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Q5VYX0

- RNLS_HUMAN

UniProt

Q5VYX0 - RNLS_HUMAN

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Protein

Renalase

Gene
RNLS, C10orf59
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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)+ + H2O2.1 Publication

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
Complete GO annotation...

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
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA165549084.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1717 Reviewed predictionAdd
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.

Family & Domainsi

Region

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

Sequence similaritiesi

Belongs to the renalase family.

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. VSP_015211Add
BLAST
Alternative sequencei316 – 34227Missing in isoform 2. VSP_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

« Hide 'large scale' publications
  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: July 9, 2014
This is version 96 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

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