RNLS_RAT
ID RNLS_RAT Reviewed; 315 AA.
AC Q5U2W9;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Renalase;
DE EC=1.6.3.5 {ECO:0000250|UniProtKB:Q5VYX0};
DE AltName: Full=Monoamine oxidase-C;
DE Short=MAO-C;
DE AltName: Full=alpha-NAD(P)H oxidase/anomerase;
DE Flags: Precursor;
GN Name=Rnls;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP FUNCTION.
RX PubMed=15841207; DOI=10.1172/jci200524066;
RA Xu J., Li G., Wang P., Velazquez H., Yao X., Li Y., Wu Y., Peixoto A.,
RA Crowley S., Desir G.V.;
RT "Renalase is a novel, soluble monoamine oxidase that regulates cardiac
RT function and blood pressure.";
RL J. Clin. Invest. 115:1275-1280(2005).
RN [3]
RP FUNCTION.
RX PubMed=18299506; DOI=10.1161/circulationaha.107.732032;
RA Li G., Xu J., Wang P., Velazquez H., Li Y., Wu Y., Desir G.V.;
RT "Catecholamines regulate the activity, secretion, and synthesis of
RT renalase.";
RL Circulation 117:1277-1282(2008).
CC -!- FUNCTION: Catalyzes the oxidation of the less abundant 1,2-dihydro-
CC beta-NAD(P) and 1,6-dihydro-beta-NAD(P) to form beta-NAD(P)(+) (By
CC similarity). The enzyme hormone is secreted by the kidney, and
CC circulates in blood and modulates cardiac function and systemic blood
CC pressure. Lowers blood pressure in vivo by decreasing cardiac
CC contractility and heart rate and preventing a compensatory increase in
CC peripheral vascular tone, suggesting a causal link to the increased
CC plasma catecholamine and heightened cardiovascular risk. High
CC concentrations of catecholamines activate plasma renalase and promotes
CC its secretion and synthesis. {ECO:0000250|UniProtKB:Q5VYX0,
CC ECO:0000269|PubMed:15841207, ECO:0000269|PubMed:18299506}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-dihydro-beta-NAD + H(+) + O2 = H2O2 + NAD(+);
CC Xref=Rhea:RHEA:40395, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:57540, ChEBI:CHEBI:88138; EC=1.6.3.5;
CC Evidence={ECO:0000250|UniProtKB:Q5VYX0};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-dihydro-beta-NADP + H(+) + O2 = H2O2 + NADP(+);
CC Xref=Rhea:RHEA:40399, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:58349, ChEBI:CHEBI:88137; EC=1.6.3.5;
CC Evidence={ECO:0000250|UniProtKB:Q5VYX0};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,6-dihydro-beta-NADP + H(+) + O2 = H2O2 + NADP(+);
CC Xref=Rhea:RHEA:48000, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:58349, ChEBI:CHEBI:88139; EC=1.6.3.5;
CC Evidence={ECO:0000250|UniProtKB:Q5VYX0};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,6-dihydro-beta-NAD + H(+) + O2 = H2O2 + NAD(+);
CC Xref=Rhea:RHEA:47996, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:57540, ChEBI:CHEBI:88140; EC=1.6.3.5;
CC Evidence={ECO:0000250|UniProtKB:Q5VYX0};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the renalase family. {ECO:0000305}.
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DR EMBL; BC085833; AAH85833.1; -; mRNA.
DR RefSeq; NP_001014189.1; NM_001014167.1.
DR AlphaFoldDB; Q5U2W9; -.
DR SMR; Q5U2W9; -.
DR STRING; 10116.ENSRNOP00000028098; -.
DR PhosphoSitePlus; Q5U2W9; -.
DR PaxDb; Q5U2W9; -.
DR PRIDE; Q5U2W9; -.
DR Ensembl; ENSRNOT00000028098; ENSRNOP00000028098; ENSRNOG00000020705.
DR GeneID; 361751; -.
DR KEGG; rno:361751; -.
DR UCSC; RGD:1309804; rat.
DR CTD; 55328; -.
DR RGD; 1309804; Rnls.
DR eggNOG; ENOG502QUZR; Eukaryota.
DR GeneTree; ENSGT00390000016052; -.
DR HOGENOM; CLU_036034_1_0_1; -.
DR InParanoid; Q5U2W9; -.
DR OMA; AFSHSNF; -.
DR OrthoDB; 915997at2759; -.
DR PhylomeDB; Q5U2W9; -.
DR TreeFam; TF332799; -.
DR BRENDA; 1.6.3.5; 5301.
DR Reactome; R-RNO-197264; Nicotinamide salvaging.
DR PRO; PR:Q5U2W9; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000020705; Expressed in liver and 19 other tissues.
DR Genevisible; Q5U2W9; RN.
DR GO; GO:0005576; C:extracellular region; ISO:RGD.
DR GO; GO:0005615; C:extracellular space; IDA:RGD.
DR GO; GO:0051379; F:epinephrine binding; ISO:RGD.
DR GO; GO:0097621; F:monoamine oxidase activity; ISO:RGD.
DR GO; GO:0070404; F:NADH binding; ISO:RGD.
DR GO; GO:0016651; F:oxidoreductase activity, acting on NAD(P)H; ISO:RGD.
DR GO; GO:0045776; P:negative regulation of blood pressure; ISO:RGD.
DR GO; GO:0010459; P:negative regulation of heart rate; ISO:RGD.
DR GO; GO:0071869; P:response to catecholamine; IEP:RGD.
DR GO; GO:0071871; P:response to epinephrine; IEP:RGD.
DR GO; GO:0002931; P:response to ischemia; IEP:RGD.
DR GO; GO:1902074; P:response to salt; IDA:RGD.
DR Gene3D; 3.50.50.60; -; 1.
DR InterPro; IPR002937; Amino_oxidase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR040174; RNLS.
DR PANTHER; PTHR23357; PTHR23357; 1.
DR Pfam; PF01593; Amino_oxidase; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
PE 2: Evidence at transcript level;
KW FAD; Flavoprotein; NAD; NADP; Oxidoreductase; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..315
FT /note="Renalase"
FT /id="PRO_0000019589"
FT BINDING 12
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 42
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 61..62
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
SQ SEQUENCE 315 AA; 34951 MW; C4B606AC2F421698 CRC64;
MFRVLVVGAG LTGSLCAALL RKEITAPLYL ALWDKAGDIG GRMTTANSPH NPRCTADLGA
QYITCTPHYA KKHQNFYEEL LAHGILEPLT SPIKGMEVKE GESNFVAPHG VSSIIKYYLK
ESGAEVFLRQ CVTQINLRDN KWEVSEDTGS TQQFDLVILT MPAPQILGLQ GDIVNLISER
QRQQLASVSY SSRYALGLFY EAGMKIDVPW AGQYITSNPC IRFISIDSKK RNTESSECGP
LLVVHTTVPF GVTHLEHSEE DVQELITQQL ETILPGLPPP VATKCWKWRY SQVTNSAANS
PGQMTLHLNP FLIYI
