ID A0A091G514_9AVES Unreviewed; 372 AA.
AC A0A091G514;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 32.
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=N303_11428 {ECO:0000313|EMBL:KFO77023.1};
OS Cuculus canorus (common cuckoo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Cuculiformes; Cuculidae; Cuculus.
OX NCBI_TaxID=55661 {ECO:0000313|EMBL:KFO77023.1, ECO:0000313|Proteomes:UP000053760};
RN [1] {ECO:0000313|EMBL:KFO77023.1, ECO:0000313|Proteomes:UP000053760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N303 {ECO:0000313|EMBL:KFO77023.1};
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KL447783; KFO77023.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091G514; -.
DR STRING; 55661.A0A091G514; -.
DR Proteomes; UP000053760; Unassembled WGS sequence.
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 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:UP000053760}.
FT DOMAIN 56..372
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 74
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 260
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT DISULFID 87..94
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT DISULFID 251..255
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFO77023.1"
FT NON_TER 372
FT /evidence="ECO:0000313|EMBL:KFO77023.1"
SQ SEQUENCE 372 AA; 40390 MW; CA4153D753232006 CRC64;
RIALRRMPSI RQTLQEMGVK VSDVFPEMRQ SRSSGVAGPR NGTAPTVLTN YLDTQYFGEI
SIGTPAQTFK VVFDTGSANL WVPSYKCSPL YSACVSHSRY NSFKSRTYIA NGTGFAIRYG
TGSVKGFLSQ DIVMVSDIPI IQVFAEATAL PAFPFIFARF DGVLGMGYPS QAIDGITPVF
DRILSQQILK EDAFSVYYSR NDPLKPGGEI ILGGSDPAYY TGDFHYLNIS KSGYWQISMK
GVSVGAEILF CKEGCSVAVD TGASYITGPA GPISVLMKAI GATETAEGEY VLECDRVPQL
PNISFNLGGK AYVLSGSAYV LRQSQYGEEV CVVAFSGLDI PPPAGPLWIL GASFIGHYYT
KFDRRHNRIG FA
//
