MARC2_BOVIN
ID MARC2_BOVIN Reviewed; 336 AA.
AC Q1LZH1;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 93.
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, MOSC2;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Hypothalamus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
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; BC116001; AAI16002.1; -; mRNA.
DR RefSeq; NP_001069848.1; NM_001076380.1.
DR AlphaFoldDB; Q1LZH1; -.
DR SMR; Q1LZH1; -.
DR STRING; 9913.ENSBTAP00000008440; -.
DR PaxDb; Q1LZH1; -.
DR PeptideAtlas; Q1LZH1; -.
DR PRIDE; Q1LZH1; -.
DR Ensembl; ENSBTAT00000008440; ENSBTAP00000008440; ENSBTAG00000016277.
DR GeneID; 615506; -.
DR KEGG; bta:615506; -.
DR CTD; 54996; -.
DR VEuPathDB; HostDB:ENSBTAG00000016277; -.
DR VGNC; VGNC:97289; MTARC2.
DR eggNOG; KOG2362; Eukaryota.
DR GeneTree; ENSGT00940000159665; -.
DR HOGENOM; CLU_028286_6_0_1; -.
DR InParanoid; Q1LZH1; -.
DR OMA; GYPFLLI; -.
DR OrthoDB; 919343at2759; -.
DR Proteomes; UP000009136; Chromosome 16.
DR Bgee; ENSBTAG00000016277; Expressed in liver and 103 other tissues.
DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR GO; GO:0030151; F:molybdenum ion binding; IBA:GO_Central.
DR GO; GO:0043546; F:molybdopterin cofactor binding; IBA:GO_Central.
DR GO; GO:0008940; F:nitrate reductase activity; IBA:GO_Central.
DR GO; GO:0098809; F:nitrite reductase activity; IEA:Ensembl.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0070458; P:cellular detoxification of nitrogen compound; IEA:Ensembl.
DR GO; GO:0042126; P:nitrate metabolic process; IBA:GO_Central.
DR GO; GO:0006809; P:nitric oxide biosynthetic process; IEA:Ensembl.
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 Isopeptide bond; Membrane; Mitochondrion; Mitochondrion outer membrane;
KW Molybdenum; Oxidoreductase; Peroxisome; Reference proteome;
KW Transit peptide; Ubl conjugation.
FT TRANSIT 1..35
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 36..336
FT /note="Mitochondrial amidoxime reducing component 2"
FT /id="PRO_0000273339"
FT DOMAIN 188..334
FT /note="MOSC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00670"
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 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 287
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q969Z3"
FT CROSSLNK 294
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q969Z3"
SQ SEQUENCE 336 AA; 37288 MW; 7B81196183014E61 CRC64;
MGAAGSSALA RLGLPALPGP RWLGVAALGL AAVALGAVAW RRARPGRRRR LQQVGTVSEL
WIYPIKSCKG VSVDAAECTA LGLRSGHLRD RFWLVIKEDG HMVTGRQEPQ LVLVSITYED
DCLILRAPGM DQLVLPTKLL SSNKLHDCRV FGLDIQGRDC GDEAAQWFTS FLKTDAFRLV
QFEKNMKARA SNEIFPSLDK NYQVAYPDCS PVMILSEASL ADLNTRMEKK VKINNFRPNI
VVTGCSAFEE DTWDELLIGN VEMKKILACP RCIMTTVDPD TGVIDRKEPL ETLKSYRLCD
PSEKSIYKSS PLFGIYYSVE KIGSLKVGDP VYQMVQ
