[1]	NUCLEOTIDE SEQUENCE [MRNA]. Atkins C.L., Lucas B.J., Lewis S.D., Yuan J., Hershey J.C., Feuerstein G.Z.; "Cloning and biochemical characterization of the rhesus renin precursor protein."; Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.

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 (By similarity).
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

AY662332; AAT74864.2; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_001028088.1; -.

UniGene

Mmu.3867

3D structure databases

SMR

Q6DLW5; 70-405.

ModBase

Q6DLW5.

Protein family/group databases

MEROPS

A01.007; -.

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.

BLOCKS

Q6DLW5.

Genome annotation databases

Ensembl

ENSMMUG00000008464; Macaca mulatta. [Contig view]

GeneID

574299; -.

KEGG

mcc:574299; -.

Phylogenomic databases

HOVERGEN

Q6DLW5; -.

Other

ProtoNet

Q6DLW5.

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 23`	`23`	`By similarity.`
`PROPEP`	`24 66`	`43`	`Activation peptide.`	`PRO_0000026085`
`CHAIN`	`67 406`	`340`	`Renin.`	`PRO_0000026086`
`ACT_SITE`	`104 104`		`By similarity.`
`ACT_SITE`	`292 292`		`By similarity.`
`CARBOHYD`	`71 71`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`141 141`		`N-linked (GlcNAc...) (Potential).`
`DISULFID`	`117 124`		`By similarity.`
`DISULFID`	`283 287`		`By similarity.`
`DISULFID`	`325 362`		`By similarity.`

Sequence information

Length: 406 AA [This is the length of the unprocessed precursor]

Molecular weight: 44961 Da [This is the MW of the unprocessed precursor]

CRC64: BFAC82495AD57220 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MDGWRRMPRW GLLLLLWGSC TFGLPTDTTT FKRIFLKRMP SIRESLKERG VDMARLGPEW 

        70         80         90        100        110        120 
SQPMKRLALG NTTSSVILTN YMDTQYYGEI GIGTPPQTFK VVFDTGSSNV WVPSSKCSRL 

       130        140        150        160        170        180 
YTACVYHKLF DASDSSSYKH NGTELTLRYS TGTVSGFLSQ DIITVGGITV TQMFGEVTEM 

       190        200        210        220        230        240 
PALPFMLAEF DGVVGMGFIE QAIGRVTPIF DNILSQGVLK EDVFSFYYNR DSENAQSLGG 

       250        260        270        280        290        300 
QIVLGGSDPQ HYEGNFHYIN LIKTGVWQIP MKGVSVGSST LLCEDGCLAL VDTGASYISG 

       310        320        330        340        350        360 
STSSIEKLME ALGAKKRLFD YVVKCNEGPT LPDISFHLGG KEYTLTSADY VFQESYSSKK 

       370        380        390        400 
LCTLAIHAMD IPPPTGPTWA LGATFIRKFY TEFDRRNNRI GFALAH

Q6DLW5 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