDS30981.1. [P00797-1]
PIRREHUK. A21454.
RefSeqNP_000528.1. NM_000537.3. [P00797-1]
UniGeneHs.3210.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1BBSX-ray2.80A/B67-406[»]
1BILX-ray2.40A/B70-406[»]
1BIMX-ray2.80A/B70-406[»]
1HRNX-ray1.80A/B70-406[»]
1RNEX-ray2.40A67-406[»]
2BKSX-ray2.20A/B67-406[»]
2BKTX-ray2.30A/B67-406[»]
2FS4X-ray2.20A/B74-406[»]
2G1NX-ray2.90A/B74-406[»]
2G1OX-ray2.70A/B74-406[»]
2G1RX-ray2.42A/B74-406[»]
2G1SX-ray2.50A/B74-406[»]
2G1YX-ray2.50A/B74-406[»]
2G20X-ray2.40A/B74-406[»]
2G21X-ray2.20A/B74-406[»]
2G22X-ray2.50A/B74-406[»]
2G24X-ray1.90A/B74-406[»]
2G26X-ray2.10A/B74-406[»]
2G27X-ray2.90A/B74-406[»]
2I4QX-ray2.30A/B73-406[»]
2IKOX-ray1.90A/B67-406[»]
2IKUX-ray2.60A/B67-406[»]
2IL2X-ray2.24A/B67-406[»]
2RENX-ray2.50A67-406[»]
2V0ZX-ray2.20C/O67-406[»]
2V10X-ray3.10C/O67-406[»]
2V11X-ray3.10C/O67-406[»]
2V12X-ray3.20C/O67-406[»]
2V13X-ray2.80A67-406[»]
2V16X-ray2.80C/O67-406[»]
2X0BX-ray4.33A/C/E/G24-406[»]
3D91X-ray2.20A/B67-406[»]
3G6ZX-ray2.00A/B67-406[»]
3G70X-ray2.00A/B67-406[»]
3G72X-ray1.90A/B67-406[»]
3GW5X-ray2.00A/B70-406[»]
3K1WX-ray1.50A/B67-406[»]
3KM4X-ray1.90A/B70-406[»]
3O9LX-ray2.40A/C67-232[»]
B/D237-406[»]
3OADX-ray2.17A/C67-232[»]
B/D237-406[»]
3OAGX-ray2.30A/C67-232[»]
B/D237-406[»]
3OOTX-ray2.55A/B67-406[»]
3OQFX-ray2.78A/B67-406[»]
3OQKX-ray2.90A/B67-406[»]
3OWNX-ray2.00A/B67-406[»]
3Q3TX-ray2.60A/B67-406[»]
3Q4BX-ray2.19A/B67-406[»]
3Q5HX-ray2.16A/B67-406[»]
3SFCX-ray2.10A/B67-406[»]
3VCMX-ray2.93A/B67-406[»]
P/Q24-66[»]
3VSWX-ray3.00A/B67-406[»]
3VSXX-ray2.80A/B67-406[»]
3VUCX-ray2.60A/B67-406[»]
3VYDX-ray2.81A/B67-406[»]
3VYEX-ray2.70A/B67-406[»]
3VYFX-ray2.80A/B67-406[»]
4AMTX-ray2.60A24-406[»]
4GJ5X-ray2.40A/B67-406[»]
4GJ6X-ray2.58A/B67-406[»]
4GJ7X-ray2.80A/B67-406[»]
4GJ8X-ray2.50A/B67-406[»]
4GJ9X-ray2.60A/B67-406[»]
4GJAX-ray2.60A/B67-406[»]
4GJBX-ray2.75A/B67-406[»]
4GJCX-ray2.40A/B67-406[»]
4GJDX-ray2.65A/B67-406[»]
ProteinModelPortalP00797.
SMRP00797. Positions 30-406.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111904. 3 interactions.
DIPDIP-59219N.
IntActP00797. 1 interaction.
MINTMINT-1381167.
STRING9606.ENSP00000272190.

Chemistry

BindingDBP00797.
ChEMBLCHEMBL286.
DrugBankDB01258. Aliskiren.
DB00212. Remikiren.
GuidetoPHARMACOLOGY2413.

Protein family/group databases

MEROPSA01.007.

PTM databases

PhosphoSiteP00797.
UniCarbKBP00797.

Polymorphism databases

DMDM132326.

Proteomic databases

PaxDbP00797.
PRIDEP00797.

Protocols and materials databases

DNASU5972.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000272190; ENSP00000272190; ENSG00000143839. [P00797-1]
ENST00000367195; ENSP00000356163; ENSG00000143839. [P00797-2]
GeneID5972.
KEGGhsa:5972.
UCSCuc001haq.2. human. [P00797-1]

Organism-specific databases

CTD5972.
GeneCardsGC01M204123.
GeneReviewsREN.
HGNCHGNC:9958. REN.
HPACAB025903.
HPA005131.
MIM179820. gene.
267430. phenotype.
613092. phenotype.
neXtProtNX_P00797.
Orphanet217330. Hyperuricemia - anemia - renal failure.
97369. Renal tubular dysgenesis of genetic origin.
PharmGKBPA297.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG248684.
HOGENOMHOG000197681.
HOVERGENHBG000482.
KOK01380.
OMAIARYYTE.
OrthoDBEOG7HQN88.
PhylomeDBP00797.
TreeFamTF314990.

Enzyme and pathway databases

ReactomeREACT_17015. Metabolism of proteins.

Gene expression databases

ArrayExpressP00797.
BgeeP00797.
CleanExHS_REN.
GenevestigatorP00797.

Family and domain databases

Gene3D2.40.70.10. 2 hits.
InterProIPR001461. Aspartic_peptidase.
IPR001969. Aspartic_peptidase_AS.
IPR012848. Aspartic_peptidase_N.
IPR021109. Peptidase_aspartic_dom.
[Graphical view]
PANTHERPTHR13683. PTHR13683. 1 hit.
PfamPF07966. A1_Propeptide. 1 hit.
PF00026. Asp. 1 hit.
[Graphical view]
PRINTSPR00792. PEPSIN.
SUPFAMSSF50630. SSF50630. 1 hit.
PROSITEPS00141. ASP_PROTEASE. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP00797.
GeneWikiRenin.
GenomeRNAi5972.
NextBio23249.
PMAP-CutDBP00797.
PROP00797.
SOURCESearch...

Entry information

Entry nameRENI_HUMAN
AccessionPrimary (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: July 9, 2014
This is version 179 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM