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A7RDN6

- RNLS_MOUSE

UniProt

A7RDN6 - RNLS_MOUSE

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Protein

Renalase

Gene
Rnls
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at transcript 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 By similarity.

Catalytic activityi

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

Cofactori

FAD By similarity.By similarity

Sites

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

GO - Molecular functioni

  1. oxidoreductase activity Source: MGI

GO - Biological processi

  1. cardiac left ventricle morphogenesis Source: MGI
  2. dopamine metabolic process Source: MGI
  3. epinephrine metabolic process Source: MGI
  4. heart contraction Source: MGI
  5. norepinephrine metabolic process Source: MGI
  6. phosphate ion homeostasis Source: MGI
  7. regulation of systemic arterial blood pressure Source: MGI
  8. response to epinephrine Source: Ensembl
  9. response to ischemia Source: Ensembl
  10. response to norepinephrine Source: MGI
  11. response to salt Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

FAD, Flavoprotein, NAD, NADP

Names & Taxonomyi

Protein namesi
Recommended name:
Renalase (EC:1.6.3.5)
Alternative name(s):
Monoamine oxidase-C
Short name:
MAO-C
Short name:
mMAO-C
alpha-NAD(P)H oxidase/anomerase
Gene namesi
Name:Rnls
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 19

Organism-specific databases

MGIiMGI:1915045. Rnls.

Subcellular locationi

Secreted 1 Publication

GO - Cellular componenti

  1. extracellular space Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1717 Reviewed predictionAdd
BLAST
Chaini18 – 342325RenalasePRO_0000376858Add
BLAST

Proteomic databases

PaxDbiA7RDN6.
PRIDEiA7RDN6.

PTM databases

PhosphoSiteiA7RDN6.

Expressioni

Tissue specificityi

Expressed predominantly in kidney and testis with lower levels in liver, heart and embryo and weak expression in brain and skeletal muscle.1 Publication

Gene expression databases

BgeeiA7RDN6.
GenevestigatoriA7RDN6.

Structurei

3D structure databases

ProteinModelPortaliA7RDN6.
SMRiA7RDN6. Positions 1-341.

Family & Domainsi

Region

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

Sequence similaritiesi

Belongs to the renalase family.

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG74071.
GeneTreeiENSGT00390000016052.
HOGENOMiHOG000007721.
InParanoidiQ80W75.
KOiK18208.
OrthoDBiEOG747PJ6.
PhylomeDBiA7RDN6.
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 11 Publication (identifier: A7RDN6-1) [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

MSRVLVVGAG LTGSLCAALL RKEITAPLYL GLWDKGGDIG GRMITASSPH    50
NPRCTADLGA QYITCSPHYV KEHQNFYEEL LAHGILKPLT SPIEGMKGKE 100
GDCNFVAPQG FSSVIKYYLK KSGAEVSLKH CVTQIHLKDN KWEVSTDTGS 150
AEQFDLVILT MPAPQILELQ GDIVNLISER QREQLKSVSY SSRYALGLFY 200
EVGMKIGVPW SCRYLSSHPC ICFISIDNKK RNIESSECGP SVVIQTTVPF 250
GVQHLEASEA DVQKLMIQQL ETILPGLPQP VATICHKWTY SQVTSSVSDR 300
PGQMTLHLKP FLVCGGDGFT HSNFNGCISS ALSVMKVLKR YI 342
Length:342
Mass (Da):37,597
Last modified:June 16, 2009 - v2
Checksum:i0445A137C6E1F981
GO
Isoform 21 Publication (identifier: A7RDN6-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     41-123: Missing.

Note: No experimental confirmation available.

Show »
Length:259
Mass (Da):28,457
Checksum:i5F3898120A31E513
GO

Sequence cautioni

The sequence AAH52355.2 differs from that shown. Reason: Erroneous termination at position 33. Translated as Trp.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei41 – 12383Missing in isoform 2. 1 PublicationVSP_053114Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti31 – 311G → A in ABG82016. 1 Publication
Sequence conflicti31 – 311G → A in BAE41716. 1 Publication
Sequence conflicti36 – 361G → A in ABG82016. 1 Publication
Sequence conflicti36 – 361G → A in BAE41716. 1 Publication
Sequence conflicti138 – 1381K → E in BAE41716. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
DQ788834 mRNA. Translation: ABG82016.1.
AK170321 mRNA. Translation: BAE41716.1.
BC052355 mRNA. Translation: AAH52355.2. Sequence problems.
RefSeqiNP_001139814.2. NM_001146342.2.
NP_001161290.1. NM_001167818.1.
UniGeneiMm.204591.

Genome annotation databases

EnsembliENSMUST00000096114; ENSMUSP00000093825; ENSMUSG00000071573.
GeneIDi67795.
KEGGimmu:67795.
UCSCiuc008hft.2. mouse. [A7RDN6-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
DQ788834 mRNA. Translation: ABG82016.1 .
AK170321 mRNA. Translation: BAE41716.1 .
BC052355 mRNA. Translation: AAH52355.2 . Sequence problems.
RefSeqi NP_001139814.2. NM_001146342.2.
NP_001161290.1. NM_001167818.1.
UniGenei Mm.204591.

3D structure databases

ProteinModelPortali A7RDN6.
SMRi A7RDN6. Positions 1-341.
ModBasei Search...
MobiDBi Search...

PTM databases

PhosphoSitei A7RDN6.

Proteomic databases

PaxDbi A7RDN6.
PRIDEi A7RDN6.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000096114 ; ENSMUSP00000093825 ; ENSMUSG00000071573 .
GeneIDi 67795.
KEGGi mmu:67795.
UCSCi uc008hft.2. mouse. [A7RDN6-1 ]

Organism-specific databases

CTDi 55328.
MGIi MGI:1915045. Rnls.

Phylogenomic databases

eggNOGi NOG74071.
GeneTreei ENSGT00390000016052.
HOGENOMi HOG000007721.
InParanoidi Q80W75.
KOi K18208.
OrthoDBi EOG747PJ6.
PhylomeDBi A7RDN6.
TreeFami TF332799.

Miscellaneous databases

NextBioi 325581.
PROi A7RDN6.
SOURCEi Search...

Gene expression databases

Bgeei A7RDN6.
Genevestigatori A7RDN6.

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. "Identification, expression and tissue distribution of a renalase homologue from mouse."
    Wang J., Qi S., Cheng W., Li L., Wang F., Li Y.-Z., Zhang S.-P.
    Mol. Biol. Rep. 35:613-620(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    Strain: Kunming.
    Tissue: Kidney.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Strain: NOD.
    Tissue: Dendritic cell.
  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).
    Tissue: Testis.

Entry informationi

Entry nameiRNLS_MOUSE
AccessioniPrimary (citable) accession number: A7RDN6
Secondary accession number(s): Q3TD88, Q80W75
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 16, 2009
Last sequence update: June 16, 2009
Last modified: July 9, 2014
This is version 49 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi