RENI_CALJA
ID RENI_CALJA Reviewed; 400 AA.
AC Q9TSZ1;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Renin {ECO:0000303|PubMed:10598135};
DE EC=3.4.23.15 {ECO:0000250|UniProtKB:P00797};
DE AltName: Full=Angiotensinogenase;
DE Flags: Precursor;
GN Name=REN;
OS Callithrix jacchus (White-tufted-ear marmoset).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Callitrichinae; Callithrix; Callithrix.
OX NCBI_TaxID=9483;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10598135; DOI=10.1097/00005344-199912000-00018;
RA Valdenaire O., Breu V., Giller T., Bur D., Fischli W.;
RT "Cloning and characterization of marmoset renin: comparison with human
RT renin.";
RL J. Cardiovasc. Pharmacol. 34:893-897(1999).
CC -!- FUNCTION: Renin is a highly specific endopeptidase, whose only known
CC function is to generate angiotensin I from angiotensinogen in the
CC plasma, initiating a cascade of reactions that produce an elevation of
CC blood pressure and increased sodium retention by the kidney.
CC {ECO:0000250|UniProtKB:P00797}.
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:0000250|UniProtKB:P00797};
CC -!- ACTIVITY REGULATION: Interaction with ATP6AP2 results in a 5-fold
CC increased efficiency in angiotensinogen processing.
CC {ECO:0000250|UniProtKB:P00797}.
CC -!- SUBUNIT: Interacts with ATP6AP2. {ECO:0000250|UniProtKB:P00797}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P00797}. Membrane
CC {ECO:0000250|UniProtKB:P00797}. Note=Associated to membranes via
CC binding to ATP6AP2. {ECO:0000250|UniProtKB:P00797}.
CC -!- SIMILARITY: Belongs to the peptidase A1 family. {ECO:0000305}.
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 EMBL; AJ132342; CAB64879.1; -; mRNA.
DR RefSeq; XP_008983729.1; XM_008985481.2.
DR AlphaFoldDB; Q9TSZ1; -.
DR SMR; Q9TSZ1; -.
DR STRING; 9483.ENSCJAP00000031097; -.
DR ChEMBL; CHEMBL6056; -.
DR DrugCentral; Q9TSZ1; -.
DR MEROPS; A01.007; -.
DR Ensembl; ENSCJAT00000061949; ENSCJAP00000046960; ENSCJAG00000016857.
DR GeneID; 100399036; -.
DR KEGG; cjc:100399036; -.
DR CTD; 5972; -.
DR eggNOG; KOG1339; Eukaryota.
DR GeneTree; ENSGT00940000157898; -.
DR HOGENOM; CLU_013253_3_3_1; -.
DR InParanoid; Q9TSZ1; -.
DR OrthoDB; 1619495at2759; -.
DR PRO; PR:Q9TSZ1; -.
DR Proteomes; UP000008225; Chromosome 19.
DR GO; GO:0045177; C:apical part of cell; IEA:Ensembl.
DR GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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 CDD; cd05487; renin_like; 1.
DR Gene3D; 2.40.70.10; -; 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; PTHR47966; 1.
DR Pfam; PF07966; A1_Propeptide; 1.
DR Pfam; PF00026; Asp; 1.
DR PRINTS; PR00792; PEPSIN.
DR SUPFAM; SSF50630; SSF50630; 1.
DR PROSITE; PS00141; ASP_PROTEASE; 2.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 2: Evidence at transcript level;
KW Aspartyl protease; Disulfide bond; Glycoprotein; Hydrolase; Membrane;
KW Protease; Reference proteome; Secreted; Signal; Zymogen.
FT SIGNAL 1..23
FT /evidence="ECO:0000250|UniProtKB:P00797"
FT PROPEP 24..60
FT /note="Activation peptide"
FT /evidence="ECO:0000250|UniProtKB:P00797"
FT /id="PRO_0000026077"
FT CHAIN 61..400
FT /note="Renin"
FT /id="PRO_0000026078"
FT DOMAIN 80..397
FT /note="Peptidase A1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT ACT_SITE 98
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT ACT_SITE 286
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT CARBOHYD 65
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 135
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 111..118
FT /evidence="ECO:0000250|UniProtKB:P00797"
FT DISULFID 277..281
FT /evidence="ECO:0000250|UniProtKB:P00797"
FT DISULFID 319..356
FT /evidence="ECO:0000250|UniProtKB:P00797"
SQ SEQUENCE 400 AA; 44038 MW; 31769217035615FA CRC64;
MDAWRGMPRW GLLLLLWGSC TFGLPTETTT FKRISLKRMP SIRESLKERG VDMARLGPER
MALVNITSSV ILTNYMDTQY YGEIGIGTPP QTFKVVFDTG SSNVWVPSSK CSRLYTACVY
HKLFDASDSS SYKHNGTELT LRYSTGTVSG FLSQDVITVG GITVTQTFGE VTEMPALPFM
LAEFDGVVGM GFSEQAIGKV TPLFDNIISQ GLLKEDVFSF YYNRDSENSQ SLGGQIVLGG
SDPQHYEGNF HYINLIRTGL WQIPMKGVSV GSSTLLCEDG CLALVDTGAS YISGSTSSIE
KLMEALGAKK RLFDYVVKCN EGPTLPDISF HLGGKEYTLT SADYVFQESY SSKKLCTLAI
HAMDIPPPTG PTWALGATFI RKFYTEFDRG NNRIGFALAR
