RENI_RAT
ID RENI_RAT Reviewed; 402 AA.
AC P08424; Q63497;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Renin {ECO:0000303|PubMed:3287330};
DE EC=3.4.23.15 {ECO:0000250|UniProtKB:P00797};
DE AltName: Full=Angiotensinogenase;
DE Flags: Precursor;
GN Name=Ren1; Synonyms=Ren;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley;
RX PubMed=3287330; DOI=10.1093/nar/16.8.3576;
RA Tada M., Fukamizu A., Seo M.S., Takahashi S., Murakami K.;
RT "Nucleotide sequence of rat renin cDNA.";
RL Nucleic Acids Res. 16:3576-3576(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3039496; DOI=10.1073/pnas.84.16.5605;
RA Burnham C.E., Hawelu-Johnson C.L., Frank B.M., Lynch K.R.;
RT "Molecular cloning of rat renin cDNA and its gene.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:5605-5609(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley;
RX PubMed=3047403; DOI=10.1016/0022-2836(88)90151-9;
RA Fukamizu A., Nishi K., Cho T., Saitoh M., Nakayama K., Ohkubo H.,
RA Nakanishi S., Murakami K.;
RT "Structure of the rat renin gene.";
RL J. Mol. Biol. 201:443-450(1988).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8490598; DOI=10.3109/10641969309041632;
RA Alam K.Y., Wang Y., Dene H., Rapp J.P.;
RT "Renin gene nucleotide sequence of coding and regulatory regions in Dahl
RT rats.";
RL Clin. Exp. Hypertens. 15:599-614(1993).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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}.
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DR EMBL; X07033; CAA30082.1; -; mRNA.
DR EMBL; J02941; AAA42030.1; -; mRNA.
DR EMBL; M37278; AAA42031.1; ALT_SEQ; Genomic_DNA.
DR EMBL; S60054; AAP13916.1; -; mRNA.
DR EMBL; BC078878; AAH78878.1; -; mRNA.
DR PIR; A29991; RERTK.
DR RefSeq; NP_036774.4; NM_012642.4.
DR PDB; 5MLG; X-ray; 2.60 A; A=22-402.
DR PDBsum; 5MLG; -.
DR AlphaFoldDB; P08424; -.
DR SMR; P08424; -.
DR BioGRID; 246843; 1.
DR STRING; 10116.ENSRNOP00000003951; -.
DR BindingDB; P08424; -.
DR ChEMBL; CHEMBL2322; -.
DR DrugCentral; P08424; -.
DR MEROPS; A01.008; -.
DR GlyGen; P08424; 3 sites.
DR PhosphoSitePlus; P08424; -.
DR PaxDb; P08424; -.
DR DNASU; 24715; -.
DR Ensembl; ENSRNOT00000003951; ENSRNOP00000003951; ENSRNOG00000002937.
DR GeneID; 24715; -.
DR KEGG; rno:24715; -.
DR UCSC; RGD:3554; rat.
DR CTD; 5972; -.
DR RGD; 3554; Ren1.
DR eggNOG; KOG1339; Eukaryota.
DR GeneTree; ENSGT00940000157898; -.
DR HOGENOM; CLU_013253_3_3_1; -.
DR InParanoid; P08424; -.
DR OMA; SWQITMK; -.
DR OrthoDB; 1619495at2759; -.
DR PhylomeDB; P08424; -.
DR TreeFam; TF314990; -.
DR Reactome; R-RNO-2022377; Metabolism of Angiotensinogen to Angiotensins.
DR PRO; PR:P08424; -.
DR Proteomes; UP000002494; Chromosome 13.
DR Bgee; ENSRNOG00000002937; Expressed in kidney and 9 other tissues.
DR ExpressionAtlas; P08424; baseline and differential.
DR Genevisible; P08424; RN.
DR GO; GO:0045177; C:apical part of cell; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005615; C:extracellular space; IDA:RGD.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; ISO:RGD.
DR GO; GO:0004175; F:endopeptidase activity; IDA:RGD.
DR GO; GO:0005159; F:insulin-like growth factor receptor binding; IDA:RGD.
DR GO; GO:0008233; F:peptidase activity; ISO:RGD.
DR GO; GO:0005102; F:signaling receptor binding; IPI:RGD.
DR GO; GO:0050435; P:amyloid-beta metabolic process; IEP:RGD.
DR GO; GO:0002003; P:angiotensin maturation; IDA:RGD.
DR GO; GO:0048469; P:cell maturation; ISO:RGD.
DR GO; GO:0071466; P:cellular response to xenobiotic stimulus; IEP:RGD.
DR GO; GO:0042756; P:drinking behavior; ISO:RGD.
DR GO; GO:0009755; P:hormone-mediated signaling pathway; ISO:RGD.
DR GO; GO:0001822; P:kidney development; ISO:RGD.
DR GO; GO:0008584; P:male gonad development; ISO:RGD.
DR GO; GO:0001823; P:mesonephros development; ISO:RGD.
DR GO; GO:0006508; P:proteolysis; ISO:RGD.
DR GO; GO:0008217; P:regulation of blood pressure; IMP:RGD.
DR GO; GO:0002016; P:regulation of blood volume by renin-angiotensin; ISO:RGD.
DR GO; GO:0043408; P:regulation of MAPK cascade; ISO:RGD.
DR GO; GO:0002018; P:renin-angiotensin regulation of aldosterone production; ISO:RGD.
DR GO; GO:0051591; P:response to cAMP; IDA:RGD.
DR GO; GO:0070305; P:response to cGMP; IDA:RGD.
DR GO; GO:0035902; P:response to immobilization stress; IEP:RGD.
DR GO; GO:0032496; P:response to lipopolysaccharide; IEP:RGD.
DR GO; GO:0010033; P:response to organic substance; ISO:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IDA:RGD.
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; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR InterPro; IPR034135; Renin-like_dom.
DR PANTHER; PTHR47966; PTHR47966; 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 1: Evidence at protein level;
KW 3D-structure; Aspartyl protease; Cleavage on pair of basic residues;
KW Disulfide bond; Glycoprotein; Hydrolase; Membrane; Protease;
KW Reference proteome; Secreted; Signal; Zymogen.
FT SIGNAL 1..26
FT /evidence="ECO:0000305"
FT PROPEP 27..64
FT /note="Activation peptide"
FT /id="PRO_0000026091"
FT CHAIN 65..402
FT /note="Renin"
FT /id="PRO_0000026092"
FT DOMAIN 84..399
FT /note="Peptidase A1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT ACT_SITE 102
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT ACT_SITE 287
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT CARBOHYD 69
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 139
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 320
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 115..122
FT /evidence="ECO:0000250|UniProtKB:P00797"
FT DISULFID 278..282
FT /evidence="ECO:0000250|UniProtKB:P00797"
FT DISULFID 321..358
FT /evidence="ECO:0000250|UniProtKB:P00797"
FT CONFLICT 200
FT /note="A -> V (in Ref. 1; CAA30082)"
FT /evidence="ECO:0000305"
FT CONFLICT 214..215
FT /note="QR -> HE (in Ref. 2; AAA42030)"
FT /evidence="ECO:0000305"
FT CONFLICT 271
FT /note="V -> L (in Ref. 1; CAA30082)"
FT /evidence="ECO:0000305"
FT STRAND 30..36
FT /evidence="ECO:0007829|PDB:5MLG"
FT HELIX 40..46
FT /evidence="ECO:0007829|PDB:5MLG"
FT HELIX 51..58
FT /evidence="ECO:0007829|PDB:5MLG"
FT STRAND 79..81
FT /evidence="ECO:0007829|PDB:5MLG"
FT STRAND 84..90
FT /evidence="ECO:0007829|PDB:5MLG"
FT TURN 91..94
FT /evidence="ECO:0007829|PDB:5MLG"
FT STRAND 95..102
FT /evidence="ECO:0007829|PDB:5MLG"
FT STRAND 108..112
FT /evidence="ECO:0007829|PDB:5MLG"
FT HELIX 120..124
FT /evidence="ECO:0007829|PDB:5MLG"
FT HELIX 130..132
FT /evidence="ECO:0007829|PDB:5MLG"
FT STRAND 137..146
FT /evidence="ECO:0007829|PDB:5MLG"
FT STRAND 151..163
FT /evidence="ECO:0007829|PDB:5MLG"
FT STRAND 166..177
FT /evidence="ECO:0007829|PDB:5MLG"
FT HELIX 180..183
FT /evidence="ECO:0007829|PDB:5MLG"
FT STRAND 190..193
FT /evidence="ECO:0007829|PDB:5MLG"
FT HELIX 197..199
FT /evidence="ECO:0007829|PDB:5MLG"
FT HELIX 201..203
FT /evidence="ECO:0007829|PDB:5MLG"
FT HELIX 207..213
FT /evidence="ECO:0007829|PDB:5MLG"
FT STRAND 217..226
FT /evidence="ECO:0007829|PDB:5MLG"
FT STRAND 235..241
FT /evidence="ECO:0007829|PDB:5MLG"
FT HELIX 244..246
FT /evidence="ECO:0007829|PDB:5MLG"
FT STRAND 247..255
FT /evidence="ECO:0007829|PDB:5MLG"
FT STRAND 261..271
FT /evidence="ECO:0007829|PDB:5MLG"
FT STRAND 274..277
FT /evidence="ECO:0007829|PDB:5MLG"
FT STRAND 282..286
FT /evidence="ECO:0007829|PDB:5MLG"
FT STRAND 292..295
FT /evidence="ECO:0007829|PDB:5MLG"
FT HELIX 297..307
FT /evidence="ECO:0007829|PDB:5MLG"
FT STRAND 316..318
FT /evidence="ECO:0007829|PDB:5MLG"
FT HELIX 321..323
FT /evidence="ECO:0007829|PDB:5MLG"
FT STRAND 330..334
FT /evidence="ECO:0007829|PDB:5MLG"
FT STRAND 337..341
FT /evidence="ECO:0007829|PDB:5MLG"
FT TURN 343..345
FT /evidence="ECO:0007829|PDB:5MLG"
FT STRAND 346..348
FT /evidence="ECO:0007829|PDB:5MLG"
FT STRAND 359..364
FT /evidence="ECO:0007829|PDB:5MLG"
FT TURN 369..371
FT /evidence="ECO:0007829|PDB:5MLG"
FT STRAND 373..377
FT /evidence="ECO:0007829|PDB:5MLG"
FT HELIX 379..384
FT /evidence="ECO:0007829|PDB:5MLG"
FT STRAND 385..390
FT /evidence="ECO:0007829|PDB:5MLG"
FT TURN 391..394
FT /evidence="ECO:0007829|PDB:5MLG"
FT STRAND 395..401
FT /evidence="ECO:0007829|PDB:5MLG"
SQ SEQUENCE 402 AA; 44276 MW; E4E22CEE449EAC3F CRC64;
MGGRRMPLWA LLLLWTSCSF SLPTDTASFG RILLKKMPSV REILEERGVD MTRISAEWGE
FIKKSSFTNV TSPVVLTNYL DTQYYGEIGI GTPSQTFKVI FDTGSANLWV PSTKCGPLYT
ACEIHNLYDS SESSSYMENG TEFTIHYGSG KVKGFLSQDV VTVGGIIVTQ TFGEVTELPL
IPFMLAKFDG VLGMGFPAQA VDGVIPVFDH ILSQRVLKEE VFSVYYSRES HLLGGEVVLG
GSDPQHYQGN FHYVSISKAG SWQITMKGVS VGPATLLCEE GCMAVVDTGT SYISGPTSSL
QLIMQALGVK EKRANNYVVN CSQVPTLPDI SFYLGGRTYT LSNMDYVQKN PFRNDDLCIL
ALQGLDIPPP TGPVWVLGAT FIRKFYTEFD RHNNRIGFAL AR
