MARC2_MOUSE
ID MARC2_MOUSE Reviewed; 338 AA.
AC Q922Q1;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Mitochondrial amidoxime reducing component 2;
DE Short=mARC2;
DE EC=1.7.-.-;
DE AltName: Full=Molybdenum cofactor sulfurase C-terminal domain-containing protein 2;
DE Short=MOSC domain-containing protein 2;
DE Short=Moco sulfurase C-terminal domain-containing protein 2;
DE Flags: Precursor;
GN Name=Mtarc2; Synonyms=Marc2, Mg87, Mosc2;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Spinal ganglion;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 [3]
RP PEROXISOMAL SUBCELLULAR LOCATION.
RC TISSUE=Kidney;
RX PubMed=17768142; DOI=10.1074/mcp.m700169-mcp200;
RA Wiese S., Gronemeyer T., Ofman R., Kunze M., Grou C.P., Almeida J.A.,
RA Eisenacher M., Stephan C., Hayen H., Schollenberger L., Korosec T.,
RA Waterham H.R., Schliebs W., Erdmann R., Berger J., Meyer H.E., Just W.,
RA Azevedo J.E., Wanders R.J., Warscheid B.;
RT "Proteomics characterization of mouse kidney peroxisomes by tandem mass
RT spectrometry and protein correlation profiling.";
RL Mol. Cell. Proteomics 6:2045-2057(2007).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, 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).
RN [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-156, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23576753; DOI=10.1073/pnas.1302961110;
RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B.,
RA Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
RT "Label-free quantitative proteomics of the lysine acetylome in mitochondria
RT identifies substrates of SIRT3 in metabolic pathways.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
CC -!- FUNCTION: Catalyzes the reduction of N-oxygenated molecules, acting as
CC a counterpart of cytochrome P450 and flavin-containing monooxygenases
CC in metabolic cycles. As a component of prodrug-converting system,
CC reduces a multitude of N-hydroxylated prodrugs particularly amidoximes,
CC leading to increased drug bioavailability. May be involved in
CC mitochondrial N(omega)-hydroxy-L-arginine (NOHA) reduction, regulating
CC endogenous nitric oxide levels and biosynthesis. Postulated to cleave
CC the N-OH bond of N-hydroxylated substrates in concert with electron
CC transfer from NADH to cytochrome b5 reductase then to cytochrome b5,
CC the ultimate electron donor that primes the active site for substrate
CC reduction. {ECO:0000250|UniProtKB:Q969Z3}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 Fe(II)-[cytochrome b5] + 2 H(+) + N(omega)-hydroxy-L-
CC arginine = 2 Fe(III)-[cytochrome b5] + H2O + L-arginine;
CC Xref=Rhea:RHEA:61644, Rhea:RHEA-COMP:10438, Rhea:RHEA-COMP:10439,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29033,
CC ChEBI:CHEBI:29034, ChEBI:CHEBI:32682, ChEBI:CHEBI:60107;
CC Evidence={ECO:0000250|UniProtKB:Q969Z3};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61645;
CC Evidence={ECO:0000250|UniProtKB:Q969Z3};
CC -!- COFACTOR:
CC Name=Mo-molybdopterin; Xref=ChEBI:CHEBI:71302; Evidence={ECO:0000250};
CC Note=Binds 1 Mo-molybdopterin (Mo-MPT) cofactor per subunit.
CC {ECO:0000250};
CC -!- SUBUNIT: Component of a complex composed of cytochrome b5, NADH-
CC cytochrome b5 reductase (CYB5R3) and MTARC2. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC {ECO:0000250|UniProtKB:P0C2C3}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P0C2C3}. Peroxisome
CC {ECO:0000269|PubMed:17768142}.
CC -!- PTM: Ubiquitinated by PRKN during mitophagy, leading to its degradation
CC and enhancement of mitophagy. Deubiquitinated by USP30.
CC {ECO:0000250|UniProtKB:Q969Z3}.
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DR EMBL; AK051230; BAC34565.1; -; mRNA.
DR EMBL; BC006888; AAH06888.1; -; mRNA.
DR CCDS; CCDS15594.1; -.
DR RefSeq; NP_598445.1; NM_133684.3.
DR AlphaFoldDB; Q922Q1; -.
DR SMR; Q922Q1; -.
DR BioGRID; 212045; 1.
DR STRING; 10090.ENSMUSP00000066715; -.
DR iPTMnet; Q922Q1; -.
DR PhosphoSitePlus; Q922Q1; -.
DR SwissPalm; Q922Q1; -.
DR EPD; Q922Q1; -.
DR jPOST; Q922Q1; -.
DR MaxQB; Q922Q1; -.
DR PaxDb; Q922Q1; -.
DR PeptideAtlas; Q922Q1; -.
DR PRIDE; Q922Q1; -.
DR ProteomicsDB; 292085; -.
DR Antibodypedia; 2381; 139 antibodies from 21 providers.
DR Ensembl; ENSMUST00000068725; ENSMUSP00000066715; ENSMUSG00000073481.
DR GeneID; 67247; -.
DR KEGG; mmu:67247; -.
DR UCSC; uc007dyq.1; mouse.
DR CTD; 54996; -.
DR MGI; MGI:1914497; Mtarc2.
DR VEuPathDB; HostDB:ENSMUSG00000073481; -.
DR eggNOG; KOG2362; Eukaryota.
DR GeneTree; ENSGT00940000159665; -.
DR HOGENOM; CLU_028286_6_0_1; -.
DR InParanoid; Q922Q1; -.
DR OMA; GYPFLLI; -.
DR OrthoDB; 919343at2759; -.
DR PhylomeDB; Q922Q1; -.
DR TreeFam; TF316807; -.
DR Reactome; R-MMU-211945; Phase I - Functionalization of compounds.
DR BioGRID-ORCS; 67247; 0 hits in 17 CRISPR screens.
DR ChiTaRS; Marc2; mouse.
DR PRO; PR:Q922Q1; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q922Q1; protein.
DR Bgee; ENSMUSG00000073481; Expressed in small intestine Peyer's patch and 266 other tissues.
DR ExpressionAtlas; Q922Q1; baseline and differential.
DR Genevisible; Q922Q1; MM.
DR GO; GO:0005743; C:mitochondrial inner membrane; HDA:MGI.
DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR GO; GO:0030151; F:molybdenum ion binding; ISO:MGI.
DR GO; GO:0043546; F:molybdopterin cofactor binding; ISO:MGI.
DR GO; GO:0008940; F:nitrate reductase activity; ISO:MGI.
DR GO; GO:0098809; F:nitrite reductase activity; ISO:MGI.
DR GO; GO:0016661; F:oxidoreductase activity, acting on other nitrogenous compounds as donors; ISO:MGI.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0070458; P:cellular detoxification of nitrogen compound; ISO:MGI.
DR GO; GO:0042126; P:nitrate metabolic process; ISO:MGI.
DR GO; GO:0006809; P:nitric oxide biosynthetic process; ISO:MGI.
DR InterPro; IPR005302; MoCF_Sase_C.
DR InterPro; IPR005303; MOSC_N.
DR InterPro; IPR011037; Pyrv_Knase-like_insert_dom_sf.
DR Pfam; PF03473; MOSC; 1.
DR Pfam; PF03476; MOSC_N; 1.
DR SUPFAM; SSF50800; SSF50800; 1.
DR PROSITE; PS51340; MOSC; 1.
PE 1: Evidence at protein level;
KW Acetylation; Isopeptide bond; Membrane; Mitochondrion;
KW Mitochondrion outer membrane; Molybdenum; Oxidoreductase; Peroxisome;
KW Reference proteome; Transit peptide; Ubl conjugation.
FT TRANSIT 1..35
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 36..338
FT /note="Mitochondrial amidoxime reducing component 2"
FT /id="PRO_0000273342"
FT DOMAIN 188..336
FT /note="MOSC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00670"
FT MOD_RES 156
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT CROSSLNK 59
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q969Z3"
FT CROSSLNK 138
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q969Z3"
FT CROSSLNK 144
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q969Z3"
FT CROSSLNK 156
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q969Z3"
FT CROSSLNK 173
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q969Z3"
FT CROSSLNK 187
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q969Z3"
FT CROSSLNK 289
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q969Z3"
FT CROSSLNK 296
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q969Z3"
SQ SEQUENCE 338 AA; 38194 MW; 436E6C7224B807DA CRC64;
MGSSSSTALA RLGLPGQPRS TWLGVAALGL AAVALGTVAW RRTRPRRRRQ LQQVGTVSKV
WIYPIKSCKG VSVCETECTD MGLRCGKVRD RFWMVVKEDG HMVTARQEPR LVLVSITLEN
NYLTLEAPGM EQIVLPIKLP SSNKIHNCRL FGLDIKGRDC GDEVAQWFTN YLKTQAYRLV
QFDTSMKGRT TKKLYPSESY LQNYEVAYPD CSPVHLISEA SLVDLNTRLK KKVKMEYFRP
NIVVSGCEAF EEDTWDELLI GDVEMKRVLS CPRCVLTTVD PDTGIIDRKE PLETLKSYRL
CDPSVKSIYQ SSPLFGMYFS VEKLGSLRVG DPVYRMVD
