[1]	NUCLEOTIDE SEQUENCE [MRNA]. DOI=10.1097/00005344-199912000-00018; PubMed=10598135 [NCBI, ExPASy, EBI, Israel, Japan] Valdenaire O., Breu V., Giller T., Bur D., Fischli W.; "Cloning and characterization of marmoset renin: comparison with human renin."; J. Cardiovasc. Pharmacol. 34:893-897(1999).

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

AJ132342; CAB64879.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

HSSP

P00797; 1HRN. [HSSP ENTRY / PDB]

SMR

Q9TSZ1; 65-400.

ModBase

Q9TSZ1.

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

Q9TSZ1.

Phylogenomic databases

HOVERGEN

Q9TSZ1; -.

Other

ProtoNet

Q9TSZ1.

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 23`	`23`	`By similarity.`
`PROPEP`	`24 60`	`37`	`Activation peptide.`	`PRO_0000026077`
`CHAIN`	`61 400`	`340`	`Renin.`	`PRO_0000026078`
`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).`
`DISULFID`	`111 118`		`By similarity.`
`DISULFID`	`277 281`		`By similarity.`
`DISULFID`	`319 356`		`By similarity.`

Sequence information

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

Molecular weight: 44038 Da [This is the MW of the unprocessed precursor]

CRC64: 31769217035615FA [This is a checksum on the sequence]

        10         20         30         40         50         60 
MDAWRGMPRW GLLLLLWGSC TFGLPTETTT FKRISLKRMP SIRESLKERG VDMARLGPER 

        70         80         90        100        110        120 
MALVNITSSV ILTNYMDTQY YGEIGIGTPP QTFKVVFDTG SSNVWVPSSK CSRLYTACVY 

       130        140        150        160        170        180 
HKLFDASDSS SYKHNGTELT LRYSTGTVSG FLSQDVITVG GITVTQTFGE VTEMPALPFM 

       190        200        210        220        230        240 
LAEFDGVVGM GFSEQAIGKV TPLFDNIISQ GLLKEDVFSF YYNRDSENSQ SLGGQIVLGG 

       250        260        270        280        290        300 
SDPQHYEGNF HYINLIRTGL WQIPMKGVSV GSSTLLCEDG CLALVDTGAS YISGSTSSIE 

       310        320        330        340        350        360 
KLMEALGAKK RLFDYVVKCN EGPTLPDISF HLGGKEYTLT SADYVFQESY SSKKLCTLAI 

       370        380        390        400 
HAMDIPPPTG PTWALGATFI RKFYTEFDRG NNRIGFALAR

Q9TSZ1 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