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P06281 (RENI1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 142. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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-1

EC=3.4.23.15
Alternative name(s):
Angiotensinogenase
Kidney renin
Gene names
Name:Ren1
Synonyms:Ren, Ren-1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length402 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, 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.

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.

Tissue specificity

Kidney.

Induction

Renal renin is synthesized by the juxtaglomerular cells of the kidney in response to decreased blood pressure and sodium concentration.

Polymorphism

In inbred mouse strains, there are at least two alleles which can occur at the Ren1 locus: Ren-1D and Ren-1C. The sequence shown is that of Ren-1C.

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.

Sequence similarities

Belongs to the peptidase A1 family.

Ontologies

Keywords
   Cellular componentMembrane
Secreted
   Coding sequence diversityPolymorphism
   DomainSignal
   Molecular functionAspartyl protease
Hydrolase
Protease
   PTMDisulfide bond
Glycoprotein
Zymogen
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processangiotensin maturation

Inferred from mutant phenotype PubMed 10617578. Source: MGI

beta-amyloid metabolic process

Inferred from electronic annotation. Source: Ensembl

cell maturation

Inferred from mutant phenotype PubMed 10617578. Source: MGI

cellular response to drug

Inferred from electronic annotation. Source: Ensembl

drinking behavior

Inferred from mutant phenotype PubMed 10617578. Source: MGI

hormone-mediated signaling pathway

Inferred from direct assay PubMed 14583438. Source: MGI

male gonad development

Inferred from expression pattern PubMed 11145610. Source: UniProtKB

mesonephros development

Inferred from expression pattern PubMed 11145610. Source: UniProtKB

regulation of MAPK cascade

Inferred from electronic annotation. Source: Ensembl

regulation of blood volume by renin-angiotensin

Inferred from mutant phenotype PubMed 10617578. Source: MGI

renin-angiotensin regulation of aldosterone production

Inferred from direct assay PubMed 19293336. Source: MGI

response to cAMP

Inferred from electronic annotation. Source: Ensembl

response to cGMP

Inferred from electronic annotation. Source: Ensembl

response to lipopolysaccharide

Inferred from electronic annotation. Source: Ensembl

response to organic substance

Inferred from direct assay PubMed 19293336. Source: MGI

   Cellular_componentextracellular space

Inferred from direct assay PubMed 10318840PubMed 19293336. Source: MGI

intracellular

Inferred from direct assay PubMed 19293336. Source: MGI

membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionaspartic-type endopeptidase activity

Inferred from electronic annotation. Source: UniProtKB-KW

endopeptidase activity

Inferred from direct assay PubMed 19293336. Source: MGI

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2121 Ref.8
Propeptide22 – 7150Activation peptide
PRO_0000026089
Chain72 – 402331Renin-1
PRO_0000026090

Sites

Active site1021 By similarity
Active site2871 By similarity

Amino acid modifications

Glycosylation691N-linked (GlcNAc...) Potential
Glycosylation1391N-linked (GlcNAc...) Potential
Glycosylation3201N-linked (GlcNAc...) Potential
Disulfide bond115 ↔ 122 By similarity
Disulfide bond278 ↔ 282 By similarity

Natural variations

Natural variant581W → R in allele Ren-1D.
Natural variant681T → I in allele Ren-1D.
Natural variant1601S → V in allele Ren-1D.
Natural variant3151E → D in allele Ren-1D. Ref.9
Natural variant3521N → Y in allele Ren-1D.

Experimental info

Sequence conflict6 – 2318Missing Ref.1
Sequence conflict241T → I Ref.1
Sequence conflict1631V → VSRV Ref.1

Sequences

Sequence LengthMass (Da)Tools
P06281 [UniParc].

Last modified January 1, 1988. Version 1.
Checksum: D42920B555E97A38

FASTA40244,343
        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 

« Hide

References

« Hide 'large scale' references
[1]"Evolution of aspartyl proteases by gene duplication: the mouse renin gene is organized in two homologous clusters of four exons."
Holm I., Ollo R., Panthier J.-J., Rougeon F.
EMBO J. 3:557-562(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: BALB/c.
[2]"Nucleotide sequence of a cDNA coding for mouse Ren1 preprorenin."
Kim W.S., Murakami K., Nakayama K.
Nucleic Acids Res. 17:9480-9480(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: BALB/c.
Tissue: Kidney.
[3]"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.
Strain: C57BL/10 and DBA/2.
[4]"The transcriptional landscape of the mammalian genome."
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. expand/collapse author list , 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.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Kidney.
[5]"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].
Tissue: Kidney.
[6]"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 1-30.
Tissue: Kidney.
[7]"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 [GENOMIC DNA] OF 1-31.
[8]"Biosynthesis of renin in mouse kidney tumor As4.1 cells."
Jones C.A., Petrovic N., Novak E.K., Swank R.T., Sigmund C.D., Gross K.W.
Eur. J. Biochem. 243:181-190(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 22-37 AND 72-80.
Strain: C57BL/10ROS X C3H/HEROS.
Tissue: Kidney.
[9]"Molecular cloning of two distinct renin genes from the DBA/2 mouse."
Mullins J.J., Burt D.W., Windass J.D., McTurk P., George H., Brammar W.J.
EMBO J. 1:1461-1466(1982) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE OF 269-316, VARIANT ASP-315.
Strain: DBA/2.
Tissue: Submandibular gland.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X00810 expand/collapse EMBL AC list , X00811, X00812, X00813, X00814, X00815, X00816, X00850, X00851 Genomic DNA. Translation: CAA25391.1.
X16642 mRNA. Translation: CAA34636.1.
K02596 Genomic DNA. Translation: AAA40045.1.
M32352 Genomic DNA. Translation: AAA40043.1.
AK052685 mRNA. Translation: BAC35094.1.
AK085309 mRNA. Translation: BAC39418.1.
BC061053 mRNA. Translation: AAH61053.1.
K02800 Genomic DNA. Translation: AAA40044.1.
M34190 Genomic DNA. Translation: AAA40042.1.
CCDSCCDS15295.1.
PIRREMSK. A00989.
RefSeqNP_112469.1. NM_031192.3.
UniGeneMm.220955.

3D structure databases

ProteinModelPortalP06281.
SMRP06281. Positions 28-402.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP06281. 1 interaction.
MINTMINT-4132153.

Chemistry

BindingDBP06281.
ChEMBLCHEMBL2615.

Protein family/group databases

MEROPSA01.007.

PTM databases

PhosphoSiteP06281.

Proteomic databases

MaxQBP06281.
PaxDbP06281.
PRIDEP06281.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000094556; ENSMUSP00000092135; ENSMUSG00000070645.
GeneID19701.
KEGGmmu:19701.
UCSCuc007cqf.1. mouse.

Organism-specific databases

CTD19701.
MGIMGI:97898. Ren1.

Phylogenomic databases

eggNOGNOG248684.
GeneTreeENSGT00710000106265.
HOGENOMHOG000197681.
HOVERGENHBG000482.
InParanoidP06281.
KOK01380.
OMAVVCEEGC.
OrthoDBEOG7HQN88.
PhylomeDBP06281.
TreeFamTF314990.

Gene expression databases

ArrayExpressP06281.
BgeeP06281.
CleanExMM_REN1.
GenevestigatorP06281.

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

NextBio297064.
PROP06281.
SOURCESearch...

Entry information

Entry nameRENI1_MOUSE
AccessionPrimary (citable) accession number: P06281
Secondary accession number(s): P97911 expand/collapse secondary AC list , Q543E5, Q62153, Q62154
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 1, 1988
Last modified: July 9, 2014
This is version 142 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

MGD cross-references

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