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   27-MAR-2024, entry version 98.
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   PhosphoSitePlus; A7RDN6; -.
DR   MaxQB; A7RDN6; -.
DR   PaxDb; 10090-ENSMUSP00000093825; -.
DR   ProteomicsDB; 300458; -. [A7RDN6-1]
DR   ProteomicsDB; 300459; -. [A7RDN6-2]
DR   UCSC; uc008hft.2; mouse. [A7RDN6-1]
DR   AGR; MGI:1915045; -.
DR   MGI; MGI:1915045; Rnls.
DR   eggNOG; ENOG502QUZR; Eukaryota.
DR   InParanoid; A7RDN6; -.
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 75 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; ISO:MGI.
DR   GO; GO:0005615; C:extracellular space; ISO:MGI.
DR   GO; GO:0051379; F:epinephrine binding; ISO:MGI.
DR   GO; GO:0097621; F:monoamine oxidase activity; ISO:MGI.
DR   GO; GO:0070404; F:NADH binding; ISO:MGI.
DR   GO; GO:0016491; F:oxidoreductase activity; IDA:MGI.
DR   GO; GO:0016651; F:oxidoreductase activity, acting on NAD(P)H; ISO:MGI.
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:0045776; P:negative regulation of blood pressure; ISO:MGI.
DR   GO; GO:0010459; P:negative regulation of heart rate; ISO: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   GO; GO:1902074; P:response to salt; ISO:MGI.
DR   Gene3D; 3.90.660.10; -; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   InterPro; IPR002937; Amino_oxidase.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR040174; RNLS.
DR   PANTHER; PTHR23357:SF1; RENALASE; 1.
DR   PANTHER; PTHR23357; UNCHARACTERIZED; 1.
DR   Pfam; PF01593; Amino_oxidase; 1.
DR   Pfam; PF13450; NAD_binding_8; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 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
//