DOXA1_MOUSE
ID DOXA1_MOUSE Reviewed; 341 AA.
AC Q8VE49; A2AQ97;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Dual oxidase maturation factor 1;
DE AltName: Full=Dual oxidase activator 1;
GN Name=Duoxa1;
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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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).
CC -!- FUNCTION: May be required for the maturation and the transport from the
CC endoplasmic reticulum to the plasma membrane of functional DUOX1.
CC {ECO:0000250}.
CC -!- SUBUNIT: May interact with NUMB. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the DUOXA family. {ECO:0000305}.
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DR EMBL; AL844566; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC019755; AAH19755.1; -; mRNA.
DR CCDS; CCDS16661.1; -.
DR RefSeq; NP_001292191.1; NM_001305262.1.
DR RefSeq; XP_006499154.1; XM_006499091.3.
DR RefSeq; XP_006499157.1; XM_006499094.3.
DR RefSeq; XP_006499158.1; XM_006499095.3.
DR RefSeq; XP_017172410.1; XM_017316921.1.
DR PDB; 6WXR; EM; 3.20 A; B=1-341.
DR PDB; 6WXU; EM; 2.70 A; B/D=1-341.
DR PDB; 6WXV; EM; 3.30 A; B=1-341.
DR PDBsum; 6WXR; -.
DR PDBsum; 6WXU; -.
DR PDBsum; 6WXV; -.
DR AlphaFoldDB; Q8VE49; -.
DR SMR; Q8VE49; -.
DR STRING; 10090.ENSMUSP00000106166; -.
DR GlyGen; Q8VE49; 3 sites.
DR PhosphoSitePlus; Q8VE49; -.
DR PaxDb; Q8VE49; -.
DR PRIDE; Q8VE49; -.
DR ProteomicsDB; 277374; -.
DR Antibodypedia; 24331; 81 antibodies from 13 providers.
DR DNASU; 213696; -.
DR Ensembl; ENSMUST00000028653; ENSMUSP00000028653; ENSMUSG00000027224.
DR Ensembl; ENSMUST00000110537; ENSMUSP00000106166; ENSMUSG00000027224.
DR GeneID; 213696; -.
DR KEGG; mmu:213696; -.
DR UCSC; uc008man.1; mouse.
DR CTD; 90527; -.
DR MGI; MGI:2384861; Duoxa1.
DR VEuPathDB; HostDB:ENSMUSG00000027224; -.
DR eggNOG; KOG3921; Eukaryota.
DR GeneTree; ENSGT00390000008240; -.
DR HOGENOM; CLU_045258_0_0_1; -.
DR InParanoid; Q8VE49; -.
DR OMA; SEWFVGQ; -.
DR OrthoDB; 835845at2759; -.
DR PhylomeDB; Q8VE49; -.
DR TreeFam; TF312996; -.
DR BioGRID-ORCS; 213696; 2 hits in 58 CRISPR screens.
DR PRO; PR:Q8VE49; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q8VE49; protein.
DR Bgee; ENSMUSG00000027224; Expressed in urinary bladder urothelium and 48 other tissues.
DR ExpressionAtlas; Q8VE49; baseline and differential.
DR Genevisible; Q8VE49; MM.
DR GO; GO:0031252; C:cell leading edge; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:InterPro.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0042743; P:hydrogen peroxide metabolic process; IGI:MGI.
DR GO; GO:0010729; P:positive regulation of hydrogen peroxide biosynthetic process; ISS:UniProtKB.
DR GO; GO:0045666; P:positive regulation of neuron differentiation; IDA:MGI.
DR GO; GO:2000379; P:positive regulation of reactive oxygen species metabolic process; IGI:MGI.
DR GO; GO:0008104; P:protein localization; ISO:MGI.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0050727; P:regulation of inflammatory response; IGI:MGI.
DR GO; GO:2000609; P:regulation of thyroid hormone generation; IGI:MGI.
DR InterPro; IPR018469; Dual_oxidase_maturation_fac.
DR PANTHER; PTHR31158; PTHR31158; 1.
DR Pfam; PF10204; DuoxA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Glycoprotein; Membrane; Protein transport;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..341
FT /note="Dual oxidase maturation factor 1"
FT /id="PRO_0000264242"
FT TOPO_DOM 1..24
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 25..45
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 46..51
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 52..72
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 73..183
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 184..204
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 205
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 206..226
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 227..249
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 250..270
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 271..341
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 84
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 109
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 121
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 112
FT /note="L -> F (in Ref. 2; AAH19755)"
FT /evidence="ECO:0000305"
FT CONFLICT 285
FT /note="Q -> L (in Ref. 2; AAH19755)"
FT /evidence="ECO:0000305"
FT CONFLICT 318
FT /note="I -> T (in Ref. 2; AAH19755)"
FT /evidence="ECO:0000305"
FT STRAND 7..11
FT /evidence="ECO:0007829|PDB:6WXU"
FT HELIX 22..41
FT /evidence="ECO:0007829|PDB:6WXU"
FT HELIX 42..44
FT /evidence="ECO:0007829|PDB:6WXU"
FT HELIX 50..72
FT /evidence="ECO:0007829|PDB:6WXU"
FT STRAND 76..86
FT /evidence="ECO:0007829|PDB:6WXU"
FT STRAND 94..103
FT /evidence="ECO:0007829|PDB:6WXU"
FT STRAND 108..111
FT /evidence="ECO:0007829|PDB:6WXU"
FT STRAND 113..117
FT /evidence="ECO:0007829|PDB:6WXU"
FT STRAND 119..122
FT /evidence="ECO:0007829|PDB:6WXU"
FT STRAND 128..130
FT /evidence="ECO:0007829|PDB:6WXU"
FT STRAND 133..136
FT /evidence="ECO:0007829|PDB:6WXV"
FT HELIX 138..147
FT /evidence="ECO:0007829|PDB:6WXU"
FT HELIX 152..159
FT /evidence="ECO:0007829|PDB:6WXU"
FT STRAND 162..164
FT /evidence="ECO:0007829|PDB:6WXU"
FT HELIX 170..199
FT /evidence="ECO:0007829|PDB:6WXU"
FT HELIX 203..224
FT /evidence="ECO:0007829|PDB:6WXU"
FT HELIX 228..231
FT /evidence="ECO:0007829|PDB:6WXU"
FT STRAND 245..247
FT /evidence="ECO:0007829|PDB:6WXU"
FT HELIX 249..273
FT /evidence="ECO:0007829|PDB:6WXU"
SQ SEQUENCE 341 AA; 37588 MW; 9555188CFEF6F8AB CRC64;
MAALGHTLPF YTGTKPTFPM DTTLAVIITI FLTALVTFII ILPGIRGKTR LFWLLRVVTS
LFIGAVILAV NFSSEWSVGH VNANTTYKAF SPKWVSVDVG LQIGLGGVNI TLTGTPVQQL
NETINYNEAF AWRLGRSYAE EYAKALEKGL PDPVLYLAEK FTPRSPCGLY NQYRLAGHYA
SAMLWVAFLC WLLANVMLSM PVLVYGGHML LATGLFQLLA LFFFSMTTSL ISPCPLRLGT
AVLHTHHGPA FWITLATGLL CILLGLVMAV AHRMQPHRLK AFFNQSSEDP VLEWGSEEGG
LLSPHYRSIA ESPETQDIPM SVASSETCFK EEHPKESDCS L
