Reviewed, UniProtKB/Swiss-Prot P06281 (RENI1_MOUSE)

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)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › 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.
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	Direct protein sequencing
Gene Ontology (GO)
Biological process	angiotensin maturation Inferred from mutant phenotype. Source: MGI cell maturation Inferred from mutant phenotype. Source: MGI drinking behavior Inferred from mutant phenotype. Source: MGI hormone-mediated signaling Inferred from direct assay. Source: MGI proteolysis Inferred from electronic annotation. Source: InterPro regulation of blood volume by renin-angiotensin Inferred from mutant phenotype. Source: MGI
Cellular component	extracellular space Inferred from direct assay. Source: MGI membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	aspartic-type endopeptidase activity Inferred from electronic annotation. Source: UniProtKB-KW
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)
	P06281-1 [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: 6370686] [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: 2685761] [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: 2691339] [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: 16141072] [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: 15489334] [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: 6089205] [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: 6392850] [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: 9030738] [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: 6327270] [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
EMBLGenBankDDBJ	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.
UniGene	Mm.220955
3D structure databases
HSSP	HSSP built from PDB template 1SMR based on UniProtKB P00796.
SMR	P06281. Positions 69-402.
ModBase	Search...
Protein family/group databases
MEROPS	A01.007.
Proteomic databases
PRIDE	P06281.
Genome annotation databases
Ensembl	ENSMUSG00000070645. Mus musculus. [Contig view]
GeneID	19701.
KEGG	mmu:19701.
Organism-specific databases
MGI	MGI:97898. Ren1.
Phylogenomic databases
HOGENOM	P06281.
HOVERGEN	P06281.
Enzyme and pathway databases
BRENDA	3.4.23.15. 244.
Gene expression databases
ArrayExpress	P06281.
Bgee	P06281.
CleanEx	MM_REN1.
GermOnline	ENSMUSG00000070645. Mus musculus.
Family and domain databases
InterPro	IPR001461. Peptidase_A1. IPR001969. Peptidase_aspartic_AS. IPR009007. Peptidase_aspartic_catalytic. IPR012848. Propep_A1. [Graphical view]
Gene3D	G3DSA:2.40.70.10. Pept_Aspartc_cat. 2 hits.
PANTHER	PTHR13683. Peptidase_A1. 1 hit.
Pfam	PF07966. A1_Propeptide. 1 hit. PF00026. Asp. 1 hit. [Graphical view]
PRINTS	PR00792. PEPSIN.
PROSITE	PS00141. ASP_PROTEASE. 2 hits. [Graphical view]
ProtoNet	Search...
Other Resources
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:	June 16, 2009
This is version 101 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)