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UniProtKB/Swiss-Prot entry P00796


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name RENI2_MOUSE
Primary accession number P00796
Secondary accession numbers P70229 P97955 Q62155
Integrated into Swiss-Prot on July 21, 1986
Sequence was last modified on July 21, 1986 (Sequence version 1)
Annotations were last modified on    September 2, 2008 (Entry version 97)
Name and origin of the protein
Protein name Renin-2 [Precursor]
Synonyms EC 3.4.23.15
Angiotensinogenase
Submandibular gland renin
Contains Renin-2 heavy chain
Renin-2 light chain
Gene name
Name: Ren2
Synonyms: Ren-2
From
Mus musculus (Mouse) [TaxID: 10090] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae; Murinae; Mus.
Protein existence 1: Evidence at protein level;
References
[1]
PROTEIN SEQUENCE OF 64-351 AND 354-401.
PubMed=6812055 [NCBI, ExPASy, EBI, Israel, Japan]
Misono K.S., Chang J.-J., Inagami T.;
"Amino acid sequence of mouse submaxillary gland renin.";
Proc. Natl. Acad. Sci. U.S.A. 79:4858-4862(1982).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1038/298090a0; PubMed=6283373 [NCBI, ExPASy, EBI, Israel, Japan]
Panthier J.-J., Foote S., Chambraud B., Strosberg A.D., Corvol P., Rougeon F.;
"Complete amino acid sequence and maturation of the mouse submaxillary gland renin precursor.";
Nature 298:90-92(1982).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N;
TISSUE=Salivary gland;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-29.
PubMed=6089205 [NCBI, ExPASy, EBI, Israel, Japan]
Panthier J.-J., Dreyfus M., Roux D.T.L., Rougeon F.;
"Mouse kidney and submaxillary gland renin genes differ in their 5' putative regulatory sequences.";
Proc. Natl. Acad. Sci. U.S.A. 81:5489-5493(1984).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-30.
DOI=10.1016/0378-1119(89)90143-1; PubMed=2691339 [NCBI, ExPASy, EBI, Israel, Japan]
Burt D.W., Mullins L.J., George H., Smith G., Brooks J., Pioli D., Brammar W.J.;
"The nucleotide sequence of a mouse renin-encoding gene, Ren-1d, and its upstream region.";
Gene 84:91-104(1989).
[6]
NUCLEOTIDE SEQUENCE OF 1-30.
PubMed=6392850 [NCBI, ExPASy, EBI, Israel, Japan]
Field L.J., Philbrick W.M., Howles P.N., Dickinson D.P., McGowan R.A., Gross K.W.;
"Expression of tissue-specific Ren-1 and Ren-2 genes of mice: comparative analysis of 5'-proximal flanking regions.";
Mol. Cell. Biol. 4:2321-2331(1984).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 267-292.
PubMed=6357783 [NCBI, ExPASy, EBI, Israel, Japan]
Panthier J.J., Rougeon F.;
"Kidney and submaxillary gland renins are encoded by two non-allelic genes in Swiss mice.";
EMBO J. 2:675-678(1983).
[8]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
DOI=10.1038/357466a0; PubMed=1608447 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"X-ray analyses of peptide-inhibitor complexes define the structural basis of specificity for human and mouse renins.";
Nature 357:466-472(1992).
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: Dimer of a heavy chain and a light chain joined by a disulfide bond.
  • SUBCELLULAR LOCATION: Secreted.
  • TISSUE SPECIFICITY: Submandibular gland.
  • MISCELLANEOUS: The active enzyme isolated from the submandibular gland has catalytic and antigenic activities similar to renal renin.
  • SIMILARITY: Belongs to the peptidase A1 family [view classification].
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
J00621; AAA40050.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC011157; AAH11157.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
K02597; AAA40048.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M34191; AAA40046.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF237860; AAA40047.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A93923; REMSS.
I77411; I77411.
RefSeq NP_112470.2; -.
UniGene Mm.220955
3D structure databases
PDB
1SMR; X-ray; 2.00 A; B=-.[ExPASy / RCSB / EBI]
PDBsum 1SMR; -.
SMR P00796; 71-401.
ModBase P00796.
Protein family/group databases
MEROPS A01.008; -.
Enzyme and pathway databases
BioCyc MetaCyc:MON-12952; -.
Organism-specific databases
MGI MGI:97899; Ren2.
Gene expression databases
ArrayExpress P00796; -.
GermOnline ENSMUSG00000070645; Mus musculus.
Family and domain databases
InterPro IPR001969; Pept_Asp_AS.
IPR009007; Pept_Aspartc_cat.
IPR001461; Peptidase_A1.
IPR012848; Propep_A1.
Graphical view of domain structure.
Gene3D G3DSA:2.40.70.10; Pept_Aspartc_cat; 2.
PANTHER PTHR13683; Peptidase_A1; 1.
Pfam PF07966; A1_Propeptide; 1.
PF00026; Asp; 1.
Pfam graphical view of domain structure.
PRINTS PR00792; PEPSIN.
PROSITE PS00141; ASP_PROTEASE; 2.
BLOCKS P00796.
Genome annotation databases
Ensembl ENSMUSG00000070645; Mus musculus. [Contig view]
GeneID 19702; -.
KEGG mmu:19702; -.
Phylogenomic databases
HOVERGEN P00796; -.
Other
LinkHub P00796; -.
SOURCE Ren2; Mus musculus.
ProtoNet P00796.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Aspartyl protease; Cleavage on pair of basic residues; Direct protein sequencing; Hydrolase; Protease; Secreted; Signal; Zymogen.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
SIGNAL   1    25  25     Probable. 
PROPEP   26    63  38     Activation peptide. PRO_0000026095
CHAIN   64   401  338     Renin-2. PRO_0000026096
CHAIN   64   351  288     Renin-2 heavy chain. PRO_0000026097
CHAIN   354   401  48     Renin-2 light chain. PRO_0000026098
ACT_SITE   101   101         
ACT_SITE   286   286         
DISULFID   114   121         
DISULFID   277   281         
DISULFID   320   357         
CONFLICT   13    13        L -> W (in Ref. 5; AAA40047). 
CONFLICT   99    99        I -> M (in Ref. 2; AAA40050). 
CONFLICT   195   198        FPAQ -> LSRS (in Ref. 2; AAA40050). 
CONFLICT   395   395        I -> V (in Ref. 2; AAA40050). 
STRAND   69    69  1      
STRAND   71    78  8      
TURN   79    81  3      
STRAND   82    89  8      
TURN   90    93  4      
STRAND   94   101  8      
TURN   102   103  2      
STRAND   107   111  5      
TURN   112   113  2      
TURN   116   117  2      
HELIX   119   123  5      
STRAND   127   127  1      
HELIX   129   131  3      
TURN   133   134  2      
STRAND   136   146  11      
TURN   147   148  2      
STRAND   149   162  14      
TURN   163   164  2      
STRAND   165   176  12      
HELIX   179   182  4      
TURN   183   184  2      
STRAND   189   192  4      
HELIX   196   198  3      
HELIX   200   202  3      
HELIX   206   212  7      
TURN   213   214  2      
STRAND   216   216  1      
STRAND   220   225  6      
STRAND   234   238  5      
HELIX   243   245  3      
STRAND   246   254  9      
STRAND   257   257  1      
TURN   258   261  4      
STRAND   262   270  9      
TURN   271   272  2      
STRAND   276   276  1      
TURN   278   279  2      
STRAND   281   285  5      
TURN   287   288  2      
STRAND   289   289  1      
STRAND   292   294  3      
HELIX   296   306  11      
TURN   307   307  1      
STRAND   309   312  4      
TURN   313   314  2      
STRAND   315   319  5      
HELIX   320   325  6      
STRAND   329   333  5      
TURN   334   335  2      
STRAND   336   340  5      
HELIX   342   345  4      
STRAND   346   346  1      
TURN   347   348  2      
STRAND   356   359  4      
STRAND   361   363  3      
TURN   368   370  3      
STRAND   374   376  3      
HELIX   378   381  4      
TURN   382   383  2      
STRAND   384   389  6      
TURN   390   393  4      
STRAND   394   401  8      
Sequence information
Length: 401 AA [This is the length of the unprocessed precursor] Molecular weight: 44283 Da [This is the MW of the unprocessed precursor] CRC64: D938931F91F82980 [This is a checksum on the sequence]
        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 

P00796 in FASTA format

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