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Database: UniProt
Entry: Q91X66_MOUSE
LinkDB: Q91X66_MOUSE
Original site: Q91X66_MOUSE 
ID   Q91X66_MOUSE            Unreviewed;       401 AA.
AC   Q91X66;
DT   01-DEC-2001, integrated into UniProtKB/TrEMBL.
DT   01-DEC-2001, sequence version 1.
DT   24-JAN-2024, entry version 109.
DE   RecName: Full=renin {ECO:0000256|ARBA:ARBA00013216};
DE            EC=3.4.23.15 {ECO:0000256|ARBA:ARBA00013216};
DE   AltName: Full=Angiotensinogenase {ECO:0000256|ARBA:ARBA00032220};
GN   Name=Ren2 {ECO:0000313|EMBL:AAH11473.1, ECO:0000313|MGI:MGI:97899};
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 {ECO:0000313|EMBL:AAH11473.1};
RN   [1] {ECO:0000313|EMBL:AAH11473.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N {ECO:0000313|EMBL:AAH11473.1};
RC   TISSUE=Salivary gland {ECO:0000313|EMBL:AAH11473.1};
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RA   Gerhard D.S., Wagner L., Feingold E.A., Shenmen C.M., Grouse L.H.,
RA   Schuler G., Klein S.L., Old S., Rasooly R., Good P., Guyer M., Peck A.M.,
RA   Derge J.G., Lipman D., Collins F.S., Jang W., Sherry S., Feolo M.,
RA   Misquitta L., Lee E., Rotmistrovsky K., Greenhut S.F., Schaefer C.F.,
RA   Buetow K., Bonner T.I., Haussler D., Kent J., Kiekhaus M., Furey T.,
RA   Brent M., Prange C., Schreiber K., Shapiro N., Bhat N.K., Hopkins R.F.,
RA   Hsie F., Driscoll T., Soares M.B., Casavant T.L., Scheetz T.E.,
RA   Brown-stein M.J., Usdin T.B., Toshiyuki S., Carninci P., Piao Y.,
RA   Dudekula D.B., Ko M.S., Kawakami K., Suzuki Y., Sugano S., Gruber C.E.,
RA   Smith M.R., Simmons B., Moore T., Waterman R., Johnson S.L., Ruan Y.,
RA   Wei C.L., Mathavan S., Gunaratne P.H., Wu J., Garcia A.M., Hulyk S.W.,
RA   Fuh E., Yuan Y., Sneed A., Kowis C., Hodgson A., Muzny D.M., McPherson J.,
RA   Gibbs R.A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S.,
RA   Sanchez A., Whiting M., Madari A., Young A.C., Wetherby K.D., Granite S.J.,
RA   Kwong P.N., Brinkley C.P., Pearson R.L., Bouffard G.G., Blakesly R.W.,
RA   Green E.D., Dickson M.C., Rodriguez A.C., Grimwood J., Schmutz J.,
RA   Myers R.M., Butterfield Y.S., Griffith M., Griffith O.L., Krzywinski M.I.,
RA   Liao N., Morin R., Morrin R., Palmquist D., Petrescu A.S., Skalska U.,
RA   Smailus D.E., Stott J.M., Schnerch A., Schein J.E., Jones S.J., Holt R.A.,
RA   Baross A., Marra M.A., Clifton S., Makowski K.A., Bosak S., Malek J.;
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).
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:0000256|ARBA:ARBA00000430};
CC   -!- SIMILARITY: Belongs to the peptidase A1 family.
CC       {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
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DR   EMBL; BC011473; AAH11473.1; -; mRNA.
DR   AlphaFoldDB; Q91X66; -.
DR   MEROPS; A01.008; -.
DR   AGR; MGI:97899; -.
DR   MGI; MGI:97899; Ren2.
DR   GO; GO:0005615; C:extracellular space; IEA:UniProt.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   GO; GO:0008217; P:regulation of blood pressure; IEA:UniProt.
DR   CDD; cd05487; renin_like; 1.
DR   Gene3D; 2.40.70.10; Acid Proteases; 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; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR   PANTHER; PTHR47966:SF24; RENIN; 1.
DR   Pfam; PF07966; A1_Propeptide; 1.
DR   Pfam; PF00026; Asp; 1.
DR   PRINTS; PR00792; PEPSIN.
DR   SUPFAM; SSF50630; Acid proteases; 1.
DR   PROSITE; PS00141; ASP_PROTEASE; 2.
DR   PROSITE; PS51767; PEPTIDASE_A1; 1.
PE   2: Evidence at transcript level;
KW   Aspartyl protease {ECO:0000256|RuleBase:RU000454};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW   ECO:0000256|PIRSR:PIRSR601461-2};
KW   Hydrolase {ECO:0000256|RuleBase:RU000454};
KW   Protease {ECO:0000256|RuleBase:RU000454};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP};
KW   Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..401
FT                   /note="renin"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004318855"
FT   DOMAIN          83..398
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   ACT_SITE        101
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   ACT_SITE        286
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   DISULFID        114..121
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT   DISULFID        277..281
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT   DISULFID        320..357
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ   SEQUENCE   401 AA;  44297 MW;  D938931F90BD2980 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 IRKFYTEFER HNNRIGFALA R
//
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