MARC1_HUMAN
ID MARC1_HUMAN Reviewed; 337 AA.
AC Q5VT66; A8K447; B2D078; Q5VVS9; Q5VVT0; Q5VVT1; Q8N9P5; Q96FN8; Q9H6C7;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Mitochondrial amidoxime-reducing component 1 {ECO:0000303|PubMed:21029045};
DE Short=mARC1 {ECO:0000303|PubMed:30397129};
DE EC=1.7.-.- {ECO:0000269|PubMed:21029045};
DE AltName: Full=Molybdenum cofactor sulfurase C-terminal domain-containing protein 1 {ECO:0000303|PubMed:30397129};
DE Short=MOSC domain-containing protein 1;
DE Short=Moco sulfurase C-terminal domain-containing protein 1;
GN Name=MTARC1 {ECO:0000312|HGNC:HGNC:26189}; Synonyms=MARC1, MOSC1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3), AND VARIANT
RP ALA-165.
RC TISSUE=Adrenal gland, and Kidney;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS HIS-15; LEU-96; ALA-165;
RP SER-246 AND HIS-247.
RG NIEHS SNPs program;
RL Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING
RP (ISOFORMS 1 AND 2).
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ALA-165.
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS ALA-165
RP AND LYS-187.
RC TISSUE=Eye;
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 [6]
RP FUNCTION, AND COFACTOR.
RX PubMed=19053771; DOI=10.1021/jm8010417;
RA Gruenewald S., Wahl B., Bittner F., Hungeling H., Kanzow S., Kotthaus J.,
RA Schwering U., Mendel R.R., Clement B.;
RT "The fourth molybdenum containing enzyme mARC: cloning and involvement in
RT the activation of N-hydroxylated prodrugs.";
RL J. Med. Chem. 51:8173-8177(2008).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [8]
RP BIOPHYSICOCHEMICAL PROPERTIES, CATALYTIC ACTIVITY, AND FUNCTION.
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).
RN [9]
RP SUBCELLULAR LOCATION, AND TOPOLOGY.
RX PubMed=23086957; DOI=10.1074/jbc.m112.419424;
RA Klein J.M., Busch J.D., Potting C., Baker M.J., Langer T., Schwarz G.;
RT "The mitochondrial amidoxime-reducing component (mARC1) is a novel signal-
RT anchored protein of the outer mitochondrial membrane.";
RL J. Biol. Chem. 287:42795-42803(2012).
RN [10]
RP MYRISTOYLATION AT GLY-2, CLEAVAGE OF INITIATOR METHIONINE, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=25255805; DOI=10.1038/ncomms5919;
RA Thinon E., Serwa R.A., Broncel M., Brannigan J.A., Brassat U., Wright M.H.,
RA Heal W.P., Wilkinson A.J., Mann D.J., Tate E.W.;
RT "Global profiling of co- and post-translationally N-myristoylated proteomes
RT in human cells.";
RL Nat. Commun. 5:4919-4919(2014).
RN [11]
RP MYRISTOYLATION AT GLY-2, CLEAVAGE OF INITIATOR METHIONINE, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=25807930; DOI=10.1002/anie.201500342;
RA Broncel M., Serwa R.A., Ciepla P., Krause E., Dallman M.J., Magee A.I.,
RA Tate E.W.;
RT "Multifunctional reagents for quantitative proteome-wide analysis of
RT protein modification in human cells and dynamic profiling of protein
RT lipidation during vertebrate development.";
RL Angew. Chem. Int. Ed. 54:5948-5951(2015).
RN [12] {ECO:0007744|PDB:6FW2}
RP X-RAY CRYSTALLOGRAPHY (1.78 ANGSTROMS) OF 53-337 IN COMPLEX WITH
RP MO-MOLYBDOPTERIN, COFACTOR, FUNCTION, AND DOMAIN.
RX PubMed=30397129; DOI=10.1073/pnas.1808576115;
RA Kubitza C., Bittner F., Ginsel C., Havemeyer A., Clement B., Scheidig A.J.;
RT "Crystal structure of human mARC1 reveals its exceptional position among
RT eukaryotic molybdenum enzymes.";
RL Proc. Natl. Acad. Sci. U.S.A. 115:11958-11963(2018).
RN [13]
RP VARIANTS ALA-165; LYS-187; SER-246 AND HIS-247, CHARACTERIZATION OF
RP VARIANTS LEU-96; ALA-165; LYS-187; SER-246; HIS-247 AND ILE-268,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND COFACTOR.
RX PubMed=24423752; DOI=10.1124/dmd.113.055202;
RA Ott G., Reichmann D., Boerger C., Cascorbi I., Bittner F., Mendel R.R.,
RA Kunze T., Clement B., Havemeyer A.;
RT "Functional characterization of protein variants encoded by non-synonymous
RT SNPs in MARC1 and MARC2 in healthy Caucasians.";
RL Drug Metab. Dispos. 42:718-725(2014).
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 (PubMed:19053771, PubMed:21029045,
CC PubMed:30397129). As a component of prodrug-converting system, reduces
CC a multitude of N-hydroxylated prodrugs particularly amidoximes, leading
CC to increased drug bioavailability (PubMed:19053771). May be involved in
CC mitochondrial N(omega)-hydroxy-L-arginine (NOHA) reduction, regulating
CC endogenous nitric oxide levels and biosynthesis (PubMed:21029045).
CC Postulated to cleave the N-OH bond of N-hydroxylated substrates in
CC concert with electron transfer from NADH to cytochrome b5 reductase
CC then to cytochrome b5, the ultimate electron donor that primes the
CC active site for substrate reduction (PubMed:21029045, PubMed:19053771).
CC {ECO:0000269|PubMed:19053771, ECO:0000269|PubMed:21029045,
CC ECO:0000269|PubMed:30397129}.
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:0000269|PubMed:21029045};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61645;
CC Evidence={ECO:0000305|PubMed:21029045};
CC -!- COFACTOR:
CC Name=Mo-molybdopterin; Xref=ChEBI:CHEBI:71302;
CC Evidence={ECO:0000269|PubMed:19053771, ECO:0000269|PubMed:24423752,
CC ECO:0000269|PubMed:30397129};
CC Note=Binds 1 Mo-molybdopterin (Mo-MPT) cofactor per subunit.
CC {ECO:0000269|PubMed:19053771, ECO:0000269|PubMed:24423752,
CC ECO:0000269|PubMed:30397129};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=180 uM for benzamidoxime {ECO:0000269|PubMed:21029045};
CC KM=86 uM for NOHA {ECO:0000269|PubMed:21029045};
CC KM=272 uM for NHAM {ECO:0000269|PubMed:21029045};
CC Vmax=34 nmol/min/mg enzyme toward benzamidoxime
CC {ECO:0000269|PubMed:21029045};
CC Vmax=105 nmol/min/mg enzyme toward benzamidoxime (at pH 6.0 and 37
CC degrees Celsius) {ECO:0000269|PubMed:24423752};
CC Vmax=55 nmol/min/mg enzyme toward NOHA {ECO:0000269|PubMed:21029045};
CC Vmax=43 nmol/min/mg enzyme toward NHAM {ECO:0000269|PubMed:21029045};
CC -!- SUBUNIT: Component of a complex composed of cytochrome b5, NADH-
CC cytochrome b5 reductase and MTARC1.
CC -!- INTERACTION:
CC Q5VT66; O15197-2: EPHB6; NbExp=3; IntAct=EBI-11903927, EBI-10182490;
CC Q5VT66; Q9BSU3: NAA11; NbExp=3; IntAct=EBI-11903927, EBI-2585120;
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC {ECO:0000269|PubMed:23086957}; Single-pass type II membrane protein
CC {ECO:0000269|PubMed:23086957}. Membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}. Note=Mitochondrial import is mediated by AA 1-40 and
CC requires ATP.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q5VT66-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5VT66-2; Sequence=VSP_022512;
CC Name=3;
CC IsoId=Q5VT66-3; Sequence=VSP_022511, VSP_022512;
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:0000269|PubMed:30397129}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB15333.1; Type=Frameshift; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/mosc1/";
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DR EMBL; AK026043; BAB15333.1; ALT_FRAME; mRNA.
DR EMBL; AK094105; BAC04286.1; -; mRNA.
DR EMBL; AK290812; BAF83501.1; -; mRNA.
DR EMBL; EU563849; ACB21046.1; -; Genomic_DNA.
DR EMBL; AL445423; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL606726; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471100; EAW93291.1; -; Genomic_DNA.
DR EMBL; BC010619; AAH10619.1; -; mRNA.
DR CCDS; CCDS1526.1; -. [Q5VT66-1]
DR RefSeq; NP_073583.3; NM_022746.3. [Q5VT66-1]
DR RefSeq; XP_011508202.1; XM_011509900.2. [Q5VT66-2]
DR RefSeq; XP_011508206.1; XM_011509904.2. [Q5VT66-3]
DR PDB; 6FW2; X-ray; 1.78 A; A=53-337.
DR PDBsum; 6FW2; -.
DR AlphaFoldDB; Q5VT66; -.
DR SMR; Q5VT66; -.
DR BioGRID; 122271; 70.
DR IntAct; Q5VT66; 17.
DR MINT; Q5VT66; -.
DR STRING; 9606.ENSP00000355877; -.
DR ChEMBL; CHEMBL3706559; -.
DR iPTMnet; Q5VT66; -.
DR PhosphoSitePlus; Q5VT66; -.
DR SwissPalm; Q5VT66; -.
DR BioMuta; MARC1; -.
DR DMDM; 74746896; -.
DR EPD; Q5VT66; -.
DR jPOST; Q5VT66; -.
DR MassIVE; Q5VT66; -.
DR MaxQB; Q5VT66; -.
DR PaxDb; Q5VT66; -.
DR PeptideAtlas; Q5VT66; -.
DR PRIDE; Q5VT66; -.
DR ProteomicsDB; 65307; -. [Q5VT66-1]
DR ProteomicsDB; 65308; -. [Q5VT66-2]
DR ProteomicsDB; 65309; -. [Q5VT66-3]
DR Antibodypedia; 34627; 119 antibodies from 21 providers.
DR DNASU; 64757; -.
DR Ensembl; ENST00000366910.10; ENSP00000355877.5; ENSG00000186205.13. [Q5VT66-1]
DR GeneID; 64757; -.
DR KEGG; hsa:64757; -.
DR MANE-Select; ENST00000366910.10; ENSP00000355877.5; NM_022746.4; NP_073583.3.
DR UCSC; uc001hms.4; human. [Q5VT66-1]
DR CTD; 64757; -.
DR DisGeNET; 64757; -.
DR GeneCards; MTARC1; -.
DR HGNC; HGNC:26189; MTARC1.
DR HPA; ENSG00000186205; Tissue enhanced (adipose tissue, breast, liver).
DR MIM; 614126; gene.
DR neXtProt; NX_Q5VT66; -.
DR OpenTargets; ENSG00000186205; -.
DR VEuPathDB; HostDB:ENSG00000186205; -.
DR eggNOG; KOG2362; Eukaryota.
DR GeneTree; ENSGT00940000162410; -.
DR HOGENOM; CLU_028286_6_0_1; -.
DR InParanoid; Q5VT66; -.
DR OMA; WIRIGNE; -.
DR OrthoDB; 919343at2759; -.
DR PhylomeDB; Q5VT66; -.
DR TreeFam; TF316807; -.
DR BRENDA; 1.16.98.B1; 2681.
DR BRENDA; 1.7.2.1; 2681.
DR PathwayCommons; Q5VT66; -.
DR Reactome; R-HSA-211945; Phase I - Functionalization of compounds.
DR SABIO-RK; Q5VT66; -.
DR SignaLink; Q5VT66; -.
DR SIGNOR; Q5VT66; -.
DR BioGRID-ORCS; 64757; 4 hits in 785 CRISPR screens.
DR ChiTaRS; MARC1; human.
DR GenomeRNAi; 64757; -.
DR Pharos; Q5VT66; Tbio.
DR PRO; PR:Q5VT66; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q5VT66; protein.
DR Bgee; ENSG00000186205; Expressed in adipose tissue and 143 other tissues.
DR ExpressionAtlas; Q5VT66; baseline and differential.
DR Genevisible; Q5VT66; HS.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005741; C:mitochondrial outer membrane; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR GO; GO:1903958; C:nitric-oxide synthase complex; IDA:FlyBase.
DR GO; GO:0030151; F:molybdenum ion binding; IDA:UniProtKB.
DR GO; GO:0043546; F:molybdopterin cofactor binding; IDA:UniProtKB.
DR GO; GO:0008940; F:nitrate reductase activity; IDA:UniProtKB.
DR GO; GO:0098809; F:nitrite reductase activity; IDA:FlyBase.
DR GO; GO:0016661; F:oxidoreductase activity, acting on other nitrogenous compounds as donors; IDA:FlyBase.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0070458; P:cellular detoxification of nitrogen compound; IMP:FlyBase.
DR GO; GO:0051410; P:detoxification of nitrogen compound; NAS:UniProtKB.
DR GO; GO:0042126; P:nitrate metabolic process; IDA:UniProtKB.
DR GO; GO:0006809; P:nitric oxide biosynthetic process; IDA:FlyBase.
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 3D-structure; Alternative splicing; Lipoprotein; Membrane; Metal-binding;
KW Mitochondrion; Mitochondrion outer membrane; Molybdenum; Myristate;
KW Oxidoreductase; Reference proteome; Signal-anchor; Transmembrane;
KW Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:25255805,
FT ECO:0000269|PubMed:25807930"
FT CHAIN 2..337
FT /note="Mitochondrial amidoxime-reducing component 1"
FT /id="PRO_0000273335"
FT TOPO_DOM 2..20
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000269|PubMed:23086957"
FT TRANSMEM 21..40
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 41..337
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:23086957"
FT DOMAIN 187..335
FT /note="MOSC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00670"
FT REGION 93..183
FT /note="MOSC N-terminal region"
FT /evidence="ECO:0000269|PubMed:30397129"
FT BINDING 67
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /evidence="ECO:0000269|PubMed:30397129,
FT ECO:0007744|PDB:6FW2"
FT BINDING 68
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /evidence="ECO:0000269|PubMed:30397129,
FT ECO:0007744|PDB:6FW2"
FT BINDING 92
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /evidence="ECO:0000269|PubMed:30397129,
FT ECO:0007744|PDB:6FW2"
FT BINDING 210
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /evidence="ECO:0000269|PubMed:30397129,
FT ECO:0007744|PDB:6FW2"
FT BINDING 211
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /evidence="ECO:0000269|PubMed:30397129,
FT ECO:0007744|PDB:6FW2"
FT BINDING 238
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /evidence="ECO:0000269|PubMed:30397129,
FT ECO:0007744|PDB:6FW2"
FT BINDING 240
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /evidence="ECO:0000269|PubMed:30397129,
FT ECO:0007744|PDB:6FW2"
FT BINDING 271
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /evidence="ECO:0000269|PubMed:30397129,
FT ECO:0007744|PDB:6FW2"
FT BINDING 272
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /evidence="ECO:0000269|PubMed:30397129,
FT ECO:0007744|PDB:6FW2"
FT BINDING 273
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /ligand_part="Mo"
FT /ligand_part_id="ChEBI:CHEBI:28685"
FT /evidence="ECO:0000269|PubMed:30397129,
FT ECO:0007744|PDB:6FW2"
FT BINDING 317
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /evidence="ECO:0000269|PubMed:30397129,
FT ECO:0007744|PDB:6FW2"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000269|PubMed:25255805,
FT ECO:0000269|PubMed:25807930"
FT VAR_SEQ 1..102
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_022511"
FT VAR_SEQ 251
FT /note="E -> EVTLCPFGSFLGFDFFFK (in isoform 2 and isoform
FT 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_022512"
FT VARIANT 15
FT /note="L -> H (in dbSNP:rs72470572)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_062273"
FT VARIANT 96
FT /note="V -> L (no effect on binding of the molybdenum
FT cofactor; no significant effect on catalytic efficiency
FT toward benzamidoxime; no significant effect on affinity for
FT benzamidoxime; dbSNP:rs12023067)"
FT /evidence="ECO:0000269|PubMed:24423752, ECO:0000269|Ref.2"
FT /id="VAR_056941"
FT VARIANT 165
FT /note="T -> A (no effect on binding of the molybdenum
FT cofactor; no significant effect on catalytic efficiency
FT toward benzamidoxime; no significant effect on affinity for
FT benzamidoxime; dbSNP:rs2642438)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:24423752,
FT ECO:0000269|Ref.2, ECO:0000269|Ref.4"
FT /id="VAR_030129"
FT VARIANT 187
FT /note="M -> K (no effect on binding of the molybdenum
FT cofactor; no significant effect on catalytic efficiency
FT toward benzamidoxime; no significant effect on affinity for
FT benzamidoxime; dbSNP:rs17850677)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:24423752"
FT /id="VAR_030130"
FT VARIANT 246
FT /note="C -> S (no effect on binding of the molybdenum
FT cofactor; no significant effect on catalytic efficiency
FT toward benzamidoxime; no significant effect on affinity for
FT benzamidoxime; dbSNP:rs3738178)"
FT /evidence="ECO:0000269|PubMed:24423752, ECO:0000269|Ref.2"
FT /id="VAR_030131"
FT VARIANT 247
FT /note="D -> H (no effect on binding of the molybdenum
FT cofactor; no significant effect on catalytic efficiency
FT toward benzamidoxime; no significant effect on affinity for
FT benzamidoxime; dbSNP:rs72470601)"
FT /evidence="ECO:0000269|PubMed:24423752, ECO:0000269|Ref.2"
FT /id="VAR_062274"
FT VARIANT 268
FT /note="M -> I (no effect on binding of the molybdenum
FT cofactor; no significant effect on catalytic efficiency
FT toward benzamidoxime; no significant effect on affinity for
FT benzamidoxime; dbSNP:rs2642419)"
FT /evidence="ECO:0000269|PubMed:24423752"
FT /id="VAR_030132"
FT STRAND 53..63
FT /evidence="ECO:0007829|PDB:6FW2"
FT STRAND 72..80
FT /evidence="ECO:0007829|PDB:6FW2"
FT STRAND 83..86
FT /evidence="ECO:0007829|PDB:6FW2"
FT STRAND 94..97
FT /evidence="ECO:0007829|PDB:6FW2"
FT STRAND 101..103
FT /evidence="ECO:0007829|PDB:6FW2"
FT TURN 106..108
FT /evidence="ECO:0007829|PDB:6FW2"
FT HELIX 110..114
FT /evidence="ECO:0007829|PDB:6FW2"
FT STRAND 116..120
FT /evidence="ECO:0007829|PDB:6FW2"
FT STRAND 123..127
FT /evidence="ECO:0007829|PDB:6FW2"
FT STRAND 134..139
FT /evidence="ECO:0007829|PDB:6FW2"
FT STRAND 146..151
FT /evidence="ECO:0007829|PDB:6FW2"
FT STRAND 154..160
FT /evidence="ECO:0007829|PDB:6FW2"
FT HELIX 163..173
FT /evidence="ECO:0007829|PDB:6FW2"
FT STRAND 179..182
FT /evidence="ECO:0007829|PDB:6FW2"
FT HELIX 192..195
FT /evidence="ECO:0007829|PDB:6FW2"
FT STRAND 205..210
FT /evidence="ECO:0007829|PDB:6FW2"
FT STRAND 212..217
FT /evidence="ECO:0007829|PDB:6FW2"
FT HELIX 218..225
FT /evidence="ECO:0007829|PDB:6FW2"
FT HELIX 234..237
FT /evidence="ECO:0007829|PDB:6FW2"
FT STRAND 240..246
FT /evidence="ECO:0007829|PDB:6FW2"
FT HELIX 250..253
FT /evidence="ECO:0007829|PDB:6FW2"
FT STRAND 256..259
FT /evidence="ECO:0007829|PDB:6FW2"
FT STRAND 262..271
FT /evidence="ECO:0007829|PDB:6FW2"
FT HELIX 274..277
FT /evidence="ECO:0007829|PDB:6FW2"
FT TURN 280..282
FT /evidence="ECO:0007829|PDB:6FW2"
FT HELIX 291..297
FT /evidence="ECO:0007829|PDB:6FW2"
FT HELIX 302..304
FT /evidence="ECO:0007829|PDB:6FW2"
FT TURN 305..307
FT /evidence="ECO:0007829|PDB:6FW2"
FT STRAND 308..310
FT /evidence="ECO:0007829|PDB:6FW2"
FT STRAND 313..322
FT /evidence="ECO:0007829|PDB:6FW2"
FT STRAND 324..327
FT /evidence="ECO:0007829|PDB:6FW2"
FT STRAND 331..334
FT /evidence="ECO:0007829|PDB:6FW2"
SQ SEQUENCE 337 AA; 37499 MW; F983AB08F3D646C4 CRC64;
MGAAGSSALA RFVLLAQSRP GWLGVAALGL TAVALGAVAW RRAWPTRRRR LLQQVGTVAQ
LWIYPVKSCK GVPVSEAECT AMGLRSGNLR DRFWLVINQE GNMVTARQEP RLVLISLTCD
GDTLTLSAAY TKDLLLPIKT PTTNAVHKCR VHGLEIEGRD CGEATAQWIT SFLKSQPYRL
VHFEPHMRPR RPHQIADLFR PKDQIAYSDT SPFLILSEAS LADLNSRLEK KVKATNFRPN
IVISGCDVYA EDSWDELLIG DVELKRVMAC SRCILTTVDP DTGVMSRKEP LETLKSYRQC
DPSERKLYGK SPLFGQYFVL ENPGTIKVGD PVYLLGQ
