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Protein

Interleukin-2 receptor subunit alpha

Gene

IL2RA

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Receptor for interleukin-2.

GO - Molecular functioni

  1. drug binding Source: Ensembl
  2. interleukin-2 binding Source: GO_Central
  3. interleukin-2 receptor activity Source: ProtInc

GO - Biological processi

  1. activation-induced cell death of T cells Source: Ensembl
  2. apoptotic process Source: ProtInc
  3. cell proliferation Source: ProtInc
  4. cell surface receptor signaling pathway Source: ProtInc
  5. immune response Source: ProtInc
  6. inflammatory response Source: GO_Central
  7. inflammatory response to antigenic stimulus Source: Ensembl
  8. negative regulation of defense response to virus Source: Ensembl
  9. negative regulation of immune response Source: Ensembl
  10. negative regulation of inflammatory response Source: Ensembl
  11. negative regulation of T cell proliferation Source: Ensembl
  12. Notch signaling pathway Source: Ensembl
  13. positive regulation of activated T cell proliferation Source: Ensembl
  14. positive regulation of T cell differentiation Source: Ensembl
  15. regulation of T cell homeostatic proliferation Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Receptor

Enzyme and pathway databases

ReactomeiREACT_1695. GPVI-mediated activation cascade.
REACT_19290. G beta:gamma signalling through PI3Kgamma.
REACT_23891. Interleukin receptor SHC signaling.
REACT_27283. Interleukin-2 signaling.

Names & Taxonomyi

Protein namesi
Recommended name:
Interleukin-2 receptor subunit alpha
Short name:
IL-2 receptor subunit alpha
Short name:
IL-2-RA
Short name:
IL-2R subunit alpha
Short name:
IL2-RA
Alternative name(s):
TAC antigen
p55
CD_antigen: CD25
Gene namesi
Name:IL2RA
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 10

Organism-specific databases

HGNCiHGNC:6008. IL2RA.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini22 – 240219ExtracellularSequence AnalysisAdd
BLAST
Transmembranei241 – 25919HelicalSequence AnalysisAdd
BLAST
Topological domaini260 – 27213CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. external side of plasma membrane Source: Ensembl
  2. integral component of membrane Source: UniProtKB-KW
  3. plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Involvement in diseasei

Diabetes mellitus, insulin-dependent, 101 Publication

Disease susceptibility is associated with variations affecting the gene represented in this entry.

Disease descriptionA multifactorial disorder of glucose homeostasis that is characterized by susceptibility to ketoacidosis in the absence of insulin therapy. Clinical features are polydipsia, polyphagia and polyuria which result from hyperglycemia-induced osmotic diuresis and secondary thirst. These derangements result in long-term complications that affect the eyes, kidneys, nerves, and blood vessels.

See also OMIM:601942

Keywords - Diseasei

Diabetes mellitus

Organism-specific databases

MIMi601942. phenotype.
606367. phenotype.
Orphaneti169100. Immunodeficiency due to CD25 deficiency.
85408. Juvenile rheumatoid factor-negative polyarthritis.
85410. Oligoarticular juvenile arthritis.
PharmGKBiPA29828.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2121Add
BLAST
Chaini22 – 272251Interleukin-2 receptor subunit alphaPRO_0000011024Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi24 ↔ 168
Disulfide bondi49 ↔ 80
Disulfide bondi51 ↔ 82
Disulfide bondi67 ↔ 125
Glycosylationi70 – 701N-linked (GlcNAc...)1 Publication
Glycosylationi89 – 891N-linked (GlcNAc...)1 Publication
Disulfide bondi152 ↔ 184
Glycosylationi218 – 2181O-linked (GalNAc...)1 Publication
Glycosylationi224 – 2241O-linked (GalNAc...)1 Publication
Glycosylationi229 – 2291O-linked (GalNAc...)1 Publication
Glycosylationi237 – 2371O-linked (GalNAc...)1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiP01589.
PRIDEiP01589.

PTM databases

PhosphoSiteiP01589.

Expressioni

Gene expression databases

BgeeiP01589.
CleanExiHS_IL2RA.
ExpressionAtlasiP01589. baseline and differential.
GenevestigatoriP01589.

Organism-specific databases

HPAiCAB002419.
HPA054622.

Interactioni

Subunit structurei

Non-covalent dimer of an alpha and a beta subunit. IL2R exists in 3 different forms: a high affinity dimer, an intermediate affinity monomer (beta subunit), and a low affinity monomer (alpha subunit). The high and intermediate affinity forms also associate with a gamma subunit.2 Publications

Protein-protein interaction databases

BioGridi109774. 4 interactions.
DIPiDIP-1080N.
IntActiP01589. 1 interaction.
MINTiMINT-8146732.
STRINGi9606.ENSP00000369293.

Structurei

Secondary structure

1
272
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi34 – 374Combined sources
Beta strandi39 – 413Combined sources
Beta strandi46 – 483Combined sources
Beta strandi55 – 573Combined sources
Beta strandi63 – 675Combined sources
Beta strandi74 – 774Combined sources
Beta strandi82 – 843Combined sources
Beta strandi135 – 1373Combined sources
Beta strandi143 – 1453Combined sources
Beta strandi147 – 1526Combined sources
Beta strandi157 – 1626Combined sources
Beta strandi164 – 1707Combined sources
Beta strandi172 – 1743Combined sources
Beta strandi175 – 1773Combined sources
Beta strandi182 – 1854Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ILMmodel-A23-83[»]
1ILNmodel-A23-83[»]
1Z92X-ray2.80B22-238[»]
2B5IX-ray2.30D22-238[»]
2ERJX-ray3.00A/E22-233[»]
3IU3X-ray2.90I/J/K22-238[»]
3NFPX-ray2.86I/K22-238[»]
ProteinModelPortaliP01589.
SMRiP01589. Positions 22-186.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP01589.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini22 – 8463Sushi 1PROSITE-ProRule annotationAdd
BLAST
Domaini123 – 18664Sushi 2PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 2 Sushi (CCP/SCR) domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal, Sushi, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG47154.
GeneTreeiENSGT00390000018872.
HOGENOMiHOG000113044.
HOVERGENiHBG052109.
InParanoidiP01589.
KOiK05068.
OMAiCQAELCD.
OrthoDBiEOG7S21ZH.
PhylomeDBiP01589.
TreeFamiTF337408.

Family and domain databases

InterProiIPR015486. IL-2_rcpt_alpha.
IPR000436. Sushi_SCR_CCP_dom.
[Graphical view]
PANTHERiPTHR10573. PTHR10573. 1 hit.
PfamiPF00084. Sushi. 2 hits.
[Graphical view]
SMARTiSM00032. CCP. 2 hits.
[Graphical view]
SUPFAMiSSF57535. SSF57535. 2 hits.
PROSITEiPS50923. SUSHI. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P01589-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDSYLLMWGL LTFIMVPGCQ AELCDDDPPE IPHATFKAMA YKEGTMLNCE
60 70 80 90 100
CKRGFRRIKS GSLYMLCTGN SSHSSWDNQC QCTSSATRNT TKQVTPQPEE
110 120 130 140 150
QKERKTTEMQ SPMQPVDQAS LPGHCREPPP WENEATERIY HFVVGQMVYY
160 170 180 190 200
QCVQGYRALH RGPAESVCKM THGKTRWTQP QLICTGEMET SQFPGEEKPQ
210 220 230 240 250
ASPEGRPESE TSCLVTTTDF QIQTEMAATM ETSIFTTEYQ VAVAGCVFLL
260 270
ISVLLLSGLT WQRRQRKSRR TI
Length:272
Mass (Da):30,819
Last modified:July 21, 1986 - v1
Checksum:i83D907C8C81D2C0E
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti272 – 2721I → T.1 Publication
Corresponds to variant rs12722712 [ dbSNP | Ensembl ].
VAR_019280

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X01057 mRNA. Translation: CAA25525.1.
X03131
, X03132, X03133, X03134, X03135, X03136, X03137, X03138 Genomic DNA. Translation: CAA26906.1.
K03122 mRNA. Translation: AAB59535.1. Sequence problems.
M11066
, M10322, M11060, M11061, M11062, M11063, M11064, M11065 Genomic DNA. Translation: AAA67527.1.
AY563103 Genomic DNA. Translation: AAS55572.1.
AL157395, AL137186 Genomic DNA. Translation: CAH73595.1.
AL137186, AL157395 Genomic DNA. Translation: CAI41069.1.
CH471072 Genomic DNA. Translation: EAW86414.1.
M15864 Genomic DNA. Translation: AAA59162.1.
BN000945 Genomic DNA. Translation: CAK26553.1.
CCDSiCCDS7076.1.
PIRiA44186. UHHU2.
RefSeqiNP_000408.1. NM_000417.2.
UniGeneiHs.231367.

Genome annotation databases

EnsembliENST00000379959; ENSP00000369293; ENSG00000134460.
GeneIDi3559.
KEGGihsa:3559.
UCSCiuc001iiz.2. human.

Polymorphism databases

DMDMi124317.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

IL2RAbase

IL2RA mutation db

SeattleSNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X01057 mRNA. Translation: CAA25525.1.
X03131
, X03132, X03133, X03134, X03135, X03136, X03137, X03138 Genomic DNA. Translation: CAA26906.1.
K03122 mRNA. Translation: AAB59535.1. Sequence problems.
M11066
, M10322, M11060, M11061, M11062, M11063, M11064, M11065 Genomic DNA. Translation: AAA67527.1.
AY563103 Genomic DNA. Translation: AAS55572.1.
AL157395, AL137186 Genomic DNA. Translation: CAH73595.1.
AL137186, AL157395 Genomic DNA. Translation: CAI41069.1.
CH471072 Genomic DNA. Translation: EAW86414.1.
M15864 Genomic DNA. Translation: AAA59162.1.
BN000945 Genomic DNA. Translation: CAK26553.1.
CCDSiCCDS7076.1.
PIRiA44186. UHHU2.
RefSeqiNP_000408.1. NM_000417.2.
UniGeneiHs.231367.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ILMmodel-A23-83[»]
1ILNmodel-A23-83[»]
1Z92X-ray2.80B22-238[»]
2B5IX-ray2.30D22-238[»]
2ERJX-ray3.00A/E22-233[»]
3IU3X-ray2.90I/J/K22-238[»]
3NFPX-ray2.86I/K22-238[»]
ProteinModelPortaliP01589.
SMRiP01589. Positions 22-186.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109774. 4 interactions.
DIPiDIP-1080N.
IntActiP01589. 1 interaction.
MINTiMINT-8146732.
STRINGi9606.ENSP00000369293.

Chemistry

BindingDBiP01589.
ChEMBLiCHEMBL2364167.
DrugBankiDB00041. Aldesleukin.
DB00074. Basiliximab.
DB00111. Daclizumab.
DB00004. Denileukin diftitox.
GuidetoPHARMACOLOGYi1695.

PTM databases

PhosphoSiteiP01589.

Polymorphism databases

DMDMi124317.

Proteomic databases

PaxDbiP01589.
PRIDEiP01589.

Protocols and materials databases

DNASUi3559.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000379959; ENSP00000369293; ENSG00000134460.
GeneIDi3559.
KEGGihsa:3559.
UCSCiuc001iiz.2. human.

Organism-specific databases

CTDi3559.
GeneCardsiGC10M006041.
HGNCiHGNC:6008. IL2RA.
HPAiCAB002419.
HPA054622.
MIMi147730. gene.
601942. phenotype.
606367. phenotype.
neXtProtiNX_P01589.
Orphaneti169100. Immunodeficiency due to CD25 deficiency.
85408. Juvenile rheumatoid factor-negative polyarthritis.
85410. Oligoarticular juvenile arthritis.
PharmGKBiPA29828.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG47154.
GeneTreeiENSGT00390000018872.
HOGENOMiHOG000113044.
HOVERGENiHBG052109.
InParanoidiP01589.
KOiK05068.
OMAiCQAELCD.
OrthoDBiEOG7S21ZH.
PhylomeDBiP01589.
TreeFamiTF337408.

Enzyme and pathway databases

ReactomeiREACT_1695. GPVI-mediated activation cascade.
REACT_19290. G beta:gamma signalling through PI3Kgamma.
REACT_23891. Interleukin receptor SHC signaling.
REACT_27283. Interleukin-2 signaling.

Miscellaneous databases

EvolutionaryTraceiP01589.
GeneWikiiIL2RA.
GenomeRNAii3559.
NextBioi13900.
PROiP01589.
SOURCEiSearch...

Gene expression databases

BgeeiP01589.
CleanExiHS_IL2RA.
ExpressionAtlasiP01589. baseline and differential.
GenevestigatoriP01589.

Family and domain databases

InterProiIPR015486. IL-2_rcpt_alpha.
IPR000436. Sushi_SCR_CCP_dom.
[Graphical view]
PANTHERiPTHR10573. PTHR10573. 1 hit.
PfamiPF00084. Sushi. 2 hits.
[Graphical view]
SMARTiSM00032. CCP. 2 hits.
[Graphical view]
SUPFAMiSSF57535. SSF57535. 2 hits.
PROSITEiPS50923. SUSHI. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning of cDNA encoding human interleukin-2 receptor."
    Nikaido T., Shimizu A., Ishida N., Sabe H., Teshigawara K., Maeda M., Uchiyama T., Yodoi J., Honjo T.
    Nature 311:631-635(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "Molecular cloning and structure of the human interleukin 2 receptor gene."
    Ishida N., Kanamori H., Noma T., Nikaido T., Sabe H., Suzuki N., Shimizu A., Honjo T.
    Nucleic Acids Res. 13:7579-7589(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  5. SeattleSNPs variation discovery resource
    Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT THR-272.
  6. "The DNA sequence and comparative analysis of human chromosome 10."
    Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
    , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
    Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "Regulation of the human interleukin-2 receptor alpha chain promoter: activation of a nonfunctional promoter by the transactivator gene of HTLV-I."
    Cross S.L., Feinberg M.B., Wolf J.B., Holbrook N.J., Wong-Stall F., Leonard W.J.
    Cell 49:47-56(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-21.
  9. "Structural analysis of recombinant soluble human interleukin-2 receptor. Primary structure, assignment of disulfide bonds and core IL-2 binding structure."
    Miedel M.C., Hulmes J.D., Weber D.V., Bailon P., Pan Y.C.
    Biochem. Biophys. Res. Commun. 154:372-379(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISULFIDE BONDS, GLYCOSYLATION AT ASN-70; ASN-89; THR-218; THR-224; THR-229 AND THR-237.
  10. "The interleukin-2 and interleukin-4 receptors studied by molecular modelling."
    Bamborough P., Hedgecock C.J., Richards W.G.
    Structure 2:839-851(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: 3D-STRUCTURE MODELING OF 23-83.
  11. "Structure of the quaternary complex of interleukin-2 with its alpha, beta, and gammac receptors."
    Wang X., Rickert M., Garcia K.C.
    Science 310:1159-1163(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 22-238 IN COMPLEX WITH IL2; IL2RB AND IL2RC, DISULFIDE BONDS.
  12. "Crystal structure of the IL-2 signaling complex: paradigm for a heterotrimeric cytokine receptor."
    Stauber D.J., Debler E.W., Horton P.A., Smith K.A., Wilson I.A.
    Proc. Natl. Acad. Sci. U.S.A. 103:2788-2793(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 22-233 IN COMPLEX WITH IL2; IL2RB AND IL2RC, DISULFIDE BONDS.
  13. "Large-scale genetic fine mapping and genotype-phenotype associations implicate polymorphism in the IL2RA region in type 1 diabetes."
    Lowe C.E., Cooper J.D., Brusko T., Walker N.M., Smyth D.J., Bailey R., Bourget K., Plagnol V., Field S., Atkinson M., Clayton D.G., Wicker L.S., Todd J.A.
    Nat. Genet. 39:1074-1082(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN IDDM10.

Entry informationi

Entry nameiIL2RA_HUMAN
AccessioniPrimary (citable) accession number: P01589
Secondary accession number(s): Q5W007
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: March 4, 2015
This is version 167 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human cell differentiation molecules
    CD nomenclature of surface proteins of human leucocytes and list of entries
  2. Human chromosome 10
    Human chromosome 10: entries, gene names and cross-references to MIM
  3. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.