[1]	NUCLEOTIDE SEQUENCE [MRNA]. STRAIN=Merino; TISSUE=Kidney; PubMed=1543532 [NCBI, ExPASy, EBI, Israel, Japan] Aldred G.P., Fu P., Crawford R.J., Fernley R.T.; "The sequence and tissue expression of ovine renin."; J. Mol. Endocrinol. 8:3-11(1992).

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).
TISSUE SPECIFICITY: Kidney.
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

L43524; AAA69809.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

I47099; I47099.

NP_001009299.1; -.

3D structure databases

HSSP

P00796; 1SMR. [HSSP ENTRY / PDB]

SMR

P52115; 63-400.

ModBase

P52115.

Protein family/group databases

MEROPS

A01.007; -.

Ontologies

GO:0005576;	Cellular component: extracellular region (inferred from electronic annotation from UniProtKB-KW).
GO:0016020;	Cellular component: membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0004190;	Molecular function: aspartic-type endopeptidase activity (inferred from electronic annotation from InterPro).
GO:0006508;	Biological process: proteolysis (inferred from electronic annotation from InterPro).
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

GeneID

443310; -.

Phylogenomic databases

HOVERGEN

P52115; -.

Other

ProtoNet

P52115.

UniRef

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

Keywords

Aspartyl protease; Glycoprotein; Hydrolase; Membrane; Protease; Secreted; Signal; Zymogen.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 17`	`17`	`Potential.`
`PROPEP`	`18 59`	`42`	`Activation peptide (Potential).`	`PRO_0000026093`
`CHAIN`	`60 400`	`341`	`Renin.`	`PRO_0000026094`
`ACT_SITE`	`98 98`		`By similarity.`
`ACT_SITE`	`286 286`		`By similarity.`
`CARBOHYD`	`65 65`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`135 135`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`353 353`		`N-linked (GlcNAc...) (Potential).`
`DISULFID`	`111 118`		`By similarity.`
`DISULFID`	`277 281`		`By similarity.`

Sequence information

Length: 400 AA [This is the length of the unprocessed precursor]

Molecular weight: 44016 Da [This is the MW of the unprocessed precursor]

CRC64: 95ED40716565FE25 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MPLWGLLLAL WGCSTFSLPA DTAAFRRIFL KKMPSVRESL KERGVDMAQL GAEWSQLTKT 

        70         80         90        100        110        120 
LSFGNRTSPV VLTNYLDTQY YGEIGIGTPP QTFKVIFDTG SANLWVPSTK CSPLYTACEI 

       130        140        150        160        170        180 
HSLYDSLESS SYVENGTEFT IYYGSGKVKG FLSQDLVTVG GITVTQTFGE VTELPLRPFM 

       190        200        210        220        230        240 
LAKFDGVLGM GFPAQAVGGV TPVFDHILAQ RVLTEDVFSV YYSRDSKNSH LLGGEIVLGG 

       250        260        270        280        290        300 
SDPQYYQENF HYVSISKPGS WQIRMKGVSV RSTTLLCEEG CMVVVDTGAS YISGPTSSLR 

       310        320        330        340        350        360 
LLMEALGAKE LSIDEYVVNC NQMPTLPDIS FHLGGKAYTL TSADYVLQDP YNNISCTLAL 

       370        380        390        400 
HGMDIPPPTG PVWVLGATFI RKFYTEFDRR NNRIGFALAR

P52115 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