[1]	NUCLEOTIDE SEQUENCE [MRNA]. Zecher M., Wu Z., Scott B., McGeehan G., Harrison R.; "The cloning and characterization of canine renin."; Submitted (MAY-2004) 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

AY630442; AAT68959.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_001003194.1; -.

UniGene

Cfa.3701

3D structure databases

SMR

Q6DYE7; 69-403.

ModBase

Q6DYE7.

Protein family/group databases

MEROPS

A01.007; -.

Ontologies

GO:0004195;	Molecular function: renin activity (inferred from electronic annotation from EC).
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; 2.

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

Q6DYE7.

Genome annotation databases

Ensembl

ENSCAFG00000009623; Canis familiaris. [Contig view]

GeneID

403838; -.

KEGG

cfa:403838; -.

Phylogenomic databases

HOVERGEN

Q6DYE7; -.

Other

ProtoNet

Q6DYE7.

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 22`	`22`	`Potential.`
`PROPEP`	`23 65`	`43`	`Activation peptide (By similarity).`	`PRO_0000026079`
`CHAIN`	`66 403`	`338`	`Renin.`	`PRO_0000026080`
`ACT_SITE`	`103 103`		`By similarity.`
`ACT_SITE`	`288 288`		`By similarity.`
`CARBOHYD`	`70 70`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`140 140`		`N-linked (GlcNAc...) (Potential).`
`DISULFID`	`116 123`		`By similarity.`
`DISULFID`	`279 283`		`By similarity.`
`DISULFID`	`322 359`		`By similarity.`

Sequence information

Length: 403 AA [This is the length of the unprocessed precursor]

Molecular weight: 44099 Da [This is the MW of the unprocessed precursor]

CRC64: B63101337155AE44 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MARCRMPRWG LLLVLWGSCT FGLPADTGAF RRIFLKKMPS IRESLKERGV DVAGLGAEWN 

        70         80         90        100        110        120 
QFTKRLSSGN STSPVVLTNY LDTQYYGEIG IGTPPQTFKV VFDTGSANLW VPSTRCSPLY 

       130        140        150        160        170        180 
TACEIHCLYD SSESSSYMEN GTTFTIRYGS GKVKGFLSQD MVTVGGITVT QTFGEVTELP 

       190        200        210        220        230        240 
LIPFMLAKFD GVLGMGFPAQ AVGGVTPVFD HILSQGVLKE EVFSVYYSRN SHLLGGEVVL 

       250        260        270        280        290        300 
GGSDPQYYQG NFHYVSISKT GSWQIKMKGV SVRSATLVCE EGCMVVVDTG ASYISGPTSS 

       310        320        330        340        350        360 
LRLLMDTLGA QELSTNEYVV NCNQVPTLPD ISFHLGGRAY TLTSKDYVLQ DPYGNEDLCT 

       370        380        390        400 
LALHGLDVPP PTGPVWVLGA SFIRKFYTEF DRHNNRIGFA LAR

Q6DYE7 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