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P00796 (RENI2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified January 22, 2014. Version 138. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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-2

EC=3.4.23.15
Alternative name(s):
Angiotensinogenase
Submandibular gland renin

Cleaved into the following 2 chains:

  1. Renin-2 heavy chain
  2. Renin-2 light chain
Gene names
Name:Ren2
Synonyms:Ren-2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length401 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, related to pepsin, 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. Its function in the salivary gland is not understood.

Catalytic activity

Cleavage of Leu-|-Xaa bond in angiotensinogen to generate angiotensin I.

Subunit structure

Dimer of a heavy chain and a light chain joined by a disulfide bond.

Subcellular location

Secreted.

Tissue specificity

Submandibular gland.

Polymorphism

Present as a single-copy gene in strains such as BALB/c and C57BL/6 while some strains such as Swiss and Akr contain two copies.

Miscellaneous

The active enzyme isolated from the submandibular gland has catalytic and antigenic activities similar to renal renin.

Sequence similarities

Belongs to the peptidase A1 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2525 Probable
Propeptide26 – 6338Activation peptide
PRO_0000026095
Chain64 – 401338Renin-2
PRO_0000026096
Chain64 – 351288Renin-2 heavy chain
PRO_0000026097
Chain354 – 40148Renin-2 light chain
PRO_0000026098

Sites

Active site1011
Active site2861

Amino acid modifications

Disulfide bond114 ↔ 121
Disulfide bond277 ↔ 281
Disulfide bond320 ↔ 357

Experimental info

Sequence conflict131L → W in AAA40047. Ref.5
Sequence conflict991I → M in AAA40050. Ref.2
Sequence conflict195 – 1984FPAQ → LSRS in AAA40050. Ref.2
Sequence conflict3951I → V in AAA40050. Ref.2

Secondary structure

...................................................................... 401
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P00796 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: D938931F91F82980

FASTA40144,283
        10         20         30         40         50         60 
MDRRRMPLWA LLLLWSPCTF SLPTGTTFER IPLKKMPSVR EILEERGVDM TRLSAEWDVF 

        70         80         90        100        110        120 
TKRSSLTDLI SPVVLTNYLN SQYYGEIGIG TPPQTFKVIF DTGSANLWVP STKCSRLYLA 

       130        140        150        160        170        180 
CGIHSLYESS DSSSYMENGD DFTIHYGSGR VKGFLSQDSV TVGGITVTQT FGEVTELPLI 

       190        200        210        220        230        240 
PFMLAQFDGV LGMGFPAQAV GGVTPVFDHI LSQGVLKEKV FSVYYNRGPH LLGGEVVLGG 

       250        260        270        280        290        300 
SDPEHYQGDF HYVSLSKTDS WQITMKGVSV GSSTLLCEEG CEVVVDTGSS FISAPTSSLK 

       310        320        330        340        350        360 
LIMQALGAKE KRLHEYVVSC SQVPTLPDIS FNLGGRAYTL SSTDYVLQYP NRRDKLCTVA 

       370        380        390        400 
LHAMDIPPPT GPVWVLGATF IRKFYTEFDR HNNRIGFALA R 

« Hide

References

« Hide 'large scale' references
[1]"Amino acid sequence of mouse submaxillary gland renin."
Misono K.S., Chang J.-J., Inagami T.
Proc. Natl. Acad. Sci. U.S.A. 79:4858-4862(1982) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 64-351 AND 354-401.
[2]"Complete amino acid sequence and maturation of the mouse submaxillary gland renin precursor."
Panthier J.-J., Foote S., Chambraud B., Strosberg A.D., Corvol P., Rougeon F.
Nature 298:90-92(1982) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"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].
Strain: FVB/N.
Tissue: Salivary gland.
[4]"Mouse kidney and submaxillary gland renin genes differ in their 5' putative regulatory sequences."
Panthier J.-J., Dreyfus M., Roux D.T.L., Rougeon F.
Proc. Natl. Acad. Sci. U.S.A. 81:5489-5493(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-29.
[5]"The nucleotide sequence of a mouse renin-encoding gene, Ren-1d, and its upstream region."
Burt D.W., Mullins L.J., George H., Smith G., Brooks J., Pioli D., Brammar W.J.
Gene 84:91-104(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-30.
[6]"Expression of tissue-specific Ren-1 and Ren-2 genes of mice: comparative analysis of 5'-proximal flanking regions."
Field L.J., Philbrick W.M., Howles P.N., Dickinson D.P., McGowan R.A., Gross K.W.
Mol. Cell. Biol. 4:2321-2331(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE OF 1-30.
[7]"Kidney and submaxillary gland renins are encoded by two non-allelic genes in Swiss mice."
Panthier J.J., Rougeon F.
EMBO J. 2:675-678(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 267-292.
[8]"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 (1.9 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J00621 mRNA. Translation: AAA40050.1.
BC011157 mRNA. Translation: AAH11157.1.
K02597 Genomic DNA. Translation: AAA40048.1.
M34191 Genomic DNA. Translation: AAA40046.1.
AF237860 Genomic DNA. Translation: AAA40047.1.
PIRREMSS. A93923.
I77411.
RefSeqNP_112470.2. NM_031193.2.
UniGeneMm.220955.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1SMRX-ray2.00A/C/E/G67-401[»]
ProteinModelPortalP00796.
SMRP00796. Positions 26-401.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSA01.008.

Proteomic databases

PRIDEP00796.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID19702.
KEGGmmu:19702.

Organism-specific databases

CTD19702.
MGIMGI:97899. Ren2.

Phylogenomic databases

HOVERGENHBG000482.
InParanoidP00796.
KOK01380.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-12952.

Gene expression databases

GenevestigatorP00796.

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

EvolutionaryTraceP00796.
NextBio297070.
PMAP-CutDBP00796.
PROP00796.
SOURCESearch...

Entry information

Entry nameRENI2_MOUSE
AccessionPrimary (citable) accession number: P00796
Secondary accession number(s): P70229, P97955, Q62155
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: January 22, 2014
This is version 138 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot