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Reviewed, UniProtKB/Swiss-Prot P00797 (RENI_HUMAN)

Last modified September 23, 2008. Version 113. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (8) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Renin
    EC=3.4.23.15
Alternative name(s):
    Angiotensinogenase
Gene names
Name: REN
OrganismHomo sapiens (Human)
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.

Subcellular location

Secreted. Membrane. Note= Associated to membranes via binding to ATP6AP2.

Involvement in disease

Defects in REN are a cause of renal tubular dysgenesis (RTD) [MIM:267430]. RTD is an 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).

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)

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 view

Molecule processing

Signal peptide1 – 2323
Propeptide24 – 6643Activation peptide
Chain67 – 406340Renin

Sites

Active site1041
Active site2921

Amino acid modifications

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

Natural variations

Alternative sequence231 – 2333Missing in isoform 2.
Natural variant331R → W: dbSNP rs11571098.
Natural variant1041D → N in RTD.
Natural variant1601Q → K: dbSNP rs11571083.
Natural variant2171G → R: dbSNP rs11571117.
Natural variant2301R → K in RTD.

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.7

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 »

40344,726

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: 6324167] [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: 3530608] [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: 6391881] [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]"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.,