RENI2_MOUSE
ID RENI2_MOUSE Reviewed; 401 AA.
AC P00796; P70229; P97955; Q62155;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Renin-2;
DE EC=3.4.23.15 {ECO:0000250|UniProtKB:P00797};
DE AltName: Full=Angiotensinogenase;
DE AltName: Full=Submandibular gland renin;
DE Contains:
DE RecName: Full=Renin-2 heavy chain;
DE Contains:
DE RecName: Full=Renin-2 light chain;
DE Flags: Precursor;
GN Name=Ren2 {ECO:0000303|PubMed:6392850, ECO:0000312|MGI:MGI:97899};
GN Synonyms=Ren-2 {ECO:0000303|PubMed:6392850};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP PROTEIN SEQUENCE OF 64-351 AND 354-401.
RX PubMed=6812055; DOI=10.1073/pnas.79.16.4858;
RA Misono K.S., Chang J.-J., Inagami T.;
RT "Amino acid sequence of mouse submaxillary gland renin.";
RL Proc. Natl. Acad. Sci. U.S.A. 79:4858-4862(1982).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=6283373; DOI=10.1038/298090a0;
RA Panthier J.-J., Foote S., Chambraud B., Strosberg A.D., Corvol P.,
RA Rougeon F.;
RT "Complete amino acid sequence and maturation of the mouse submaxillary
RT gland renin precursor.";
RL Nature 298:90-92(1982).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Salivary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-29.
RX PubMed=6089205; DOI=10.1073/pnas.81.17.5489;
RA Panthier J.-J., Dreyfus M., Roux D.T.L., Rougeon F.;
RT "Mouse kidney and submaxillary gland renin genes differ in their 5'
RT putative regulatory sequences.";
RL Proc. Natl. Acad. Sci. U.S.A. 81:5489-5493(1984).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-30.
RX PubMed=2691339; DOI=10.1016/0378-1119(89)90143-1;
RA Burt D.W., Mullins L.J., George H., Smith G., Brooks J., Pioli D.,
RA Brammar W.J.;
RT "The nucleotide sequence of a mouse renin-encoding gene, Ren-1d, and its
RT upstream region.";
RL Gene 84:91-104(1989).
RN [6]
RP NUCLEOTIDE SEQUENCE OF 1-30, AND TISSUE SPECIFICITY.
RX PubMed=6392850; DOI=10.1128/mcb.4.11.2321-2331.1984;
RA Field L.J., Philbrick W.M., Howles P.N., Dickinson D.P., McGowan R.A.,
RA Gross K.W.;
RT "Expression of tissue-specific Ren-1 and Ren-2 genes of mice: comparative
RT analysis of 5'-proximal flanking regions.";
RL Mol. Cell. Biol. 4:2321-2331(1984).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 267-292.
RX PubMed=6357783; DOI=10.1002/j.1460-2075.1983.tb01483.x;
RA Panthier J.J., Rougeon F.;
RT "Kidney and submaxillary gland renins are encoded by two non-allelic genes
RT in Swiss mice.";
RL EMBO J. 2:675-678(1983).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS), ACTIVE SITES, AND DISULFIDE BONDS.
RX PubMed=1608447; DOI=10.1038/357466a0;
RA Dhanaraj V., Dealwis C.G., Frazao C., Badasso M., Sibanda B.L.,
RA Tickle I.J., Cooper J.B., Driessen H.P.C., Newman M., Aguilar C.,
RA Wood S.P., Blundell T.L., Hobart P.M., Geoghegan K.F., Ammirati M.J.,
RA Danley D.E., O'Connor B.A., Hoover D.J.;
RT "X-ray analyses of peptide-inhibitor complexes define the structural basis
RT of specificity for human and mouse renins.";
RL Nature 357:466-472(1992).
CC -!- FUNCTION: Renin is a highly specific endopeptidase, related to pepsin,
CC whose only known function is to generate angiotensin I from
CC angiotensinogen in the plasma, initiating a cascade of reactions that
CC produce an elevation of blood pressure and increased sodium retention
CC by the kidney. {ECO:0000250|UniProtKB:P00797}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Cleavage of Leu-|-Xaa bond in angiotensinogen to generate
CC angiotensin I.; EC=3.4.23.15;
CC Evidence={ECO:0000250|UniProtKB:P00797};
CC -!- SUBUNIT: Dimer of a heavy chain and a light chain joined by a disulfide
CC bond. {ECO:0000269|PubMed:6812055}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P00797}.
CC -!- TISSUE SPECIFICITY: Submandibular gland. {ECO:0000269|PubMed:6392850}.
CC -!- POLYMORPHISM: Present as a single-copy gene in strains such as BALB/c
CC and C57BL/6 while some strains such as Swiss and Akr contain two
CC copies.
CC -!- MISCELLANEOUS: The active enzyme isolated from the submandibular gland
CC has catalytic and antigenic activities similar to renal renin.
CC -!- SIMILARITY: Belongs to the peptidase A1 family. {ECO:0000305}.
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DR EMBL; J00621; AAA40050.1; -; mRNA.
DR EMBL; BC011157; AAH11157.1; -; mRNA.
DR EMBL; K02597; AAA40048.1; -; Genomic_DNA.
DR EMBL; M34191; AAA40046.1; -; Genomic_DNA.
DR EMBL; AF237860; AAA40047.1; -; Genomic_DNA.
DR PIR; A93923; REMSS.
DR PIR; I77411; I77411.
DR RefSeq; NP_112470.2; NM_031193.2.
DR PDB; 1SMR; X-ray; 2.00 A; A/C/E/G=67-401.
DR PDBsum; 1SMR; -.
DR AlphaFoldDB; P00796; -.
DR SMR; P00796; -.
DR ELM; P00796; -.
DR MEROPS; A01.008; -.
DR CPTAC; non-CPTAC-3737; -.
DR jPOST; P00796; -.
DR MaxQB; P00796; -.
DR PeptideAtlas; P00796; -.
DR PRIDE; P00796; -.
DR ProteomicsDB; 253113; -.
DR DNASU; 19702; -.
DR GeneID; 19702; -.
DR KEGG; mmu:19702; -.
DR CTD; 19702; -.
DR MGI; MGI:97899; Ren2.
DR InParanoid; P00796; -.
DR OrthoDB; 1619495at2759; -.
DR BioCyc; MetaCyc:MON-12952; -.
DR BioGRID-ORCS; 19702; 0 hits in 15 CRISPR screens.
DR EvolutionaryTrace; P00796; -.
DR PRO; PR:P00796; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P00796; protein.
DR GO; GO:0045177; C:apical part of cell; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005615; C:extracellular space; IDA:MGI.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; ISO:MGI.
DR GO; GO:0004175; F:endopeptidase activity; IDA:MGI.
DR GO; GO:0005159; F:insulin-like growth factor receptor binding; ISO:MGI.
DR GO; GO:0008233; F:peptidase activity; ISO:MGI.
DR GO; GO:0005102; F:signaling receptor binding; ISO:MGI.
DR GO; GO:0002003; P:angiotensin maturation; ISO:MGI.
DR GO; GO:0010467; P:gene expression; IMP:MGI.
DR GO; GO:0001822; P:kidney development; ISO:MGI.
DR GO; GO:0045777; P:positive regulation of blood pressure; IDA:MGI.
DR GO; GO:0006508; P:proteolysis; ISO:MGI.
DR GO; GO:0008217; P:regulation of blood pressure; ISO:MGI.
DR GO; GO:0043408; P:regulation of MAPK cascade; ISO:MGI.
DR GO; GO:0051591; P:response to cAMP; ISO:MGI.
DR GO; GO:0070305; P:response to cGMP; ISO:MGI.
DR GO; GO:0009410; P:response to xenobiotic stimulus; ISO:MGI.
DR CDD; cd05487; renin_like; 1.
DR Gene3D; 2.40.70.10; -; 2.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
DR InterPro; IPR001969; Aspartic_peptidase_AS.
DR InterPro; IPR012848; Aspartic_peptidase_N.
DR InterPro; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR InterPro; IPR034135; Renin-like_dom.
DR PANTHER; PTHR47966; PTHR47966; 1.
DR Pfam; PF07966; A1_Propeptide; 1.
DR Pfam; PF00026; Asp; 1.
DR PRINTS; PR00792; PEPSIN.
DR SUPFAM; SSF50630; SSF50630; 1.
DR PROSITE; PS00141; ASP_PROTEASE; 2.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Aspartyl protease; Cleavage on pair of basic residues;
KW Direct protein sequencing; Disulfide bond; Hydrolase; Protease;
KW Reference proteome; Secreted; Signal; Zymogen.
FT SIGNAL 1..25
FT /evidence="ECO:0000305"
FT PROPEP 26..63
FT /note="Activation peptide"
FT /evidence="ECO:0000269|PubMed:6812055"
FT /id="PRO_0000026095"
FT CHAIN 64..401
FT /note="Renin-2"
FT /id="PRO_0000026096"
FT CHAIN 64..351
FT /note="Renin-2 heavy chain"
FT /evidence="ECO:0000305|PubMed:6812055"
FT /id="PRO_0000026097"
FT CHAIN 354..401
FT /note="Renin-2 light chain"
FT /evidence="ECO:0000305|PubMed:6812055"
FT /id="PRO_0000026098"
FT DOMAIN 83..398
FT /note="Peptidase A1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT ACT_SITE 101
FT /evidence="ECO:0000269|PubMed:1608447"
FT ACT_SITE 286
FT /evidence="ECO:0000269|PubMed:1608447"
FT DISULFID 114..121
FT /evidence="ECO:0000269|PubMed:1608447"
FT DISULFID 277..281
FT /evidence="ECO:0000269|PubMed:1608447"
FT DISULFID 320..357
FT /evidence="ECO:0000269|PubMed:1608447"
FT CONFLICT 13
FT /note="L -> W (in Ref. 5; AAA40047)"
FT /evidence="ECO:0000305"
FT CONFLICT 99
FT /note="I -> M (in Ref. 2; AAA40050)"
FT /evidence="ECO:0000305"
FT CONFLICT 195..198
FT /note="FPAQ -> LSRS (in Ref. 2; AAA40050)"
FT /evidence="ECO:0000305"
FT CONFLICT 395
FT /note="I -> V (in Ref. 2; AAA40050)"
FT /evidence="ECO:0000305"
FT STRAND 71..78
FT /evidence="ECO:0007829|PDB:1SMR"
FT TURN 79..81
FT /evidence="ECO:0007829|PDB:1SMR"
FT STRAND 82..89
FT /evidence="ECO:0007829|PDB:1SMR"
FT TURN 90..93
FT /evidence="ECO:0007829|PDB:1SMR"
FT STRAND 94..101
FT /evidence="ECO:0007829|PDB:1SMR"
FT STRAND 107..111
FT /evidence="ECO:0007829|PDB:1SMR"
FT HELIX 119..123
FT /evidence="ECO:0007829|PDB:1SMR"
FT HELIX 129..131
FT /evidence="ECO:0007829|PDB:1SMR"
FT STRAND 136..146
FT /evidence="ECO:0007829|PDB:1SMR"
FT STRAND 149..162
FT /evidence="ECO:0007829|PDB:1SMR"
FT STRAND 165..176
FT /evidence="ECO:0007829|PDB:1SMR"
FT HELIX 179..182
FT /evidence="ECO:0007829|PDB:1SMR"
FT STRAND 186..192
FT /evidence="ECO:0007829|PDB:1SMR"
FT HELIX 196..198
FT /evidence="ECO:0007829|PDB:1SMR"
FT HELIX 200..202
FT /evidence="ECO:0007829|PDB:1SMR"
FT HELIX 206..212
FT /evidence="ECO:0007829|PDB:1SMR"
FT STRAND 216..225
FT /evidence="ECO:0007829|PDB:1SMR"
FT STRAND 228..231
FT /evidence="ECO:0007829|PDB:1SMR"
FT STRAND 234..240
FT /evidence="ECO:0007829|PDB:1SMR"
FT HELIX 243..245
FT /evidence="ECO:0007829|PDB:1SMR"
FT STRAND 246..254
FT /evidence="ECO:0007829|PDB:1SMR"
FT TURN 258..261
FT /evidence="ECO:0007829|PDB:1SMR"
FT STRAND 262..270
FT /evidence="ECO:0007829|PDB:1SMR"
FT STRAND 281..285
FT /evidence="ECO:0007829|PDB:1SMR"
FT STRAND 289..294
FT /evidence="ECO:0007829|PDB:1SMR"
FT HELIX 296..306
FT /evidence="ECO:0007829|PDB:1SMR"
FT STRAND 309..312
FT /evidence="ECO:0007829|PDB:1SMR"
FT STRAND 315..319
FT /evidence="ECO:0007829|PDB:1SMR"
FT HELIX 320..325
FT /evidence="ECO:0007829|PDB:1SMR"
FT STRAND 329..333
FT /evidence="ECO:0007829|PDB:1SMR"
FT STRAND 336..340
FT /evidence="ECO:0007829|PDB:1SMR"
FT HELIX 342..345
FT /evidence="ECO:0007829|PDB:1SMR"
FT STRAND 356..363
FT /evidence="ECO:0007829|PDB:1SMR"
FT TURN 368..370
FT /evidence="ECO:0007829|PDB:1SMR"
FT STRAND 374..376
FT /evidence="ECO:0007829|PDB:1SMR"
FT HELIX 378..381
FT /evidence="ECO:0007829|PDB:1SMR"
FT STRAND 384..389
FT /evidence="ECO:0007829|PDB:1SMR"
FT TURN 390..393
FT /evidence="ECO:0007829|PDB:1SMR"
FT STRAND 394..400
FT /evidence="ECO:0007829|PDB:1SMR"
SQ SEQUENCE 401 AA; 44283 MW; D938931F91F82980 CRC64;
MDRRRMPLWA LLLLWSPCTF SLPTGTTFER IPLKKMPSVR EILEERGVDM TRLSAEWDVF
TKRSSLTDLI SPVVLTNYLN SQYYGEIGIG TPPQTFKVIF DTGSANLWVP STKCSRLYLA
CGIHSLYESS DSSSYMENGD DFTIHYGSGR VKGFLSQDSV TVGGITVTQT FGEVTELPLI
PFMLAQFDGV LGMGFPAQAV GGVTPVFDHI LSQGVLKEKV FSVYYNRGPH LLGGEVVLGG
SDPEHYQGDF HYVSLSKTDS WQITMKGVSV GSSTLLCEEG CEVVVDTGSS FISAPTSSLK
LIMQALGAKE KRLHEYVVSC SQVPTLPDIS FNLGGRAYTL SSTDYVLQYP NRRDKLCTVA
LHAMDIPPPT GPVWVLGATF IRKFYTEFDR HNNRIGFALA R
