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Protein

Interleukin-22 receptor subunit alpha-2

Gene

IL22RA2

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

Functioni

Isoform 2 is a receptor for IL22. Binds to IL22, prevents interaction with the functional IL-22R complex and blocks the activity of IL22 (in vitro). May play an important role as an IL22 antagonist in the regulation of inflammatory responses.
Isoform 1 may play a role in establishing and maintaining successful pregnancy.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei99 – 991Critical for IL22-bindingBy similarity
Sitei151 – 1511Critical for IL22-bindingBy similarity

GO - Molecular functioni

  • interleukin-22 binding Source: UniProtKB
  • interleukin-22 receptor activity Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Receptor

Enzyme and pathway databases

ReactomeiR-HSA-8854691. Interleukin-19, 20, 22, 24.
SignaLinkiQ969J5.
SIGNORiQ969J5.

Names & Taxonomyi

Protein namesi
Recommended name:
Interleukin-22 receptor subunit alpha-2
Short name:
IL-22 receptor subunit alpha-2
Short name:
IL-22R-alpha-2
Short name:
IL-22RA2
Alternative name(s):
Cytokine receptor class-II member 10
Cytokine receptor family 2 member 10
Short name:
CRF2-10
Cytokine receptor family type 2, soluble 1
Short name:
CRF2-S1
Interleukin-22-binding protein
Short name:
IL-22BP
Short name:
IL22BP
ZcytoR16
Gene namesi
Name:IL22RA2
ORF Names:UNQ5793/PRO19598/PRO19822
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 6

Organism-specific databases

HGNCiHGNC:14901. IL22RA2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134983729.

Polymorphism and mutation databases

BioMutaiIL22RA2.
DMDMi61213728.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 21211 PublicationAdd
BLAST
Chaini22 – 263242Interleukin-22 receptor subunit alpha-2PRO_0000011016Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi56 – 561N-linked (GlcNAc...)Sequence analysis
Disulfide bondi238 ↔ 2591 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ969J5.
PRIDEiQ969J5.

Expressioni

Tissue specificityi

Expressed in placenta, spleen, breast, skin and lung. Also detected in intestinal tract, testis, brain, heart and thymus. No expression found in prostate, bladder, kidney, ovary, muscle, bone marrow, liver and uterus. Isoform 1 is expressed only in placenta. Isoform 2 is expressed in placenta and breast and at lower level in spleen, skin, thymus and stomach.3 Publications

Gene expression databases

BgeeiQ969J5.
CleanExiHS_IL22RA2.
GenevisibleiQ969J5. HS.

Organism-specific databases

HPAiCAB034906.
HPA030582.

Interactioni

GO - Molecular functioni

  • interleukin-22 binding Source: UniProtKB

Protein-protein interaction databases

BioGridi125503. 2 interactions.
IntActiQ969J5. 3 interactions.
MINTiMINT-7010488.
STRINGi9606.ENSP00000296980.

Structurei

Secondary structure

1
263
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi32 – 398Combined sources
Beta strandi42 – 487Combined sources
Beta strandi59 – 668Combined sources
Beta strandi105 – 1139Combined sources
Beta strandi116 – 1194Combined sources
Helixi122 – 1243Combined sources
Beta strandi131 – 1399Combined sources
Helixi154 – 1574Combined sources
Beta strandi164 – 1663Combined sources
Beta strandi177 – 1793Combined sources
Helixi184 – 1874Combined sources
Helixi195 – 1984Combined sources
Beta strandi202 – 2076Combined sources
Beta strandi216 – 2238Combined sources
Beta strandi239 – 2457Combined sources
Turni246 – 2494Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3G9VX-ray2.76A/C21-263[»]
ProteinModelPortaliQ969J5.
SMRiQ969J5. Positions 26-255.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ969J5.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini26 – 6843Fibronectin type-III 1Add
BLAST
Domaini100 – 16162Fibronectin type-III 2Add
BLAST
Domaini162 – 263102Fibronectin type-III 3Add
BLAST

Sequence similaritiesi

Belongs to the type II cytokine receptor family.Curated
Contains 3 fibronectin type-III domains.Curated

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiENOG410IVX1. Eukaryota.
ENOG410YNE2. LUCA.
GeneTreeiENSGT00530000063352.
HOGENOMiHOG000082681.
HOVERGENiHBG052067.
InParanoidiQ969J5.
KOiK05139.
OMAiPYYGRVR.
OrthoDBiEOG7C2R12.
PhylomeDBiQ969J5.
TreeFamiTF332537.

Family and domain databases

Gene3Di2.60.40.10. 2 hits.
InterProiIPR003961. FN3_dom.
IPR013783. Ig-like_fold.
IPR015373. Interferon/interleukin_rcp_dom.
[Graphical view]
PfamiPF09294. Interfer-bind. 1 hit.
PF01108. Tissue_fac. 1 hit.
[Graphical view]
SUPFAMiSSF49265. SSF49265. 3 hits.

Sequences (3)i

Sequence statusi: Complete.

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

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q969J5-1) [UniParc]FASTAAdd to basket

Also known as: Long, CRF2-10L, CRF2-s1-long

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
MMPKHCFLGF LISFFLTGVA GTQSTHESLK PQRVQFQSRN FHNILQWQPG
60 70 80 90 100
RALTGNSSVY FVQYKIMFSC SMKSSHQKPS GCWQHISCNF PGCRTLAKYG
110 120 130 140 150
QRQWKNKEDC WGTQELSCDL TSETSDIQEP YYGRVRAASA GSYSEWSMTP
160 170 180 190 200
RFTPWWETKI DPPVMNITQV NGSLLVILHA PNLPYRYQKE KNVSIEDYYE
210 220 230 240 250
LLYRVFIINN SLEKEQKVYE GAHRAVEIEA LTPHSSYCVV AEIYQPMLDR
260
RSQRSEERCV EIP
Length:263
Mass (Da):30,550
Last modified:December 1, 2001 - v1
Checksum:iC96ECEC5D78AC79B
GO
Isoform 2 (identifier: Q969J5-2) [UniParc]FASTAAdd to basket

Also known as: Short, CRF2-10, CRF2-s1-short

The sequence of this isoform differs from the canonical sequence as follows:
     67-98: Missing.

Show »
Length:231
Mass (Da):26,980
Checksum:i24A6912BFF75100F
GO
Isoform 3 (identifier: Q969J5-3) [UniParc]FASTAAdd to basket

Also known as: CRF2-10S

The sequence of this isoform differs from the canonical sequence as follows:
     67-98: Missing.
     158-162: TKIDP → RAKGL
     163-263: Missing.

Show »
Length:130
Mass (Da):15,128
Checksum:iA165814C641F5E5B
GO

Sequence cautioni

The sequence AAQ89097.1 differs from that shown. Reason: Erroneous initiation. Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti16 – 161L → P.1 Publication
Corresponds to variant rs28385692 [ dbSNP | Ensembl ].
VAR_021493
Natural varianti190 – 1901E → K.1 Publication
Corresponds to variant rs28362173 [ dbSNP | Ensembl ].
VAR_021494

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei67 – 9832Missing in isoform 2 and isoform 3. 6 PublicationsVSP_013105Add
BLAST
Alternative sequencei158 – 1625TKIDP → RAKGL in isoform 3. 1 PublicationVSP_013106
Alternative sequencei163 – 263101Missing in isoform 3. 1 PublicationVSP_013107Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ313161 mRNA. Translation: CAC85634.1.
AJ313162 mRNA. Translation: CAC85635.1.
AY040566 mRNA. Translation: AAK85714.1.
AY040567 mRNA. Translation: AAK85715.1.
AY040568 mRNA. Translation: AAK85716.1.
AJ297262 mRNA. Translation: CAC83097.1.
AY044429 mRNA. Translation: AAK91775.1.
AY358111 mRNA. Translation: AAQ88478.1.
AY358737 mRNA. Translation: AAQ89097.1. Different initiation.
AY779023 Genomic DNA. Translation: AAV31775.1.
AL050337 Genomic DNA. Translation: CAI21589.1.
AL050337 Genomic DNA. Translation: CAI21591.1.
AL050337 Genomic DNA. Translation: CAI21590.1.
CH471051 Genomic DNA. Translation: EAW47933.1.
BC125167 mRNA. Translation: AAI25168.1.
BC125168 mRNA. Translation: AAI25169.1.
CCDSiCCDS5182.1. [Q969J5-1]
CCDS5183.1. [Q969J5-2]
CCDS5184.1. [Q969J5-3]
RefSeqiNP_443194.1. NM_052962.2. [Q969J5-1]
NP_851826.1. NM_181309.1. [Q969J5-2]
NP_851827.1. NM_181310.1. [Q969J5-3]
UniGeneiHs.126891.

Genome annotation databases

EnsembliENST00000296980; ENSP00000296980; ENSG00000164485. [Q969J5-1]
ENST00000339602; ENSP00000340920; ENSG00000164485. [Q969J5-3]
ENST00000349184; ENSP00000296979; ENSG00000164485. [Q969J5-2]
GeneIDi116379.
KEGGihsa:116379.
UCSCiuc003qhl.4. human. [Q969J5-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

SeattleSNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ313161 mRNA. Translation: CAC85634.1.
AJ313162 mRNA. Translation: CAC85635.1.
AY040566 mRNA. Translation: AAK85714.1.
AY040567 mRNA. Translation: AAK85715.1.
AY040568 mRNA. Translation: AAK85716.1.
AJ297262 mRNA. Translation: CAC83097.1.
AY044429 mRNA. Translation: AAK91775.1.
AY358111 mRNA. Translation: AAQ88478.1.
AY358737 mRNA. Translation: AAQ89097.1. Different initiation.
AY779023 Genomic DNA. Translation: AAV31775.1.
AL050337 Genomic DNA. Translation: CAI21589.1.
AL050337 Genomic DNA. Translation: CAI21591.1.
AL050337 Genomic DNA. Translation: CAI21590.1.
CH471051 Genomic DNA. Translation: EAW47933.1.
BC125167 mRNA. Translation: AAI25168.1.
BC125168 mRNA. Translation: AAI25169.1.
CCDSiCCDS5182.1. [Q969J5-1]
CCDS5183.1. [Q969J5-2]
CCDS5184.1. [Q969J5-3]
RefSeqiNP_443194.1. NM_052962.2. [Q969J5-1]
NP_851826.1. NM_181309.1. [Q969J5-2]
NP_851827.1. NM_181310.1. [Q969J5-3]
UniGeneiHs.126891.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3G9VX-ray2.76A/C21-263[»]
ProteinModelPortaliQ969J5.
SMRiQ969J5. Positions 26-255.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi125503. 2 interactions.
IntActiQ969J5. 3 interactions.
MINTiMINT-7010488.
STRINGi9606.ENSP00000296980.

Polymorphism and mutation databases

BioMutaiIL22RA2.
DMDMi61213728.

Proteomic databases

PaxDbiQ969J5.
PRIDEiQ969J5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000296980; ENSP00000296980; ENSG00000164485. [Q969J5-1]
ENST00000339602; ENSP00000340920; ENSG00000164485. [Q969J5-3]
ENST00000349184; ENSP00000296979; ENSG00000164485. [Q969J5-2]
GeneIDi116379.
KEGGihsa:116379.
UCSCiuc003qhl.4. human. [Q969J5-1]

Organism-specific databases

CTDi116379.
GeneCardsiIL22RA2.
HGNCiHGNC:14901. IL22RA2.
HPAiCAB034906.
HPA030582.
MIMi606648. gene.
neXtProtiNX_Q969J5.
PharmGKBiPA134983729.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IVX1. Eukaryota.
ENOG410YNE2. LUCA.
GeneTreeiENSGT00530000063352.
HOGENOMiHOG000082681.
HOVERGENiHBG052067.
InParanoidiQ969J5.
KOiK05139.
OMAiPYYGRVR.
OrthoDBiEOG7C2R12.
PhylomeDBiQ969J5.
TreeFamiTF332537.

Enzyme and pathway databases

ReactomeiR-HSA-8854691. Interleukin-19, 20, 22, 24.
SignaLinkiQ969J5.
SIGNORiQ969J5.

Miscellaneous databases

ChiTaRSiIL22RA2. human.
EvolutionaryTraceiQ969J5.
GenomeRNAii116379.
PROiQ969J5.
SOURCEiSearch...

Gene expression databases

BgeeiQ969J5.
CleanExiHS_IL22RA2.
GenevisibleiQ969J5. HS.

Family and domain databases

Gene3Di2.60.40.10. 2 hits.
InterProiIPR003961. FN3_dom.
IPR013783. Ig-like_fold.
IPR015373. Interferon/interleukin_rcp_dom.
[Graphical view]
PfamiPF09294. Interfer-bind. 1 hit.
PF01108. Tissue_fac. 1 hit.
[Graphical view]
SUPFAMiSSF49265. SSF49265. 3 hits.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A novel, soluble homologue of the human IL-10 receptor with preferential expression in placenta."
    Gruenberg B.H., Schoenemeyer A., Weiss B., Toschi L., Kunz S., Wolk K., Asadullah K., Sabat R.
    Genes Immun. 2:329-334(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), TISSUE SPECIFICITY.
    Tissue: Mammary gland and Placenta.
  2. "Identification, cloning, and characterization of a novel soluble receptor that binds IL-22 and neutralizes its activity."
    Kotenko S.V., Izotova L.S., Mirochnitchenko O.V., Esterova E., Dickensheets H., Donnelly R.P., Pestka S.
    J. Immunol. 166:7096-7103(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), FUNCTION.
  3. "Cloning and characterization of IL-22 binding protein, a natural antagonist of IL-10-related T cell-derived inducible factor/IL-22."
    Dumoutier L., Lejeune D., Colau D., Renauld J.-C.
    J. Immunol. 166:7090-7095(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION.
    Tissue: Mammary gland.
  4. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, TISSUE SPECIFICITY.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
  6. SeattleSNPs variation discovery resource
    Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS PRO-16 AND LYS-190.
  7. "The DNA sequence and analysis of human chromosome 6."
    Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
    Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  9. "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] (ISOFORM 2).
  10. "Signal peptide prediction based on analysis of experimentally verified cleavage sites."
    Zhang Z., Henzel W.J.
    Protein Sci. 13:2819-2824(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 22-36.
  11. "Cloning of murine IL-22 receptor alpha 2 and comparison with its human counterpart."
    Weiss B., Wolk K., Gruenberg B.H., Volk H.D., Sterry W., Asadullah K., Sabat R.
    Genes Immun. 5:330-336(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  12. "Cloning and characterization of mouse IL-22 binding protein."
    Wei C.-C., Ho T.-W., Liang W.-G., Chen G.-Y., Chang M.-S.
    Genes Immun. 4:204-211(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  13. "Crystal structure of a soluble decoy receptor IL-22BP bound to interleukin-22."
    de Moura P.R., Watanabe L., Bleicher L., Colau D., Dumoutier L., Lemaire M.M., Renauld J.C., Polikarpov I.
    FEBS Lett. 583:1072-1077(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.76 ANGSTROMS) OF 21-231 (ISOFORM 2), DISULFIDE BOND.

Entry informationi

Entry nameiI22R2_HUMAN
AccessioniPrimary (citable) accession number: Q969J5
Secondary accession number(s): Q08AH7
, Q6UWM1, Q96A41, Q96QR0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: December 1, 2001
Last modified: July 6, 2016
This is version 125 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. 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.