Q1HG44 (DOXA2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Dual oxidase maturation factor 2

Alternative name(s):
Dual oxidase activator 2

Gene names

Name:

DUOXA2

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	320 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Required for the maturation and the transport from the endoplasmic reticulum to the plasma membrane of functional DUOX2. May play a role in thyroid hormone synthesis. Ref.1
Subcellular location	Endoplasmic reticulum membrane; Multi-pass membrane protein Ref.1.
Tissue specificity	Specifically expressed in thyroid. Also detected in salivary glands. Ref.1
Post-translational modification	N-glycosylated. Ref.1
Involvement in disease	Defects in DUOXA2 are the cause of thyroid dyshormonogenesis 5 (TDH5) [MIM:274900]. A disorder due to thyroid dyshormonogenesis, causing hypothyroidism, goiter, and variable mental deficits derived from unrecognized and untreated hypothyroidism. Ref.4
Sequence similarities	Belongs to the DUOXA family.

Ontologies

Keywords
Biological process	Protein transport Transport
Cellular component	Endoplasmic reticulum Membrane
Coding sequence diversity	Polymorphism
Disease	Congenital hypothyroidism
Domain	Transmembrane Transmembrane helix
PTM	Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	protein transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 320	320	Dual oxidase maturation factor 2		PRO_0000264245
Regions
	Topological domain	1 – 21	21	Extracellular Potential
	Transmembrane	22 – 42	21	Helical; Potential
	Topological domain	43 – 56	14	Cytoplasmic Potential
	Transmembrane	57 – 77	21	Helical; Potential
	Topological domain	78 – 183	106	Extracellular Potential
	Transmembrane	184 – 204	21	Helical; Potential
	Topological domain	205 – 206	2	Cytoplasmic Potential
	Transmembrane	207 – 227	21	Helical; Potential
	Topological domain	228 – 247	20	Extracellular Potential
	Transmembrane	248 – 268	21	Helical; Potential
	Topological domain	269 – 320	52	Cytoplasmic Potential
Amino acid modifications
	Glycosylation	84	1	N-linked (GlcNAc...) Potential
	Glycosylation	109	1	N-linked (GlcNAc...) Potential
	Glycosylation	121	1	N-linked (GlcNAc...) Potential
Natural variations
	Natural variant	100	1	R → G. Ref.1 Corresponds to variant rs2576090 [ dbSNP | Ensembl ].		VAR_047367

Sequences

	Sequence		Length	Mass (Da)
	Q1HG44 [UniParc]. Last modified November 25, 2008. Version 2. Checksum: 5B2F58E575A30E72	FASTA	320	34,787
	10 20 30 40 50 60 MTLWNGVLPF YPQPRHAAGF SVPLLIVILV FLALAASFLL ILPGIRGHSR WFWLVRVLLS 70 80 90 100 110 120 LFIGAEIVAV HFSAEWFVGT VNTNTSYKAF SAARVTARVR LLVGLEGINI TLTGTPVHQL 130 140 150 160 170 180 NETIDYNEQF TWRLKENYAA EYANALEKGL PDPVLYLAEK FTPSSPCGLY HQYHLAGHYA 190 200 210 220 230 240 SATLWVAFCF WLLSNVLLST PAPLYGGLAL LTTGAFALFG VFALASISSV PLCPLRLGSS 250 260 270 280 290 300 ALTTQYGAAF WVTLATGVLC LFLGGAVVSL QYVRPSALRT LLDQSAKDCS QERGGSPLIL 310 320 GDPLHKQAAL PDLKCITTNL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification of the maturation factor for dual oxidase. Evolution of an eukaryotic operon equivalent." Grasberger H., Refetoff S. J. Biol. Chem. 281:18269-18272(2006) [PubMed: 16651268] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, GLYCOSYLATION, VARIANT GLY-100. Tissue: Thyroid.
[2]	"Analysis of the DNA sequence and duplication history of human chromosome 15." Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A. , Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C. Nature 440:671-675(2006) [PubMed: 16572171] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]	"Biallelic inactivation of the dual oxidase maturation factor 2 (DUOXA2) gene as a novel cause of congenital hypothyroidism." Zamproni I., Grasberger H., Cortinovis F., Vigone M.C., Chiumello G., Mora S., Onigata K., Fugazzola L., Refetoff S., Persani L., Weber G. J. Clin. Endocrinol. Metab. 93:605-610(2008) [PubMed: 18042646] [Abstract] Cited for: INVOLVEMENT IN TDH5.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	DQ489734 mRNA. Translation: ABF48256.1. AC091117 Genomic DNA. No translation available. BC137465 mRNA. Translation: AAI37466.1.
IPI	IPI00183661.
RefSeq	NP_997464.2. NM_207581.3.
UniGene	Hs.497987.
3D structure databases
ProteinModelPortal	Q1HG44.
ModBase	Search...
Protein-protein interaction databases
STRING	Q1HG44.
Polymorphism databases
DMDM	215274003.
Proteomic databases
PRIDE	Q1HG44.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000323030; ENSP00000319705; ENSG00000140274.
GeneID	405753.
KEGG	hsa:405753.
Organism-specific databases
CTD	405753.
GeneCards	GC15P045406.
HGNC	HGNC:32698. DUOXA2.
MIM	274900. phenotype. 612772. gene.
neXtProt	NX_Q1HG44.
Orphanet	95716. Familial thyroid dyshormonogenesis.
PharmGKB	PA145008523.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG15022.
GeneTree	ENSGT00390000008240.
HOGENOM	HBG402784.
HOVERGEN	HBG080429.
InParanoid	Q1HG44.
OMA	VPLCPLR.
OrthoDB	EOG4DNF56.
PhylomeDB	Q1HG44.
Gene expression databases
ArrayExpress	Q1HG44.
Bgee	Q1HG44.
CleanEx	HS_DUOXA2.
Genevestigator	Q1HG44.
GermOnline	ENSG00000140274. Homo sapiens.
Family and domain databases
InterPro	IPR018469. Dual_oxidase_maturation_fac. [Graphical view]
Pfam	PF10204. DuoxA. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	107951.
SOURCE	Search...

Entry information

Entry name

DOXA2_HUMAN

Accession

Primary (citable) accession number: Q1HG44
Secondary accession number(s): B2RPI9

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 12, 2006
Last sequence update:	November 25, 2008
Last modified:	January 25, 2012
This is version 50 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.