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P00797

- RENI_HUMAN

UniProt

P00797 - RENI_HUMAN

Protein

Renin

Gene

REN

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 181 (01 Oct 2014)
      Sequence version 1 (01 Jan 1988)
      Previous versions | rss
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    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

    1. aspartic-type endopeptidase activity Source: HGNC
    2. peptidase activity Source: HGNC
    3. receptor binding Source: HGNC

    GO - Biological processi

    1. angiotensin maturation Source: HGNC
    2. beta-amyloid metabolic process Source: Ensembl
    3. cell maturation Source: Ensembl
    4. cellular protein metabolic process Source: Reactome
    5. cellular response to drug Source: Ensembl
    6. drinking behavior Source: Ensembl
    7. hormone-mediated signaling pathway Source: Ensembl
    8. kidney development Source: BHF-UCL
    9. male gonad development Source: Ensembl
    10. mesonephros development Source: Ensembl
    11. proteolysis Source: HGNC
    12. regulation of blood pressure Source: ProtInc
    13. regulation of MAPK cascade Source: HGNC
    14. renin-angiotensin regulation of aldosterone production Source: Ensembl
    15. response to cAMP Source: Ensembl
    16. response to cGMP Source: Ensembl
    17. response to lipopolysaccharide Source: Ensembl

    Keywords - Molecular functioni

    Aspartyl protease, Hydrolase, Protease

    Enzyme and pathway databases

    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: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:9958. REN.

    Subcellular locationi

    Secreted. Membrane
    Note: Associated to membranes via binding to ATP6AP2.

    GO - Cellular componenti

    1. extracellular region Source: Reactome
    2. extracellular space Source: HGNC
    3. intracellular Source: Ensembl
    4. plasma membrane Source: Reactome

    Keywords - Cellular componenti

    Membrane, Secreted

    Pathology & Biotechi

    Involvement in diseasei

    Renal tubular dysgenesis (RTD) [MIM:267430]: Autosomal 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).1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    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) [MIM:613092]: A renal disease characterized by juvenile onset of hyperuricemia, slowly progressive renal failure and anemia.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    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.

    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

    ArrayExpressiP00797.
    BgeeiP00797.
    CleanExiHS_REN.
    GenevestigatoriP00797.

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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[»]
    ProteinModelPortaliP00797.
    SMRiP00797. Positions 30-406.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP00797.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase A1 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG248684.
    HOGENOMiHOG000197681.
    HOVERGENiHBG000482.
    KOiK01380.
    OMAiIARYYTE.
    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. Align

    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

    MDGWRRMPRW GLLLLLWGSC TFGLPTDTTT FKRIFLKRMP SIRESLKERG    50
    VDMARLGPEW SQPMKRLTLG NTTSSVILTN YMDTQYYGEI GIGTPPQTFK 100
    VVFDTGSSNV WVPSSKCSRL YTACVYHKLF DASDSSSYKH NGTELTLRYS 150
    TGTVSGFLSQ DIITVGGITV TQMFGEVTEM PALPFMLAEF DGVVGMGFIE 200
    QAIGRVTPIF DNIISQGVLK EDVFSFYYNR DSENSQSLGG QIVLGGSDPQ 250
    HYEGNFHYIN LIKTGVWQIQ MKGVSVGSST LLCEDGCLAL VDTGASYISG 300
    STSSIEKLME ALGAKKRLFD YVVKCNEGPT LPDISFHLGG KEYTLTSADY 350
    VFQESYSSKK LCTLAIHAMD IPPPTGPTWA LGATFIRKFY TEFDRRNNRI 400
    GFALAR 406
    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:
    EMBL
    GenBank
    DDBJ
    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]

    Polymorphism databases

    DMDMi132326.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Wikipedia

    Renin entry

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS30981.1. [P00797-1 ]
    PIRi A21454. REHUK.
    RefSeqi NP_000528.1. NM_000537.3. [P00797-1 ]
    UniGenei Hs.3210.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1BBS X-ray 2.80 A/B 67-406 [» ]
    1BIL X-ray 2.40 A/B 70-406 [» ]
    1BIM X-ray 2.80 A/B 70-406 [» ]
    1HRN X-ray 1.80 A/B 70-406 [» ]
    1RNE X-ray 2.40 A 67-406 [» ]
    2BKS X-ray 2.20 A/B 67-406 [» ]
    2BKT X-ray 2.30 A/B 67-406 [» ]
    2FS4 X-ray 2.20 A/B 74-406 [» ]
    2G1N X-ray 2.90 A/B 74-406 [» ]
    2G1O X-ray 2.70 A/B 74-406 [» ]
    2G1R X-ray 2.42 A/B 74-406 [» ]
    2G1S X-ray 2.50 A/B 74-406 [» ]
    2G1Y X-ray 2.50 A/B 74-406 [» ]
    2G20 X-ray 2.40 A/B 74-406 [» ]
    2G21 X-ray 2.20 A/B 74-406 [» ]
    2G22 X-ray 2.50 A/B 74-406 [» ]
    2G24 X-ray 1.90 A/B 74-406 [» ]
    2G26 X-ray 2.10 A/B 74-406 [» ]
    2G27 X-ray 2.90 A/B 74-406 [» ]
    2I4Q X-ray 2.30 A/B 73-406 [» ]
    2IKO X-ray 1.90 A/B 67-406 [» ]
    2IKU X-ray 2.60 A/B 67-406 [» ]
    2IL2 X-ray 2.24 A/B 67-406 [» ]
    2REN X-ray 2.50 A 67-406 [» ]
    2V0Z X-ray 2.20 C/O 67-406 [» ]
    2V10 X-ray 3.10 C/O 67-406 [» ]
    2V11 X-ray 3.10 C/O 67-406 [» ]
    2V12 X-ray 3.20 C/O 67-406 [» ]
    2V13 X-ray 2.80 A 67-406 [» ]
    2V16 X-ray 2.80 C/O 67-406 [» ]
    2X0B X-ray 4.33 A/C/E/G 24-406 [» ]
    3D91 X-ray 2.20 A/B 67-406 [» ]
    3G6Z X-ray 2.00 A/B 67-406 [» ]
    3G70 X-ray 2.00 A/B 67-406 [» ]
    3G72 X-ray 1.90 A/B 67-406 [» ]
    3GW5 X-ray 2.00 A/B 70-406 [» ]
    3K1W X-ray 1.50 A/B 67-406 [» ]
    3KM4 X-ray 1.90 A/B 70-406 [» ]
    3O9L X-ray 2.40 A/C 67-232 [» ]
    B/D 237-406 [» ]
    3OAD X-ray 2.17 A/C 67-232 [» ]
    B/D 237-406 [» ]
    3OAG X-ray 2.30 A/C 67-232 [» ]
    B/D 237-406 [» ]
    3OOT X-ray 2.55 A/B 67-406 [» ]
    3OQF X-ray 2.78 A/B 67-406 [» ]
    3OQK X-ray 2.90 A/B 67-406 [» ]
    3OWN X-ray 2.00 A/B 67-406 [» ]
    3Q3T X-ray 2.60 A/B 67-406 [» ]
    3Q4B X-ray 2.19 A/B 67-406 [» ]
    3Q5H X-ray 2.16 A/B 67-406 [» ]
    3SFC X-ray 2.10 A/B 67-406 [» ]
    3VCM X-ray 2.93 A/B 67-406 [» ]
    P/Q 24-66 [» ]
    3VSW X-ray 3.00 A/B 67-406 [» ]
    3VSX X-ray 2.80 A/B 67-406 [» ]
    3VUC X-ray 2.60 A/B 67-406 [» ]
    3VYD X-ray 2.81 A/B 67-406 [» ]
    3VYE X-ray 2.70 A/B 67-406 [» ]
    3VYF X-ray 2.80 A/B 67-406 [» ]
    4AMT X-ray 2.60 A 24-406 [» ]
    4GJ5 X-ray 2.40 A/B 67-406 [» ]
    4GJ6 X-ray 2.58 A/B 67-406 [» ]
    4GJ7 X-ray 2.80 A/B 67-406 [» ]
    4GJ8 X-ray 2.50 A/B 67-406 [» ]
    4GJ9 X-ray 2.60 A/B 67-406 [» ]
    4GJA X-ray 2.60 A/B 67-406 [» ]
    4GJB X-ray 2.75 A/B 67-406 [» ]
    4GJC X-ray 2.40 A/B 67-406 [» ]
    4GJD X-ray 2.65 A/B 67-406 [» ]
    ProteinModelPortali P00797.
    SMRi P00797. Positions 30-406.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111904. 3 interactions.
    DIPi DIP-59219N.
    IntActi P00797. 1 interaction.
    MINTi MINT-1381167.
    STRINGi 9606.ENSP00000272190.

    Chemistry

    BindingDBi P00797.
    ChEMBLi CHEMBL286.
    DrugBanki DB01258. Aliskiren.
    DB00212. Remikiren.
    GuidetoPHARMACOLOGYi 2413.

    Protein family/group databases

    MEROPSi A01.007.

    PTM databases

    PhosphoSitei P00797.
    UniCarbKBi P00797.

    Polymorphism databases

    DMDMi 132326.

    Proteomic databases

    PaxDbi P00797.
    PRIDEi P00797.

    Protocols and materials databases

    DNASUi 5972.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000272190 ; ENSP00000272190 ; ENSG00000143839 . [P00797-1 ]
    GeneIDi 5972.
    KEGGi hsa:5972.
    UCSCi uc001haq.2. human. [P00797-1 ]

    Organism-specific databases

    CTDi 5972.
    GeneCardsi GC01M204123.
    GeneReviewsi REN.
    HGNCi HGNC:9958. REN.
    HPAi CAB025903.
    HPA005131.
    MIMi 179820. gene.
    267430. phenotype.
    613092. phenotype.
    neXtProti NX_P00797.
    Orphaneti 217330. Hyperuricemia - anemia - renal failure.
    97369. Renal tubular dysgenesis of genetic origin.
    PharmGKBi PA297.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG248684.
    HOGENOMi HOG000197681.
    HOVERGENi HBG000482.
    KOi K01380.
    OMAi IARYYTE.
    OrthoDBi EOG7HQN88.
    PhylomeDBi P00797.
    TreeFami TF314990.

    Enzyme and pathway databases

    Reactomei REACT_147707. Metabolism of Angiotensinogen to Angiotensins.

    Miscellaneous databases

    EvolutionaryTracei P00797.
    GeneWikii Renin.
    GenomeRNAii 5972.
    NextBioi 23249.
    PMAP-CutDB P00797.
    PROi P00797.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P00797.
    Bgeei P00797.
    CleanExi HS_REN.
    Genevestigatori P00797.

    Family and domain databases

    Gene3Di 2.40.70.10. 2 hits.
    InterProi IPR001461. Aspartic_peptidase.
    IPR001969. Aspartic_peptidase_AS.
    IPR012848. Aspartic_peptidase_N.
    IPR021109. Peptidase_aspartic_dom.
    [Graphical view ]
    PANTHERi PTHR13683. PTHR13683. 1 hit.
    Pfami PF07966. A1_Propeptide. 1 hit.
    PF00026. Asp. 1 hit.
    [Graphical view ]
    PRINTSi PR00792. PEPSIN.
    SUPFAMi SSF50630. SSF50630. 1 hit.
    PROSITEi PS00141. ASP_PROTEASE. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 181 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