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Q9TSZ1 (RENI_CALJA) Reviewed, UniProtKB/Swiss-Prot

Last modified December 11, 2013. Version 73. 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
OrganismCallithrix jacchus (White-tufted-ear marmoset) [Reference proteome]
Taxonomic identifier9483 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniPlatyrrhiniCebidaeCallitrichinaeCallithrix

Protein attributes

Sequence length400 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
   PTMDisulfide 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 – 6037Activation peptide
PRO_0000026077
Chain61 – 400340Renin
PRO_0000026078

Sites

Active site981 By similarity
Active site2861 By similarity

Amino acid modifications

Glycosylation651N-linked (GlcNAc...) Potential
Glycosylation1351N-linked (GlcNAc...) Potential
Disulfide bond111 ↔ 118 By similarity
Disulfide bond277 ↔ 281 By similarity
Disulfide bond319 ↔ 356 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9TSZ1 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 31769217035615FA

FASTA40044,038
        10         20         30         40         50         60 
MDAWRGMPRW GLLLLLWGSC TFGLPTETTT FKRISLKRMP SIRESLKERG VDMARLGPER 

        70         80         90        100        110        120 
MALVNITSSV ILTNYMDTQY YGEIGIGTPP QTFKVVFDTG SSNVWVPSSK CSRLYTACVY 

       130        140        150        160        170        180 
HKLFDASDSS SYKHNGTELT LRYSTGTVSG FLSQDVITVG GITVTQTFGE VTEMPALPFM 

       190        200        210        220        230        240 
LAEFDGVVGM GFSEQAIGKV TPLFDNIISQ GLLKEDVFSF YYNRDSENSQ SLGGQIVLGG 

       250        260        270        280        290        300 
SDPQHYEGNF HYINLIRTGL WQIPMKGVSV GSSTLLCEDG CLALVDTGAS YISGSTSSIE 

       310        320        330        340        350        360 
KLMEALGAKK RLFDYVVKCN EGPTLPDISF HLGGKEYTLT SADYVFQESY SSKKLCTLAI 

       370        380        390        400 
HAMDIPPPTG PTWALGATFI RKFYTEFDRG NNRIGFALAR 

« Hide

References

[1]"Cloning and characterization of marmoset renin: comparison with human renin."
Valdenaire O., Breu V., Giller T., Bur D., Fischli W.
J. Cardiovasc. Pharmacol. 34:893-897(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ132342 mRNA. Translation: CAB64879.1.
RefSeqXP_002760737.1. XM_002760691.1.

3D structure databases

ProteinModelPortalQ9TSZ1.
SMRQ9TSZ1. Positions 68-400.
ModBaseSearch...
MobiDBSearch...

Chemistry

ChEMBLCHEMBL6056.

Protein family/group databases

MEROPSA01.007.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSCJAT00000032861; ENSCJAP00000031097; ENSCJAG00000016857.
GeneID100399036.

Organism-specific databases

CTD5972.

Phylogenomic databases

GeneTreeENSGT00710000106265.
HOGENOMHOG000197681.
HOVERGENHBG000482.

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...

Entry information

Entry nameRENI_CALJA
AccessionPrimary (citable) accession number: Q9TSZ1
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: May 1, 2000
Last modified: December 11, 2013
This is version 73 of the entry and version 1 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