ID G3USD2_MELGA Unreviewed; 462 AA.
AC G3USD2;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 29-SEP-2021, sequence version 2.
DT 24-JAN-2024, entry version 58.
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};
GN Name=REN {ECO:0000313|Ensembl:ENSMGAP00000018605.2};
OS Meleagris gallopavo (Wild turkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Meleagridinae; Meleagris.
OX NCBI_TaxID=9103 {ECO:0000313|Ensembl:ENSMGAP00000018605.2, ECO:0000313|Proteomes:UP000001645};
RN [1] {ECO:0000313|Ensembl:ENSMGAP00000018605.2, ECO:0000313|Proteomes:UP000001645}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20838655; DOI=10.1371/journal.pbio.1000475;
RA Dalloul R.A., Long J.A., Zimin A.V., Aslam L., Beal K., Blomberg L.A.,
RA Bouffard P., Burt D.W., Crasta O., Crooijmans R.P., Cooper K.,
RA Coulombe R.A., De S., Delany M.E., Dodgson J.B., Dong J.J., Evans C.,
RA Frederickson K.M., Flicek P., Florea L., Folkerts O., Groenen M.A.,
RA Harkins T.T., Herrero J., Hoffmann S., Megens H.J., Jiang A., de Jong P.,
RA Kaiser P., Kim H., Kim K.W., Kim S., Langenberger D., Lee M.K., Lee T.,
RA Mane S., Marcais G., Marz M., McElroy A.P., Modise T., Nefedov M.,
RA Notredame C., Paton I.R., Payne W.S., Pertea G., Prickett D., Puiu D.,
RA Qioa D., Raineri E., Ruffier M., Salzberg S.L., Schatz M.C., Scheuring C.,
RA Schmidt C.J., Schroeder S., Searle S.M., Smith E.J., Smith J.,
RA Sonstegard T.S., Stadler P.F., Tafer H., Tu Z.J., Van Tassell C.P.,
RA Vilella A.J., Williams K.P., Yorke J.A., Zhang L., Zhang H.B., Zhang X.,
RA Zhang Y., Reed K.M.;
RT "Multi-platform next-generation sequencing of the domestic turkey
RT (Meleagris gallopavo): genome assembly and analysis.";
RL PLoS Biol. 8:E1000475-E1000475(2010).
RN [2] {ECO:0000313|Ensembl:ENSMGAP00000018605.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (JUL-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 AlphaFoldDB; G3USD2; -.
DR MEROPS; A01.008; -.
DR Ensembl; ENSMGAT00000019567.2; ENSMGAP00000018605.2; ENSMGAG00000002701.3.
DR GeneTree; ENSGT00940000157898; -.
DR HOGENOM; CLU_013253_3_3_1; -.
DR InParanoid; G3USD2; -.
DR Proteomes; UP000001645; Chromosome 28.
DR Bgee; ENSMGAG00000002701; Expressed in liver and 9 other cell types or tissues.
DR GO; GO:0045177; C:apical part of cell; IEA:Ensembl.
DR GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0005102; F:signaling receptor binding; IEA:Ensembl.
DR GO; GO:0002003; P:angiotensin maturation; IEA:Ensembl.
DR GO; GO:0001822; P:kidney development; IEA:Ensembl.
DR GO; GO:0043408; P:regulation of MAPK cascade; IEA:Ensembl.
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:UP000001645}.
FT DOMAIN 141..459
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 159
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 347
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT DISULFID 170..179
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT DISULFID 338..342
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ SEQUENCE 462 AA; 49850 MW; 74D2CAA6F8F18777 CRC64;
MAQQHLSLHS NLQHDAFHLQ NQRAEPQHIT NPPVCAGYPY STVSPYPRIP LRGRDPAGSC
CHLELGSSRA GRCGLLGVST APSSARRIAL RRMPSIRQTL QEMGVKVSDV FPELRQRRGG
AGGPQNGTAP TLLTNYLDTQ YYGEISIGTP PQTFKVVFDT GSANLWVPSC KCSPLYSACI
SHSRYDSSKS RTYIANGTGF AIRYGTGSVK GFLSQDVVMV SDIPIIQVFA EATVLPAFPF
IFARFDGVLG MGYPSQAIDG ITPVFDRIIS QQILKEDVSP PYVLHSRNAP LKPGGEIILG
GTDPAYYTGD FHYLSISRNG YWQISMKGVS VGAEILFCKE GCSVAIDTGA SYITGPAGPV
SVLMKAIGAA EMTEGEYVVD CEKVPQLPNI SFHLGGKAYT LSGSAYVLRV SCYGEDICVV
ALSGLDVPPP AGPLWILGAS FIGHYYTKFD RRNNRIGFAT AR
//