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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)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei104 – 1041
    Active sitei292 – 2921

    GO - Molecular functioni

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

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Aspartyl protease, Hydrolase, Protease

    Enzyme and pathway databases

    BRENDAi3.4.23.15. 2681.
    ReactomeiREACT_147707. Metabolism of Angiotensinogen to Angiotensins.

    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
    ProteomesiUP000005640 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)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti104 – 1041D → N in RTD. 1 Publication
    VAR_035088
    Natural varianti230 – 2301R → K in RTD. 1 Publication
    VAR_035087
    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)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti16 – 161L → R in HNFJ2; affects ER translocation and processing of nascent preprorenin, resulting in abolished prorenin and renin biosynthesis and secretion. 1 Publication
    VAR_063770

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

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

    Chemistry

    DrugBankiDB00212. Remikiren.

    Polymorphism and mutation databases

    BioMutaiREN.
    DMDMi132326.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 23231 PublicationAdd
    BLAST
    Propeptidei24 – 6643Activation peptide1 PublicationPRO_0000026081Add
    BLAST
    Chaini67 – 406340ReninPRO_0000026082Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi71 – 711N-linked (GlcNAc...)
    Disulfide bondi117 ↔ 1241 Publication
    Glycosylationi141 – 1411N-linked (GlcNAc...)
    Disulfide bondi283 ↔ 2871 Publication
    Disulfide bondi325 ↔ 3621 Publication

    Keywords - PTMi

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

    Proteomic databases

    PaxDbiP00797.
    PRIDEiP00797.

    PTM databases

    PhosphoSiteiP00797.
    UniCarbKBiP00797.

    Miscellaneous databases

    PMAP-CutDBP00797.

    Expressioni

    Gene expression databases

    BgeeiP00797.
    CleanExiHS_REN.
    GenevisibleiP00797. HS.

    Organism-specific databases

    HPAiCAB025903.
    HPA005131.

    Interactioni

    Subunit structurei

    Interacts with ATP6AP2.2 Publications

    Protein-protein interaction databases

    BioGridi111904. 3 interactions.
    DIPiDIP-59219N.
    IntActiP00797. 1 interaction.
    MINTiMINT-1381167.
    STRINGi9606.ENSP00000272190.

    Structurei

    Secondary structure

    1
    406
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi33 – 353Combined sources
    Helixi42 – 498Combined sources
    Helixi53 – 564Combined sources
    Beta strandi59 – 613Combined sources
    Beta strandi74 – 818Combined sources
    Turni82 – 843Combined sources
    Beta strandi85 – 928Combined sources
    Turni93 – 964Combined sources
    Beta strandi97 – 1048Combined sources
    Beta strandi110 – 1145Combined sources
    Helixi119 – 1213Combined sources
    Helixi122 – 1254Combined sources
    Helixi132 – 1343Combined sources
    Beta strandi139 – 14911Combined sources
    Beta strandi152 – 16514Combined sources
    Beta strandi168 – 17912Combined sources
    Helixi182 – 1854Combined sources
    Beta strandi189 – 1957Combined sources
    Helixi199 – 2013Combined sources
    Helixi203 – 2053Combined sources
    Helixi209 – 2157Combined sources
    Beta strandi219 – 22810Combined sources
    Beta strandi233 – 2364Combined sources
    Beta strandi240 – 2467Combined sources
    Helixi249 – 2513Combined sources
    Beta strandi252 – 2609Combined sources
    Beta strandi262 – 2665Combined sources
    Beta strandi268 – 2714Combined sources
    Beta strandi274 – 2763Combined sources
    Beta strandi279 – 2824Combined sources
    Turni284 – 2863Combined sources
    Beta strandi287 – 2915Combined sources
    Beta strandi296 – 3005Combined sources
    Helixi302 – 31211Combined sources
    Beta strandi315 – 3173Combined sources
    Beta strandi318 – 3203Combined sources
    Beta strandi321 – 3244Combined sources
    Helixi325 – 3306Combined sources
    Beta strandi334 – 3385Combined sources
    Beta strandi341 – 3455Combined sources
    Helixi347 – 3504Combined sources
    Beta strandi360 – 3689Combined sources
    Turni373 – 3753Combined sources
    Beta strandi379 – 3813Combined sources
    Helixi383 – 3864Combined sources
    Beta strandi389 – 3946Combined sources
    Turni395 – 3984Combined sources
    Beta strandi399 – 4057Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    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. Positions 29-406.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP00797.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase A1 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG248684.
    GeneTreeiENSGT00760000118929.
    HOGENOMiHOG000197681.
    HOVERGENiHBG000482.
    InParanoidiP00797.
    KOiK01380.
    OMAiNFIARYY.
    OrthoDBiEOG7HQN88.
    PhylomeDBiP00797.
    TreeFamiTF314990.

    Family and domain databases

    Gene3Di2.40.70.10. 2 hits.
    InterProiIPR001461. Aspartic_peptidase.
    IPR001969. Aspartic_peptidase_AS.
    IPR012848. Aspartic_peptidase_N.
    IPR021109. Peptidase_aspartic_dom.
    [Graphical view]
    PANTHERiPTHR13683. PTHR13683. 1 hit.
    PfamiPF07966. A1_Propeptide. 1 hit.
    PF00026. Asp. 1 hit.
    [Graphical view]
    PRINTSiPR00792. PEPSIN.
    SUPFAMiSSF50630. SSF50630. 1 hit.
    PROSITEiPS00141. ASP_PROTEASE. 2 hits.
    [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)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti55 – 551R → S in AAA60364 (PubMed:3530608).Curated
    Sequence conflicti189 – 1891E → Q in AAA60364 (PubMed:3530608).Curated
    Sequence conflicti304 – 3041S → C in AAA60364 (PubMed:3530608).Curated
    Sequence conflicti351 – 3511V → I (PubMed:6138751).Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti16 – 161L → R in HNFJ2; affects ER translocation and processing of nascent preprorenin, resulting in abolished prorenin and renin biosynthesis and secretion. 1 Publication
    VAR_063770
    Natural varianti33 – 331R → W.
    Corresponds to variant rs11571098 [ dbSNP | Ensembl ].
    VAR_020375
    Natural varianti104 – 1041D → N in RTD. 1 Publication
    VAR_035088
    Natural varianti160 – 1601Q → K.
    Corresponds to variant rs11571083 [ dbSNP | Ensembl ].
    VAR_029171
    Natural varianti217 – 2171G → R.
    Corresponds to variant rs11571117 [ dbSNP | Ensembl ].
    VAR_020376
    Natural varianti230 – 2301R → K in RTD. 1 Publication
    VAR_035087

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei231 – 2333Missing in isoform 2. CuratedVSP_012899

    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.2. 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
    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. Positions 29-406.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi111904. 3 interactions.
    DIPiDIP-59219N.
    IntActiP00797. 1 interaction.
    MINTiMINT-1381167.
    STRINGi9606.ENSP00000272190.

    Chemistry

    BindingDBiP00797.
    ChEMBLiCHEMBL286.
    DrugBankiDB00212. Remikiren.
    GuidetoPHARMACOLOGYi2413.

    Protein family/group databases

    MEROPSiA01.007.

    PTM databases

    PhosphoSiteiP00797.
    UniCarbKBiP00797.

    Polymorphism and mutation databases

    BioMutaiREN.
    DMDMi132326.

    Proteomic databases

    PaxDbiP00797.
    PRIDEiP00797.

    Protocols and materials databases

    DNASUi5972.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000272190; ENSP00000272190; ENSG00000143839. [P00797-1]
    GeneIDi5972.
    KEGGihsa:5972.
    UCSCiuc001haq.2. human. [P00797-1]

    Organism-specific databases

    CTDi5972.
    GeneCardsiGC01M204123.
    GeneReviewsiREN.
    HGNCiHGNC:9958. REN.
    HPAiCAB025903.
    HPA005131.
    MIMi179820. gene.
    267430. phenotype.
    613092. phenotype.
    neXtProtiNX_P00797.
    Orphaneti217330. Hyperuricemia - anemia - renal failure.
    97369. Renal tubular dysgenesis of genetic origin.
    PharmGKBiPA297.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiNOG248684.
    GeneTreeiENSGT00760000118929.
    HOGENOMiHOG000197681.
    HOVERGENiHBG000482.
    InParanoidiP00797.
    KOiK01380.
    OMAiNFIARYY.
    OrthoDBiEOG7HQN88.
    PhylomeDBiP00797.
    TreeFamiTF314990.

    Enzyme and pathway databases

    BRENDAi3.4.23.15. 2681.
    ReactomeiREACT_147707. Metabolism of Angiotensinogen to Angiotensins.

    Miscellaneous databases

    EvolutionaryTraceiP00797.
    GeneWikiiRenin.
    GenomeRNAii5972.
    NextBioi23249.
    PMAP-CutDBP00797.
    PROiP00797.
    SOURCEiSearch...

    Gene expression databases

    BgeeiP00797.
    CleanExiHS_REN.
    GenevisibleiP00797. HS.

    Family and domain databases

    Gene3Di2.40.70.10. 2 hits.
    InterProiIPR001461. Aspartic_peptidase.
    IPR001969. Aspartic_peptidase_AS.
    IPR012848. Aspartic_peptidase_N.
    IPR021109. Peptidase_aspartic_dom.
    [Graphical view]
    PANTHERiPTHR13683. PTHR13683. 1 hit.
    PfamiPF07966. A1_Propeptide. 1 hit.
    PF00026. Asp. 1 hit.
    [Graphical view]
    PRINTSiPR00792. PEPSIN.
    SUPFAMiSSF50630. SSF50630. 1 hit.
    PROSITEiPS00141. ASP_PROTEASE. 2 hits.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
    2. "New possibilities for intracellular renin and inactive renin now that the structure of the human renin gene has been elucidated."
      Morris B.J.
      Clin. Sci. 71:345-355(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 2).
    3. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Tissue: Fetal liver.
    4. Rieder M.J., da Ponte S.H., Kuldanek S.A., Rajkumar N., Smith J.D., Toth E.J., Krauss R.M., Nickerson D.A.
      Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    5. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    6. NIEHS SNPs program
      Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    7. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Colon and Ovary.
    9. "Molecular cloning and nucleotide sequence of a human renin cDNA fragment."
      Soubrier F., Panthier J.-J., Corvol P., Rougeon F.
      Nucleic Acids Res. 11:7181-7190(1983) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 108-406 (ISOFORM 1).
    10. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-33.
    11. "Identification of negative and positive regulatory elements in the human renin gene."
      Burt D.W., Nakamura N., Kelley P., Dzau V.J.
      J. Biol. Chem. 264:7357-7362(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-33.
    12. "Segmental homology between the promoter region of the human renin gene and the mouse ren1 and ren2 promoter regions."
      Soubrier F., Panthier J.J., Houot A.-M., Rougeon F., Corvol P.
      Gene 41:85-92(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-33.
    13. "Isolation and characterization of recombinant human prorenin in Chinese hamster ovary cells."
      Ishizuka Y., Shoda A., Yoshida S., Kawamura Y., Haraguchi K., Murakami K.
      J. Biochem. 109:30-35(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 24-42 AND 67-86.
    14. "Pivotal role of the renin/prorenin receptor in angiotensin II production and cellular responses to renin."
      Nguyen G., Delarue F., Burckle C., Bouzhir L., Giller T., Sraer J.-D.
      J. Clin. Invest. 109:1417-1427(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ATP6AP2, CHARACTERIZATION.
    15. "Structure of recombinant human renin, a target for cardiovascular-active drugs, at 2.5-A resolution."
      Sielecki A.R., Hayakawa K., Fujinaga M., Murphy M.E.P., Fraser M., Muir A.K., Carilli C.T., Lewicki J.A., Baxter J.D., James M.N.G.
      Science 243:1346-1351(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
    16. Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
    17. Cited for: X-RAY CRYSTALLOGRAPHY (4.33 ANGSTROMS) OF 24-406 OF MUTANT ALA-292 IN COMPLEX WITH ANGIOTENSINOGEN, DISULFIDE BONDS.
    18. Cited for: VARIANTS RTD ASN-104 AND LYS-230.
    19. Cited for: VARIANT HNFJ2 ARG-16, CHARACTERIZATION OF VARIANT HNFJ2 ARG-16.

    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: June 24, 2015
    This is version 188 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

    External Data

    Dasty 3

    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 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.