ID A0A091RCF0_9GRUI Unreviewed; 318 AA.
AC A0A091RCF0;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 36.
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 ORFNames=N332_09861 {ECO:0000313|EMBL:KFQ36912.1};
OS Mesitornis unicolor (brown roatelo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Gruiformes; Mesitornithidae; Mesitornis.
OX NCBI_TaxID=54374 {ECO:0000313|EMBL:KFQ36912.1, ECO:0000313|Proteomes:UP000053369};
RN [1] {ECO:0000313|EMBL:KFQ36912.1, ECO:0000313|Proteomes:UP000053369}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N332 {ECO:0000313|EMBL:KFQ36912.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) 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 -!- SIMILARITY: Belongs to the peptidase A1 family.
CC {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
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DR EMBL; KK813022; KFQ36912.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091RCF0; -.
DR MEROPS; A01.007; -.
DR Proteomes; UP000053369; Unassembled WGS sequence.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 2.60.40.1960; -; 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 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000053369}.
FT DOMAIN 2..318
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 20
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 206
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT DISULFID 33..40
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT DISULFID 197..201
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT DISULFID 240..277
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFQ36912.1"
FT NON_TER 318
FT /evidence="ECO:0000313|EMBL:KFQ36912.1"
SQ SEQUENCE 318 AA; 34315 MW; E5E66221081B087D CRC64;
QYFGEISIGT PAQTFKVVFD TGSANLWVPS YKCSPLYSAC VSHSRYDSAK SRTYIANGTD
FAIHYGTGSL KGVLSQDIVM VSDIPIIQVF AEATALPAFP FIFARFDGVL GMGYPSQAID
GITPVFDHIL SQQILKEDVF SVYYSRNSPL KPGGEIILGG SDPAYYTGDF HYLNISKSGY
WQISMKGVSV GAEILFCKEG CSVAIDTGAS FITGPAGPIS VLMKAIGATE TAEGEYLVDC
DQVPQLPNIS FHLGGKVYTL SGSAYILRQS QYGEDVCVVA FSGLDIPPPA GPIWILGASF
IGHYYTKFDR RNNRIGFA
//