ID R0KYH8_ANAPL Unreviewed; 361 AA.
AC R0KYH8;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 41.
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=Anapl_15774 {ECO:0000313|EMBL:EOA94264.1};
OS Anas platyrhynchos (Mallard) (Anas boschas).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Anseriformes; Anatidae;
OC Anatinae; Anas.
OX NCBI_TaxID=8839 {ECO:0000313|EMBL:EOA94264.1, ECO:0000313|Proteomes:UP000296049};
RN [1] {ECO:0000313|Proteomes:UP000296049}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23749191; DOI=10.1038/ng.2657;
RA Huang Y., Li Y., Burt D.W., Chen H., Zhang Y., Qian W., Kim H., Gan S.,
RA Zhao Y., Li J., Yi K., Feng H., Zhu P., Li B., Liu Q., Fairley S.,
RA Magor K.E., Du Z., Hu X., Goodman L., Tafer H., Vignal A., Lee T.,
RA Kim K.W., Sheng Z., An Y., Searle S., Herrero J., Groenen M.A.,
RA Crooijmans R.P., Faraut T., Cai Q., Webster R.G., Aldridge J.R.,
RA Warren W.C., Bartschat S., Kehr S., Marz M., Stadler P.F., Smith J.,
RA Kraus R.H., Zhao Y., Ren L., Fei J., Morisson M., Kaiser P., Griffin D.K.,
RA Rao M., Pitel F., Wang J., Li N.;
RT "The duck genome and transcriptome provide insight into an avian influenza
RT virus reservoir species.";
RL Nat. Genet. 45:776-783(2013).
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; KB744902; EOA94264.1; -; Genomic_DNA.
DR Proteomes; UP000296049; 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; 3.
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; 2.
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:UP000296049}.
FT DOMAIN 58..358
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 76
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 263
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT DISULFID 87..96
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT DISULFID 254..258
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EOA94264.1"
FT NON_TER 361
FT /evidence="ECO:0000313|EMBL:EOA94264.1"
SQ SEQUENCE 361 AA; 38865 MW; 24B468EB97F58044 CRC64;
ALRIALRRMP SIRQTLQEMG VKVADVFPEL RQGRRSGAAG PRNGTAPTLL TNYLDTQYFG
EISIGTPPQT FKVVFDTGSA NLWVPSCKCS PLYSACVSHS RYDSSKSRTY IANGTGXAIR
YGTGSVKGFL SQDVVMVSDI PIIQVFAEAT ALPAFPFIFA RFDGVLGMGY PSQAIDGITP
VFDRILSQQI LQEDVFSVYY SRXNAPLKPG GEIILGGSDP AYYTGDFHYL SVSKSGYWQI
SMKGVSVGAE VLFCKEGCSV AIDTGASYIT GPAGPVSVLM KAIGAAEMAE GEESPSRHLC
HGLCSSLQQS QYGEDVCVVA FSGLDIPPPA GPLWILGASF IGHYYTKFDR RNNRIGFATA
R
//
