ID U6CS53_NEOVI Unreviewed; 404 AA.
AC U6CS53;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 24-JAN-2024, entry version 44.
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=RENI {ECO:0000313|EMBL:CCP72398.1};
OS Neovison vison (American mink) (Mustela vison).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Mustelinae; Neogale.
OX NCBI_TaxID=452646 {ECO:0000313|EMBL:CCP72398.1};
RN [1] {ECO:0000313|EMBL:CCP72398.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Pool of brain {ECO:0000313|EMBL:CCP72398.1};
RA Anistoroaei R., Christensen K.;
RT "An American mink transcriptome.";
RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSNVIP00000021118.1}
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; HAAF01000572; CCP72398.1; -; mRNA.
DR MEROPS; A01.008; -.
DR Ensembl; ENSNVIT00000024607.1; ENSNVIP00000021118.1; ENSNVIG00000016512.1.
DR GeneTree; ENSGT00940000157898; -.
DR OrthoDB; 1120702at2759; -.
DR Proteomes; UP000694425; Unplaced.
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:0048469; P:cell maturation; IEA:Ensembl.
DR GO; GO:0042756; P:drinking behavior; IEA:Ensembl.
DR GO; GO:0009755; P:hormone-mediated signaling pathway; IEA:Ensembl.
DR GO; GO:0008584; P:male gonad development; IEA:Ensembl.
DR GO; GO:0001823; P:mesonephros development; IEA:Ensembl.
DR GO; GO:0043408; P:regulation of MAPK cascade; IEA:Ensembl.
DR GO; GO:0002018; P:renin-angiotensin regulation of aldosterone production; 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; 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 2: Evidence at transcript level;
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:UP000694425};
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_5040664230"
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; 44102 MW; AA0A2AB16395BD3B CRC64;
MAQWSRMPRW GLLLVIWGVC TYGLPADTGA FGRIFLKKMP SIRESLKERG VDVARLGADW
SLFTKRLSFS NGTSPVVLTN YLDTQYYGEI GIGTPPQTFK VIFDTGSANL WVPSTKCSPL
YTACEIHSLY DSSESSSYME NGTAFTIHYG SGKVKGFLSQ DMVTVGGITV TQTFGEVTEL
PLIPFMLAKF DGVLGMGFPA QAVGGVTPVF DHILSQGVLK EDVFSVYYSR DSHLLGGELV
LGGSDPQYYQ GNFHYVSVSQ TGSWQIKMKG VSVRSATVVC EEGCMVVVDT GASYISGPTS
SLRLLMDTLG AKELSTNEYV VNCNQVPTLP DISFHLGGRA YTLTSSDYVL QDSYGNDDLC
TLALHGLDVP PPTGPVWVLG ASFIRKFYTE FDRHNNRIGF ALAR
//
