ID U5L0U9_KOGSI Unreviewed; 407 AA.
AC U5L0U9;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 37.
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};
DE Flags: Fragment;
GN Name=REN {ECO:0000313|EMBL:AGV55502.1};
OS Kogia sima (Dwarf sperm whale) (Physeter simus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Physeteridae; Kogia.
OX NCBI_TaxID=9752 {ECO:0000313|EMBL:AGV55502.1};
RN [1] {ECO:0000313|EMBL:AGV55502.1}
RP NUCLEOTIDE SEQUENCE.
RA Xu S., Yang Y., Zhou X., Xu J., Zhou K., Yang G.;
RT "Enhanced osmoregulation during secondary aquatic adaptation: ongoing
RT evolution of the osmoregulatory genes in cetaceans.";
RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
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 -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the peptidase A1 family.
CC {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
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DR EMBL; KC153379; AGV55502.1; -; Genomic_DNA.
DR AlphaFoldDB; U5L0U9; -.
DR MEROPS; A01.008; -.
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; 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; 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 3: Inferred from homology;
KW Aspartyl protease {ECO:0000256|RuleBase:RU000454};
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR601461-2};
KW Hydrolase {ECO:0000256|RuleBase:RU000454};
KW Protease {ECO:0000256|RuleBase:RU000454}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..407
FT /note="renin"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004662153"
FT DOMAIN 86..404
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 104
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 292
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT DISULFID 117..124
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT DISULFID 283..287
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT DISULFID 326..363
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AGV55502.1"
FT NON_TER 407
FT /evidence="ECO:0000313|EMBL:AGV55502.1"
SQ SEQUENCE 407 AA; 44906 MW; 2B2A3F0E6AAF3AF0 CRC64;
VDQWSRMPRW GLLLVLWGSC TFGLPADTGA FRRIFLKKMP SVWESLKERG VDVARLGAEW
SQLTKTLSFG NRTSPVVLTN YLDTQYYGEI SIGTPPQTFK VIFDTGSANL WVPSTKCSPL
YTACEIHSLY DSSESSSYVE NGTEFTIHYG SGKVKGFLSQ DLVTVGGITV TQTFGEVTEL
PLIPFMLAKF DGVLGMGFPA QAIEGVTPVF DHILSQRVLK EDVFSVYYSR AGENSHLLGG
EIVLGGSDPQ YYQENFHYVS VSKTGSWQIR MKGVSVRSTT LLCEEGCMVV VDTGASYISG
PTSSLRLLME TLGAKELSTD EYVVNCNQVP TLPDISFHLG GRAYTLTSAD YVLQDPYNSD
DLCTLALHGL DVPPPTGPVW VLGASFIRKF YTEFDRRNNR IGFALAR
//
