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UniProtKB/Swiss-Prot entry P06281


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

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Entry information
Entry name RENI1_MOUSE
Primary accession number P06281
Secondary accession numbers P97911 Q543E5 Q62153 Q62154
Integrated into Swiss-Prot on January 1, 1988
Sequence was last modified on January 1, 1988 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 93)
Name and origin of the protein
Protein name Renin-1 [Precursor]
Synonyms EC 3.4.23.15
Angiotensinogenase
Kidney renin
Gene name
Name: Ren1
Synonyms: Ren, Ren-1
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]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=BALB/c;
PubMed=6370686 [NCBI, ExPASy, EBI, Israel, Japan]
Holm I., Ollo R., Panthier J.-J., Rougeon F.;
"Evolution of aspartyl proteases by gene duplication: the mouse renin gene is organized in two homologous clusters of four exons.";
EMBO J. 3:557-562(1984).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=BALB/c;
TISSUE=Kidney;
DOI=10.1093/nar/17.22.9279; PubMed=2685761 [NCBI, ExPASy, EBI, Israel, Japan]
Kim W.S., Murakami K., Nakayama K.;
"Nucleotide sequence of a cDNA coding for mouse Ren1 preprorenin.";
Nucleic Acids Res. 17:9480-9480(1989).
[3]
NUCLEOTIDE SEQUENCE.
STRAIN=C57BL/10, and DBA/2;
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).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J;
TISSUE=Kidney;
DOI=10.1126/science.1112014; PubMed=16141072 [NCBI, ExPASy, EBI, Israel, Japan]
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J., Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Kidney;
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).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-30.
TISSUE=Kidney;
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).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-31.
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).
[8]
PROTEIN SEQUENCE OF 22-37 AND 72-80.
STRAIN=C57BL/10ROS X C3H/HEROS;
TISSUE=Kidney;
PubMed=9030738 [NCBI, ExPASy, EBI, Israel, Japan]
Jones C.A., Petrovic N., Novak E.K., Swank R.T., Sigmund C.D., Gross K.W.;
"Biosynthesis of renin in mouse kidney tumor As4.1 cells.";
Eur. J. Biochem. 243:181-190(1997).
[9]
NUCLEOTIDE SEQUENCE OF 269-316, AND VARIANT ASP-315.
STRAIN=DBA/2;
TISSUE=Submandibular gland;
PubMed=6327270 [NCBI, ExPASy, EBI, Israel, Japan]
Mullins J.J., Burt D.W., Windass J.D., McTurk P., George H., Brammar W.J.;
"Molecular cloning of two distinct renin genes from the DBA/2 mouse.";
EMBO J. 1:1461-1466(1982).
Comments
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
X00810; CAA25391.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X00811; CAA25391.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X00812; CAA25391.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X00813; CAA25391.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X00814; CAA25391.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X00815; CAA25391.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X00816; CAA25391.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X00850; CAA25391.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X00851; CAA25391.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X16642; CAA34636.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
K02596; AAA40045.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M32352; AAA40043.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK052685; BAC35094.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK085309; BAC39418.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC061053; AAH61053.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
K02800; AAA40044.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M34190; AAA40042.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A00989; REMSK.
RefSeq NP_112469.1; -.
UniGene Mm.220955
3D structure databases
HSSP P00796; 1SMR. [HSSP ENTRY / PDB]
SMR P06281; 69-402.
ModBase P06281.
Protein family/group databases
MEROPS A01.007; -.
Organism-specific databases
MGI MGI:97898; Ren1.
Gene expression databases
ArrayExpress P06281; -.
CleanEx MM_REN1; -.
GermOnline ENSMUSG00000070645; Mus musculus.
Ontologies
GO
GO:0005615; Cellular component: extracellular space (inferred from direct assay from MGI).
GO:0002003; Biological process: angiotensin maturation (inferred from mutant phenotype from MGI).
GO:0048469; Biological process: cell maturation (inferred from mutant phenotype from MGI).
GO:0042756; Biological process: drinking behavior (inferred from mutant phenotype from MGI).
GO:0009755; Biological process: hormone-mediated signaling (inferred from direct assay from MGI).
GO:0002016; Biological process: regulation of blood volume by renin-angiotensin (inferred from mutant phenotype from MGI).
QuickGo view.
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 P06281.
Genome annotation databases
Ensembl ENSMUSG00000070645; Mus musculus. [Contig view]
GeneID 19701; -.
KEGG mmu:19701; -.
Phylogenomic databases
HOGENOM P06281; -.
HOVERGEN P06281; -.
Other
SOURCE Ren1; Mus musculus.
ProtoNet P06281.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Aspartyl protease; Direct protein sequencing; Glycoprotein; Hydrolase; Membrane; Polymorphism; Protease; Secreted; Signal; Zymogen.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
SIGNAL   1    21  21      
PROPEP   22    71  50     Activation peptide. PRO_0000026089
CHAIN   72   402  331     Renin-1. PRO_0000026090
ACT_SITE   102   102        By similarity. 
ACT_SITE   287   287        By similarity. 
CARBOHYD   69    69        N-linked (GlcNAc...) (Potential). 
CARBOHYD   139   139        N-linked (GlcNAc...) (Potential). 
CARBOHYD   320   320        N-linked (GlcNAc...) (Potential). 
DISULFID   115   122        By similarity. 
DISULFID   278   282        By similarity. 
VARIANT   58    58  1     W -> R (in allele Ren-1D). 
VARIANT   68    68  1     T -> I (in allele Ren-1D). 
VARIANT   160   160  1     S -> V (in allele Ren-1D). 
VARIANT   315   315  1     E -> D (in allele Ren-1D). 
VARIANT   352   352  1     N -> Y (in allele Ren-1D). 
CONFLICT   6    23        Missing (in Ref. 1). 
CONFLICT   24    24        T -> I (in Ref. 1). 
CONFLICT   163   163        V -> VSRV (in Ref. 1). 
Sequence information
Length: 402 AA [This is the length of the unprocessed precursor] Molecular weight: 44343 Da [This is the MW of the unprocessed precursor] CRC64: D42920B555E97A38 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MDRRRMPLWA LLLLWSPCTF SLPTRTATFE RIPLKKMPSV REILEERGVD MTRLSAEWGV 

        70         80         90        100        110        120 
FTKRPSLTNL TSPVVLTNYL NTQYYGEIGI GTPPQTFKVI FDTGSANLWV PSTKCSRLYL 

       130        140        150        160        170        180 
ACGIHSLYES SDSSSYMENG SDFTIHYGSG RVKGFLSQDS VTVGGITVTQ TFGEVTELPL 

       190        200        210        220        230        240 
IPFMLAKFDG VLGMGFPAQA VGGVTPVFDH ILSQGVLKEE VFSVYYNRGS HLLGGEVVLG 

       250        260        270        280        290        300 
GSDPQHYQGN FHYVSISKTD SWQITMKGVS VGSSTLLCEE GCAVVVDTGS SFISAPTSSL 

       310        320        330        340        350        360 
KLIMQALGAK EKRIEEYVVN CSQVPTLPDI SFDLGGRAYT LSSTDYVLQY PNRRDKLCTL 

       370        380        390        400 
ALHAMDIPPP TGPVWVLGAT FIRKFYTEFD RHNNRIGFAL AR 

P06281 in FASTA format

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