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Protein

Aryl hydrocarbon receptor nuclear translocator

Gene

Arnt

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Required for activity of the Ah (dioxin) receptor. This protein is required for the ligand-binding subunit to translocate from the cytosol to the nucleus after ligand binding. The complex then initiates transcription of genes involved in the activation of PAH procarcinogens. The heterodimer with HIF1A or EPAS1/HIF2A functions as a transcriptional regulator of the adaptive response to hypoxia (By similarity).By similarity

GO - Molecular functioni

  • aryl hydrocarbon receptor activity Source: MGI
  • aryl hydrocarbon receptor binding Source: MGI
  • DNA binding Source: MGI
  • enhancer binding Source: MGI
  • protein heterodimerization activity Source: MGI
  • sequence-specific DNA binding Source: Ensembl
  • transcription coactivator activity Source: MGI
  • transcription factor activity, RNA polymerase II distal enhancer sequence-specific binding Source: Ensembl
  • transcription factor activity, sequence-specific DNA binding Source: MGI
  • transcription factor activity, transcription factor binding Source: MGI
  • transcription factor binding Source: MGI

GO - Biological processi

  • cell differentiation Source: MGI
  • embryonic placenta development Source: MGI
  • intracellular receptor signaling pathway Source: GOC
  • positive regulation of hormone biosynthetic process Source: MGI
  • positive regulation of protein sumoylation Source: BHF-UCL
  • positive regulation of transcription, DNA-templated Source: MGI
  • positive regulation of transcription from RNA polymerase II promoter Source: MGI
  • positive regulation of vascular endothelial growth factor production Source: MGI
  • regulation of transcription from RNA polymerase II promoter in response to oxidative stress Source: MGI
  • response to hypoxia Source: MGI
  • response to toxic substance Source: MGI
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
Aryl hydrocarbon receptor nuclear translocator
Short name:
ARNT protein
Alternative name(s):
Dioxin receptor, nuclear translocator
Hypoxia-inducible factor 1-beta
Short name:
HIF-1-beta
Short name:
HIF1-beta
Gene namesi
Name:Arnt
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 3

Organism-specific databases

MGIiMGI:88071. Arnt.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: MGI
  • nucleus Source: MGI
  • RNA polymerase II transcription factor complex Source: MGI
  • transcription factor complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 791790Aryl hydrocarbon receptor nuclear translocatorPRO_0000127119Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei77 – 771PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP53762.
MaxQBiP53762.
PaxDbiP53762.
PRIDEiP53762.

PTM databases

iPTMnetiP53762.
PhosphoSiteiP53762.

Expressioni

Tissue specificityi

Ubiquitous.

Gene expression databases

BgeeiP53762.
CleanExiMM_ARNT.
ExpressionAtlasiP53762. baseline and differential.
GenevisibleiP53762. MM.

Interactioni

Subunit structurei

Heterodimer with HIF1A (By similarity). Efficient DNA binding requires dimerization with another bHLH protein. Forms a heterodimer with AHR, AHRR, HIF1A and EPAS1/HIF2A as well as with other bHLH proteins. Interacts with NOCA7 and TACC3.By similarity2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Sim1Q610452EBI-78852,EBI-78890

GO - Molecular functioni

Protein-protein interaction databases

BioGridi198205. 3 interactions.
DIPiDIP-280N.
IntActiP53762. 7 interactions.
STRINGi10090.ENSMUSP00000099810.

Structurei

Secondary structure

1
791
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi99 – 11517Combined sources
Helixi117 – 1204Combined sources
Beta strandi122 – 1243Combined sources
Helixi128 – 14114Combined sources
Helixi161 – 17212Combined sources
Beta strandi174 – 1807Combined sources
Turni181 – 1833Combined sources
Beta strandi185 – 1895Combined sources
Helixi193 – 1975Combined sources
Helixi201 – 2044Combined sources
Beta strandi206 – 2083Combined sources
Helixi209 – 2124Combined sources
Helixi215 – 2173Combined sources
Helixi218 – 2247Combined sources
Beta strandi260 – 2689Combined sources
Beta strandi303 – 31412Combined sources
Beta strandi335 – 3428Combined sources
Beta strandi362 – 3676Combined sources
Beta strandi371 – 3766Combined sources
Helixi380 – 3845Combined sources
Helixi388 – 3914Combined sources
Helixi396 – 3994Combined sources
Turni402 – 4043Combined sources
Helixi405 – 41713Combined sources
Turni418 – 4203Combined sources
Beta strandi422 – 4309Combined sources
Beta strandi436 – 44712Combined sources
Turni449 – 4513Combined sources
Beta strandi454 – 46310Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4ZP4X-ray2.35A/C82-464[»]
4ZPHX-ray2.80A/C82-464[»]
4ZPKX-ray3.60A82-464[»]
4ZPRX-ray3.90A82-464[»]
4ZQDX-ray2.87A/C82-464[»]
ProteinModelPortaliP53762.
SMRiP53762. Positions 98-465.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini89 – 14254bHLHPROSITE-ProRule annotationAdd
BLAST
Domaini161 – 23575PAS 1PROSITE-ProRule annotationAdd
BLAST
Domaini349 – 41971PAS 2PROSITE-ProRule annotationAdd
BLAST
Domaini424 – 46744PACAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi99 – 1024Poly-Arg
Compositional biasi503 – 5075Poly-Gln
Compositional biasi740 – 7434Poly-Ser

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.
HOGENOMiHOG000234380.
HOVERGENiHBG000164.
InParanoidiP53762.
KOiK09097.
OMAiIVEFCHP.
OrthoDBiEOG7V1FQ8.
TreeFamiTF319983.

Family and domain databases

Gene3Di4.10.280.10. 1 hit.
InterProiIPR011598. bHLH_dom.
IPR001067. Nuc_translocat.
IPR001610. PAC.
IPR000014. PAS.
IPR013767. PAS_fold.
[Graphical view]
PfamiPF00010. HLH. 1 hit.
PF00989. PAS. 1 hit.
[Graphical view]
PRINTSiPR00785. NCTRNSLOCATR.
SMARTiSM00353. HLH. 1 hit.
SM00086. PAC. 1 hit.
SM00091. PAS. 2 hits.
[Graphical view]
SUPFAMiSSF47459. SSF47459. 1 hit.
SSF55785. SSF55785. 4 hits.
TIGRFAMsiTIGR00229. sensory_box. 1 hit.
PROSITEiPS50888. BHLH. 1 hit.
PS50112. PAS. 2 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform Long (identifier: P53762-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAATTANPEM TSDVPSLGPT IASGNPGPGI QGGGAVVQRA IKRRSGLDFD
60 70 80 90 100
DEVEVNTKFL RCDDDQMCND KERFARSDDE QSSADKERLA RENHSEIERR
110 120 130 140 150
RRNKMTAYIT ELSDMVPTCS ALARKPDKLT ILRMAVSHMK SLRGTGNTST
160 170 180 190 200
DGSYKPSFLT DQELKHLILE AADGFLFIVS CETGRVVYVS DSVTPVLNQP
210 220 230 240 250
QSEWFGSTLY DQVHPDDVDK LREQLSTSEN ALTGRVLDLK TGTVKKEGQQ
260 270 280 290 300
SSMRMCMGSR RSFICRMRCG TSSVDPVSMN RLSFLRNRCR NGLGSVKEGE
310 320 330 340 350
PHFVVVHCTG YIKAWPPAGV SLPDDDPEAG QGSKFCLVAI GRLQVTSSPN
360 370 380 390 400
CTDMSNICQP TEFISRHNIE GIFTFVDHRC VATVGYQPQE LLGKNIVEFC
410 420 430 440 450
HPEDQQLLRD SFQQVVKLKG QVLSVMFRFR SKTREWLWMR TSSFTFQNPY
460 470 480 490 500
SDEIEYIICT NTNVKNSSQE PRPTLSNTIP RSQLGPTANL SLEMGTGQLP
510 520 530 540 550
SRQQQQQHTE LDMVPGRDGL ASYNHSQVSV QPVASAGSEH SKPLEKSEGL
560 570 580 590 600
FAQDRDPRFP EIYPSITADQ SKGISSSTVP ATQQLFSQGS SFPPNPRPAE
610 620 630 640 650
NFRNSGLTPP VTIVQPSSSA GQILAQISRH SNPAQGSAPT WTSSSRPGFA
660 670 680 690 700
AQQVPTQATA KTRSSQFGVN NFQTSSSFSA MSLPGAPTAS SGTAAYPALP
710 720 730 740 750
NRGSNFPPET GQTTGQFQAR TAEGVGVWPQ WQGQQPHHRS SSSEQHVQQT
760 770 780 790
QAQAPSQPEV FQEMLSMLGD QSNTYNNEEF PDLTMFPPFS E
Length:791
Mass (Da):86,963
Last modified:July 27, 2011 - v3
Checksum:iBDEC0991CD57D402
GO
Isoform Short (identifier: P53762-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     77-100: SDDEQSSADKERLARENHSEIERR → TKFL

Show »
Length:771
Mass (Da):84,613
Checksum:i1577F629BAE8F38B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti411 – 4111S → T in AAA61732 (PubMed:7961746).Curated
Sequence conflicti534 – 5341A → R in AAA61732 (PubMed:7961746).Curated
Sequence conflicti644 – 6441S → T in AAA56717 (PubMed:8065341).Curated
Sequence conflicti650 – 6501A → C in AAA61732 (PubMed:7961746).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei77 – 10024SDDEQ…EIERR → TKFL in isoform Short. 1 PublicationVSP_002093Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U10325 mRNA. Translation: AAA56717.1.
U14333 mRNA. Translation: AAA61732.1.
AK153355 mRNA. Translation: BAE31928.1.
CH466620 Genomic DNA. Translation: EDL38816.1.
BC012870 mRNA. Translation: AAH12870.1.
CCDSiCCDS17614.1. [P53762-1]
PIRiA55448.
A56241.
RefSeqiNP_001032826.1. NM_001037737.2. [P53762-1]
UniGeneiMm.250265.

Genome annotation databases

EnsembliENSMUST00000102749; ENSMUSP00000099810; ENSMUSG00000015522. [P53762-1]
GeneIDi11863.
KEGGimmu:11863.
UCSCiuc008qjr.2. mouse. [P53762-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U10325 mRNA. Translation: AAA56717.1.
U14333 mRNA. Translation: AAA61732.1.
AK153355 mRNA. Translation: BAE31928.1.
CH466620 Genomic DNA. Translation: EDL38816.1.
BC012870 mRNA. Translation: AAH12870.1.
CCDSiCCDS17614.1. [P53762-1]
PIRiA55448.
A56241.
RefSeqiNP_001032826.1. NM_001037737.2. [P53762-1]
UniGeneiMm.250265.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4ZP4X-ray2.35A/C82-464[»]
4ZPHX-ray2.80A/C82-464[»]
4ZPKX-ray3.60A82-464[»]
4ZPRX-ray3.90A82-464[»]
4ZQDX-ray2.87A/C82-464[»]
ProteinModelPortaliP53762.
SMRiP53762. Positions 98-465.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi198205. 3 interactions.
DIPiDIP-280N.
IntActiP53762. 7 interactions.
STRINGi10090.ENSMUSP00000099810.

PTM databases

iPTMnetiP53762.
PhosphoSiteiP53762.

Proteomic databases

EPDiP53762.
MaxQBiP53762.
PaxDbiP53762.
PRIDEiP53762.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000102749; ENSMUSP00000099810; ENSMUSG00000015522. [P53762-1]
GeneIDi11863.
KEGGimmu:11863.
UCSCiuc008qjr.2. mouse. [P53762-1]

Organism-specific databases

CTDi405.
MGIiMGI:88071. Arnt.

Phylogenomic databases

eggNOGiENOG410IQ5T. Eukaryota.
ENOG410XVHF. LUCA.
GeneTreeiENSGT00760000118788.
HOGENOMiHOG000234380.
HOVERGENiHBG000164.
InParanoidiP53762.
KOiK09097.
OMAiIVEFCHP.
OrthoDBiEOG7V1FQ8.
TreeFamiTF319983.

Enzyme and pathway databases

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

Miscellaneous databases

ChiTaRSiArnt. mouse.
PROiP53762.
SOURCEiSearch...

Gene expression databases

BgeeiP53762.
CleanExiMM_ARNT.
ExpressionAtlasiP53762. baseline and differential.
GenevisibleiP53762. MM.

Family and domain databases

Gene3Di4.10.280.10. 1 hit.
InterProiIPR011598. bHLH_dom.
IPR001067. Nuc_translocat.
IPR001610. PAC.
IPR000014. PAS.
IPR013767. PAS_fold.
[Graphical view]
PfamiPF00010. HLH. 1 hit.
PF00989. PAS. 1 hit.
[Graphical view]
PRINTSiPR00785. NCTRNSLOCATR.
SMARTiSM00353. HLH. 1 hit.
SM00086. PAC. 1 hit.
SM00091. PAS. 2 hits.
[Graphical view]
SUPFAMiSSF47459. SSF47459. 1 hit.
SSF55785. SSF55785. 4 hits.
TIGRFAMsiTIGR00229. sensory_box. 1 hit.
PROSITEiPS50888. BHLH. 1 hit.
PS50112. PAS. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of functional domains of the aryl hydrocarbon receptor nuclear translocator protein (ARNT)."
    Reisz-Porszasz S., Probst M.R., Fukunaga B.N., Hankinson O.
    Mol. Cell. Biol. 14:6075-6086(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
    Strain: C57BL/6J.
    Tissue: Liver.
  2. "Transcriptional activation function of the mouse Ah receptor nuclear translocator."
    Li H., Dong L., Whitlock J.P. Jr.
    J. Biol. Chem. 269:28098-28105(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT).
    Strain: C57BL/6J.
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  4. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: FVB/N.
    Tissue: Mammary tumor.
  6. "Identification of a novel mechanism of regulation of Ah (dioxin) receptor function."
    Mimura J., Ema M., Sogawa K., Fujii-Kuriyama Y.
    Genes Dev. 13:20-25(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH AHRR.
  7. "Isolation and characterization of AINT: a novel ARNT interacting protein expressed during murine embryonic development."
    Sadek C.M., Jalaguier S., Feeney E.P., Aitola M., Damdimopoulos A.E., Pelto-Huikko M., Gustafsson J.-A.
    Mech. Dev. 97:13-26(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TACC3.
  8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-77, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Spleen.

Entry informationi

Entry nameiARNT_MOUSE
AccessioniPrimary (citable) accession number: P53762
Secondary accession number(s): Q60661, Q921F3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: July 27, 2011
Last modified: June 8, 2016
This is version 150 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.