ID D6RF21_HUMAN Unreviewed; 92 AA. AC D6RF21; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 02-SEP-2026, entry version 87. DE SubName: Full=5-methyltetrahydrofolate-homocysteine methyltransferase reductase {ECO:0000313|Ensembl:ENSP00000426710.1}; GN Name=MTRR {ECO:0000313|Ensembl:ENSP00000426710.1}; 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 {ECO:0000313|Ensembl:ENSP00000426710.1, ECO:0000313|Proteomes:UP000005640}; RN [1] {ECO:0000313|Ensembl:ENSP00000426710.1, ECO:0000313|Proteomes:UP000005640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=11237011; DOI=10.1038/35057062; RG International Human Genome Sequencing Consortium; RA Lander E.S., Linton L.M., Birren B., Nusbaum C., Zody M.C., Baldwin J., RA Devon K., Dewar K., Doyle M., FitzHugh W., Funke R., Gage D., Harris K., RA Heaford A., Howland J., Kann L., Lehoczky J., LeVine R., McEwan P., RA McKernan K., Meldrim J., Mesirov J.P., Miranda C., Morris W., Naylor J., RA Raymond C., Rosetti M., Santos R., Sheridan A., Sougnez C., RA Stange-Thomann N., Stojanovic N., Subramanian A., Wyman D., Rogers J., RA Sulston J., Ainscough R., Beck S., Bentley D., Burton J., Clee C., RA Carter N., Coulson A., Deadman R., Deloukas P., Dunham A., Dunham I., RA Durbin R., French L., Grafham D., Gregory S., Hubbard T., Humphray S., RA Hunt A., Jones M., Lloyd C., McMurray A., Matthews L., Mercer S., Milne S., RA Mullikin J.C., Mungall A., Plumb R., Ross M., Shownkeen R., Sims S., RA Waterston R.H., Wilson R.K., Hillier L.W., McPherson J.D., Marra M.A., RA Mardis E.R., Fulton L.A., Chinwalla A.T., Pepin K.H., Gish W.R., RA Chissoe S.L., Wendl M.C., Delehaunty K.D., Miner T.L., Delehaunty A., RA Kramer J.B., Cook L.L., Fulton R.S., Johnson D.L., Minx P.J., Clifton S.W., RA Hawkins T., Branscomb E., Predki P., Richardson P., Wenning S., Slezak T., RA Doggett N., Cheng J.F., Olsen A., Lucas S., Elkin C., Uberbacher E., RA Frazier M., Gibbs R.A., Muzny D.M., Scherer S.E., Bouck J.B., RA Sodergren E.J., Worley K.C., Rives C.M., Gorrell J.H., Metzker M.L., RA Naylor S.L., Kucherlapati R.S., Nelson D.L., Weinstock G.M., Sakaki Y., RA Fujiyama A., Hattori M., Yada T., Toyoda A., Itoh T., Kawagoe C., RA Watanabe H., Totoki Y., Taylor T., Weissenbach J., Heilig R., Saurin W., RA Artiguenave F., Brottier P., Bruls T., Pelletier E., Robert C., Wincker P., RA Smith D.R., Doucette-Stamm L., Rubenfield M., Weinstock K., Lee H.M., RA Dubois J., Rosenthal A., Platzer M., Nyakatura G., Taudien S., Rump A., RA Yang H., Yu J., Wang J., Huang G., Gu J., Hood L., Rowen L., Madan A., RA Qin S., Davis R.W., Federspiel N.A., Abola A.P., Proctor M.J., Myers R.M., RA Schmutz J., Dickson M., Grimwood J., Cox D.R., Olson M.V., Kaul R., RA Raymond C., Shimizu N., Kawasaki K., Minoshima S., Evans G.A., RA Athanasiou M., Schultz R., Roe B.A., Chen F., Pan H., Ramser J., RA Lehrach H., Reinhardt R., McCombie W.R., de la Bastide M., Dedhia N., RA Blocker H., Hornischer K., Nordsiek G., Agarwala R., Aravind L., RA Bailey J.A., Bateman A., Batzoglou S., Birney E., Bork P., Brown D.G., RA Burge C.B., Cerutti L., Chen H.C., Church D., Clamp M., Copley R.R., RA Doerks T., Eddy S.R., Eichler E.E., Furey T.S., Galagan J., Gilbert J.G., RA Harmon C., Hayashizaki Y., Haussler D., Hermjakob H., Hokamp K., Jang W., RA Johnson L.S., Jones T.A., Kasif S., Kaspryzk A., Kennedy S., Kent W.J., RA Kitts P., Koonin E.V., Korf I., Kulp D., Lancet D., Lowe T.M., RA McLysaght A., Mikkelsen T., Moran J.V., Mulder N., Pollara V.J., RA Ponting C.P., Schuler G., Schultz J., Slater G., Smit A.F., Stupka E., RA Szustakowski J., Thierry-Mieg D., Thierry-Mieg J., Wagner L., Wallis J., RA Wheeler R., Williams A., Wolf Y.I., Wolfe K.H., Yang S.P., Yeh R.F., RA Collins F., Guyer M.S., Peterson J., Felsenfeld A., Wetterstrand K.A., RA Patrinos A., Morgan M.J., de Jong P., Catanese J.J., Osoegawa K., RA Shizuya H., Choi S., Chen Y.J.; RT "Initial sequencing and analysis of the human genome."; RL Nature 409:860-921(2001). RN [2] {ECO:0000313|Ensembl:ENSP00000426710.1, ECO:0000313|Proteomes:UP000005640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15372022; DOI=10.1038/nature02919; RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S., RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., RA Dickson M., Cheng J.F., Eichler E.E., Olsen A., Pennacchio L.A., RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.; RT "The DNA sequence and comparative analysis of human chromosome 5."; RL Nature 431:268-274(2004). RN [3] {ECO:0000313|Ensembl:ENSP00000426710.1, ECO:0000313|Proteomes:UP000005640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15496913; DOI=10.1038/nature03001; RG International Human Genome Sequencing Consortium; RT "Finishing the euchromatic sequence of the human genome."; RL Nature 431:931-945(2004). RN [4] {ECO:0007829|PubMed:21269460} 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., Burckstummer 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 [5] {ECO:0000313|Ensembl:ENSP00000426710.1} RP IDENTIFICATION. RG Ensembl; RL Submitted (JAN-2026) to UniProtKB. CC -!- COFACTOR: CC Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000256|PROSITE- CC ProRule:PRU00088}; CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00088}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AC010346; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC025174; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR AlphaFoldDB; D6RF21; -. DR SMR; D6RF21; -. DR MassIVE; D6RF21; -. DR ProteomicsDB; 14433; -. DR Ensembl; ENST00000513439.5; ENSP00000426710.1; ENSG00000124275.16. DR UCSC; uc063cej.1; human. DR HGNC; HGNC:7473; MTRR. DR VEuPathDB; HostDB:ENSG00000124275; -. DR GeneTree; ENSGT00940000155822; -. DR OrthoDB; 1856718at2759; -. DR ChiTaRS; MTRR; human. DR Proteomes; UP000005640; Chromosome 5. DR Bgee; ENSG00000124275; Expressed in endothelial cell and 199 other cell types or tissues. DR ExpressionAtlas; D6RF21; baseline and differential. DR GO; GO:0010181; F:FMN binding; IEA:InterPro. DR Gene3D; 3.40.50.360; -; 1. DR InterPro; IPR008254; Flavodoxin/NO_synth. DR InterPro; IPR029039; Flavoprotein-like_sf. DR PANTHER; PTHR19384:SF84; METHIONINE SYNTHASE REDUCTASE; 1. DR PANTHER; PTHR19384; NITRIC OXIDE SYNTHASE-RELATED; 1. DR Pfam; PF00258; Flavodoxin_1; 1. DR SUPFAM; SSF52218; Flavoproteins; 1. DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1. PE 1: Evidence at protein level; KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630, ECO:0000256|PROSITE- KW ProRule:PRU00088}; FMN {ECO:0000256|PROSITE-ProRule:PRU00088}; KW Proteomics identification {ECO:0007829|PeptideAtlas:D6RF21, KW ECO:0007829|ProteomicsDB:D6RF21}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}. FT DOMAIN 4..92 FT /note="Flavodoxin-like" FT /evidence="ECO:0000259|PROSITE:PS50902" FT BINDING 10..14 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00088" SQ SEQUENCE 92 AA; 10251 MW; 8E532E011921438B CRC64; MRRFLLLYAT QQGQAKAIAE EICEQAVVHG FSADLHCISE SDKYDLKTET APLVVVVSTT GTGDPPDTAR KFVKEIQNQT LPVDFFAHLR SR //