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Database: UniProt
Entry: A0A091RCF0_9GRUI
LinkDB: A0A091RCF0_9GRUI
Original site: A0A091RCF0_9GRUI 
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
//
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