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Protein

Renin

Gene

REN

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 activityi

Cleavage of Leu-|-Xaa bond in angiotensinogen to generate angiotensin I.

Enzyme regulationi

Interaction with ATP6AP2 results in a 5-fold increased efficiency in angiotensinogen processing.

Kineticsi

  1. KM=1 µM for angiotensinogen (in absence of ATP6AP2)
  2. KM=0.15 µM for angiotensinogen (in presence of membrane-bound ATP6AP2)

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Active sitei1041
    Active sitei2921

    GO - Molecular functioni

    • aspartic-type endopeptidase activity Source: HGNC
    • peptidase activity Source: HGNC
    • receptor binding Source: HGNC

    GO - Biological processi

    • angiotensin maturation Source: HGNC
    • beta-amyloid metabolic process Source: Ensembl
    • cell maturation Source: Ensembl
    • cellular response to drug Source: Ensembl
    • drinking behavior Source: Ensembl
    • hormone-mediated signaling pathway Source: Ensembl
    • kidney development Source: BHF-UCL
    • male gonad development Source: Ensembl
    • mesonephros development Source: Ensembl
    • proteolysis Source: HGNC
    • regulation of blood pressure Source: ProtInc
    • regulation of MAPK cascade Source: HGNC
    • renin-angiotensin regulation of aldosterone production Source: Ensembl
    • response to cAMP Source: Ensembl
    • response to cGMP Source: Ensembl
    • response to immobilization stress Source: Ensembl
    • response to lipopolysaccharide Source: Ensembl
    Complete GO annotation...

    Keywords - Molecular functioni

    Aspartyl protease, Hydrolase, Protease

    Enzyme and pathway databases

    BioCyciZFISH:HS07113-MONOMER.
    BRENDAi3.4.23.15. 2681.
    ReactomeiR-HSA-2022377. Metabolism of Angiotensinogen to Angiotensins.
    SIGNORiP00797.

    Protein family/group databases

    MEROPSiA01.007.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Renin (EC:3.4.23.15)
    Alternative name(s):
    Angiotensinogenase
    Gene namesi
    Name:REN
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    Proteomesi
    • UP000005640 Componenti: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:9958. REN.

    Subcellular locationi

    GO - Cellular componenti

    • extracellular region Source: Reactome
    • extracellular space Source: HGNC
    • lysosome Source: GO_Central
    • plasma membrane Source: Reactome
    Complete GO annotation...

    Keywords - Cellular componenti

    Membrane, Secreted

    Pathology & Biotechi

    Involvement in diseasei

    Renal tubular dysgenesis (RTD)1 Publication
    The disease is caused by mutations affecting the gene represented in this entry.
    Disease descriptionAutosomal recessive severe disorder of renal tubular development characterized by persistent fetal anuria and perinatal death, probably due to pulmonary hypoplasia from early-onset oligohydramnios (the Potter phenotype).
    See also OMIM:267430
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Natural variantiVAR_035088104D → N in RTD. 1 Publication1
    Natural variantiVAR_035087230R → K in RTD. 1 PublicationCorresponds to variant rs121917742dbSNPEnsembl.1
    Familial juvenile hyperuricemic nephropathy 2 (HNFJ2)1 Publication
    The disease is caused by mutations affecting the gene represented in this entry.
    Disease descriptionA renal disease characterized by juvenile onset of hyperuricemia, slowly progressive renal failure and anemia.
    See also OMIM:613092
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Natural variantiVAR_06377016L → R in HNFJ2; affects ER translocation and processing of nascent preprorenin, resulting in abolished prorenin and renin biosynthesis and secretion. 1 PublicationCorresponds to variant rs121917743dbSNPEnsembl.1

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    DisGeNETi5972.
    MalaCardsiREN.
    MIMi267430. phenotype.
    613092. phenotype.
    OpenTargetsiENSG00000143839.
    Orphaneti217330. Hyperuricemia - anemia - renal failure.
    97369. Renal tubular dysgenesis of genetic origin.
    PharmGKBiPA297.

    Chemistry databases

    ChEMBLiCHEMBL286.
    DrugBankiDB09026. Aliskiren.
    DB00212. Remikiren.
    GuidetoPHARMACOLOGYi2413.

    Polymorphism and mutation databases

    BioMutaiREN.
    DMDMi132326.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Signal peptidei1 – 231 PublicationAdd BLAST23
    PropeptideiPRO_000002608124 – 66Activation peptide1 PublicationAdd BLAST43
    ChainiPRO_000002608267 – 406ReninAdd BLAST340

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Glycosylationi71N-linked (GlcNAc...)1
    Disulfide bondi117 ↔ 1241 Publication
    Glycosylationi141N-linked (GlcNAc...)1
    Disulfide bondi283 ↔ 2871 Publication
    Disulfide bondi325 ↔ 3621 Publication

    Keywords - PTMi

    Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, Zymogen

    Proteomic databases

    PaxDbiP00797.
    PeptideAtlasiP00797.
    PRIDEiP00797.

    PTM databases

    iPTMnetiP00797.
    PhosphoSitePlusiP00797.
    UniCarbKBiP00797.

    Miscellaneous databases

    PMAP-CutDBP00797.

    Expressioni

    Gene expression databases

    BgeeiENSG00000143839.
    CleanExiHS_REN.
    GenevisibleiP00797. HS.

    Organism-specific databases

    HPAiCAB025903.
    HPA005131.

    Interactioni

    Subunit structurei

    Interacts with ATP6AP2.2 Publications

    GO - Molecular functioni

    • receptor binding Source: HGNC

    Protein-protein interaction databases

    BioGridi111904. 5 interactors.
    DIPiDIP-59219N.
    IntActiP00797. 2 interactors.
    MINTiMINT-1381167.
    STRINGi9606.ENSP00000272190.

    Chemistry databases

    BindingDBiP00797.

    Structurei

    Secondary structure

    1406
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi33 – 35Combined sources3
    Helixi42 – 49Combined sources8
    Helixi53 – 56Combined sources4
    Beta strandi59 – 61Combined sources3
    Beta strandi74 – 81Combined sources8
    Turni82 – 84Combined sources3
    Beta strandi85 – 92Combined sources8
    Turni93 – 96Combined sources4
    Beta strandi97 – 104Combined sources8
    Beta strandi110 – 114Combined sources5
    Helixi119 – 121Combined sources3
    Helixi122 – 125Combined sources4
    Helixi132 – 134Combined sources3
    Beta strandi139 – 149Combined sources11
    Beta strandi152 – 165Combined sources14
    Beta strandi168 – 179Combined sources12
    Helixi182 – 185Combined sources4
    Beta strandi189 – 195Combined sources7
    Helixi199 – 201Combined sources3
    Helixi203 – 205Combined sources3
    Helixi209 – 215Combined sources7
    Beta strandi219 – 228Combined sources10
    Beta strandi233 – 236Combined sources4
    Beta strandi240 – 246Combined sources7
    Helixi249 – 251Combined sources3
    Beta strandi252 – 260Combined sources9
    Beta strandi262 – 266Combined sources5
    Beta strandi268 – 271Combined sources4
    Beta strandi274 – 276Combined sources3
    Beta strandi279 – 282Combined sources4
    Turni284 – 286Combined sources3
    Beta strandi287 – 291Combined sources5
    Beta strandi296 – 300Combined sources5
    Helixi302 – 312Combined sources11
    Beta strandi315 – 317Combined sources3
    Beta strandi318 – 320Combined sources3
    Beta strandi321 – 324Combined sources4
    Helixi325 – 330Combined sources6
    Beta strandi334 – 338Combined sources5
    Beta strandi341 – 345Combined sources5
    Helixi347 – 350Combined sources4
    Beta strandi360 – 368Combined sources9
    Turni373 – 375Combined sources3
    Beta strandi379 – 381Combined sources3
    Helixi383 – 386Combined sources4
    Beta strandi389 – 394Combined sources6
    Turni395 – 398Combined sources4
    Beta strandi399 – 405Combined sources7

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1BBSX-ray2.80A/B67-406[»]
    1BILX-ray2.40A/B70-406[»]
    1BIMX-ray2.80A/B70-406[»]
    1HRNX-ray1.80A/B70-406[»]
    1RNEX-ray2.40A67-406[»]
    2BKSX-ray2.20A/B67-406[»]
    2BKTX-ray2.30A/B67-406[»]
    2FS4X-ray2.20A/B74-406[»]
    2G1NX-ray2.90A/B74-406[»]
    2G1OX-ray2.70A/B74-406[»]
    2G1RX-ray2.42A/B74-406[»]
    2G1SX-ray2.50A/B74-406[»]
    2G1YX-ray2.50A/B74-406[»]
    2G20X-ray2.40A/B74-406[»]
    2G21X-ray2.20A/B74-406[»]
    2G22X-ray2.50A/B74-406[»]
    2G24X-ray1.90A/B74-406[»]
    2G26X-ray2.10A/B74-406[»]
    2G27X-ray2.90A/B74-406[»]
    2I4QX-ray2.30A/B73-406[»]
    2IKOX-ray1.90A/B67-406[»]
    2IKUX-ray2.60A/B67-406[»]
    2IL2X-ray2.24A/B67-406[»]
    2RENX-ray2.50A67-406[»]
    2V0ZX-ray2.20C/O67-406[»]
    2V10X-ray3.10C/O67-406[»]
    2V11X-ray3.10C/O67-406[»]
    2V12X-ray3.20C/O67-406[»]
    2V13X-ray2.80A67-406[»]
    2V16X-ray2.80C/O67-406[»]
    2X0BX-ray4.33A/C/E/G24-406[»]
    3D91X-ray2.20A/B67-406[»]
    3G6ZX-ray2.00A/B67-406[»]
    3G70X-ray2.00A/B67-406[»]
    3G72X-ray1.90A/B67-406[»]
    3GW5X-ray2.00A/B70-406[»]
    3K1WX-ray1.50A/B67-406[»]
    3KM4X-ray1.90A/B70-406[»]
    3O9LX-ray2.40A/C67-232[»]
    B/D237-406[»]
    3OADX-ray2.17A/C67-232[»]
    B/D237-406[»]
    3OAGX-ray2.30A/C67-232[»]
    B/D237-406[»]
    3OOTX-ray2.55A/B67-406[»]
    3OQFX-ray2.78A/B67-406[»]
    3OQKX-ray2.90A/B67-406[»]
    3OWNX-ray2.00A/B67-406[»]
    3Q3TX-ray2.60A/B67-406[»]
    3Q4BX-ray2.19A/B67-406[»]
    3Q5HX-ray2.16A/B67-406[»]
    3SFCX-ray2.10A/B67-406[»]
    3VCMX-ray2.93A/B67-406[»]
    P/Q24-66[»]
    3VSWX-ray3.00A/B67-406[»]
    3VSXX-ray2.80A/B67-406[»]
    3VUCX-ray2.60A/B67-406[»]
    3VYDX-ray2.81A/B67-406[»]
    3VYEX-ray2.70A/B67-406[»]
    3VYFX-ray2.80A/B67-406[»]
    4AMTX-ray2.60A24-406[»]
    4GJ5X-ray2.40A/B67-406[»]
    4GJ6X-ray2.58A/B67-406[»]
    4GJ7X-ray2.80A/B67-406[»]
    4GJ8X-ray2.50A/B67-406[»]
    4GJ9X-ray2.60A/B67-406[»]
    4GJAX-ray2.60A/B67-406[»]
    4GJBX-ray2.75A/B67-406[»]
    4GJCX-ray2.40A/B67-406[»]
    4GJDX-ray2.65A/B67-406[»]
    4PYVX-ray2.65A/B67-406[»]
    4Q1NX-ray2.09A/B67-406[»]
    4RYCX-ray2.45A/B67-406[»]
    4RYGX-ray2.65A/B67-406[»]
    4RZ1X-ray2.60A/B67-406[»]
    4S1GX-ray2.10A/B67-406[»]
    4XX3X-ray2.40A/B67-406[»]
    4XX4X-ray2.40A/B67-406[»]
    ProteinModelPortaliP00797.
    SMRiP00797.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP00797.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Domaini86 – 403Peptidase A1PROSITE-ProRule annotationAdd BLAST318

    Sequence similaritiesi

    Belongs to the peptidase A1 family.Curated
    Contains 1 peptidase A1 domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiKOG1339. Eukaryota.
    ENOG410XNV7. LUCA.
    GeneTreeiENSGT00760000118929.
    HOGENOMiHOG000197681.
    HOVERGENiHBG000482.
    InParanoidiP00797.
    KOiK01380.
    OMAiKNSENSH.
    OrthoDBiEOG091G0JP7.
    PhylomeDBiP00797.
    TreeFamiTF314990.

    Family and domain databases

    Gene3Di2.40.70.10. 2 hits.
    InterProiIPR001461. Aspartic_peptidase_A1.
    IPR001969. Aspartic_peptidase_AS.
    IPR012848. Aspartic_peptidase_N.
    IPR033121. PEPTIDASE_A1.
    IPR021109. Peptidase_aspartic_dom.
    [Graphical view]
    PfamiPF07966. A1_Propeptide. 1 hit.
    PF00026. Asp. 1 hit.
    [Graphical view]
    PRINTSiPR00792. PEPSIN.
    SUPFAMiSSF50630. SSF50630. 1 hit.
    PROSITEiPS00141. ASP_PROTEASE. 2 hits.
    PS51767. PEPTIDASE_A1. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

    Isoform 1 (identifier: P00797-1) [UniParc]FASTAAdd to basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

            10         20         30         40         50
    MDGWRRMPRW GLLLLLWGSC TFGLPTDTTT FKRIFLKRMP SIRESLKERG
    60 70 80 90 100
    VDMARLGPEW SQPMKRLTLG NTTSSVILTN YMDTQYYGEI GIGTPPQTFK
    110 120 130 140 150
    VVFDTGSSNV WVPSSKCSRL YTACVYHKLF DASDSSSYKH NGTELTLRYS
    160 170 180 190 200
    TGTVSGFLSQ DIITVGGITV TQMFGEVTEM PALPFMLAEF DGVVGMGFIE
    210 220 230 240 250
    QAIGRVTPIF DNIISQGVLK EDVFSFYYNR DSENSQSLGG QIVLGGSDPQ
    260 270 280 290 300
    HYEGNFHYIN LIKTGVWQIQ MKGVSVGSST LLCEDGCLAL VDTGASYISG
    310 320 330 340 350
    STSSIEKLME ALGAKKRLFD YVVKCNEGPT LPDISFHLGG KEYTLTSADY
    360 370 380 390 400
    VFQESYSSKK LCTLAIHAMD IPPPTGPTWA LGATFIRKFY TEFDRRNNRI

    GFALAR
    Length:406
    Mass (Da):45,057
    Last modified:January 1, 1988 - v1
    Checksum:i5AFDF8E973B21EDA
    GO
    Isoform 2 (identifier: P00797-2) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         231-233: Missing.

    Show »
    Length:403
    Mass (Da):44,726
    Checksum:i4DEF0016D9EF5854
    GO

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Sequence conflicti55R → S in AAA60364 (PubMed:3530608).Curated1
    Sequence conflicti189E → Q in AAA60364 (PubMed:3530608).Curated1
    Sequence conflicti304S → C in AAA60364 (PubMed:3530608).Curated1
    Sequence conflicti351V → I (PubMed:6138751).Curated1

    Natural variant

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Natural variantiVAR_06377016L → R in HNFJ2; affects ER translocation and processing of nascent preprorenin, resulting in abolished prorenin and renin biosynthesis and secretion. 1 PublicationCorresponds to variant rs121917743dbSNPEnsembl.1
    Natural variantiVAR_02037533R → W.Corresponds to variant rs11571098dbSNPEnsembl.1
    Natural variantiVAR_035088104D → N in RTD. 1 Publication1
    Natural variantiVAR_029171160Q → K.Corresponds to variant rs11571083dbSNPEnsembl.1
    Natural variantiVAR_020376217G → R.Corresponds to variant rs11571117dbSNPEnsembl.1
    Natural variantiVAR_035087230R → K in RTD. 1 PublicationCorresponds to variant rs121917742dbSNPEnsembl.1

    Alternative sequence

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Alternative sequenceiVSP_012899231 – 233Missing in isoform 2. Curated3

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    L00073
    , L00064, L00065, L00066, L00067, L00068, L00069, L00070, L00071, L00072 Genomic DNA. Translation: AAA60363.1.
    M26901, M26899, M26900 Genomic DNA. Translation: AAA60364.1.
    M10152
    , M10030, M10128, M10150, M10151 Genomic DNA. Translation: AAD03461.1.
    AY436324 Genomic DNA. Translation: AAR03502.1.
    CR536498 mRNA. Translation: CAG38737.1.
    EU332871 Genomic DNA. Translation: ABY87560.1.
    AL592114, AL592146 Genomic DNA. Translation: CAH71224.1.
    AL592146, AL592114 Genomic DNA. Translation: CAI16594.1.
    BC033474 mRNA. Translation: AAH33474.1.
    BC047752 mRNA. Translation: AAH47752.1.
    M15410 Genomic DNA. Translation: AAA60263.1.
    M26440 Genomic DNA. Translation: AAA60365.1.
    M13253 Genomic DNA. Translation: AAA60262.1.
    CCDSiCCDS30981.1. [P00797-1]
    PIRiA21454. REHUK.
    RefSeqiNP_000528.1. NM_000537.3. [P00797-1]
    UniGeneiHs.3210.

    Genome annotation databases

    EnsembliENST00000272190; ENSP00000272190; ENSG00000143839. [P00797-1]
    GeneIDi5972.
    KEGGihsa:5972.
    UCSCiuc001haq.3. human. [P00797-1]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Wikipedia

    Renin entry

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    L00073
    , L00064, L00065, L00066, L00067, L00068, L00069, L00070, L00071, L00072 Genomic DNA. Translation: AAA60363.1.
    M26901, M26899, M26900 Genomic DNA. Translation: AAA60364.1.
    M10152
    , M10030, M10128, M10150, M10151 Genomic DNA. Translation: AAD03461.1.
    AY436324 Genomic DNA. Translation: AAR03502.1.
    CR536498 mRNA. Translation: CAG38737.1.
    EU332871 Genomic DNA. Translation: ABY87560.1.
    AL592114, AL592146 Genomic DNA. Translation: CAH71224.1.
    AL592146, AL592114 Genomic DNA. Translation: CAI16594.1.
    BC033474 mRNA. Translation: AAH33474.1.
    BC047752 mRNA. Translation: AAH47752.1.
    M15410 Genomic DNA. Translation: AAA60263.1.
    M26440 Genomic DNA. Translation: AAA60365.1.
    M13253 Genomic DNA. Translation: AAA60262.1.
    CCDSiCCDS30981.1. [P00797-1]
    PIRiA21454. REHUK.
    RefSeqiNP_000528.1. NM_000537.3. [P00797-1]
    UniGeneiHs.3210.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1BBSX-ray2.80A/B67-406[»]
    1BILX-ray2.40A/B70-406[»]
    1BIMX-ray2.80A/B70-406[»]
    1HRNX-ray1.80A/B70-406[»]
    1RNEX-ray2.40A67-406[»]
    2BKSX-ray2.20A/B67-406[»]
    2BKTX-ray2.30A/B67-406[»]
    2FS4X-ray2.20A/B74-406[»]
    2G1NX-ray2.90A/B74-406[»]
    2G1OX-ray2.70A/B74-406[»]
    2G1RX-ray2.42A/B74-406[»]
    2G1SX-ray2.50A/B74-406[»]
    2G1YX-ray2.50A/B74-406[»]
    2G20X-ray2.40A/B74-406[»]
    2G21X-ray2.20A/B74-406[»]
    2G22X-ray2.50A/B74-406[»]
    2G24X-ray1.90A/B74-406[»]
    2G26X-ray2.10A/B74-406[»]
    2G27X-ray2.90A/B74-406[»]
    2I4QX-ray2.30A/B73-406[»]
    2IKOX-ray1.90A/B67-406[»]
    2IKUX-ray2.60A/B67-406[»]
    2IL2X-ray2.24A/B67-406[»]
    2RENX-ray2.50A67-406[»]
    2V0ZX-ray2.20C/O67-406[»]
    2V10X-ray3.10C/O67-406[»]
    2V11X-ray3.10C/O67-406[»]
    2V12X-ray3.20C/O67-406[»]
    2V13X-ray2.80A67-406[»]
    2V16X-ray2.80C/O67-406[»]
    2X0BX-ray4.33A/C/E/G24-406[»]
    3D91X-ray2.20A/B67-406[»]
    3G6ZX-ray2.00A/B67-406[»]
    3G70X-ray2.00A/B67-406[»]
    3G72X-ray1.90A/B67-406[»]
    3GW5X-ray2.00A/B70-406[»]
    3K1WX-ray1.50A/B67-406[»]
    3KM4X-ray1.90A/B70-406[»]
    3O9LX-ray2.40A/C67-232[»]
    B/D237-406[»]
    3OADX-ray2.17A/C67-232[»]
    B/D237-406[»]
    3OAGX-ray2.30A/C67-232[»]
    B/D237-406[»]
    3OOTX-ray2.55A/B67-406[»]
    3OQFX-ray2.78A/B67-406[»]
    3OQKX-ray2.90A/B67-406[»]
    3OWNX-ray2.00A/B67-406[»]
    3Q3TX-ray2.60A/B67-406[»]
    3Q4BX-ray2.19A/B67-406[»]
    3Q5HX-ray2.16A/B67-406[»]
    3SFCX-ray2.10A/B67-406[»]
    3VCMX-ray2.93A/B67-406[»]
    P/Q24-66[»]
    3VSWX-ray3.00A/B67-406[»]
    3VSXX-ray2.80A/B67-406[»]
    3VUCX-ray2.60A/B67-406[»]
    3VYDX-ray2.81A/B67-406[»]
    3VYEX-ray2.70A/B67-406[»]
    3VYFX-ray2.80A/B67-406[»]
    4AMTX-ray2.60A24-406[»]
    4GJ5X-ray2.40A/B67-406[»]
    4GJ6X-ray2.58A/B67-406[»]
    4GJ7X-ray2.80A/B67-406[»]
    4GJ8X-ray2.50A/B67-406[»]
    4GJ9X-ray2.60A/B67-406[»]
    4GJAX-ray2.60A/B67-406[»]
    4GJBX-ray2.75A/B67-406[»]
    4GJCX-ray2.40A/B67-406[»]
    4GJDX-ray2.65A/B67-406[»]
    4PYVX-ray2.65A/B67-406[»]
    4Q1NX-ray2.09A/B67-406[»]
    4RYCX-ray2.45A/B67-406[»]
    4RYGX-ray2.65A/B67-406[»]
    4RZ1X-ray2.60A/B67-406[»]
    4S1GX-ray2.10A/B67-406[»]
    4XX3X-ray2.40A/B67-406[»]
    4XX4X-ray2.40A/B67-406[»]
    ProteinModelPortaliP00797.
    SMRiP00797.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi111904. 5 interactors.
    DIPiDIP-59219N.
    IntActiP00797. 2 interactors.
    MINTiMINT-1381167.
    STRINGi9606.ENSP00000272190.

    Chemistry databases

    BindingDBiP00797.
    ChEMBLiCHEMBL286.
    DrugBankiDB09026. Aliskiren.
    DB00212. Remikiren.
    GuidetoPHARMACOLOGYi2413.

    Protein family/group databases

    MEROPSiA01.007.

    PTM databases

    iPTMnetiP00797.
    PhosphoSitePlusiP00797.
    UniCarbKBiP00797.

    Polymorphism and mutation databases

    BioMutaiREN.
    DMDMi132326.

    Proteomic databases

    PaxDbiP00797.
    PeptideAtlasiP00797.
    PRIDEiP00797.

    Protocols and materials databases

    DNASUi5972.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000272190; ENSP00000272190; ENSG00000143839. [P00797-1]
    GeneIDi5972.
    KEGGihsa:5972.
    UCSCiuc001haq.3. human. [P00797-1]

    Organism-specific databases

    CTDi5972.
    DisGeNETi5972.
    GeneCardsiREN.
    GeneReviewsiREN.
    HGNCiHGNC:9958. REN.
    HPAiCAB025903.
    HPA005131.
    MalaCardsiREN.
    MIMi179820. gene.
    267430. phenotype.
    613092. phenotype.
    neXtProtiNX_P00797.
    OpenTargetsiENSG00000143839.
    Orphaneti217330. Hyperuricemia - anemia - renal failure.
    97369. Renal tubular dysgenesis of genetic origin.
    PharmGKBiPA297.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiKOG1339. Eukaryota.
    ENOG410XNV7. LUCA.
    GeneTreeiENSGT00760000118929.
    HOGENOMiHOG000197681.
    HOVERGENiHBG000482.
    InParanoidiP00797.
    KOiK01380.
    OMAiKNSENSH.
    OrthoDBiEOG091G0JP7.
    PhylomeDBiP00797.
    TreeFamiTF314990.

    Enzyme and pathway databases

    BioCyciZFISH:HS07113-MONOMER.
    BRENDAi3.4.23.15. 2681.
    ReactomeiR-HSA-2022377. Metabolism of Angiotensinogen to Angiotensins.
    SIGNORiP00797.

    Miscellaneous databases

    EvolutionaryTraceiP00797.
    GeneWikiiRenin.
    GenomeRNAii5972.
    PMAP-CutDBP00797.
    PROiP00797.
    SOURCEiSearch...

    Gene expression databases

    BgeeiENSG00000143839.
    CleanExiHS_REN.
    GenevisibleiP00797. HS.

    Family and domain databases

    Gene3Di2.40.70.10. 2 hits.
    InterProiIPR001461. Aspartic_peptidase_A1.
    IPR001969. Aspartic_peptidase_AS.
    IPR012848. Aspartic_peptidase_N.
    IPR033121. PEPTIDASE_A1.
    IPR021109. Peptidase_aspartic_dom.
    [Graphical view]
    PfamiPF07966. A1_Propeptide. 1 hit.
    PF00026. Asp. 1 hit.
    [Graphical view]
    PRINTSiPR00792. PEPSIN.
    SUPFAMiSSF50630. SSF50630. 1 hit.
    PROSITEiPS00141. ASP_PROTEASE. 2 hits.
    PS51767. PEPTIDASE_A1. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Entry informationi

    Entry nameiRENI_HUMAN
    AccessioniPrimary (citable) accession number: P00797
    Secondary accession number(s): Q6FI38, Q6T5C2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: January 1, 1988
    Last modified: November 2, 2016
    This is version 200 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. Peptidase families
      Classification of peptidase families and list of entries
    7. SIMILARITY comments
      Index of protein domains and families

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.