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Reviewed, UniProtKB/Swiss-Prot Q6DLW5 (RENI_MACMU)

Last modified September 1, 2009. Version 41. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · 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
OrganismMacaca mulatta (Rhesus macaque)
Taxonomic identifier9544 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniCercopithecidaeCercopithecinaeMacaca

Protein attributes

Sequence length406 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript 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 By similarity.

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 By similarity.

Subunit structure

Interacts with ATP6AP2 By similarity.

Subcellular location

Secreted By similarity. Membrane By similarity. Note: Associated to membranes via binding to ATP6AP2 By similarity.

Sequence similarities

Belongs to the peptidase A1 family.

Ontologies

Keywords
   Cellular componentMembrane
Secreted
   DomainSignal
   Molecular functionAspartyl protease
Hydrolase
Protease
   PTMCleavage on pair of basic residues
Disulfide bond
Glycoprotein
Zymogen
Gene Ontology (GO)
   Biological processproteolysis

Inferred from electronic annotation. Source: InterPro

   Cellular componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionaspartic-type endopeptidase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323 By similarity
Propeptide24 – 6643Activation peptide
PRO_0000026085
Chain67 – 406340Renin
PRO_0000026086

Sites

Active site1041 By similarity
Active site2921 By similarity

Amino acid modifications

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

Sequences

Sequence LengthMass (Da)Tools
Q6DLW5-1 [UniParc].

Last modified April 26, 2005. Version 2.
Checksum: BFAC82495AD57220

FASTA40644,961
        10         20         30         40         50         60 
MDGWRRMPRW GLLLLLWGSC TFGLPTDTTT FKRIFLKRMP SIRESLKERG VDMARLGPEW 

        70         80         90        100        110        120 
SQPMKRLALG 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 DNILSQGVLK EDVFSFYYNR DSENAQSLGG 

       250        260        270        280        290        300 
QIVLGGSDPQ HYEGNFHYIN LIKTGVWQIP MKGVSVGSST LLCEDGCLAL VDTGASYISG 

       310        320        330        340        350        360 
STSSIEKLME ALGAKKRLFD YVVKCNEGPT LPDISFHLGG KEYTLTSADY VFQESYSSKK 

       370        380        390        400 
LCTLAIHAMD IPPPTGPTWA LGATFIRKFY TEFDRRNNRI GFALAH 

« Hide

References

[1]"Cloning and biochemical characterization of the rhesus renin precursor protein."
Atkins C.L., Lucas B.J., Lewis S.D., Yuan J., Hershey J.C., Feuerstein G.Z.
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases

AY662332 mRNA. Translation: AAT74864.2.
RefSeqNP_001028088.1.
UniGeneMmu.3867

3D structure databases

SMRQ6DLW5. Positions 70-405.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ6DLW5.

Protein family/group databases

MEROPSA01.007.

Genome annotation databases

EnsemblENSMMUT00000011836; ENSMMUP00000011102; ENSMMUG00000008464; Macaca mulatta. [Genome view]
GeneID574299.
KEGGmcc:574299.

Organism-specific databases

CTD574299.

Phylogenomic databases

HOVERGENQ6DLW5.

Enzyme and pathway databases

BRENDA3.4.23.15. 1774.

Family and domain databases

InterProIPR001461. Peptidase_A1.
IPR001969. Peptidase_aspartic_AS.
IPR009007. Peptidase_aspartic_catalytic.
IPR012848. Propep_A1.
[Graphical view]
Gene3DG3DSA:2.40.70.10. Pept_Aspartc_cat. 1 hit.
PANTHERPTHR13683. Peptidase_A1. 1 hit.
PfamPF07966. A1_Propeptide. 1 hit.
PF00026. Asp. 1 hit.
[Graphical view]
PRINTSPR00792. PEPSIN.
PROSITEPS00141. ASP_PROTEASE. 2 hits.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameRENI_MACMU
AccessionPrimary (citable) accession number: Q6DLW5
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: April 26, 2005
Last modified: September 1, 2009
This is version 41 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents