RNLS_MOUSE
ID RNLS_MOUSE Reviewed; 342 AA.
AC A7RDN6; Q3TD88; Q80W75;
DT 16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 2.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Renalase {ECO:0000303|PubMed:17846919};
DE EC=1.6.3.5 {ECO:0000250|UniProtKB:Q5VYX0};
DE AltName: Full=Monoamine oxidase-C {ECO:0000303|PubMed:17846919};
DE Short=MAO-C;
DE Short=mMAO-C {ECO:0000303|PubMed:17846919};
DE Flags: Precursor;
GN Name=Rnls {ECO:0000312|MGI:MGI:1915045};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC STRAIN=Kunming {ECO:0000312|EMBL:ABG82016.1};
RC TISSUE=Kidney {ECO:0000312|EMBL:ABG82016.1};
RX PubMed=17846919; DOI=10.1007/s11033-007-9131-1;
RA Wang J., Qi S., Cheng W., Li L., Wang F., Li Y.-Z., Zhang S.-P.;
RT "Identification, expression and tissue distribution of a renalase homologue
RT from mouse.";
RL Mol. Biol. Rep. 35:613-620(2008).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=NOD {ECO:0000312|EMBL:BAE41716.1};
RC TISSUE=Dendritic cell {ECO:0000312|EMBL:BAE41716.1};
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Testis {ECO:0000312|EMBL:AAH52355.2};
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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)(+). The
CC enzyme hormone is secreted by the kidney, and circulates in blood and
CC modulates cardiac function and systemic blood pressure. Lowers blood
CC pressure in vivo by decreasing cardiac contractility and heart rate and
CC preventing a compensatory increase in peripheral vascular tone,
CC suggesting a causal link to the increased plasma catecholamine and
CC heightened cardiovascular risk. High concentrations of catecholamines
CC activate plasma renalase and promotes its secretion and synthesis.
CC {ECO:0000250|UniProtKB:Q5VYX0}.
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;
CC Evidence={ECO:0000250|UniProtKB:Q5VYX0};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17846919}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1 {ECO:0000269|PubMed:17846919};
CC IsoId=A7RDN6-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:16141072};
CC IsoId=A7RDN6-2; Sequence=VSP_053114;
CC -!- TISSUE SPECIFICITY: Expressed predominantly in kidney and testis with
CC lower levels in liver, heart and embryo and weak expression in brain
CC and skeletal muscle. {ECO:0000269|PubMed:17846919}.
CC -!- SIMILARITY: Belongs to the renalase family. {ECO:0000255}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH52355.2; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR EMBL; DQ788834; ABG82016.1; -; mRNA.
DR EMBL; AK170321; BAE41716.1; -; mRNA.
DR EMBL; BC052355; AAH52355.2; ALT_SEQ; mRNA.
DR RefSeq; NP_001139814.2; NM_001146342.2.
DR RefSeq; NP_001161290.1; NM_001167818.1.
DR AlphaFoldDB; A7RDN6; -.
DR SMR; A7RDN6; -.
DR STRING; 10090.ENSMUSP00000093825; -.
DR PhosphoSitePlus; A7RDN6; -.
DR MaxQB; A7RDN6; -.
DR PaxDb; A7RDN6; -.
DR PRIDE; A7RDN6; -.
DR ProteomicsDB; 300458; -. [A7RDN6-1]
DR ProteomicsDB; 300459; -. [A7RDN6-2]
DR UCSC; uc008hft.2; mouse. [A7RDN6-1]
DR MGI; MGI:1915045; Rnls.
DR eggNOG; ENOG502QUZR; Eukaryota.
DR InParanoid; A7RDN6; -.
DR OrthoDB; 915997at2759; -.
DR PhylomeDB; A7RDN6; -.
DR TreeFam; TF332799; -.
DR BRENDA; 1.6.3.5; 3474.
DR Reactome; R-MMU-197264; Nicotinamide salvaging.
DR BioGRID-ORCS; 67795; 1 hit in 70 CRISPR screens.
DR ChiTaRS; Rnls; mouse.
DR PRO; PR:A7RDN6; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; A7RDN6; protein.
DR GO; GO:0005576; C:extracellular region; IBA:GO_Central.
DR GO; GO:0016491; F:oxidoreductase activity; IDA:MGI.
DR GO; GO:0016651; F:oxidoreductase activity, acting on NAD(P)H; IBA:GO_Central.
DR GO; GO:0003214; P:cardiac left ventricle morphogenesis; IMP:MGI.
DR GO; GO:0042417; P:dopamine metabolic process; IMP:MGI.
DR GO; GO:0042414; P:epinephrine metabolic process; IMP:MGI.
DR GO; GO:0060047; P:heart contraction; IMP:MGI.
DR GO; GO:0042415; P:norepinephrine metabolic process; IMP:MGI.
DR GO; GO:0055062; P:phosphate ion homeostasis; IMP:MGI.
DR GO; GO:0003073; P:regulation of systemic arterial blood pressure; IMP:MGI.
DR GO; GO:0071873; P:response to norepinephrine; IMP:MGI.
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 1: Evidence at protein level;
KW Alternative splicing; FAD; Flavoprotein; NAD; NADP; Oxidoreductase;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..342
FT /note="Renalase"
FT /evidence="ECO:0000255"
FT /id="PRO_0000376858"
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"
FT VAR_SEQ 41..123
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_053114"
FT CONFLICT 31
FT /note="G -> A (in Ref. 1; ABG82016 and 2; BAE41716)"
FT /evidence="ECO:0000305"
FT CONFLICT 36
FT /note="G -> A (in Ref. 1; ABG82016 and 2; BAE41716)"
FT /evidence="ECO:0000305"
FT CONFLICT 138
FT /note="K -> E (in Ref. 2; BAE41716)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 342 AA; 37597 MW; 0445A137C6E1F981 CRC64;
MSRVLVVGAG LTGSLCAALL RKEITAPLYL GLWDKGGDIG GRMITASSPH NPRCTADLGA
QYITCSPHYV KEHQNFYEEL LAHGILKPLT SPIEGMKGKE GDCNFVAPQG FSSVIKYYLK
KSGAEVSLKH CVTQIHLKDN KWEVSTDTGS AEQFDLVILT MPAPQILELQ GDIVNLISER
QREQLKSVSY SSRYALGLFY EVGMKIGVPW SCRYLSSHPC ICFISIDNKK RNIESSECGP
SVVIQTTVPF GVQHLEASEA DVQKLMIQQL ETILPGLPQP VATICHKWTY SQVTSSVSDR
PGQMTLHLKP FLVCGGDGFT HSNFNGCISS ALSVMKVLKR YI
