P06281 (RENI1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Renin-1
EC=3.4.23.15

Alternative name(s):
Angiotensinogenase
Kidney renin

Gene names

Name:	Ren1
Synonyms:	Ren, Ren-1

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	402 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 component	Membrane Secreted
Coding sequence diversity	Polymorphism
Domain	Signal
Molecular function	Aspartyl protease Hydrolase Protease
PTM	Disulfide bond Glycoprotein Zymogen
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	angiotensin maturation Inferred from mutant phenotype PubMed 10617578. Source: MGI beta-amyloid metabolic process Inferred from electronic annotation. Source: Compara cell maturation Inferred from mutant phenotype PubMed 10617578. Source: MGI cellular response to drug Inferred from electronic annotation. Source: Compara 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 proteolysis Inferred from electronic annotation. Source: UniProtKB-KW regulation of MAPK cascade Inferred from electronic annotation. Source: Compara renin-angiotensin regulation of aldosterone production Inferred from direct assay PubMed 19293336. Source: MGI response to cAMP Inferred from electronic annotation. Source: Compara response to cGMP Inferred from electronic annotation. Source: Compara response to lipopolysaccharide Inferred from electronic annotation. Source: Compara response to stress Inferred from electronic annotation. Source: Compara
Cellular_component	cytoplasmic part Inferred from electronic annotation. Source: Compara extracellular 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_function	aspartic-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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 21	21	Ref.8
	Propeptide	22 – 71	50	Activation peptide		PRO_0000026089
	Chain	72 – 402	331	Renin-1		PRO_0000026090
Sites
	Active site	102	1	By similarity
	Active site	287	1	By similarity
Amino acid modifications
	Glycosylation	69	1	N-linked (GlcNAc...) Potential
	Glycosylation	139	1	N-linked (GlcNAc...) Potential
	Glycosylation	320	1	N-linked (GlcNAc...) Potential
	Disulfide bond	115 ↔ 122		By similarity
	Disulfide bond	278 ↔ 282		By similarity
Natural variations
	Natural variant	58	1	W → R in allele Ren-1D.
	Natural variant	68	1	T → I in allele Ren-1D.
	Natural variant	160	1	S → V in allele Ren-1D.
	Natural variant	315	1	E → D in allele Ren-1D. Ref.9
	Natural variant	352	1	N → Y in allele Ren-1D.
Experimental info
	Sequence conflict	6 – 23	18	Missing Ref.1
	Sequence conflict	24	1	T → I Ref.1
	Sequence conflict	163	1	V → VSRV Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P06281 [UniParc]. Last modified January 1, 1988. Version 1. Checksum: D42920B555E97A38	FASTA	402	44,343
	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

References

	« Hide 'large scale' referencesShow '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. , 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 , 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.
IPI	IPI00121828.
PIR	REMSK. A00989.
RefSeq	NP_112469.1. NM_031192.3.
UniGene	Mm.220955.
3D structure databases
ProteinModelPortal	P06281.
SMR	P06281. Positions 28-64, 68-402.
ModBase	Search...
Protein family/group databases
MEROPS	A01.007.
PTM databases
PhosphoSite	P06281.
Proteomic databases
PaxDb	P06281.
PRIDE	P06281.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000094556; ENSMUSP00000092135; ENSMUSG00000070645.
GeneID	19701.
KEGG	mmu:19701.
Organism-specific databases
CTD	19701.
MGI	MGI:97898. Ren1.
Phylogenomic databases
eggNOG	NOG248684.
GeneTree	ENSGT00700000104424.
HOGENOM	HOG000197681.
HOVERGEN	HBG000482.
InParanoid	P06281.
KO	K01380.
OMA	DPQHYQG.
OrthoDB	EOG4W3SN8.
Gene expression databases
ArrayExpress	P06281.
Bgee	P06281.
CleanEx	MM_REN1.
Genevestigator	P06281.
GermOnline	ENSMUSG00000070645. Mus musculus.
Family and domain databases
Gene3D	2.40.70.10. 2 hits.
InterPro	IPR001461. Peptidase_A1. IPR021109. Peptidase_aspartic. IPR001969. Peptidase_aspartic_AS. IPR012848. Propep_A1. [Graphical view]
PANTHER	PTHR13683. PTHR13683. 1 hit.
Pfam	PF07966. A1_Propeptide. 1 hit. PF00026. Asp. 1 hit. [Graphical view]
PRINTS	PR00792. PEPSIN.
SUPFAM	SSF50630. Pept_Aspartic. 1 hit.
PROSITE	PS00141. ASP_PROTEASE. 2 hits. [Graphical view]
ProtoNet	Search...
Other
BindingDB	P06281.
ChEMBL	CHEMBL2615.
NextBio	297064.
SOURCE	Search...

Entry information

Entry name

RENI1_MOUSE

Accession

Primary (citable) accession number: P06281
Secondary accession number(s): P97911 , Q543E5, Q62153, Q62154

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1988
Last sequence update:	January 1, 1988
Last modified:	April 3, 2013
This is version 132 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program