P00796 (RENI2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Renin-2
EC=3.4.23.15

Alternative name(s):
Angiotensinogenase
Submandibular gland renin

Cleaved into the following 2 chains:

1. Renin-2 heavy chain
2. Renin-2 light chain

Gene names

Name:	Ren2
Synonyms:	Ren-2

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	401 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Renin is a highly specific endopeptidase, related to pepsin, 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. Its function in the salivary gland is not understood.
Catalytic activity	Cleavage of Leu-|-Xaa bond in angiotensinogen to generate angiotensin I.
Subunit structure	Dimer of a heavy chain and a light chain joined by a disulfide bond.
Subcellular location	Secreted.
Tissue specificity	Submandibular gland.
Polymorphism	Present as a single-copy gene in strains such as BALB/c and C57BL/6 while some strains such as Swiss and Akr contain two copies.
Miscellaneous	The active enzyme isolated from the submandibular gland has catalytic and antigenic activities similar to renal renin.
Sequence similarities	Belongs to the peptidase A1 family.

Ontologies

Keywords
Cellular component	Secreted
Domain	Signal
Molecular function	Aspartyl protease Hydrolase Protease
PTM	Cleavage on pair of basic residues Disulfide bond Zymogen
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	positive regulation of blood pressure Inferred from direct assay PubMed 19307186. Source: MGI proteolysis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	extracellular space Inferred from direct assay PubMed 19307186. Source: MGI
Molecular_function	aspartic-type endopeptidase activity Inferred from electronic annotation. Source: UniProtKB-KW endopeptidase activity Inferred from direct assay PubMed 19307186. Source: MGI
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 25

25

Probable

Propeptide

26 – 63

38

Activation peptide

PRO_0000026095

Chain

64 – 401

338

Renin-2

PRO_0000026096

Chain

64 – 351

288

Renin-2 heavy chain

PRO_0000026097

Chain

354 – 401

48

Renin-2 light chain

PRO_0000026098

Sites

Active site

101

1

Active site

286

1

Amino acid modifications

Disulfide bond

114 ↔ 121

Disulfide bond

277 ↔ 281

Disulfide bond

320 ↔ 357

Experimental info

Sequence conflict

13

1

L → W in AAA40047. Ref.5

Sequence conflict

99

1

I → M in AAA40050. Ref.2

Sequence conflict

195 – 198

4

FPAQ → LSRS in AAA40050. Ref.2

Sequence conflict

395

1

I → V in AAA40050. Ref.2

Secondary structure

1

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401

Helix Strand Turn

Details...

Beta strand

71 – 78

8

Turn

79 – 81

3

Beta strand

82 – 89

8

Turn

90 – 93

4

Beta strand

94 – 101

8

Beta strand

107 – 111

5

Helix

119 – 123

5

Helix

129 – 131

3

Beta strand

136 – 146

11

Beta strand

149 – 162

14

Beta strand

165 – 176

12

Helix

179 – 182

4

Beta strand

186 – 192

7

Helix

196 – 198

3

Helix

200 – 202

3

Helix

206 – 212

7

Beta strand

216 – 225

10

Beta strand

228 – 231

4

Beta strand

234 – 240

7

Helix

243 – 245

3

Beta strand

246 – 254

9

Turn

258 – 261

4

Beta strand

262 – 270

9

Beta strand

281 – 285

5

Beta strand

289 – 294

6

Helix

296 – 306

11

Beta strand

309 – 312

4

Beta strand

315 – 319

5

Helix

320 – 325

6

Beta strand

329 – 333

5

Beta strand

336 – 340

5

Helix

342 – 345

4

Beta strand

356 – 363

8

Turn

368 – 370

3

Beta strand

374 – 376

3

Helix

378 – 381

4

Beta strand

384 – 389

6

Turn

390 – 393

4

Beta strand

394 – 400

7

Sequences

	Sequence		Length	Mass (Da)
	P00796 [UniParc]. Last modified July 21, 1986. Version 1. Checksum: D938931F91F82980	FASTA	401	44,283
	10 20 30 40 50 60 MDRRRMPLWA LLLLWSPCTF SLPTGTTFER IPLKKMPSVR EILEERGVDM TRLSAEWDVF 70 80 90 100 110 120 TKRSSLTDLI SPVVLTNYLN SQYYGEIGIG TPPQTFKVIF DTGSANLWVP STKCSRLYLA 130 140 150 160 170 180 CGIHSLYESS DSSSYMENGD DFTIHYGSGR VKGFLSQDSV TVGGITVTQT FGEVTELPLI 190 200 210 220 230 240 PFMLAQFDGV LGMGFPAQAV GGVTPVFDHI LSQGVLKEKV FSVYYNRGPH LLGGEVVLGG 250 260 270 280 290 300 SDPEHYQGDF HYVSLSKTDS WQITMKGVSV GSSTLLCEEG CEVVVDTGSS FISAPTSSLK 310 320 330 340 350 360 LIMQALGAKE KRLHEYVVSC SQVPTLPDIS FNLGGRAYTL SSTDYVLQYP NRRDKLCTVA 370 380 390 400 LHAMDIPPPT GPVWVLGATF IRKFYTEFDR HNNRIGFALA R

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Amino acid sequence of mouse submaxillary gland renin." Misono K.S., Chang J.-J., Inagami T. Proc. Natl. Acad. Sci. U.S.A. 79:4858-4862(1982) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 64-351 AND 354-401.
[2]	"Complete amino acid sequence and maturation of the mouse submaxillary gland renin precursor." Panthier J.-J., Foote S., Chambraud B., Strosberg A.D., Corvol P., Rougeon F. Nature 298:90-92(1982) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: FVB/N. Tissue: Salivary gland.
[4]	"Mouse kidney and submaxillary gland renin genes differ in their 5' putative regulatory sequences." Panthier J.-J., Dreyfus M., Roux D.T.L., Rougeon F. Proc. Natl. Acad. Sci. U.S.A. 81:5489-5493(1984) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-29.
[5]	"The nucleotide sequence of a mouse renin-encoding gene, Ren-1d, and its upstream region." Burt D.W., Mullins L.J., George H., Smith G., Brooks J., Pioli D., Brammar W.J. Gene 84:91-104(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-30.
[6]	"Expression of tissue-specific Ren-1 and Ren-2 genes of mice: comparative analysis of 5'-proximal flanking regions." Field L.J., Philbrick W.M., Howles P.N., Dickinson D.P., McGowan R.A., Gross K.W. Mol. Cell. Biol. 4:2321-2331(1984) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE OF 1-30.
[7]	"Kidney and submaxillary gland renins are encoded by two non-allelic genes in Swiss mice." Panthier J.J., Rougeon F. EMBO J. 2:675-678(1983) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 267-292.
[8]	"X-ray analyses of peptide-inhibitor complexes define the structural basis of specificity for human and mouse renins." Dhanaraj V., Dealwis C.G., Frazao C., Badasso M., Sibanda B.L., Tickle I.J., Cooper J.B., Driessen H.P.C., Newman M., Aguilar C., Wood S.P., Blundell T.L., Hobart P.M., Geoghegan K.F., Ammirati M.J., Danley D.E., O'Connor B.A., Hoover D.J. Nature 357:466-472(1992) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

J00621 mRNA. Translation: AAA40050.1.
BC011157 mRNA. Translation: AAH11157.1.
K02597 Genomic DNA. Translation: AAA40048.1.
M34191 Genomic DNA. Translation: AAA40046.1.
AF237860 Genomic DNA. Translation: AAA40047.1.

IPI

IPI00316248.

PIR

REMSS. A93923.
I77411.

RefSeq

NP_112470.2. NM_031193.2.

UniGene

Mm.220955.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1SMR	X-ray	2.00	A/C/E/G	67-401	[»]

ProteinModelPortal

P00796.

SMR

P00796. Positions 26-63, 67-401.

ModBase

Search...

Protein family/group databases

MEROPS

A01.008.

Proteomic databases

PRIDE

P00796.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

19702.

KEGG

mmu:19702.

UCSC

uc007cqf.1. mouse.

Organism-specific databases

CTD

19702.

MGI

MGI:97899. Ren2.

Phylogenomic databases

HOVERGEN

HBG000482.

InParanoid

P00796.

KO

K01380.

Enzyme and pathway databases

BioCyc

MetaCyc:MONOMER-12952.

Gene expression databases

Genevestigator

P00796.

GermOnline

ENSMUSG00000070645. Mus musculus.

Family and domain databases

Gene3D

2.40.70.10. 2 hits.

InterPro

IPR001461. Peptidase_A1.
IPR021109. Peptidase_aspartic.
IPR001969. Peptidase_aspartic_AS.
IPR012848. Propep_A1.
[Graphical view]

PANTHER

PTHR13683. PTHR13683. 1 hit.

Pfam

PF07966. A1_Propeptide. 1 hit.
PF00026. Asp. 1 hit.
[Graphical view]

PRINTS

PR00792. PEPSIN.

SUPFAM

SSF50630. Pept_Aspartic. 1 hit.

PROSITE

PS00141. ASP_PROTEASE. 2 hits.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P00796.

NextBio

297070.

PMAP-CutDB

P00796.

SOURCE

Search...

Entry information

Entry name

RENI2_MOUSE

Accession

Primary (citable) accession number: P00796
Secondary accession number(s): P70229, P97955, Q62155

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	July 21, 1986
Last modified:	April 3, 2013
This is version 134 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program