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Protein

Aryl hydrocarbon receptor nuclear translocator homolog

Gene

tgo

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Heterodimers of tgo/trh are involved in the control of breathless expression. Plays a role in the cellular or tissue response to oxygen deprivation.4 Publications

GO - Molecular functioni

  • myosin binding Source: FlyBase
  • protein heterodimerization activity Source: FlyBase
  • RNA polymerase II transcription factor activity, sequence-specific DNA binding Source: FlyBase
  • sequence-specific DNA binding Source: FlyBase
  • transcription factor activity, sequence-specific DNA binding Source: FlyBase

GO - Biological processi

  • brain development Source: FlyBase
  • cellular response to hypoxia Source: FlyBase
  • cellular response to insulin stimulus Source: FlyBase
  • central nervous system development Source: FlyBase
  • dendrite morphogenesis Source: FlyBase
  • epithelial cell fate determination, open tracheal system Source: FlyBase
  • glial cell migration Source: FlyBase
  • limb development Source: FlyBase
  • muscle organ development Source: FlyBase
  • negative regulation of transcription from RNA polymerase II promoter Source: FlyBase
  • neuron development Source: FlyBase
  • oogenesis Source: FlyBase
  • open tracheal system development Source: FlyBase
  • peripheral nervous system development Source: FlyBase
  • positive regulation of transcription from RNA polymerase II promoter Source: FlyBase
  • regulation of R7 cell differentiation Source: FlyBase
  • regulation of transcription, DNA-templated Source: FlyBase
  • regulation of transcription from RNA polymerase II promoter Source: FlyBase
  • transcription from RNA polymerase II promoter Source: GOC
Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiR-DME-1234158. Regulation of gene expression by Hypoxia-inducible Factor.
SignaLinkiO15945.

Names & Taxonomyi

Protein namesi
Recommended name:
Aryl hydrocarbon receptor nuclear translocator homolog
Short name:
dARNT
Alternative name(s):
Hypoxia-inducible factor 1-beta
Protein tango
Gene namesi
Name:tgo
Synonyms:ARNT, HIF-1-beta
ORF Names:CG11987
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 3R

Organism-specific databases

FlyBaseiFBgn0264075. tgo.

Subcellular locationi

  • Nucleus PROSITE-ProRule annotation

GO - Cellular componenti

  • cytoplasm Source: InterPro
  • nucleus Source: FlyBase
  • protein complex Source: FlyBase
  • transcription factor complex Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 642642Aryl hydrocarbon receptor nuclear translocator homologPRO_0000127117Add
BLAST

Proteomic databases

PaxDbiO15945.

Expressioni

Tissue specificityi

At stage 11, expression is detected in tracheal pits. At later stages, strong expression is also detected in the CNS.2 Publications

Developmental stagei

Expressed both maternally and zygotically in pupae at a low level.2 Publications

Gene expression databases

BgeeiO15945.
GenevisibleiO15945. DM.

Interactioni

Subunit structurei

Efficient DNA binding requires dimerization with another bHLH protein. Heterodimer with ahr, trh or sim.3 Publications

GO - Molecular functioni

  • myosin binding Source: FlyBase
  • protein heterodimerization activity Source: FlyBase

Protein-protein interaction databases

BioGridi66252. 7 interactions.
IntActiO15945. 3 interactions.
MINTiMINT-875932.
STRINGi7227.FBpp0081483.

Structurei

3D structure databases

ProteinModelPortaliO15945.
SMRiO15945. Positions 10-421.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini13 – 6654bHLHPROSITE-ProRule annotationAdd
BLAST
Domaini85 – 15672PAS 1PROSITE-ProRule annotationAdd
BLAST
Domaini271 – 34171PAS 2PROSITE-ProRule annotationAdd
BLAST
Domaini346 – 38944PACAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi404 – 563160Gln-richAdd
BLAST
Compositional biasi566 – 60439His/Pro-richAdd
BLAST

Sequence similaritiesi

Contains 1 bHLH (basic helix-loop-helix) domain.PROSITE-ProRule annotation
Contains 2 PAS (PER-ARNT-SIM) domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiENOG410IQ5T. Eukaryota.
ENOG410XVHF. LUCA.
GeneTreeiENSGT00760000118788.
InParanoidiO15945.
KOiK09097.
OMAiNGNRQQP.
OrthoDBiEOG7V1FQ8.
PhylomeDBiO15945.

Family and domain databases

Gene3Di4.10.280.10. 1 hit.
InterProiIPR011598. bHLH_dom.
IPR001067. Nuc_translocat.
IPR000014. PAS.
IPR013767. PAS_fold.
[Graphical view]
PfamiPF00010. HLH. 1 hit.
PF00989. PAS. 1 hit.
[Graphical view]
PRINTSiPR00785. NCTRNSLOCATR.
SMARTiSM00353. HLH. 1 hit.
SM00091. PAS. 2 hits.
[Graphical view]
SUPFAMiSSF47459. SSF47459. 1 hit.
SSF55785. SSF55785. 3 hits.
TIGRFAMsiTIGR00229. sensory_box. 1 hit.
PROSITEiPS50888. BHLH. 1 hit.
PS50112. PAS. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O15945-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDEANIQDKE RFASRENHCE IERRRRNKMT AYITELSDMV PTCSALARKP
60 70 80 90 100
DKLTILRMAV AHMKALRGTG NTSSDGTYKP SFLTDQELKH LILEAADGFL
110 120 130 140 150
FVVSCDSGRV IYVSDSVTPV LNYTQSDWYG TSLYEHIHPD DREKIREQLS
160 170 180 190 200
TQESQNAGRI LDLKSGTVKK EGHQSSMRLS MGARRGFICR MRVGNVNPES
210 220 230 240 250
MVSGHLNRLK QRNSLGPSRD GTNYAVVHCT GYIKNWPPTD MFPNMHMERD
260 270 280 290 300
VDDMSSHCCL VAIGRLQVTS TAANDMSGSN NQSEFITRHA MDGKFTFVDQ
310 320 330 340 350
RVLNILGYTP TELLGKICYD FFHPEDQSHM KESFDQVLKQ KGQMFSLLYR
360 370 380 390 400
ARAKNSEYVW LRTQAYAFLN PYTDEVEYIV CTNSSGKTMH GAPLDAAAAH
410 420 430 440 450
TPEQVQQQQQ QEQHVYVQAA PGVDYARREL TPVGSATNDG MYQTHMLAMQ
460 470 480 490 500
APTPQQQQQQ QQRPGSAQTT PVGYTYDTTH SPYSAGGPSP LAKIPKSGTS
510 520 530 540 550
PTPVAPNSWA ALRPQQQQQQ QQPVTEGYQY QQTSPARSPS GPTYTQLSAG
560 570 580 590 600
NGNRQQAQPG AYQAGPPPPP NAPGMWDWQQ AGGHPHPPHP TAHPHHPHAH
610 620 630 640
PGGPAGAGQP QGQEFSDMLQ MLDHTPTTFE DLNINMFSTP FE
Length:642
Mass (Da):71,475
Last modified:March 21, 2012 - v3
Checksum:i0D2EB5D7651C98CC
GO

Sequence cautioni

The sequence AAA28838.1 differs from that shown. Reason: Frameshift at position 607. Curated
The sequence AAB69695.1 differs from that shown. Reason: Frameshift at position 614. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti110 – 1101V → M in BAA22868 (PubMed:9374395).Curated
Sequence conflicti410 – 4101Q → QQQ in AAB69695 (PubMed:9284047).Curated
Sequence conflicti410 – 4101Q → QQQ in AAB88882 (PubMed:9409674).Curated
Sequence conflicti410 – 4101Q → QQQ in AAD38396 (PubMed:10581393).Curated
Sequence conflicti465 – 4651G → R in BAA22868 (PubMed:9374395).Curated
Sequence conflicti488 – 4881P → T in AAB69695 (PubMed:9284047).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB002556 mRNA. Translation: BAA22868.1.
AF016053 mRNA. Translation: AAB69695.1. Frameshift.
AF020426 mRNA. Translation: AAB88882.1.
AF154417 mRNA. Translation: AAD38396.1.
AE014297 Genomic DNA. Translation: AAF54329.1.
AY069581 mRNA. Translation: AAL39726.1.
M14550 Genomic DNA. Translation: AAA28838.1. Frameshift.
RefSeqiNP_001262397.1. NM_001275468.1.
NP_731308.1. NM_169254.2.
UniGeneiDm.3376.

Genome annotation databases

EnsemblMetazoaiFBtr0082005; FBpp0081483; FBgn0264075.
FBtr0336755; FBpp0307731; FBgn0264075.
GeneIDi41084.
KEGGidme:Dmel_CG11987.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB002556 mRNA. Translation: BAA22868.1.
AF016053 mRNA. Translation: AAB69695.1. Frameshift.
AF020426 mRNA. Translation: AAB88882.1.
AF154417 mRNA. Translation: AAD38396.1.
AE014297 Genomic DNA. Translation: AAF54329.1.
AY069581 mRNA. Translation: AAL39726.1.
M14550 Genomic DNA. Translation: AAA28838.1. Frameshift.
RefSeqiNP_001262397.1. NM_001275468.1.
NP_731308.1. NM_169254.2.
UniGeneiDm.3376.

3D structure databases

ProteinModelPortaliO15945.
SMRiO15945. Positions 10-421.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi66252. 7 interactions.
IntActiO15945. 3 interactions.
MINTiMINT-875932.
STRINGi7227.FBpp0081483.

Proteomic databases

PaxDbiO15945.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0082005; FBpp0081483; FBgn0264075.
FBtr0336755; FBpp0307731; FBgn0264075.
GeneIDi41084.
KEGGidme:Dmel_CG11987.

Organism-specific databases

CTDi41084.
FlyBaseiFBgn0264075. tgo.

Phylogenomic databases

eggNOGiENOG410IQ5T. Eukaryota.
ENOG410XVHF. LUCA.
GeneTreeiENSGT00760000118788.
InParanoidiO15945.
KOiK09097.
OMAiNGNRQQP.
OrthoDBiEOG7V1FQ8.
PhylomeDBiO15945.

Enzyme and pathway databases

ReactomeiR-DME-1234158. Regulation of gene expression by Hypoxia-inducible Factor.
SignaLinkiO15945.

Miscellaneous databases

ChiTaRSitgo. fly.
GenomeRNAii41084.
NextBioi822075.
PROiO15945.

Gene expression databases

BgeeiO15945.
GenevisibleiO15945. DM.

Family and domain databases

Gene3Di4.10.280.10. 1 hit.
InterProiIPR011598. bHLH_dom.
IPR001067. Nuc_translocat.
IPR000014. PAS.
IPR013767. PAS_fold.
[Graphical view]
PfamiPF00010. HLH. 1 hit.
PF00989. PAS. 1 hit.
[Graphical view]
PRINTSiPR00785. NCTRNSLOCATR.
SMARTiSM00353. HLH. 1 hit.
SM00091. PAS. 2 hits.
[Graphical view]
SUPFAMiSSF47459. SSF47459. 1 hit.
SSF55785. SSF55785. 3 hits.
TIGRFAMsiTIGR00229. sensory_box. 1 hit.
PROSITEiPS50888. BHLH. 1 hit.
PS50112. PAS. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Transcriptional regulation of breathless FGF receptor gene by binding of TRACHEALESS/dARNT heterodimers to three central midline elements in Drosophila developing trachea."
    Ohshiro T., Saigo K.
    Development 124:3975-3986(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBUNIT.
    Tissue: Embryo.
  2. "The PAS domain confers target gene specificity of Drosophila bHLH/PAS proteins."
    Zelzer E., Wappner P., Shilo B.-Z.
    Genes Dev. 11:2079-2089(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBUNIT, TISSUE SPECIFICITY.
    Tissue: Embryo.
  3. "The Drosophila tango gene encodes a bHLH-PAS protein that is orthologous to mammalian Arnt and controls CNS midline and tracheal development."
    Sonnenfeld M., Ward M., Nystroem G., Mosher J., Stahl S., Crews S.
    Development 124:4571-4582(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBUNIT, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
    Tissue: Embryo.
  4. "Isolation and characterization of the hypoxia-inducible factor 1beta in Drosophila melanogaster."
    Ma E., Haddad G.G.
    Brain Res. Mol. Brain Res. 73:11-16(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DEVELOPMENTAL STAGE.
    Strain: Canton-S.
    Tissue: Embryo, Head and Pupae.
  5. "The genome sequence of Drosophila melanogaster."
    Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
    , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  6. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Embryo.
  8. "Structure of the segmentation gene paired and the Drosophila PRD gene set as part of a gene network."
    Frigerio G., Burri M., Bopp D., Baumgartner S., Noll M.
    Cell 47:735-746(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 586-623.

Entry informationi

Entry nameiARNT_DROME
AccessioniPrimary (citable) accession number: O15945
Secondary accession number(s): O16167
, O44082, Q24461, Q9VHI2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: March 21, 2012
Last modified: May 11, 2016
This is version 157 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.