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Q5VYX0 (RNLS_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 96. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Renalase

EC=1.6.3.5
Alternative name(s):
Monoamine oxidase-C
Short name=MAO-C
alpha-NAD(P)H oxidase/anomerase
Gene names
Name:RNLS
Synonyms:C10orf59
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length342 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the oxidation of the less abundant alpha-NAD(P)H isoform toform 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. Ref.4 Ref.5

Catalytic activity

Alpha-NAD(P)H + O2 = beta-NAD(P)+ + H2O2. Ref.6

Cofactor

FAD. Ref.7

Subcellular location

Secreted Ref.4.

Tissue specificity

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. Ref.4

Sequence similarities

Belongs to the renalase family.

Ontologies

Keywords
   Cellular componentSecreted
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainSignal
   LigandFAD
Flavoprotein
NAD
NADP
   Molecular functionOxidoreductase
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processresponse to epinephrine

Inferred from electronic annotation. Source: Ensembl

response to ischemia

Inferred from electronic annotation. Source: Ensembl

response to salt

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentextracellular space

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionoxidoreductase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q5VYX0-1)

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.
Isoform 2 (identifier: Q5VYX0-2)

The sequence of this isoform differs from the canonical sequence as follows:
     294-315: TNAAANCPGQMTLHHKPFLACG → PSAGVILGCAKSPWMMAIGFPI
     316-342: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1717 Potential
Chain18 – 342325Renalase
PRO_0000019588

Regions

Region61 – 622FAD-binding

Sites

Binding site121FAD
Binding site421FAD

Natural variations

Alternative sequence294 – 31522TNAAA…FLACG → PSAGVILGCAKSPWMMAIGF PI in isoform 2.
VSP_015211
Alternative sequence316 – 34227Missing in isoform 2.
VSP_015212
Natural variant371E → D. Ref.3
Corresponds to variant rs2296545 [ dbSNP | Ensembl ].
VAR_023310

Secondary structure

................................................................... 342
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified December 7, 2004. Version 1.
Checksum: 952827FF7926AF48

FASTA34237,847
        10         20         30         40         50         60 
MAQVLIVGAG MTGSLCAALL RRQTSGPLYL AVWDKAEDSG GRMTTACSPH NPQCTADLGA 

        70         80         90        100        110        120 
QYITCTPHYA KKHQRFYDEL LAYGVLRPLS SPIEGMVMKE GDCNFVAPQG ISSIIKHYLK 

       130        140        150        160        170        180 
ESGAEVYFRH RVTQINLRDD KWEVSKQTGS PEQFDLIVLT MPVPEILQLQ GDITTLISEC 

       190        200        210        220        230        240 
QRQQLEAVSY SSRYALGLFY EAGTKIDVPW AGQYITSNPC IRFVSIDNKK RNIESSEIGP 

       250        260        270        280        290        300 
SLVIHTTVPF GVTYLEHSIE DVQELVFQQL ENILPGLPQP IATKCQKWRH SQVTNAAANC 

       310        320        330        340 
PGQMTLHHKP FLACGGDGFT QSNFDGCITS ALCVLEALKN YI 

« Hide

Isoform 2 [UniParc].

Checksum: 8C1EBF93073E4690
Show »

FASTA31534,949

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]"Renalase is an alpha-NAD(P)H oxidase/anomerase."
Beaupre B.A., Carmichael B.R., Hoag M.R., Shah D.D., Moran G.R.
J. Am. Chem. Soc. 135:13980-13987(2013) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS31239.1. [Q5VYX0-1]
CCDS7388.1. [Q5VYX0-2]
RefSeqNP_001026879.2. NM_001031709.2. [Q5VYX0-1]
NP_060833.1. NM_018363.3. [Q5VYX0-2]
UniGeneHs.149849.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3QJ4X-ray2.50A/B1-342[»]
ProteinModelPortalQ5VYX0.
SMRQ5VYX0. Positions 1-341.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid120609. 1 interaction.
IntActQ5VYX0. 1 interaction.

PTM databases

PhosphoSiteQ5VYX0.

Polymorphism databases

DMDM73914006.

Proteomic databases

PaxDbQ5VYX0.
PRIDEQ5VYX0.

Protocols and materials databases

DNASU55328.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000331772; ENSP00000332530; ENSG00000184719. [Q5VYX0-1]
ENST00000371947; ENSP00000361015; ENSG00000184719. [Q5VYX0-2]
GeneID55328.
KEGGhsa:55328.
UCSCuc001kfd.2. human. [Q5VYX0-2]
uc001kfe.3. human. [Q5VYX0-1]

Organism-specific databases

CTD55328.
GeneCardsGC10M090024.
HGNCHGNC:25641. RNLS.
MIM609360. gene.
neXtProtNX_Q5VYX0.
PharmGKBPA165549084.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG3380.
HOGENOMHOG000007721.
InParanoidQ5VYX0.
KOK18208.
OMAGQMTLHH.
OrthoDBEOG747PJ6.
PhylomeDBQ5VYX0.
TreeFamTF332799.

Enzyme and pathway databases

BioCycMetaCyc:G66-32717-MONOMER.

Gene expression databases

ArrayExpressQ5VYX0.
BgeeQ5VYX0.
CleanExHS_C10orf59.
GenevestigatorQ5VYX0.

Family and domain databases

InterProIPR002937. Amino_oxidase.
[Graphical view]
PfamPF01593. Amino_oxidase. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiRenalase.
GenomeRNAi55328.
NextBio59608.
PROQ5VYX0.
SOURCESearch...

Entry information

Entry nameRNLS_HUMAN
AccessionPrimary (citable) accession number: Q5VYX0
Secondary accession number(s): Q9BS33, Q9NUP8
Entry history
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: December 7, 2004
Last modified: July 9, 2014
This is version 96 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 10

Human chromosome 10: entries, gene names and cross-references to MIM