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Q6DLW5 (RENI_MACMU) Reviewed, UniProtKB/Swiss-Prot

Last modified December 11, 2013. Version 69. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·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
OrganismMacaca mulatta (Rhesus macaque) [Reference proteome]
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
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processproteolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   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 [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

EMBL
GenBank
DDBJ
AY662332 mRNA. Translation: AAT74864.2.
RefSeqNP_001028088.1. NM_001032916.1.
UniGeneMmu.3867.

3D structure databases

ProteinModelPortalQ6DLW5.
SMRQ6DLW5. Positions 69-405.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9544.ENSMMUP00000011102.

Chemistry

BindingDBQ6DLW5.
ChEMBLCHEMBL1287631.

Protein family/group databases

MEROPSA01.007.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID574299.
KEGGmcc:574299.

Organism-specific databases

CTD5972.

Phylogenomic databases

eggNOGNOG248684.
HOGENOMHOG000197681.
HOVERGENHBG000482.
InParanoidQ6DLW5.
KOK01380.

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

NextBio19975645.

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: December 11, 2013
This is version 69 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries