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Renin-1 (EC 3.4.23.15) (Angiotensinogenase) (Kidney renin)

 RENI1_MOUSE             Reviewed;         402 AA.
P06281; P97911; Q543E5; Q62153; Q62154;
01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
01-JAN-1988, sequence version 1.
20-JUN-2018, entry version 174.
RecName: Full=Renin-1;
EC=3.4.23.15;
AltName: Full=Angiotensinogenase;
AltName: Full=Kidney renin;
Flags: Precursor;
Name=Ren1; Synonyms=Ren, Ren-1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=BALB/cJ;
PubMed=6370686;
Holm I., Ollo R., Panthier J.-J., Rougeon F.;
"Evolution of aspartyl proteases by gene duplication: the mouse renin
gene is organized in two homologous clusters of four exons.";
EMBO J. 3:557-562(1984).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=BALB/cJ; TISSUE=Kidney;
PubMed=2685761; DOI=10.1093/nar/17.22.9279;
Kim W.S., Murakami K., Nakayama K.;
"Nucleotide sequence of a cDNA coding for mouse Ren1 preprorenin.";
Nucleic Acids Res. 17:9480-9480(1989).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE REN-1D), AND VARIANTS
ARG-58; ILE-68; VAL-160; ASP-315 AND TYR-352.
STRAIN=C57BL/10, and DBA/2J;
PubMed=2691339; DOI=10.1016/0378-1119(89)90143-1;
Burt D.W., Mullins L.J., George H., Smith G., Brooks J., Pioli D.,
Brammar W.J.;
"The nucleotide sequence of a mouse renin-encoding gene, Ren-1d, and
its upstream region.";
Gene 84:91-104(1989).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Kidney;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Kidney;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-30.
TISSUE=Kidney;
PubMed=6089205; DOI=10.1073/pnas.81.17.5489;
Panthier J.-J., Dreyfus M., Roux D.T.L., Rougeon F.;
"Mouse kidney and submaxillary gland renin genes differ in their 5'
putative regulatory sequences.";
Proc. Natl. Acad. Sci. U.S.A. 81:5489-5493(1984).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-31.
PubMed=6392850; DOI=10.1128/MCB.4.11.2321;
Field L.J., Philbrick W.M., Howles P.N., Dickinson D.P., McGowan R.A.,
Gross K.W.;
"Expression of tissue-specific Ren-1 and Ren-2 genes of mice:
comparative analysis of 5'-proximal flanking regions.";
Mol. Cell. Biol. 4:2321-2331(1984).
[8]
PROTEIN SEQUENCE OF 22-37 AND 72-80.
STRAIN=C57BL/10ROS X C3H/HEROS; TISSUE=Kidney;
PubMed=9030738; DOI=10.1111/j.1432-1033.1997.0181a.x;
Jones C.A., Petrovic N., Novak E.K., Swank R.T., Sigmund C.D.,
Gross K.W.;
"Biosynthesis of renin in mouse kidney tumor As4.1 cells.";
Eur. J. Biochem. 243:181-190(1997).
[9]
NUCLEOTIDE SEQUENCE OF 269-316, AND VARIANT ASP-315.
STRAIN=DBA/2J; TISSUE=Submandibular gland;
PubMed=6327270;
Mullins J.J., Burt D.W., Windass J.D., McTurk P., George H.,
Brammar W.J.;
"Molecular cloning of two distinct renin genes from the DBA/2 mouse.";
EMBO J. 1:1461-1466(1982).
[10]
VARIANT [LARGE SCALE ANALYSIS] TYR-352, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Kidney;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: Renin is a highly specific endopeptidase, whose only
known function is to generate angiotensin I from angiotensinogen
in the plasma, initiating a cascade of reactions that produce an
elevation of blood pressure and increased sodium retention by the
kidney.
-!- CATALYTIC ACTIVITY: Cleavage of Leu-|-Xaa bond in angiotensinogen
to generate angiotensin I.
-!- ENZYME REGULATION: Interaction with ATP6AP2 results in a 5-fold
increased efficiency in angiotensinogen processing. {ECO:0000250}.
-!- SUBUNIT: Interacts with ATP6AP2. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Membrane
{ECO:0000250}. Note=Associated to membranes via binding to
ATP6AP2. {ECO:0000250}.
-!- TISSUE SPECIFICITY: Kidney.
-!- INDUCTION: Renal renin is synthesized by the juxtaglomerular cells
of the kidney in response to decreased blood pressure and sodium
concentration.
-!- POLYMORPHISM: In inbred mouse strains, there are at least two
alleles which can occur at the Ren1 locus: Ren-1D and Ren-1C. The
sequence shown is that of Ren-1C.
-!- POLYMORPHISM: Present as a single-copy gene in strains such as
BALB/c and C57BL/6 while some strains such as Swiss and Akr
contain two copies.
-!- SIMILARITY: Belongs to the peptidase A1 family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; X00810; CAA25391.1; -; Genomic_DNA.
EMBL; X00811; CAA25391.1; JOINED; Genomic_DNA.
EMBL; X00812; CAA25391.1; JOINED; Genomic_DNA.
EMBL; X00813; CAA25391.1; JOINED; Genomic_DNA.
EMBL; X00814; CAA25391.1; JOINED; Genomic_DNA.
EMBL; X00815; CAA25391.1; JOINED; Genomic_DNA.
EMBL; X00816; CAA25391.1; JOINED; Genomic_DNA.
EMBL; X00850; CAA25391.1; JOINED; Genomic_DNA.
EMBL; X00851; CAA25391.1; JOINED; Genomic_DNA.
EMBL; X16642; CAA34636.1; -; mRNA.
EMBL; K02596; AAA40045.1; -; Genomic_DNA.
EMBL; M32352; AAA40043.1; -; Genomic_DNA.
EMBL; AK052685; BAC35094.1; -; mRNA.
EMBL; AK085309; BAC39418.1; -; mRNA.
EMBL; BC061053; AAH61053.1; -; mRNA.
EMBL; K02800; AAA40044.1; -; Genomic_DNA.
EMBL; M34190; AAA40042.1; -; Genomic_DNA.
CCDS; CCDS15295.1; -.
PIR; A00989; REMSK.
RefSeq; NP_112469.1; NM_031192.3.
UniGene; Mm.220955; -.
PDB; 5MKT; X-ray; 3.20 A; A=22-402.
PDBsum; 5MKT; -.
ProteinModelPortal; P06281; -.
SMR; P06281; -.
IntAct; P06281; 1.
MINT; P06281; -.
STRING; 10090.ENSMUSP00000092135; -.
BindingDB; P06281; -.
ChEMBL; CHEMBL2615; -.
PhosphoSitePlus; P06281; -.
MaxQB; P06281; -.
PaxDb; P06281; -.
PeptideAtlas; P06281; -.
PRIDE; P06281; -.
Ensembl; ENSMUST00000094556; ENSMUSP00000092135; ENSMUSG00000070645.
GeneID; 19701; -.
KEGG; mmu:19701; -.
UCSC; uc007cqf.1; mouse.
CTD; 19701; -.
MGI; MGI:97898; Ren1.
eggNOG; KOG1339; Eukaryota.
eggNOG; ENOG410XNV7; LUCA.
GeneTree; ENSGT00760000118929; -.
HOGENOM; HOG000197681; -.
HOVERGEN; HBG000482; -.
InParanoid; P06281; -.
KO; K01380; -.
OMA; LGKYYTE; -.
OrthoDB; EOG091G0JP7; -.
PhylomeDB; P06281; -.
TreeFam; TF314990; -.
Reactome; R-MMU-2022377; Metabolism of Angiotensinogen to Angiotensins.
PRO; PR:P06281; -.
Proteomes; UP000000589; Chromosome 1.
Bgee; ENSMUSG00000070645; -.
CleanEx; MM_REN1; -.
ExpressionAtlas; P06281; baseline and differential.
Genevisible; P06281; MM.
GO; GO:0045177; C:apical part of cell; ISO:MGI.
GO; GO:0005737; C:cytoplasm; ISO:MGI.
GO; GO:0005615; C:extracellular space; IDA:MGI.
GO; GO:0005622; C:intracellular; IDA:MGI.
GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
GO; GO:0004190; F:aspartic-type endopeptidase activity; ISO:MGI.
GO; GO:0004175; F:endopeptidase activity; IDA:MGI.
GO; GO:0005159; F:insulin-like growth factor receptor binding; ISO:MGI.
GO; GO:0008233; F:peptidase activity; ISO:MGI.
GO; GO:0005102; F:signaling receptor binding; ISO:MGI.
GO; GO:0050435; P:amyloid-beta metabolic process; IEA:Ensembl.
GO; GO:0002003; P:angiotensin maturation; IMP:MGI.
GO; GO:0048469; P:cell maturation; IMP:MGI.
GO; GO:0035690; P:cellular response to drug; IEA:Ensembl.
GO; GO:0042756; P:drinking behavior; IMP:MGI.
GO; GO:0009755; P:hormone-mediated signaling pathway; IDA:MGI.
GO; GO:0001822; P:kidney development; ISO:MGI.
GO; GO:0008584; P:male gonad development; IEP:UniProtKB.
GO; GO:0001823; P:mesonephros development; IEP:UniProtKB.
GO; GO:0006508; P:proteolysis; ISO:MGI.
GO; GO:0008217; P:regulation of blood pressure; ISO:MGI.
GO; GO:0002016; P:regulation of blood volume by renin-angiotensin; IMP:MGI.
GO; GO:0043408; P:regulation of MAPK cascade; ISO:MGI.
GO; GO:0002018; P:renin-angiotensin regulation of aldosterone production; IDA:MGI.
GO; GO:0051591; P:response to cAMP; ISO:MGI.
GO; GO:0070305; P:response to cGMP; ISO:MGI.
GO; GO:0042493; P:response to drug; ISO:MGI.
GO; GO:0035902; P:response to immobilization stress; IEA:Ensembl.
GO; GO:0032496; P:response to lipopolysaccharide; IEA:Ensembl.
GO; GO:0010033; P:response to organic substance; IDA:MGI.
CDD; cd05487; renin_like; 1.
Gene3D; 2.40.70.10; -; 2.
InterPro; IPR001461; Aspartic_peptidase_A1.
InterPro; IPR001969; Aspartic_peptidase_AS.
InterPro; IPR012848; Aspartic_peptidase_N.
InterPro; IPR033121; PEPTIDASE_A1.
InterPro; IPR021109; Peptidase_aspartic_dom_sf.
InterPro; IPR034135; Renin-like_dom.
PANTHER; PTHR13683; PTHR13683; 1.
Pfam; PF07966; A1_Propeptide; 1.
Pfam; PF00026; Asp; 1.
PRINTS; PR00792; PEPSIN.
SUPFAM; SSF50630; SSF50630; 1.
PROSITE; PS00141; ASP_PROTEASE; 2.
PROSITE; PS51767; PEPTIDASE_A1; 1.
1: Evidence at protein level;
3D-structure; Aspartyl protease; Complete proteome;
Direct protein sequencing; Disulfide bond; Glycoprotein; Hydrolase;
Membrane; Polymorphism; Protease; Reference proteome; Secreted;
Signal; Zymogen.
SIGNAL 1 21 {ECO:0000269|PubMed:9030738}.
PROPEP 22 71 Activation peptide.
{ECO:0000269|PubMed:9030738}.
/FTId=PRO_0000026089.
CHAIN 72 402 Renin-1.
/FTId=PRO_0000026090.
DOMAIN 84 399 Peptidase A1. {ECO:0000255|PROSITE-
ProRule:PRU01103}.
ACT_SITE 102 102 {ECO:0000255|PROSITE-ProRule:PRU10094}.
ACT_SITE 287 287 {ECO:0000255|PROSITE-ProRule:PRU10094}.
CARBOHYD 69 69 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 139 139 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 320 320 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 115 122 {ECO:0000250}.
DISULFID 278 282 {ECO:0000250}.
VARIANT 58 58 W -> R (in allele Ren-1D).
{ECO:0000269|PubMed:2691339}.
VARIANT 68 68 T -> I (in allele Ren-1D).
{ECO:0000269|PubMed:2691339}.
VARIANT 160 160 S -> V (in allele Ren-1D; requires 2
nucleotide substitutions).
{ECO:0000269|PubMed:2691339}.
VARIANT 315 315 E -> D (in allele Ren-1D).
{ECO:0000269|PubMed:2691339,
ECO:0000269|PubMed:6327270}.
VARIANT 352 352 N -> Y (in allele Ren-1D).
{ECO:0000244|PubMed:21183079,
ECO:0000269|PubMed:2691339}.
CONFLICT 6 23 Missing (in Ref. 1). {ECO:0000305}.
CONFLICT 24 24 T -> I (in Ref. 1). {ECO:0000305}.
CONFLICT 163 163 V -> VSRV (in Ref. 1). {ECO:0000305}.
HELIX 40 47 {ECO:0000244|PDB:5MKT}.
STRAND 84 90 {ECO:0000244|PDB:5MKT}.
TURN 91 94 {ECO:0000244|PDB:5MKT}.
STRAND 95 104 {ECO:0000244|PDB:5MKT}.
STRAND 108 112 {ECO:0000244|PDB:5MKT}.
HELIX 120 123 {ECO:0000244|PDB:5MKT}.
HELIX 130 132 {ECO:0000244|PDB:5MKT}.
STRAND 137 145 {ECO:0000244|PDB:5MKT}.
STRAND 148 150 {ECO:0000244|PDB:5MKT}.
STRAND 152 163 {ECO:0000244|PDB:5MKT}.
STRAND 166 177 {ECO:0000244|PDB:5MKT}.
HELIX 180 183 {ECO:0000244|PDB:5MKT}.
STRAND 190 193 {ECO:0000244|PDB:5MKT}.
HELIX 207 214 {ECO:0000244|PDB:5MKT}.
STRAND 217 226 {ECO:0000244|PDB:5MKT}.
STRAND 235 241 {ECO:0000244|PDB:5MKT}.
HELIX 244 246 {ECO:0000244|PDB:5MKT}.
STRAND 248 255 {ECO:0000244|PDB:5MKT}.
STRAND 258 266 {ECO:0000244|PDB:5MKT}.
STRAND 269 271 {ECO:0000244|PDB:5MKT}.
STRAND 274 277 {ECO:0000244|PDB:5MKT}.
STRAND 282 285 {ECO:0000244|PDB:5MKT}.
STRAND 292 294 {ECO:0000244|PDB:5MKT}.
HELIX 297 305 {ECO:0000244|PDB:5MKT}.
STRAND 330 334 {ECO:0000244|PDB:5MKT}.
STRAND 337 341 {ECO:0000244|PDB:5MKT}.
STRAND 369 371 {ECO:0000244|PDB:5MKT}.
STRAND 373 376 {ECO:0000244|PDB:5MKT}.
HELIX 379 384 {ECO:0000244|PDB:5MKT}.
STRAND 385 390 {ECO:0000244|PDB:5MKT}.
TURN 391 394 {ECO:0000244|PDB:5MKT}.
STRAND 395 400 {ECO:0000244|PDB:5MKT}.
SEQUENCE 402 AA; 44343 MW; D42920B555E97A38 CRC64;
MDRRRMPLWA LLLLWSPCTF SLPTRTATFE RIPLKKMPSV REILEERGVD MTRLSAEWGV
FTKRPSLTNL TSPVVLTNYL NTQYYGEIGI GTPPQTFKVI FDTGSANLWV PSTKCSRLYL
ACGIHSLYES SDSSSYMENG SDFTIHYGSG RVKGFLSQDS VTVGGITVTQ TFGEVTELPL
IPFMLAKFDG VLGMGFPAQA VGGVTPVFDH ILSQGVLKEE VFSVYYNRGS HLLGGEVVLG
GSDPQHYQGN FHYVSISKTD SWQITMKGVS VGSSTLLCEE GCAVVVDTGS SFISAPTSSL
KLIMQALGAK EKRIEEYVVN CSQVPTLPDI SFDLGGRAYT LSSTDYVLQY PNRRDKLCTL
ALHAMDIPPP TGPVWVLGAT FIRKFYTEFD RHNNRIGFAL AR


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