Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Renin-2

Gene

Ren2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 activityi

Cleavage of Leu-|-Xaa bond in angiotensinogen to generate angiotensin I.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei1011
Active sitei2861

GO - Molecular functioni

  • aspartic-type endopeptidase activity Source: GO_Central
  • endopeptidase activity Source: MGI

GO - Biological processi

  • angiotensin maturation Source: GO_Central
  • positive regulation of blood pressure Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Aspartyl protease, Hydrolase, Protease

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-12952.

Protein family/group databases

MEROPSiA01.008.

Names & Taxonomyi

Protein namesi
Recommended name:
Renin-2 (EC:3.4.23.15)
Alternative name(s):
Angiotensinogenase
Submandibular gland renin
Cleaved into the following 2 chains:
Gene namesi
Name:Ren2
Synonyms:Ren-2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:97899. Ren2.

Subcellular locationi

GO - Cellular componenti

  • extracellular space Source: MGI
  • lysosome Source: GO_Central
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 25CuratedAdd BLAST25
PropeptideiPRO_000002609526 – 63Activation peptide1 PublicationAdd BLAST38
ChainiPRO_000002609664 – 401Renin-2Add BLAST338
ChainiPRO_000002609764 – 351Renin-2 heavy chainAdd BLAST288
ChainiPRO_0000026098354 – 401Renin-2 light chainAdd BLAST48

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi114 ↔ 121
Disulfide bondi277 ↔ 281
Disulfide bondi320 ↔ 357

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Zymogen

Proteomic databases

MaxQBiP00796.
PaxDbiP00796.
PeptideAtlasiP00796.
PRIDEiP00796.

Miscellaneous databases

PMAP-CutDBP00796.

Expressioni

Tissue specificityi

Submandibular gland.

Interactioni

Subunit structurei

Dimer of a heavy chain and a light chain joined by a disulfide bond.

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000092135.

Structurei

Secondary structure

1401
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi71 – 78Combined sources8
Turni79 – 81Combined sources3
Beta strandi82 – 89Combined sources8
Turni90 – 93Combined sources4
Beta strandi94 – 101Combined sources8
Beta strandi107 – 111Combined sources5
Helixi119 – 123Combined sources5
Helixi129 – 131Combined sources3
Beta strandi136 – 146Combined sources11
Beta strandi149 – 162Combined sources14
Beta strandi165 – 176Combined sources12
Helixi179 – 182Combined sources4
Beta strandi186 – 192Combined sources7
Helixi196 – 198Combined sources3
Helixi200 – 202Combined sources3
Helixi206 – 212Combined sources7
Beta strandi216 – 225Combined sources10
Beta strandi228 – 231Combined sources4
Beta strandi234 – 240Combined sources7
Helixi243 – 245Combined sources3
Beta strandi246 – 254Combined sources9
Turni258 – 261Combined sources4
Beta strandi262 – 270Combined sources9
Beta strandi281 – 285Combined sources5
Beta strandi289 – 294Combined sources6
Helixi296 – 306Combined sources11
Beta strandi309 – 312Combined sources4
Beta strandi315 – 319Combined sources5
Helixi320 – 325Combined sources6
Beta strandi329 – 333Combined sources5
Beta strandi336 – 340Combined sources5
Helixi342 – 345Combined sources4
Beta strandi356 – 363Combined sources8
Turni368 – 370Combined sources3
Beta strandi374 – 376Combined sources3
Helixi378 – 381Combined sources4
Beta strandi384 – 389Combined sources6
Turni390 – 393Combined sources4
Beta strandi394 – 400Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1SMRX-ray2.00A/C/E/G67-401[»]
ProteinModelPortaliP00796.
SMRiP00796.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00796.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini83 – 398Peptidase A1PROSITE-ProRule annotationAdd BLAST316

Sequence similaritiesi

Belongs to the peptidase A1 family.Curated
Contains 1 peptidase A1 domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG1339. Eukaryota.
ENOG410XNV7. LUCA.
HOVERGENiHBG000482.
InParanoidiP00796.
KOiK01380.

Family and domain databases

Gene3Di2.40.70.10. 2 hits.
InterProiIPR001461. Aspartic_peptidase_A1.
IPR001969. Aspartic_peptidase_AS.
IPR012848. Aspartic_peptidase_N.
IPR033121. PEPTIDASE_A1.
IPR021109. Peptidase_aspartic_dom.
[Graphical view]
PANTHERiPTHR13683. PTHR13683. 1 hit.
PfamiPF07966. A1_Propeptide. 1 hit.
PF00026. Asp. 1 hit.
[Graphical view]
PRINTSiPR00792. PEPSIN.
SUPFAMiSSF50630. SSF50630. 1 hit.
PROSITEiPS00141. ASP_PROTEASE. 2 hits.
PS51767. PEPTIDASE_A1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P00796-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDRRRMPLWA LLLLWSPCTF SLPTGTTFER IPLKKMPSVR EILEERGVDM
60 70 80 90 100
TRLSAEWDVF TKRSSLTDLI SPVVLTNYLN SQYYGEIGIG TPPQTFKVIF
110 120 130 140 150
DTGSANLWVP STKCSRLYLA CGIHSLYESS DSSSYMENGD DFTIHYGSGR
160 170 180 190 200
VKGFLSQDSV TVGGITVTQT FGEVTELPLI PFMLAQFDGV LGMGFPAQAV
210 220 230 240 250
GGVTPVFDHI LSQGVLKEKV FSVYYNRGPH LLGGEVVLGG SDPEHYQGDF
260 270 280 290 300
HYVSLSKTDS WQITMKGVSV GSSTLLCEEG CEVVVDTGSS FISAPTSSLK
310 320 330 340 350
LIMQALGAKE KRLHEYVVSC SQVPTLPDIS FNLGGRAYTL SSTDYVLQYP
360 370 380 390 400
NRRDKLCTVA LHAMDIPPPT GPVWVLGATF IRKFYTEFDR HNNRIGFALA

R
Length:401
Mass (Da):44,283
Last modified:July 21, 1986 - v1
Checksum:iD938931F91F82980
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti13L → W in AAA40047 (PubMed:2691339).Curated1
Sequence conflicti99I → M in AAA40050 (PubMed:6283373).Curated1
Sequence conflicti195 – 198FPAQ → LSRS in AAA40050 (PubMed:6283373).Curated4
Sequence conflicti395I → V in AAA40050 (PubMed:6283373).Curated1

Polymorphismi

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.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiA93923. REMSS.
I77411.
RefSeqiNP_112470.2. NM_031193.2.
UniGeneiMm.220955.

Genome annotation databases

GeneIDi19702.
KEGGimmu:19702.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiA93923. REMSS.
I77411.
RefSeqiNP_112470.2. NM_031193.2.
UniGeneiMm.220955.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1SMRX-ray2.00A/C/E/G67-401[»]
ProteinModelPortaliP00796.
SMRiP00796.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000092135.

Protein family/group databases

MEROPSiA01.008.

Proteomic databases

MaxQBiP00796.
PaxDbiP00796.
PeptideAtlasiP00796.
PRIDEiP00796.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi19702.
KEGGimmu:19702.

Organism-specific databases

CTDi19702.
MGIiMGI:97899. Ren2.

Phylogenomic databases

eggNOGiKOG1339. Eukaryota.
ENOG410XNV7. LUCA.
HOVERGENiHBG000482.
InParanoidiP00796.
KOiK01380.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-12952.

Miscellaneous databases

EvolutionaryTraceiP00796.
PMAP-CutDBP00796.
PROiP00796.
SOURCEiSearch...

Family and domain databases

Gene3Di2.40.70.10. 2 hits.
InterProiIPR001461. Aspartic_peptidase_A1.
IPR001969. Aspartic_peptidase_AS.
IPR012848. Aspartic_peptidase_N.
IPR033121. PEPTIDASE_A1.
IPR021109. Peptidase_aspartic_dom.
[Graphical view]
PANTHERiPTHR13683. PTHR13683. 1 hit.
PfamiPF07966. A1_Propeptide. 1 hit.
PF00026. Asp. 1 hit.
[Graphical view]
PRINTSiPR00792. PEPSIN.
SUPFAMiSSF50630. SSF50630. 1 hit.
PROSITEiPS00141. ASP_PROTEASE. 2 hits.
PS51767. PEPTIDASE_A1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiRENI2_MOUSE
AccessioniPrimary (citable) accession number: P00796
Secondary accession number(s): P70229, P97955, Q62155
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: November 2, 2016
This is version 154 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

The active enzyme isolated from the submandibular gland has catalytic and antigenic activities similar to renal renin.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Peptidase families
    Classification of peptidase families and list of entries
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.