DOXA1_XENLA
ID DOXA1_XENLA Reviewed; 308 AA.
AC Q6DDK3;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 49.
DE RecName: Full=Dual oxidase maturation factor 1;
DE AltName: Full=Dual oxidase activator 1;
GN Name=duoxa1;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Possible role in maturation and transport from the
CC endoplasmic reticulum to the plasma membrane of functional dual
CC oxidase. {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; BC077555; AAH77555.1; -; mRNA.
DR RefSeq; NP_001086852.1; NM_001093383.1.
DR AlphaFoldDB; Q6DDK3; -.
DR SMR; Q6DDK3; -.
DR DNASU; 446687; -.
DR GeneID; 446687; -.
DR KEGG; xla:446687; -.
DR CTD; 446687; -.
DR Xenbase; XB-GENE-6255655; duoxa1.L.
DR OrthoDB; 835845at2759; -.
DR Proteomes; UP000186698; Chromosome 3L.
DR Bgee; 446687; Expressed in zone of skin and 2 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:0015031; P:protein transport; IEA:UniProtKB-KW.
DR InterPro; IPR018469; Dual_oxidase_maturation_fac.
DR PANTHER; PTHR31158; PTHR31158; 1.
DR Pfam; PF10204; DuoxA; 1.
PE 2: Evidence at transcript level;
KW Glycoprotein; Membrane; Protein transport; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..308
FT /note="Dual oxidase maturation factor 1"
FT /id="PRO_0000264243"
FT TOPO_DOM 1..21
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 22..42
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 43..49
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 50..70
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 71..91
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 92..112
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 113..175
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 176..198
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 199
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 200..220
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 221..247
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 248..268
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 269..308
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT CARBOHYD 290
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 308 AA; 34968 MW; 98EBEAEA115673C9 CRC64;
MQANIFPFYP QPRTPFKFDT KIIEIIIICI VTACTFIIIL PGIRGKSRSI WLLRILTSLF
IGAVILAVNF TSDWEMGTIT ATTVYKSFSH SMLNASIGLW IGLKGLNITL IGNPEYQLNE
TINYNEEFAW ESANQFETSY KDALERGLPF PIVYVAEKFT ISSDCGLFQQ YCISTYYSSG
IMWIAFCSWI LYNVLFSMPV ILYGIYMMFV TAICMLVSLI SFASVRKAPV CNIQFGNSIL
KTHFGVSYWL SLITGLLCLI ISLVLLFLYK TQPKVLQLIF SYGEEEDLSN KSENEEEHSS
VLSLNEIL