ID A0A087Y4E0_POEFO Unreviewed; 375 AA.
AC A0A087Y4E0;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 2.
DT 27-MAR-2024, entry version 47.
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};
OS Poecilia formosa (Amazon molly) (Limia formosa).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=48698 {ECO:0000313|Ensembl:ENSPFOP00000012893.2, ECO:0000313|Proteomes:UP000028760};
RN [1] {ECO:0000313|Proteomes:UP000028760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=female {ECO:0000313|Proteomes:UP000028760};
RA Schartl M., Warren W.;
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPFOP00000012893.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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; AYCK01009225; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AYCK01009226; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A087Y4E0; -.
DR STRING; 48698.ENSPFOP00000012893; -.
DR Ensembl; ENSPFOT00000012911.2; ENSPFOP00000012893.2; ENSPFOG00000012876.2.
DR eggNOG; KOG1339; Eukaryota.
DR GeneTree; ENSGT00940000157898; -.
DR OMA; KMPSIRD; -.
DR Proteomes; UP000028760; 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; IPR012848; Aspartic_peptidase_N.
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; 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 3: Inferred from homology;
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 Reference proteome {ECO:0000313|Proteomes:UP000028760};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..375
FT /note="renin"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001833964"
FT DOMAIN 78..375
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 96
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 282
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT DISULFID 109..116
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT DISULFID 273..277
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT DISULFID 315..352
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ SEQUENCE 375 AA; 40886 MW; 76466446AB47D473 CRC64;
MTPLPNCWMY LVALSLAVNS SHGLRRIALK KMPSIRETLQ EMGVSAEQVL AELAQMNAAD
PNNGTVPTPL TNYLDTQYFG EISIGSPAQM FNVVFDTGSA NLWVPSQRCS PFSTACFTHN
RYDSSQSHTH VENGTGFSIY YASGTIRGFL SEDVVVVGGL PVVQVFAEAT SLSAMPFIFA
KFDGVLGMGY PNVAIDGITP VFDQIMSQHI LKEEVFSIYY SRDPKQSPGG ELLLGGTDPN
YYTGNFNYLE TREMGKWEVT MKGVTVGAEM MFCAEGCTAV IDTGSSYITG PASSVSMLMK
TIGAQLDETG YKVNCDTVKM LPSVTFHLGG QDYSLTHEDY IIWQSQFEGD VCIVTFRGLD
VPPPTGPIWI LGANF
//
