ID F7BKI2_HORSE Unreviewed; 404 AA.
AC F7BKI2;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2023, sequence version 4.
DT 27-MAR-2024, entry version 75.
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:ENSECAP00000016896.4,
GN ECO:0000313|VGNC:VGNC:22299};
OS Equus caballus (Horse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX NCBI_TaxID=9796 {ECO:0000313|Ensembl:ENSECAP00000016896.4, ECO:0000313|Proteomes:UP000002281};
RN [1] {ECO:0000313|Ensembl:ENSECAP00000016896.4, ECO:0000313|Proteomes:UP000002281}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000016896.4,
RC ECO:0000313|Proteomes:UP000002281};
RX PubMed=19892987; DOI=10.1126/science.1178158;
RG Broad Institute Genome Sequencing Platform;
RG Broad Institute Whole Genome Assembly Team;
RA Wade C.M., Giulotto E., Sigurdsson S., Zoli M., Gnerre S., Imsland F.,
RA Lear T.L., Adelson D.L., Bailey E., Bellone R.R., Bloecker H., Distl O.,
RA Edgar R.C., Garber M., Leeb T., Mauceli E., MacLeod J.N., Penedo M.C.T.,
RA Raison J.M., Sharpe T., Vogel J., Andersson L., Antczak D.F., Biagi T.,
RA Binns M.M., Chowdhary B.P., Coleman S.J., Della Valle G., Fryc S.,
RA Guerin G., Hasegawa T., Hill E.W., Jurka J., Kiialainen A., Lindgren G.,
RA Liu J., Magnani E., Mickelson J.R., Murray J., Nergadze S.G., Onofrio R.,
RA Pedroni S., Piras M.F., Raudsepp T., Rocchi M., Roeed K.H., Ryder O.A.,
RA Searle S., Skow L., Swinburne J.E., Syvaenen A.C., Tozaki T., Valberg S.J.,
RA Vaudin M., White J.R., Zody M.C., Lander E.S., Lindblad-Toh K.;
RT "Genome sequence, comparative analysis, and population genetics of the
RT domestic horse.";
RL Science 326:865-867(2009).
RN [2] {ECO:0000313|Ensembl:ENSECAP00000016896.4}
RP IDENTIFICATION.
RC STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000016896.4};
RG Ensembl;
RL Submitted (NOV-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 -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
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 AlphaFoldDB; F7BKI2; -.
DR STRING; 9796.ENSECAP00000016896; -.
DR MEROPS; A01.008; -.
DR PaxDb; 9796-ENSECAP00000016896; -.
DR Ensembl; ENSECAT00000020572.4; ENSECAP00000016896.4; ENSECAG00000019104.4.
DR VGNC; VGNC:22299; REN.
DR GeneTree; ENSGT00940000157898; -.
DR HOGENOM; CLU_013253_3_3_1; -.
DR InParanoid; F7BKI2; -.
DR OMA; KMPSIRD; -.
DR OrthoDB; 1120702at2759; -.
DR TreeFam; TF314990; -.
DR Proteomes; UP000002281; Chromosome 5.
DR Bgee; ENSECAG00000019104; Expressed in leukocyte and 7 other cell types or tissues.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0002003; P:angiotensin maturation; IBA:GO_Central.
DR CDD; cd05487; renin_like; 1.
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 InterPro; IPR034135; Renin-like_dom.
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:UP000002281};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..404
FT /note="renin"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5040327786"
FT DOMAIN 86..401
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 104
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 289
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT DISULFID 117..124
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT DISULFID 280..284
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT DISULFID 323..360
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ SEQUENCE 404 AA; 44641 MW; 9E9FB4FD27B50027 CRC64;
MNQRSRMPRW GLLLVLWGSY AFGLPADTGA FRRIFLRKMP SVRESLRERG VDVSRIGAEW
SQFTKRLSRD NSTSPVVLTN YLDTQYYGEI GIGTPPQTFK VIFDTGSANL WVPSTKCSPL
YAACEIHSLY DSSESSSYME NGTEFTIRYG SGKVKGFLSQ DMVTVGGITV TQTFAEVTEL
PLIPFMLAKF DGVLGMGFPA QAVGGVTPVF DHILSQRVLK EDVFSVYYSR NSHLLGGEIV
LGGSDPQYYQ GNFHYVSVSK TDSWQIKMKG VSVRSATLLC EEGCMVVVDT GASYISGPTS
SLRLLMETLG AKELSSDEYV VNCNQVPTLP DISFHLGGRA YTLTSADYVL QDPYSNDDLC
TLALHGLDVP PPTGPVWVLG ASFIRKFYTE FDRHNNRIGF ALAR
//
