DOXA1_CAEEL
ID DOXA1_CAEEL Reviewed; 397 AA.
AC P34298;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 20-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Dual oxidase maturation factor 1 {ECO:0000312|WormBase:C06E1.3};
GN Name=doxa-1 {ECO:0000312|WormBase:C06E1.3};
GN ORFNames=C06E1.3 {ECO:0000312|WormBase:C06E1.3};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=7906398; DOI=10.1038/368032a0;
RA Wilson R., Ainscough R., Anderson K., Baynes C., Berks M., Bonfield J.,
RA Burton J., Connell M., Copsey T., Cooper J., Coulson A., Craxton M.,
RA Dear S., Du Z., Durbin R., Favello A., Fraser A., Fulton L., Gardner A.,
RA Green P., Hawkins T., Hillier L., Jier M., Johnston L., Jones M.,
RA Kershaw J., Kirsten J., Laisster N., Latreille P., Lightning J., Lloyd C.,
RA Mortimore B., O'Callaghan M., Parsons J., Percy C., Rifken L., Roopra A.,
RA Saunders D., Shownkeen R., Sims M., Smaldon N., Smith A., Smith M.,
RA Sonnhammer E., Staden R., Sulston J., Thierry-Mieg J., Thomas K.,
RA Vaudin M., Vaughan K., Waterston R., Watson A., Weinstock L.,
RA Wilkinson-Sproat J., Wohldman P.;
RT "2.2 Mb of contiguous nucleotide sequence from chromosome III of C.
RT elegans.";
RL Nature 368:32-38(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3]
RP FUNCTION, INTERACTION WITH BLI-3 AND TSP-15, AND TISSUE SPECIFICITY.
RX PubMed=23028364; DOI=10.1371/journal.pgen.1002957;
RA Moribe H., Konakawa R., Koga D., Ushiki T., Nakamura K., Mekada E.;
RT "Tetraspanin is required for generation of reactive oxygen species by the
RT dual oxidase system in Caenorhabditis elegans.";
RL PLoS Genet. 8:E1002957-E1002957(2012).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=25480962; DOI=10.1534/g3.114.015982;
RA Xu Z., Luo J., Li Y., Ma L.;
RT "The BLI-3/TSP-15/DOXA-1 dual oxidase complex is required for iodide
RT toxicity in Caenorhabditis elegans.";
RL G3 (Bethesda) 5:195-203(2015).
CC -!- FUNCTION: Plays a role in cuticle biogenesis (PubMed:23028364,
CC PubMed:25480962). In complex with tsp-15 and the dual oxidase bli-3,
CC promotes the generation of reactive oxygen species (ROS) and tyrosine
CC cross-linking of collagen, thus stabilizing cuticular extracellular
CC matrix (PubMed:23028364). {ECO:0000269|PubMed:23028364,
CC ECO:0000269|PubMed:25480962}.
CC -!- SUBUNIT: Interacts with bli-3 and tsp-15.
CC {ECO:0000269|PubMed:23028364}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in the hypodermis, specifically in seam
CC cells, the terminal bulb of the pharynx, the distal region of the
CC gonadal arm, vulva, spermatheca and uterus.
CC {ECO:0000269|PubMed:23028364}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown results in a blistered
CC cuticle phenotype and resistance to iodide toxicity.
CC {ECO:0000269|PubMed:25480962}.
CC -!- SIMILARITY: Belongs to the DUOXA family. {ECO:0000305}.
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DR EMBL; FO080280; CCD62563.1; -; Genomic_DNA.
DR PIR; A88533; A88533.
DR RefSeq; NP_498886.2; NM_066485.5.
DR AlphaFoldDB; P34298; -.
DR SMR; P34298; -.
DR BioGRID; 47168; 1.
DR ComplexPortal; CPX-1020; BLI-3/DOXA-1/TSP-15 dual oxidase complex.
DR STRING; 6239.C06E1.3; -.
DR EPD; P34298; -.
DR PaxDb; P34298; -.
DR EnsemblMetazoa; C06E1.3.1; C06E1.3.1; WBGene00015519.
DR GeneID; 182313; -.
DR KEGG; cel:CELE_C06E1.3; -.
DR UCSC; C06E1.3; c. elegans.
DR CTD; 182313; -.
DR WormBase; C06E1.3; CE30481; WBGene00015519; doxa-1.
DR eggNOG; KOG3921; Eukaryota.
DR GeneTree; ENSGT00390000008240; -.
DR HOGENOM; CLU_694896_0_0_1; -.
DR InParanoid; P34298; -.
DR OMA; MHAFVIF; -.
DR OrthoDB; 835845at2759; -.
DR PhylomeDB; P34298; -.
DR PRO; PR:P34298; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00015519; Expressed in larva and 3 other tissues.
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:1990204; C:oxidoreductase complex; IDA:ComplexPortal.
DR GO; GO:0005886; C:plasma membrane; IDA:ComplexPortal.
DR GO; GO:0040002; P:collagen and cuticulin-based cuticle development; IDA:ComplexPortal.
DR GO; GO:0015031; P:protein transport; IEA:InterPro.
DR InterPro; IPR018469; Dual_oxidase_maturation_fac.
DR PANTHER; PTHR31158; PTHR31158; 1.
DR Pfam; PF10204; DuoxA; 1.
PE 1: Evidence at protein level;
KW Glycoprotein; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..397
FT /note="Dual oxidase maturation factor 1"
FT /evidence="ECO:0000305"
FT /id="PRO_0000065156"
FT TRANSMEM 26..46
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 57..77
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 191..211
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 218..238
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 261..281
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 324..376
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 341..371
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 109
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 327
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 330
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 397 AA; 43801 MW; 3E6A11E2A8264A56 CRC64;
MWWFGGNPSP SDYPNAAIPN FNMHAFVIFS VFLIPLIAYI LILPGVRRKR VVTTVTYVLM
LAVGGALIAS LIYPCWASGS QMIYTQFRGH SNERILAKIG VEIGLQKVNV TLKFERLLSS
NDVLPGSDMT ELYYNEGFDI SGISSMAEAL HHGLENGLPY PMLSVLEYFS LNQDSFDWGR
HYRVAGHYTH AAIWFAFACW CLSVVLMLFL PHNAYKSILA TGISCLIACL VYLLLSPCEL
RIAFTGENFE RVDLTATFSF CFYLIFAIGI LCVLCGLGLG ICEHWRIYTL STFLDASLDE
HVGPKWKKLP TGGPALQGVQ IGAYGTNTTN SSRDKNDISS DKTAGSSGFQ SRTSTCQSSA
SSASLRSQSS IETVHDEAEL ERTHVHFLQE PCSSSST
