MARC2_HUMAN
ID MARC2_HUMAN Reviewed; 335 AA.
AC Q969Z3; B2D0R5; D3DTB3; Q0JSK7; Q5VT67; Q5VXC7; Q7L317; Q9H066; Q9NWU0;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Mitochondrial amidoxime reducing component 2 {ECO:0000303|PubMed:21029045};
DE Short=mARC2 {ECO:0000303|PubMed:21029045};
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 {ECO:0000312|HGNC:HGNC:26064}; Synonyms=MARC2, MOSC2;
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] (ISOFORM 2).
RC TISSUE=Uterus;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS SER-3 AND SER-244.
RG NIEHS SNPs program;
RL Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Cervix, Colon, and Lung;
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 193-335.
RC TISSUE=Carcinoma;
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 [8]
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 [9]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND CATALYTIC ACTIVITY.
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 [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [11]
RP UBIQUITINATION AT LYS-59; LYS-138; LYS-144; LYS-156; LYS-166; LYS-173;
RP LYS-187; LYS-287 AND LYS-294.
RX PubMed=25621951; DOI=10.1038/ncb3097;
RA Cunningham C.N., Baughman J.M., Phu L., Tea J.S., Yu C., Coons M.,
RA Kirkpatrick D.S., Bingol B., Corn J.E.;
RT "USP30 and parkin homeostatically regulate atypical ubiquitin chains on
RT mitochondria.";
RL Nat. Cell Biol. 17:160-169(2015).
RN [12]
RP VARIANTS SER-244 AND TRP-245, CHARACTERIZATION OF VARIANTS SER-244 AND
RP TRP-245, 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:21029045, PubMed:24423752). As a component
CC of prodrug-converting system, reduces a multitude of N-hydroxylated
CC prodrugs particularly amidoximes, leading to increased drug
CC bioavailability (PubMed:21029045, PubMed:24423752). 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).
CC {ECO:0000269|PubMed:21029045, ECO:0000269|PubMed:24423752}.
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:24423752};
CC Note=Binds 1 Mo-molybdopterin (Mo-MPT) cofactor per subunit.
CC {ECO:0000269|PubMed:24423752};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=830 uM for benzamidoxime {ECO:0000269|PubMed:21029045,
CC ECO:0000269|PubMed:24423752};
CC KM=400 uM for benzamidoxime (at pH 6.0 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:24423752};
CC KM=3 mM for NOHA {ECO:0000269|PubMed:21029045,
CC ECO:0000269|PubMed:24423752};
CC KM=3.7 mM for NHAM {ECO:0000269|PubMed:21029045,
CC ECO:0000269|PubMed:24423752};
CC Vmax=307 nmol/min/mg enzyme toward benzamidoxime
CC {ECO:0000269|PubMed:21029045, ECO:0000269|PubMed:24423752};
CC Vmax=119 nmol/min/mg enzyme toward benzamidoxime (at pH 6.0 and 37
CC degrees Celsius) {ECO:0000269|PubMed:24423752};
CC Vmax=373 nmol/min/mg enzyme toward NOHA {ECO:0000269|PubMed:21029045,
CC ECO:0000269|PubMed:24423752};
CC Vmax=36.5 nmol/min/mg enzyme toward NHAM
CC {ECO:0000269|PubMed:21029045, ECO:0000269|PubMed:24423752};
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; Peripheral membrane
CC protein. Peroxisome {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q969Z3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q969Z3-2; Sequence=VSP_022513, VSP_022514;
CC -!- PTM: Ubiquitinated by PRKN during mitophagy, leading to its degradation
CC and enhancement of mitophagy. Deubiquitinated by USP30.
CC {ECO:0000269|PubMed:25621951}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA91287.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/mosc2/";
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DR EMBL; AL136931; CAB66865.1; -; mRNA.
DR EMBL; AM393631; CAL38507.1; -; mRNA.
DR EMBL; EU567145; ACB21048.1; -; Genomic_DNA.
DR EMBL; AL359353; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL606726; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471100; EAW93293.1; -; Genomic_DNA.
DR EMBL; CH471100; EAW93294.1; -; Genomic_DNA.
DR EMBL; BC011973; AAH11973.1; -; mRNA.
DR EMBL; BC015829; AAH15829.2; -; mRNA.
DR EMBL; BC016859; AAH16859.1; -; mRNA.
DR EMBL; AK000612; BAA91287.1; ALT_INIT; mRNA.
DR CCDS; CCDS1525.1; -. [Q969Z3-1]
DR CCDS; CCDS81425.1; -. [Q969Z3-2]
DR RefSeq; NP_001304267.1; NM_001317338.1. [Q969Z3-1]
DR RefSeq; NP_001317971.1; NM_001331042.1. [Q969Z3-2]
DR RefSeq; NP_060368.2; NM_017898.4. [Q969Z3-1]
DR AlphaFoldDB; Q969Z3; -.
DR SMR; Q969Z3; -.
DR BioGRID; 120329; 45.
DR IntAct; Q969Z3; 10.
DR MINT; Q969Z3; -.
DR STRING; 9606.ENSP00000355880; -.
DR ChEMBL; CHEMBL4523423; -.
DR iPTMnet; Q969Z3; -.
DR PhosphoSitePlus; Q969Z3; -.
DR BioMuta; MARC2; -.
DR DMDM; 74760692; -.
DR EPD; Q969Z3; -.
DR jPOST; Q969Z3; -.
DR MassIVE; Q969Z3; -.
DR MaxQB; Q969Z3; -.
DR PaxDb; Q969Z3; -.
DR PeptideAtlas; Q969Z3; -.
DR PRIDE; Q969Z3; -.
DR ProteomicsDB; 75882; -. [Q969Z3-1]
DR ProteomicsDB; 75883; -. [Q969Z3-2]
DR Antibodypedia; 2381; 139 antibodies from 21 providers.
DR DNASU; 54996; -.
DR Ensembl; ENST00000359316.6; ENSP00000352266.2; ENSG00000117791.16. [Q969Z3-2]
DR Ensembl; ENST00000366913.8; ENSP00000355880.3; ENSG00000117791.16. [Q969Z3-1]
DR GeneID; 54996; -.
DR KEGG; hsa:54996; -.
DR MANE-Select; ENST00000366913.8; ENSP00000355880.3; NM_017898.5; NP_060368.2.
DR UCSC; uc001hmq.4; human. [Q969Z3-1]
DR CTD; 54996; -.
DR DisGeNET; 54996; -.
DR GeneCards; MTARC2; -.
DR HGNC; HGNC:26064; MTARC2.
DR HPA; ENSG00000117791; Tissue enhanced (kidney, liver).
DR MIM; 614127; gene.
DR neXtProt; NX_Q969Z3; -.
DR OpenTargets; ENSG00000117791; -.
DR VEuPathDB; HostDB:ENSG00000117791; -.
DR eggNOG; KOG2362; Eukaryota.
DR GeneTree; ENSGT00940000159665; -.
DR HOGENOM; CLU_028286_6_2_1; -.
DR InParanoid; Q969Z3; -.
DR OMA; GYPFLLI; -.
DR OrthoDB; 919343at2759; -.
DR PhylomeDB; Q969Z3; -.
DR TreeFam; TF316807; -.
DR BRENDA; 1.16.98.B1; 2681.
DR BRENDA; 1.7.2.1; 2681.
DR PathwayCommons; Q969Z3; -.
DR Reactome; R-HSA-211945; Phase I - Functionalization of compounds.
DR SABIO-RK; Q969Z3; -.
DR SignaLink; Q969Z3; -.
DR BioGRID-ORCS; 54996; 2 hits in 828 CRISPR screens.
DR ChiTaRS; MARC2; human.
DR GeneWiki; MOSC2; -.
DR GenomeRNAi; 54996; -.
DR Pharos; Q969Z3; Tbio.
DR PRO; PR:Q969Z3; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q969Z3; protein.
DR Bgee; ENSG00000117791; Expressed in right lobe of liver and 192 other tissues.
DR ExpressionAtlas; Q969Z3; baseline and differential.
DR Genevisible; Q969Z3; HS.
DR GO; GO:0005741; C:mitochondrial outer membrane; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; IDA:LIFEdb.
DR GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
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; IMP: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 Acetylation; Alternative splicing; Isopeptide bond; Membrane;
KW Mitochondrion; Mitochondrion outer membrane; Molybdenum; Oxidoreductase;
KW Peroxisome; Reference proteome; Transit peptide; Ubl conjugation.
FT TRANSIT 1..35
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 36..335
FT /note="Mitochondrial amidoxime reducing component 2"
FT /id="PRO_0000273340"
FT DOMAIN 188..334
FT /note="MOSC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00670"
FT MOD_RES 156
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q922Q1"
FT CROSSLNK 59
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:25621951"
FT CROSSLNK 138
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:25621951"
FT CROSSLNK 144
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:25621951"
FT CROSSLNK 156
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin); alternate"
FT /evidence="ECO:0000269|PubMed:25621951"
FT CROSSLNK 166
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:25621951"
FT CROSSLNK 173
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:25621951"
FT CROSSLNK 187
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:25621951"
FT CROSSLNK 287
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:25621951"
FT CROSSLNK 294
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:25621951"
FT VAR_SEQ 251..257
FT /note="DTWDELL -> ASATRRD (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11230166"
FT /id="VSP_022513"
FT VAR_SEQ 258..335
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11230166"
FT /id="VSP_022514"
FT VARIANT 3
FT /note="A -> S (in dbSNP:rs72472370)"
FT /evidence="ECO:0000269|Ref.3"
FT /id="VAR_062275"
FT VARIANT 244
FT /note="G -> S (decreased catalytic efficiency toward
FT benzamidoxime; no effect on affinity for benzamidoxime; no
FT effect on binding of the molybdenum cofactor;
FT dbSNP:rs3795535)"
FT /evidence="ECO:0000269|PubMed:24423752, ECO:0000269|Ref.3"
FT /id="VAR_030133"
FT VARIANT 245
FT /note="C -> W (decreased catalytic activity toward
FT benzamidoxime; no effect on affinity for benzamidoxime; no
FT effect on binding of the molybdenum cofactor;
FT dbSNP:rs76664695)"
FT /evidence="ECO:0000269|PubMed:24423752"
FT /id="VAR_070777"
FT CONFLICT 169
FT /note="T -> A (in Ref. 2; CAL38507)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 335 AA; 38023 MW; 4C6A9B8B9AC0F74D CRC64;
MGASSSSALA RLGLPARPWP RWLGVAALGL AAVALGTVAW RRAWPRRRRR LQQVGTVAKL
WIYPVKSCKG VPVSEAECTA MGLRSGNLRD RFWLVIKEDG HMVTARQEPR LVLISIIYEN
NCLIFRAPDM DQLVLPSKQP SSNKLHNCRI FGLDIKGRDC GNEAAKWFTN FLKTEAYRLV
QFETNMKGRT SRKLLPTLDQ NFQVAYPDYC PLLIMTDASL VDLNTRMEKK MKMENFRPNI
VVTGCDAFEE DTWDELLIGS VEVKKVMACP RCILTTVDPD TGVIDRKQPL DTLKSYRLCD
PSERELYKLS PLFGIYYSVE KIGSLRVGDP VYRMV
