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   27-MAR-2024, entry version 152.
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; 75.
DR   IntAct; Q5VT66; 18.
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; 9606-ENSP00000355877; -.
DR   PeptideAtlas; Q5VT66; -.
DR   ProteomicsDB; 65307; -. [Q5VT66-1]
DR   ProteomicsDB; 65308; -. [Q5VT66-2]
DR   ProteomicsDB; 65309; -. [Q5VT66-3]
DR   Pumba; Q5VT66; -.
DR   Antibodypedia; 34627; 138 antibodies from 22 providers.
DR   DNASU; 64757; -.
DR   Ensembl; ENST00000366910.10; ENSP00000355877.5; ENSG00000186205.14. [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   AGR; HGNC:26189; -.
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; AHDRSFM; -.
DR   OrthoDB; 5490564at2759; -.
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 821 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 145 other cell types or tissues.
DR   ExpressionAtlas; Q5VT66; baseline and differential.
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; MOCOS_middle.
DR   InterPro; IPR011037; Pyrv_Knase-like_insert_dom_sf.
DR   PANTHER; PTHR14237:SF25; MITOCHONDRIAL AMIDOXIME-REDUCING COMPONENT 1; 1.
DR   PANTHER; PTHR14237; MOLYBDOPTERIN COFACTOR SULFURASE MOSC; 1.
DR   Pfam; PF03473; MOSC; 1.
DR   Pfam; PF03476; MOSC_N; 1.
DR   SUPFAM; SSF141673; MOSC N-terminal domain-like; 1.
DR   SUPFAM; SSF50800; PK beta-barrel domain-like; 1.
DR   PROSITE; PS51340; MOSC; 1.
DR   Genevisible; Q5VT66; HS.
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
//