MARC2_RAT
ID MARC2_RAT Reviewed; 338 AA.
AC O88994;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 25-MAY-2022, entry version 100.
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 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 [MRNA].
RC STRAIN=GK; TISSUE=Kidney;
RA Page R.A.;
RT "Isolation of a novel gene, MG87, from the diabetic kidney.";
RL Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate;
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).
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 {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}. Peroxisome {ECO:0000250}.
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; AF095741; AAC64190.1; -; mRNA.
DR EMBL; BC061734; AAH61734.1; -; mRNA.
DR RefSeq; NP_599237.1; NM_134410.2.
DR AlphaFoldDB; O88994; -.
DR SMR; O88994; -.
DR STRING; 10116.ENSRNOP00000034963; -.
DR iPTMnet; O88994; -.
DR PhosphoSitePlus; O88994; -.
DR jPOST; O88994; -.
DR PaxDb; O88994; -.
DR PRIDE; O88994; -.
DR GeneID; 171451; -.
DR KEGG; rno:171451; -.
DR UCSC; RGD:621257; rat.
DR CTD; 54996; -.
DR RGD; 621257; Marc2.
DR eggNOG; KOG2362; Eukaryota.
DR InParanoid; O88994; -.
DR PhylomeDB; O88994; -.
DR PRO; PR:O88994; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR GO; GO:0030151; F:molybdenum ion binding; ISO:RGD.
DR GO; GO:0043546; F:molybdopterin cofactor binding; ISO:RGD.
DR GO; GO:0008940; F:nitrate reductase activity; ISO:RGD.
DR GO; GO:0098809; F:nitrite reductase activity; ISO:RGD.
DR GO; GO:0016661; F:oxidoreductase activity, acting on other nitrogenous compounds as donors; ISO:RGD.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0070458; P:cellular detoxification of nitrogen compound; ISO:RGD.
DR GO; GO:0042126; P:nitrate metabolic process; ISO:RGD.
DR GO; GO:0006809; P:nitric oxide biosynthetic process; ISO:RGD.
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 2: Evidence at transcript 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_0000273344"
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:0000250|UniProtKB:Q922Q1"
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; 38248 MW; 2FF2E1AFEFF8F7C6 CRC64;
MGSSSSTALA RLGLPGQPRS TWLGVAALGL AAVALGTVAW RRARPRRRRQ LQQVGTVSKV
WIYPIKSCKG VSVCETECTD MGLRCGKVRD RFWMVVKEDG HMITARQEPR LVLVTITLEN
NYLMLEAPGM EPIVLPIKLP SSNKIHDCRL FGLDIKGRDC GDEVARWFTS YLKTQAYRLV
QFDTKMKGRT TKKLYPSESY LQNYEVAYPD CSPIHLISEA SLVDLNTRLQ KKVKMEYFRP
NIVVSGCEAF EEDTWDELLI GDVEMKRVLS CPRCVLTTVD PDTGIIDRKE PLETLKSYRL
CDPSVKSLYQ SSPLFGMYFS VEKIGSLRVG DPVYRMVD
