MARC1_MOUSE
ID MARC1_MOUSE Reviewed; 340 AA.
AC Q9CW42; Q8R2L6;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Mitochondrial amidoxime-reducing component 1 {ECO:0000250|UniProtKB:Q5VT66};
DE Short=mARC1 {ECO:0000250|UniProtKB:Q5VT66};
DE EC=1.7.-.- {ECO:0000250|UniProtKB:Q5VT66};
DE AltName: Full=Molybdenum cofactor sulfurase C-terminal domain-containing protein 1 {ECO:0000250|UniProtKB:Q5VT66};
DE Short=MOSC domain-containing protein 1;
DE Short=Moco sulfurase C-terminal domain-containing protein 1;
GN Name=Mtarc1; Synonyms=Marc1 {ECO:0000312|MGI:MGI:1913362}, Mosc1;
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=Liver, and Mammary gland;
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] OF 161-340.
RC STRAIN=C57BL/6J; TISSUE=Mammary gland;
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 IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=12865426; DOI=10.1074/jbc.m304940200;
RA Da Cruz S., Xenarios I., Langridge J., Vilbois F., Parone P.A.,
RA Martinou J.-C.;
RT "Proteomic analysis of the mouse liver mitochondrial inner membrane.";
RL J. Biol. Chem. 278:41566-41571(2003).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
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 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:Q5VT66}.
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:Q5VT66};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61645;
CC Evidence={ECO:0000250|UniProtKB:Q5VT66};
CC -!- COFACTOR:
CC Name=Mo-molybdopterin; Xref=ChEBI:CHEBI:71302;
CC Evidence={ECO:0000250|UniProtKB:Q5VT66};
CC Note=Binds 1 Mo-molybdopterin (Mo-MPT) cofactor per subunit.
CC {ECO:0000250|UniProtKB:Q5VT66};
CC -!- SUBUNIT: Component of a complex composed of cytochrome b5, NADH-
CC cytochrome b5 reductase and MTARC1. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC {ECO:0000250|UniProtKB:Q5VT66}; Single-pass type II membrane protein
CC {ECO:0000250|UniProtKB:Q5VT66}. Membrane
CC {ECO:0000250|UniProtKB:Q5VT66}; Lipid-anchor
CC {ECO:0000250|UniProtKB:Q5VT66}. Note=Mitochondrial import is mediated
CC by AA 1-40 and requires ATP. {ECO:0000250|UniProtKB:Q5VT66}.
CC -!- DOMAIN: Comprises two structural domains, the molybdenum cofactor/Moco
CC sulfurase C-terminal (MOSC) domain and the MOSC N-terminal region,
CC forming a cleft that accommodates Moco. The MOSC domain, which contains
CC a large seven-stranded mostly antiparallel beta-barrel, engages
CC multiple interactions with Moco both pterin ring and phosphate group,
CC allowing for a tight coordination of Moco within the core of the
CC enzyme. {ECO:0000250|UniProtKB:Q5VT66}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH28441.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB23724.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK004989; BAB23724.1; ALT_FRAME; mRNA.
DR EMBL; BC028441; AAH28441.1; ALT_INIT; mRNA.
DR CCDS; CCDS69987.1; -.
DR RefSeq; NP_001277202.1; NM_001290273.1.
DR AlphaFoldDB; Q9CW42; -.
DR SMR; Q9CW42; -.
DR STRING; 10090.ENSMUSP00000035804; -.
DR iPTMnet; Q9CW42; -.
DR PhosphoSitePlus; Q9CW42; -.
DR SwissPalm; Q9CW42; -.
DR jPOST; Q9CW42; -.
DR MaxQB; Q9CW42; -.
DR PaxDb; Q9CW42; -.
DR PRIDE; Q9CW42; -.
DR ProteomicsDB; 287310; -.
DR Ensembl; ENSMUST00000048462; ENSMUSP00000035804; ENSMUSG00000026621.
DR GeneID; 66112; -.
DR KEGG; mmu:66112; -.
DR UCSC; uc007dyp.2; mouse.
DR CTD; 64757; -.
DR MGI; MGI:1913362; Mtarc1.
DR VEuPathDB; HostDB:ENSMUSG00000026621; -.
DR eggNOG; KOG2362; Eukaryota.
DR GeneTree; ENSGT00940000162410; -.
DR HOGENOM; CLU_028286_6_0_1; -.
DR InParanoid; Q9CW42; -.
DR OrthoDB; 919343at2759; -.
DR Reactome; R-MMU-211945; Phase I - Functionalization of compounds.
DR BioGRID-ORCS; 66112; 0 hits in 12 CRISPR screens.
DR ChiTaRS; Marc2; mouse.
DR PRO; PR:Q9CW42; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q9CW42; protein.
DR Bgee; ENSMUSG00000026621; Expressed in left lobe of liver and 64 other tissues.
DR ExpressionAtlas; Q9CW42; baseline and differential.
DR Genevisible; Q9CW42; MM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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:1903958; C:nitric-oxide synthase complex; ISO:MGI.
DR GO; GO:0030151; F:molybdenum ion binding; ISS:UniProtKB.
DR GO; GO:0043546; F:molybdopterin cofactor binding; ISS:UniProtKB.
DR GO; GO:0008940; F:nitrate reductase activity; ISO:MGI.
DR GO; GO:0050421; F:nitrite reductase (NO-forming) 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 Lipoprotein; Membrane; Metal-binding; Mitochondrion;
KW Mitochondrion outer membrane; Molybdenum; Myristate; Oxidoreductase;
KW Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q5VT66"
FT CHAIN 2..340
FT /note="Mitochondrial amidoxime-reducing component 1"
FT /id="PRO_0000273336"
FT TOPO_DOM 2..24
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250"
FT TRANSMEM 25..44
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 45..340
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT DOMAIN 191..338
FT /note="MOSC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00670"
FT REGION 96..186
FT /note="MOSC N-terminal region"
FT /evidence="ECO:0000250|UniProtKB:Q5VT66"
FT BINDING 70
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /evidence="ECO:0000250|UniProtKB:Q5VT66"
FT BINDING 71
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /evidence="ECO:0000250|UniProtKB:Q5VT66"
FT BINDING 95
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /evidence="ECO:0000250|UniProtKB:Q5VT66"
FT BINDING 214
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /evidence="ECO:0000250|UniProtKB:Q5VT66"
FT BINDING 241
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /evidence="ECO:0000250|UniProtKB:Q5VT66"
FT BINDING 243
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /evidence="ECO:0000250|UniProtKB:Q5VT66"
FT BINDING 274
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /evidence="ECO:0000250|UniProtKB:Q5VT66"
FT BINDING 275
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /evidence="ECO:0000250|UniProtKB:Q5VT66"
FT BINDING 276
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /ligand_part="Mo"
FT /ligand_part_id="ChEBI:CHEBI:28685"
FT /evidence="ECO:0000250|UniProtKB:Q5VT66"
FT BINDING 320
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /evidence="ECO:0000250|UniProtKB:Q5VT66"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000250|UniProtKB:Q5VT66"
FT CONFLICT 251
FT /note="V -> I (in Ref. 2; AAH28441)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 340 AA; 37979 MW; 2EB4A29C10E7DC50 CRC64;
MGAGSWALTL FGFSAFRVPG QPRSTWLGVA ALGLAAVALG TVAWRRARPR RRRRLQQVGT
VAQLWIYPIK SCKGLSVSEA ECTAMGLRYG HLRDRFWLVI NEEGNMVTAR QEPRLVLISL
TCEDDTLTLS AAYTKDLLLP ITPPATNPLL QCRVHGLEIQ GRDCGEDAAQ WVSSFLKMQS
CRLVHFEPHM RPRSSRQMKA VFRTKDQVAY SDASPFLVLS EASLEDLNSR LERRVKATNF
RPNIVISGCG VYAEDSWNEV LIGDVELKRV MACTRCLLTT VDPDTGISDR KEPLETLKSY
RLCDPSEQAL YGKLPIFGQY FALENPGTIR VGDPVYLLGQ
