DOXA2_MOUSE
ID DOXA2_MOUSE Reviewed; 320 AA.
AC Q9D311; A2AQ98; Q9D7U8;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Dual oxidase maturation factor 2;
GN Name=Duoxa2;
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].
RC STRAIN=C57BL/6J; TISSUE=Colon, and Stomach;
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 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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Colon;
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: Required for the maturation and the transport from the
CC endoplasmic reticulum to the plasma membrane of functional DUOX2. May
CC play a role in thyroid hormone synthesis (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Heterodimer with DUXA2; disulfide-linked. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Multi-pass membrane protein {ECO:0000250}.
CC -!- PTM: N-glycosylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the DUOXA family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB25910.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK008816; BAB25910.1; ALT_FRAME; mRNA.
DR EMBL; AK018569; BAB31281.1; -; mRNA.
DR EMBL; AL844566; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC031111; AAH31111.1; -; mRNA.
DR CCDS; CCDS16660.1; -.
DR RefSeq; NP_080053.1; NM_025777.2.
DR AlphaFoldDB; Q9D311; -.
DR SMR; Q9D311; -.
DR STRING; 10090.ENSMUSP00000028656; -.
DR GlyGen; Q9D311; 3 sites.
DR PhosphoSitePlus; Q9D311; -.
DR PaxDb; Q9D311; -.
DR PRIDE; Q9D311; -.
DR ProteomicsDB; 277375; -.
DR Antibodypedia; 2475; 100 antibodies from 18 providers.
DR DNASU; 66811; -.
DR Ensembl; ENSMUST00000028656; ENSMUSP00000028656; ENSMUSG00000027225.
DR GeneID; 66811; -.
DR KEGG; mmu:66811; -.
DR UCSC; uc008mam.1; mouse.
DR CTD; 405753; -.
DR MGI; MGI:1914061; Duoxa2.
DR VEuPathDB; HostDB:ENSMUSG00000027225; -.
DR eggNOG; KOG3921; Eukaryota.
DR GeneTree; ENSGT00390000008240; -.
DR HOGENOM; CLU_045258_0_0_1; -.
DR InParanoid; Q9D311; -.
DR OMA; IGLMHIN; -.
DR OrthoDB; 835845at2759; -.
DR PhylomeDB; Q9D311; -.
DR TreeFam; TF312996; -.
DR BioGRID-ORCS; 66811; 3 hits in 74 CRISPR screens.
DR PRO; PR:Q9D311; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q9D311; protein.
DR Bgee; ENSMUSG00000027225; Expressed in morula and 23 other tissues.
DR Genevisible; Q9D311; MM.
DR GO; GO:0045177; C:apical part of cell; ISS:UniProtKB.
DR GO; GO:0031252; C:cell leading edge; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
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; ISS:UniProtKB.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0042743; P:hydrogen peroxide metabolic process; IGI:MGI.
DR GO; GO:2000147; P:positive regulation of cell motility; ISS:UniProtKB.
DR GO; GO:0010729; P:positive regulation of hydrogen peroxide biosynthetic process; ISS:UniProtKB.
DR GO; GO:0008104; P:protein localization; ISO:MGI.
DR GO; GO:0051604; P:protein maturation; 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 2: Evidence at transcript level;
KW Disulfide bond; Endoplasmic reticulum; Glycoprotein; Membrane;
KW Protein transport; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..320
FT /note="Dual oxidase maturation factor 2"
FT /id="PRO_0000264246"
FT TRANSMEM 22..42
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 43..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..206
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 207..227
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 228..249
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 250..270
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 271..320
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 DISULFID 167
FT /note="Interchain (with C-568 in DUXA2)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 233
FT /note="Interchain (with C-582 in DUXA2)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT CONFLICT 79..80
FT /note="GR -> EE (in Ref. 1; BAB25910)"
FT /evidence="ECO:0000305"
FT CONFLICT 146
FT /note="L -> F (in Ref. 1; BAB25910)"
FT /evidence="ECO:0000305"
FT CONFLICT 176
FT /note="A -> P (in Ref. 1; BAB25910)"
FT /evidence="ECO:0000305"
FT CONFLICT 209
FT /note="A -> V (in Ref. 1; BAB25910)"
FT /evidence="ECO:0000305"
FT CONFLICT 217
FT /note="T -> A (in Ref. 1; BAB25910)"
FT /evidence="ECO:0000305"
FT CONFLICT 235
FT /note="F -> S (in Ref. 1; BAB25910)"
FT /evidence="ECO:0000305"
FT CONFLICT 242
FT /note="L -> F (in Ref. 1; BAB25910)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 320 AA; 35427 MW; 4B7D4C81685162F7 CRC64;
MTAWDGVLPF YPQPRHAASF SVPLLIVILV FLSLAASFLF ILPGIRGHSR WFWLVRVLLS
LFIGAEIVAV HFSGDWFVGR VWTNTSYKAF SPSRVQVHVG LHVGLAGVNI TLRGTPRQQL
NETIDYNERF TWRLNEDYTK EYVHALEKGL PDPVLYLAEK FTPSSPCGLY HQYHLAGHYA
AATLWVAFCF WIIANALLSM PAPLYGGLAL LTTGAFTLFG VFAFASISSV PLCHFRLGSA
VLTPYYGASF WLTLATGILS LLLGGAVVIL HYTRPSALRS FLDLSVKDCS NQAKGNSPLT
LNNPQHEQLK SPDLNITTLL
