[1]	NUCLEOTIDE SEQUENCE [MRNA]. STRAIN=Sprague-Dawley; DOI=10.1093/nar/16.8.3576; PubMed=3287330 [NCBI, ExPASy, EBI, Israel, Japan] Tada M., Fukamizu A., Seo M.S., Takahashi S., Murakami K.; "Nucleotide sequence of rat renin cDNA."; Nucleic Acids Res. 16:3576-3576(1988).
[2]	NUCLEOTIDE SEQUENCE [MRNA]. PubMed=3039496 [NCBI, ExPASy, EBI, Israel, Japan] Burnham C.E., Hawelu-Johnson C.L., Frank B.M., Lynch K.R.; "Molecular cloning of rat renin cDNA and its gene."; Proc. Natl. Acad. Sci. U.S.A. 84:5605-5609(1987).
[3]	NUCLEOTIDE SEQUENCE. STRAIN=Sprague-Dawley; DOI=10.1016/0022-2836(88)90151-9; PubMed=3047403 [NCBI, ExPASy, EBI, Israel, Japan] Fukamizu A., Nishi K., Cho T., Saitoh M., Nakayama K., Ohkubo H., Nakanishi S., Murakami K.; "Structure of the rat renin gene."; J. Mol. Biol. 201:443-450(1988).
[4]	NUCLEOTIDE SEQUENCE. PubMed=8490598 [NCBI, ExPASy, EBI, Israel, Japan] Alam K.Y., Wang Y., Dene H., Rapp J.P.; "Renin gene nucleotide sequence of coding and regulatory regions in Dahl rats."; Clin. Exp. Hypertens. 15:599-614(1993).
[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).

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: Interacts with ATP6AP2 (By similarity).
SUBCELLULAR LOCATION: Secreted (By similarity). Membrane (By similarity). Note=Associated to membranes via binding to ATP6AP2 (By similarity).
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

X07033; CAA30082.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
J02941; AAA42030.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M37278; AAA42031.1; ALT_SEQ; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
S60054; AAP13916.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC078878; AAH78878.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

A29991; RERTK.

NP_036774.4; -.

3D structure databases

HSSP

P00796; 1SMR. [HSSP ENTRY / PDB]

ModBase

P08424.

Protein family/group databases

MEROPS

A01.007; -.

Organism-specific databases

RGD

3554; Ren1.

Gene expression databases

ArrayExpress

P08424; -.

GermOnline

ENSRNOG00000002937; Rattus norvegicus.

Ontologies

GO:0016020;	Cellular component: membrane (inferred from electronic annotation from UniProtKB-KW).
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; 1.

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.

Genome annotation databases

Ensembl

ENSRNOG00000002937; Rattus norvegicus. [Contig view]

GeneID

24715; -.

KEGG

rno:24715; -.

Phylogenomic databases

HOVERGEN

P08424; -.

Other

NextBio

604209; -.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Aspartyl protease; Cleavage on pair of basic residues; Glycoprotein; Hydrolase; Membrane; Protease; Secreted; Signal; Zymogen.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 26`	`26`	`Probable.`
`PROPEP`	`27 64`	`38`	`Activation peptide.`	`PRO_0000026091`
`CHAIN`	`65 402`	`338`	`Renin.`	`PRO_0000026092`
`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.`
`CONFLICT`	`200 200`		`A -> V (in Ref. 1; CAA30082).`
`CONFLICT`	`214 215`		`QR -> HE (in Ref. 2; AAA42030).`
`CONFLICT`	`271 271`		`V -> L (in Ref. 1; CAA30082).`

Sequence information

Length: 402 AA [This is the length of the unprocessed precursor]

Molecular weight: 44276 Da [This is the MW of the unprocessed precursor]

CRC64: E4E22CEE449EAC3F [This is a checksum on the sequence]

        10         20         30         40         50         60 
MGGRRMPLWA LLLLWTSCSF SLPTDTASFG RILLKKMPSV REILEERGVD MTRISAEWGE 

        70         80         90        100        110        120 
FIKKSSFTNV TSPVVLTNYL DTQYYGEIGI GTPSQTFKVI FDTGSANLWV PSTKCGPLYT 

       130        140        150        160        170        180 
ACEIHNLYDS SESSSYMENG TEFTIHYGSG KVKGFLSQDV VTVGGIIVTQ TFGEVTELPL 

       190        200        210        220        230        240 
IPFMLAKFDG VLGMGFPAQA VDGVIPVFDH ILSQRVLKEE VFSVYYSRES HLLGGEVVLG 

       250        260        270        280        290        300 
GSDPQHYQGN FHYVSISKAG SWQITMKGVS VGPATLLCEE GCMAVVDTGT SYISGPTSSL 

       310        320        330        340        350        360 
QLIMQALGVK EKRANNYVVN CSQVPTLPDI SFYLGGRTYT LSNMDYVQKN PFRNDDLCIL 

       370        380        390        400 
ALQGLDIPPP TGPVWVLGAT FIRKFYTEFD RHNNRIGFAL AR

P08424 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools