FXRD1_MOUSE
ID FXRD1_MOUSE Reviewed; 487 AA.
AC Q3TQB2; Q8R1D0;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=FAD-dependent oxidoreductase domain-containing protein 1;
DE EC=1.-.-.-;
GN Name=Foxred1;
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] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Cerebellum, and Lung;
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] (ISOFORM 2).
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney;
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: Required for the assembly of the mitochondrial membrane
CC respiratory chain NADH dehydrogenase (Complex I). Involved in mid-late
CC stages of complex I assembly. {ECO:0000250|UniProtKB:Q96CU9}.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC -!- SUBUNIT: Associates with components of the mitochondrial respiratory
CC chain complex I. {ECO:0000250|UniProtKB:Q96CU9}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:Q96CU9}; Single-pass membrane protein
CC {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q3TQB2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3TQB2-2; Sequence=VSP_022630;
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DR EMBL; AK144759; BAE26052.1; -; mRNA.
DR EMBL; AK163722; BAE37472.1; -; mRNA.
DR EMBL; BC024806; AAH24806.1; -; mRNA.
DR CCDS; CCDS22958.1; -. [Q3TQB2-2]
DR CCDS; CCDS80974.1; -. [Q3TQB2-1]
DR RefSeq; NP_001278377.1; NM_001291448.1. [Q3TQB2-1]
DR RefSeq; NP_758495.1; NM_172291.2. [Q3TQB2-2]
DR AlphaFoldDB; Q3TQB2; -.
DR SMR; Q3TQB2; -.
DR STRING; 10090.ENSMUSP00000038924; -.
DR iPTMnet; Q3TQB2; -.
DR PhosphoSitePlus; Q3TQB2; -.
DR EPD; Q3TQB2; -.
DR MaxQB; Q3TQB2; -.
DR PaxDb; Q3TQB2; -.
DR PeptideAtlas; Q3TQB2; -.
DR PRIDE; Q3TQB2; -.
DR ProteomicsDB; 271618; -. [Q3TQB2-1]
DR ProteomicsDB; 271619; -. [Q3TQB2-2]
DR Antibodypedia; 32986; 170 antibodies from 27 providers.
DR DNASU; 235169; -.
DR Ensembl; ENSMUST00000043805; ENSMUSP00000038924; ENSMUSG00000039048. [Q3TQB2-2]
DR Ensembl; ENSMUST00000127996; ENSMUSP00000118037; ENSMUSG00000039048. [Q3TQB2-1]
DR GeneID; 235169; -.
DR KEGG; mmu:235169; -.
DR UCSC; uc009ost.2; mouse. [Q3TQB2-2]
DR UCSC; uc009osu.2; mouse. [Q3TQB2-1]
DR CTD; 55572; -.
DR MGI; MGI:2446262; Foxred1.
DR VEuPathDB; HostDB:ENSMUSG00000039048; -.
DR eggNOG; KOG2853; Eukaryota.
DR GeneTree; ENSGT00390000006114; -.
DR HOGENOM; CLU_007884_4_4_1; -.
DR InParanoid; Q3TQB2; -.
DR OMA; PDHNALI; -.
DR OrthoDB; 752680at2759; -.
DR PhylomeDB; Q3TQB2; -.
DR TreeFam; TF314003; -.
DR BioGRID-ORCS; 235169; 25 hits in 74 CRISPR screens.
DR ChiTaRS; Foxred1; mouse.
DR PRO; PR:Q3TQB2; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q3TQB2; protein.
DR Bgee; ENSMUSG00000039048; Expressed in spermatocyte and 253 other tissues.
DR ExpressionAtlas; Q3TQB2; baseline and differential.
DR Genevisible; Q3TQB2; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005743; C:mitochondrial inner membrane; ISS:UniProtKB.
DR GO; GO:0005747; C:mitochondrial respiratory chain complex I; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0032981; P:mitochondrial respiratory chain complex I assembly; ISS:UniProtKB.
DR Gene3D; 3.50.50.60; -; 1.
DR InterPro; IPR006076; FAD-dep_OxRdtase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR Pfam; PF01266; DAO; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Electron transport; FAD; Flavoprotein; Membrane;
KW Mitochondrion; Mitochondrion inner membrane; Oxidoreductase;
KW Reference proteome; Respiratory chain; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..487
FT /note="FAD-dependent oxidoreductase domain-containing
FT protein 1"
FT /id="PRO_0000274144"
FT TRANSMEM 62..82
FT /note="Helical"
FT /evidence="ECO:0000255"
FT VAR_SEQ 403
FT /note="E -> EHLLHLQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_022630"
SQ SEQUENCE 487 AA; 54178 MW; C3694EF4015CA11F CRC64;
MFRRALRLGL GPGLPYRGLR TRKGGFTLDW DAKVSDFKKK VDSILPGKKY EVLYDTSHLP
PEQADVVIIG GGILGLSVAF WLKKLESRRG AIRVLVVEQD HTYSRASSTG PSVGGIWQQF
SVPENVQLSL FSINFLRNIN EYLAVVDAPP VELQFNPSGC LLLASEKDAA TLENNVKMQR
QEGAKVCLMS PEQLQTKFPW INVEGVALAS YGLEDEGWFD AWSLLQGLRR KVQSMGVFFC
QGEVTRFITS STPMKTPTGE HVVLRRINNV HVKMDKSLEY QPVECAVVIN AAGAWSGKIA
ELAGVGKGLP GTLQGTKLPV EPRKRYVHLW HCPQGPGLET PLVADISGVY FRREGLGSNY
LGGCSPTEEE EPDPTNLNVD HDFFQNKVWP HLVQRVPSFK TLEVQSAWAG YYDYNTFDQN
GVVGPHPLVV NMYFATGFSG RGLQHAPGIG RAVAEIMLEG HFKTIDMSPF LFTRFYLGEK
LQEYNIL
