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Q5VYX0

- RNLS_HUMAN

UniProt

Q5VYX0 - RNLS_HUMAN

Protein

Renalase

Gene

RNLS

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 97 (01 Oct 2014)
      Sequence version 1 (07 Dec 2004)
      Previous versions | rss
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    Functioni

    Catalyzes the oxidation of the less abundant alpha-NAD(P)H isoform to form beta-NAD(P)+. The enzyme hormone is secreted by the kidney, and circulates in blood and modulates cardiac function and systemic blood pressure. Lowers blood pressure in vivo by decreasing cardiac contractility and heart rate and preventing a compensatory increase in peripheral vascular tone, suggesting a causal link to the increased plasma catecholamine and heightened cardiovascular risk. High concentrations of catecholamines activate plasma renalase and promotes its secretion and synthesis.2 Publications

    Catalytic activityi

    Alpha-NAD(P)H + O2 = beta-NAD(P)+ + H2O2.

    Cofactori

    FAD.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei12 – 121FAD
    Binding sitei42 – 421FAD

    GO - Molecular functioni

    1. oxidoreductase activity Source: UniProtKB-KW

    GO - Biological processi

    1. response to epinephrine Source: Ensembl
    2. response to ischemia Source: Ensembl
    3. response to salt Source: Ensembl

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    FAD, Flavoprotein, NAD, NADP

    Enzyme and pathway databases

    BioCyciMetaCyc:G66-32717-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Renalase (EC:1.6.3.5)
    Alternative name(s):
    Monoamine oxidase-C
    Short name:
    MAO-C
    alpha-NAD(P)H oxidase/anomerase
    Gene namesi
    Name:RNLS
    Synonyms:C10orf59
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 10

    Organism-specific databases

    HGNCiHGNC:25641. RNLS.

    Subcellular locationi

    Secreted 1 Publication

    GO - Cellular componenti

    1. extracellular space Source: Ensembl

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA165549084.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1717Sequence AnalysisAdd
    BLAST
    Chaini18 – 342325RenalasePRO_0000019588Add
    BLAST

    Proteomic databases

    PaxDbiQ5VYX0.
    PRIDEiQ5VYX0.

    PTM databases

    PhosphoSiteiQ5VYX0.

    Expressioni

    Tissue specificityi

    Secreted into the blood by the kidney. Highly expressed in the kidney, expressed at lower level in heart, skeletal muscle and small intestine. Its plasma concentration is markedly reduced in patients with end-stage renal disease, as compared with healthy subjects.1 Publication

    Gene expression databases

    ArrayExpressiQ5VYX0.
    BgeeiQ5VYX0.
    CleanExiHS_C10orf59.
    GenevestigatoriQ5VYX0.

    Interactioni

    Protein-protein interaction databases

    BioGridi120609. 1 interaction.
    IntActiQ5VYX0. 1 interaction.

    Structurei

    Secondary structure

    1
    342
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi2 – 76
    Helixi11 – 2111
    Beta strandi28 – 336
    Beta strandi35 – 395
    Helixi41 – 433
    Beta strandi45 – 473
    Beta strandi55 – 595
    Beta strandi63 – 653
    Helixi69 – 724
    Helixi74 – 829
    Beta strandi103 – 1064
    Helixi113 – 12210
    Beta strandi125 – 1295
    Beta strandi132 – 1376
    Beta strandi139 – 14911
    Beta strandi152 – 1598
    Helixi163 – 1664
    Helixi173 – 1764
    Helixi179 – 1868
    Beta strandi193 – 1997
    Beta strandi211 – 2144
    Beta strandi219 – 2268
    Helixi227 – 2304
    Beta strandi241 – 2466
    Helixi248 – 2536
    Turni254 – 2563
    Helixi259 – 27315
    Beta strandi281 – 2888
    Beta strandi292 – 2954
    Beta strandi298 – 3003
    Beta strandi304 – 3074
    Turni308 – 3103
    Beta strandi311 – 3144
    Helixi317 – 3193
    Helixi324 – 33815

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3QJ4X-ray2.50A/B1-342[»]
    ProteinModelPortaliQ5VYX0.
    SMRiQ5VYX0. Positions 1-341.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni61 – 622FAD-binding

    Sequence similaritiesi

    Belongs to the renalase family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG3380.
    HOGENOMiHOG000007721.
    InParanoidiQ5VYX0.
    KOiK18208.
    OMAiGQMTLHH.
    OrthoDBiEOG747PJ6.
    PhylomeDBiQ5VYX0.
    TreeFamiTF332799.

    Family and domain databases

    InterProiIPR002937. Amino_oxidase.
    [Graphical view]
    PfamiPF01593. Amino_oxidase. 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. Align

    Isoform 1 (identifier: Q5VYX0-1) [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

    MAQVLIVGAG MTGSLCAALL RRQTSGPLYL AVWDKAEDSG GRMTTACSPH    50
    NPQCTADLGA QYITCTPHYA KKHQRFYDEL LAYGVLRPLS SPIEGMVMKE 100
    GDCNFVAPQG ISSIIKHYLK ESGAEVYFRH RVTQINLRDD KWEVSKQTGS 150
    PEQFDLIVLT MPVPEILQLQ GDITTLISEC QRQQLEAVSY SSRYALGLFY 200
    EAGTKIDVPW AGQYITSNPC IRFVSIDNKK RNIESSEIGP SLVIHTTVPF 250
    GVTYLEHSIE DVQELVFQQL ENILPGLPQP IATKCQKWRH SQVTNAAANC 300
    PGQMTLHHKP FLACGGDGFT QSNFDGCITS ALCVLEALKN YI 342
    Length:342
    Mass (Da):37,847
    Last modified:December 7, 2004 - v1
    Checksum:i952827FF7926AF48
    GO
    Isoform 2 (identifier: Q5VYX0-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         294-315: TNAAANCPGQMTLHHKPFLACG → PSAGVILGCAKSPWMMAIGFPI
         316-342: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:315
    Mass (Da):34,949
    Checksum:i8C1EBF93073E4690
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti37 – 371E → D.1 Publication
    Corresponds to variant rs2296545 [ dbSNP | Ensembl ].
    VAR_023310

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei294 – 31522TNAAA…FLACG → PSAGVILGCAKSPWMMAIGF PI in isoform 2. 1 PublicationVSP_015211Add
    BLAST
    Alternative sequencei316 – 34227Missing in isoform 2. 1 PublicationVSP_015212Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK002080 mRNA. Translation: BAA92073.1.
    AL353149, AL365185, AL139406 Genomic DNA. Translation: CAH70340.1.
    AL353149, AL139406, AL365185 Genomic DNA. Translation: CAH70341.1.
    AL365185, AL353149, AL139406 Genomic DNA. Translation: CAH73628.1.
    AL365185, AL139406, AL353149 Genomic DNA. Translation: CAH73629.1.
    AL139406, AL353149, AL365185 Genomic DNA. Translation: CAH73711.1.
    AL139406, AL353149, AL365185 Genomic DNA. Translation: CAH73712.1.
    BC005364 mRNA. Translation: AAH05364.1.
    CCDSiCCDS31239.1. [Q5VYX0-1]
    CCDS7388.1. [Q5VYX0-2]
    RefSeqiNP_001026879.2. NM_001031709.2. [Q5VYX0-1]
    NP_060833.1. NM_018363.3. [Q5VYX0-2]
    UniGeneiHs.149849.

    Genome annotation databases

    EnsembliENST00000331772; ENSP00000332530; ENSG00000184719. [Q5VYX0-1]
    ENST00000371947; ENSP00000361015; ENSG00000184719. [Q5VYX0-2]
    GeneIDi55328.
    KEGGihsa:55328.
    UCSCiuc001kfd.2. human. [Q5VYX0-2]
    uc001kfe.3. human. [Q5VYX0-1]

    Polymorphism databases

    DMDMi73914006.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK002080 mRNA. Translation: BAA92073.1 .
    AL353149 , AL365185 , AL139406 Genomic DNA. Translation: CAH70340.1 .
    AL353149 , AL139406 , AL365185 Genomic DNA. Translation: CAH70341.1 .
    AL365185 , AL353149 , AL139406 Genomic DNA. Translation: CAH73628.1 .
    AL365185 , AL139406 , AL353149 Genomic DNA. Translation: CAH73629.1 .
    AL139406 , AL353149 , AL365185 Genomic DNA. Translation: CAH73711.1 .
    AL139406 , AL353149 , AL365185 Genomic DNA. Translation: CAH73712.1 .
    BC005364 mRNA. Translation: AAH05364.1 .
    CCDSi CCDS31239.1. [Q5VYX0-1 ]
    CCDS7388.1. [Q5VYX0-2 ]
    RefSeqi NP_001026879.2. NM_001031709.2. [Q5VYX0-1 ]
    NP_060833.1. NM_018363.3. [Q5VYX0-2 ]
    UniGenei Hs.149849.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3QJ4 X-ray 2.50 A/B 1-342 [» ]
    ProteinModelPortali Q5VYX0.
    SMRi Q5VYX0. Positions 1-341.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 120609. 1 interaction.
    IntActi Q5VYX0. 1 interaction.

    PTM databases

    PhosphoSitei Q5VYX0.

    Polymorphism databases

    DMDMi 73914006.

    Proteomic databases

    PaxDbi Q5VYX0.
    PRIDEi Q5VYX0.

    Protocols and materials databases

    DNASUi 55328.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000331772 ; ENSP00000332530 ; ENSG00000184719 . [Q5VYX0-1 ]
    ENST00000371947 ; ENSP00000361015 ; ENSG00000184719 . [Q5VYX0-2 ]
    GeneIDi 55328.
    KEGGi hsa:55328.
    UCSCi uc001kfd.2. human. [Q5VYX0-2 ]
    uc001kfe.3. human. [Q5VYX0-1 ]

    Organism-specific databases

    CTDi 55328.
    GeneCardsi GC10M090024.
    HGNCi HGNC:25641. RNLS.
    MIMi 609360. gene.
    neXtProti NX_Q5VYX0.
    PharmGKBi PA165549084.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG3380.
    HOGENOMi HOG000007721.
    InParanoidi Q5VYX0.
    KOi K18208.
    OMAi GQMTLHH.
    OrthoDBi EOG747PJ6.
    PhylomeDBi Q5VYX0.
    TreeFami TF332799.

    Enzyme and pathway databases

    BioCyci MetaCyc:G66-32717-MONOMER.

    Miscellaneous databases

    GeneWikii Renalase.
    GenomeRNAii 55328.
    NextBioi 59608.
    PROi Q5VYX0.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q5VYX0.
    Bgeei Q5VYX0.
    CleanExi HS_C10orf59.
    Genevestigatori Q5VYX0.

    Family and domain databases

    InterProi IPR002937. Amino_oxidase.
    [Graphical view ]
    Pfami PF01593. Amino_oxidase. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Placenta.
    2. "The DNA sequence and comparative analysis of human chromosome 10."
      Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
      , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
      Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. "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), VARIANT ASP-37.
      Tissue: Kidney.
    4. "Renalase is a novel, soluble monoamine oxidase that regulates cardiac function and blood pressure."
      Xu J., Li G., Wang P., Velazquez H., Yao X., Li Y., Wu Y., Peixoto A., Crowley S., Desir G.V.
      J. Clin. Invest. 115:1275-1280(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    5. "Renalase, a catecholamine-metabolising enzyme?"
      Boomsma F., Tipton K.F.
      J. Neural Transm. 114:775-776(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    6. Cited for: CATALYTIC ACTIVITY (ISOFORM 1).
    7. "FAD-binding site and NADP reactivity in human renalase: a new enzyme involved in blood pressure regulation."
      Milani M., Ciriello F., Baroni S., Pandini V., Canevari G., Bolognesi M., Aliverti A.
      J. Mol. Biol. 411:463-473(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), COFACTOR, FAD-BINDING SITES.

    Entry informationi

    Entry nameiRNLS_HUMAN
    AccessioniPrimary (citable) accession number: Q5VYX0
    Secondary accession number(s): Q9BS33, Q9NUP8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 30, 2005
    Last sequence update: December 7, 2004
    Last modified: October 1, 2014
    This is version 97 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, Reference proteome

    Documents

    1. Human chromosome 10
      Human chromosome 10: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3