ID   MARC2_PIG               Reviewed;          40 AA.
AC   P0C2C3;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   25-MAY-2022, entry version 40.
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: Fragments;
GN   Name=MTARC2; Synonyms=MARC2, MOSC2;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   PROTEIN SEQUENCE, ENZYME ACTIVITY, COFACTOR, IDENTIFICATION IN A COMPLEX
RP   WITH CYTOCHROME B5 AND CYB5R3, SUBCELLULAR LOCATION, AND TISSUE
RP   SPECIFICITY.
RX   PubMed=16973608; DOI=10.1074/jbc.m607697200;
RA   Havemeyer A., Bittner F., Wollers S., Mendel R., Kunze T., Clement B.;
RT   "Identification of the missing component in the mitochondrial benzamidoxime
RT   prodrug converting system as a novel molybdenum enzyme.";
RL   J. Biol. Chem. 281:34796-34802(2006).
RN   [2]
RP   SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=21029045; DOI=10.1042/bj20100960;
RA   Kotthaus J., Wahl B., Havemeyer A., Kotthaus J., Schade D.,
RA   Garbe-Schonberg D., Mendel R., Bittner F., Clement B.;
RT   "Reduction of N(omega)-hydroxy-L-arginine by the mitochondrial amidoxime
RT   reducing component (mARC).";
RL   Biochem. J. 433:383-391(2011).
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;
CC         Evidence={ECO:0000269|PubMed:16973608};
CC       Note=Binds 1 Mo-molybdopterin (Mo-MPT) cofactor per subunit.
CC       {ECO:0000269|PubMed:16973608};
CC   -!- SUBUNIT: Component of a complex composed of cytochrome b5, NADH-
CC       cytochrome b5 reductase (CYB5R3) and MTARC2.
CC       {ECO:0000269|PubMed:16973608}.
CC   -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000250}. Mitochondrion outer
CC       membrane; Peripheral membrane protein.
CC   -!- TISSUE SPECIFICITY: Expressed in the liver (at protein level).
CC       {ECO:0000269|PubMed:16973608, ECO:0000269|PubMed:21029045}.
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   AlphaFoldDB; P0C2C3; -.
DR   STRING; 9823.ENSSSCP00000011541; -.
DR   PeptideAtlas; P0C2C3; -.
DR   PRIDE; P0C2C3; -.
DR   SABIO-RK; P0C2C3; -.
DR   Proteomes; UP000008227; Unplaced.
DR   Proteomes; UP000314985; Unplaced.
DR   GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Isopeptide bond; Membrane; Mitochondrion;
KW   Mitochondrion outer membrane; Molybdenum; Oxidoreductase; Peroxisome;
KW   Reference proteome; Ubl conjugation.
FT   CHAIN           <1..40
FT                   /note="Mitochondrial amidoxime reducing component 2"
FT                   /id="PRO_0000273343"
FT   CROSSLNK        10
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250|UniProtKB:Q969Z3"
FT   CROSSLNK        31
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250|UniProtKB:Q969Z3"
FT   NON_CONS        9..10
FT                   /evidence="ECO:0000305"
FT   NON_CONS        14..15
FT                   /evidence="ECO:0000305"
FT   NON_CONS        31..32
FT                   /evidence="ECO:0000305"
FT   NON_TER         1
SQ   SEQUENCE   40 AA;  4602 MW;  708EE6D2CFE39C53 CRC64;
     LWIYPVKSCK TEAYRCILTT VDPDTGVIDR KVGDPVYRMV