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Protein

Eosinophil cationic protein

Gene

RNASE3

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

Functioni

Cytotoxin and helminthotoxin with low-efficiency ribonuclease activity. Possesses a wide variety of biological activities. Exhibits antibacterial activity, including cytoplasmic membrane depolarization of preferentially Gram-negative, but also Gram-positive strains. Promotes E.coli outer membrane detachment, alteration of the overall cell shape and partial loss of cell content.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei42 – 421Proton acceptor
Sitei60 – 601May be involved in LPS-binding
Sitei62 – 621May be involved in LPS- and LTA-binding
Active sitei155 – 1551Proton donor

GO - Molecular functioni

  • endonuclease activity Source: GO_Central
  • nucleic acid binding Source: InterPro
  • ribonuclease activity Source: ProtInc

GO - Biological processi

  • antibacterial humoral response Source: UniProtKB
  • defense response to Gram-positive bacterium Source: UniProtKB
  • innate immune response in mucosa Source: UniProtKB
  • nucleic acid phosphodiester bond hydrolysis Source: GOC
  • RNA catabolic process Source: ProtInc
  • RNA phosphodiester bond hydrolysis Source: GOC
Complete GO annotation...

Keywords - Molecular functioni

Antibiotic, Antimicrobial, Endonuclease, Hydrolase, Nuclease

Names & Taxonomyi

Protein namesi
Recommended name:
Eosinophil cationic protein (EC:3.1.27.-)
Short name:
ECP
Alternative name(s):
Ribonuclease 3
Short name:
RNase 3
Gene namesi
Name:RNASE3
Synonyms:ECP, RNS3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 14

Organism-specific databases

HGNCiHGNC:10046. RNASE3.

Subcellular locationi

  • Secreted

  • Note: Located in the matrix of eosinophil large specific granule, which are released following activation by an immune stimulus.

GO - Cellular componenti

  • extracellular exosome Source: UniProtKB
  • extracellular region Source: ProtInc
  • extracellular space Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi40 – 401I → A: Loss of in vitro formation of amyloid-like aggregates. 1 Publication

Organism-specific databases

PharmGKBiPA34414.

Chemistry

DrugBankiDB01411. Pranlukast.

Polymorphism and mutation databases

BioMutaiRNASE3.
DMDMi147744558.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 27272 PublicationsAdd
BLAST
Chaini28 – 160133Eosinophil cationic proteinPRO_0000030862Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi50 ↔ 110
Modified residuei60 – 601Nitrated tyrosine1 Publication
Disulfide bondi64 ↔ 123
Disulfide bondi82 ↔ 138
Glycosylationi84 – 841N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi89 ↔ 98
Glycosylationi92 – 921N-linked (GlcNAc...)Sequence Analysis
Glycosylationi119 – 1191N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Disulfide bond, Glycoprotein, Nitration

Proteomic databases

PaxDbiP12724.
PRIDEiP12724.

PTM databases

PhosphoSiteiP12724.

Expressioni

Gene expression databases

BgeeiP12724.
CleanExiHS_RNASE3.
GenevisibleiP12724. HS.

Organism-specific databases

HPAiHPA056183.

Interactioni

Subunit structurei

Interacts with bacterial lipopolysaccharide (LPS) and lipoteichoic acid (LTA). In vitro interacts with and insert into lipid bilayers composed of dioleoyl phosphatidylcholine and dioleoyl phosphatidylglycerol. In vitro, tends to form amyloid-like aggregates at pH 3, but not at pH 5, nor 7.1 Publication

Protein-protein interaction databases

BioGridi111966. 1 interaction.
STRINGi9606.ENSP00000302324.

Structurei

Secondary structure

1
160
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi30 – 323Combined sources
Helixi34 – 429Combined sources
Helixi50 – 534Combined sources
Helixi55 – 584Combined sources
Beta strandi61 – 633Combined sources
Beta strandi66 – 738Combined sources
Helixi75 – 817Combined sources
Beta strandi90 – 923Combined sources
Turni93 – 953Combined sources
Beta strandi98 – 1003Combined sources
Beta strandi105 – 1139Combined sources
Beta strandi118 – 1203Combined sources
Beta strandi125 – 1328Combined sources
Beta strandi134 – 1407Combined sources
Turni143 – 1453Combined sources
Beta strandi150 – 15910Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1DYTX-ray1.75A/B28-160[»]
1H1HX-ray2.00A28-160[»]
1QMTX-ray2.40A28-160[»]
2KB5NMR-A28-160[»]
2LVZNMR-A28-160[»]
4A2OX-ray1.69A/B28-160[»]
4A2YX-ray1.70A/B28-160[»]
4OWZX-ray1.47A/B28-160[»]
4OXBX-ray1.50A/B28-160[»]
4OXFX-ray1.50A/B28-160[»]
ProteinModelPortaliP12724.
SMRiP12724. Positions 28-160.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP12724.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni28 – 7245Required for nearly all of the bactericidal activity; partially involved in LPS-binding and bacterial membrane depolarizationAdd
BLAST
Regioni65 – 695Substrate binding

Sequence similaritiesi

Belongs to the pancreatic ribonuclease family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG118739.
GeneTreeiENSGT00390000007840.
HOGENOMiHOG000276882.
HOVERGENiHBG008396.
InParanoidiP12724.
KOiK10787.
OMAiPKCDDAM.
OrthoDBiEOG7KDFCP.
PhylomeDBiP12724.
TreeFamiTF333393.

Family and domain databases

Gene3Di3.10.130.10. 1 hit.
InterProiIPR001427. RNaseA.
IPR023411. RNaseA_AS.
IPR023412. RNaseA_domain.
[Graphical view]
PANTHERiPTHR11437. PTHR11437. 1 hit.
PfamiPF00074. RnaseA. 1 hit.
[Graphical view]
PRINTSiPR00794. RIBONUCLEASE.
ProDomiPD000535. RNaseA. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00092. RNAse_Pc. 1 hit.
[Graphical view]
SUPFAMiSSF54076. SSF54076. 1 hit.
PROSITEiPS00127. RNASE_PANCREATIC. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P12724-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVPKLFTSQI CLLLLLGLMG VEGSLHARPP QFTRAQWFAI QHISLNPPRC
60 70 80 90 100
TIAMRAINNY RWRCKNQNTF LRTTFANVVN VCGNQSIRCP HNRTLNNCHR
110 120 130 140 150
SRFRVPLLHC DLINPGAQNI SNCTYADRPG RRFYVVACDN RDPRDSPRYP
160
VVPVHLDTTI
Length:160
Mass (Da):18,385
Last modified:May 15, 2007 - v2
Checksum:iD7BED24F67B23FA9
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti72 – 721R → C.1 Publication
Corresponds to variant rs151169198 [ dbSNP | Ensembl ].
VAR_014109
Natural varianti124 – 1241T → R.7 Publications
Corresponds to variant rs2073342 [ dbSNP | Ensembl ].
VAR_013149
Natural varianti130 – 1301G → R.
Corresponds to variant rs12147890 [ dbSNP | Ensembl ].
VAR_029017

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X15161 mRNA. Translation: CAA33251.1.
M28128 mRNA. Translation: AAA50283.1.
X16545 Genomic DNA. Translation: CAA34545.1.
X55990 Genomic DNA. Translation: CAA39462.1.
AF294019 Genomic DNA. Translation: AAG31589.1.
AF294020 Genomic DNA. Translation: AAG31590.1.
AF294021 Genomic DNA. Translation: AAG31591.1.
AF294022 Genomic DNA. Translation: AAG31592.1.
AF294023 Genomic DNA. Translation: AAG31593.1.
AF294024 Genomic DNA. Translation: AAG31594.1.
AF294025 Genomic DNA. Translation: AAG31595.1.
AF294026 Genomic DNA. Translation: AAG31596.1.
AL133371 Genomic DNA. No translation available.
BC096060 mRNA. Translation: AAH96060.1.
BC096061 mRNA. Translation: AAH96061.1.
BC096062 mRNA. Translation: AAH96062.1.
AF441204 Genomic DNA. Translation: AAL35279.1.
AF441205 Genomic DNA. Translation: AAL35280.1.
AF441206 Genomic DNA. Translation: AAL35281.1.
CCDSiCCDS9560.1.
PIRiB35328. JL0106.
RefSeqiNP_002926.2. NM_002935.2.
UniGeneiHs.73839.

Genome annotation databases

EnsembliENST00000304639; ENSP00000302324; ENSG00000169397.
GeneIDi6037.
KEGGihsa:6037.
UCSCiuc001vyj.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X15161 mRNA. Translation: CAA33251.1.
M28128 mRNA. Translation: AAA50283.1.
X16545 Genomic DNA. Translation: CAA34545.1.
X55990 Genomic DNA. Translation: CAA39462.1.
AF294019 Genomic DNA. Translation: AAG31589.1.
AF294020 Genomic DNA. Translation: AAG31590.1.
AF294021 Genomic DNA. Translation: AAG31591.1.
AF294022 Genomic DNA. Translation: AAG31592.1.
AF294023 Genomic DNA. Translation: AAG31593.1.
AF294024 Genomic DNA. Translation: AAG31594.1.
AF294025 Genomic DNA. Translation: AAG31595.1.
AF294026 Genomic DNA. Translation: AAG31596.1.
AL133371 Genomic DNA. No translation available.
BC096060 mRNA. Translation: AAH96060.1.
BC096061 mRNA. Translation: AAH96061.1.
BC096062 mRNA. Translation: AAH96062.1.
AF441204 Genomic DNA. Translation: AAL35279.1.
AF441205 Genomic DNA. Translation: AAL35280.1.
AF441206 Genomic DNA. Translation: AAL35281.1.
CCDSiCCDS9560.1.
PIRiB35328. JL0106.
RefSeqiNP_002926.2. NM_002935.2.
UniGeneiHs.73839.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1DYTX-ray1.75A/B28-160[»]
1H1HX-ray2.00A28-160[»]
1QMTX-ray2.40A28-160[»]
2KB5NMR-A28-160[»]
2LVZNMR-A28-160[»]
4A2OX-ray1.69A/B28-160[»]
4A2YX-ray1.70A/B28-160[»]
4OWZX-ray1.47A/B28-160[»]
4OXBX-ray1.50A/B28-160[»]
4OXFX-ray1.50A/B28-160[»]
ProteinModelPortaliP12724.
SMRiP12724. Positions 28-160.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111966. 1 interaction.
STRINGi9606.ENSP00000302324.

Chemistry

DrugBankiDB01411. Pranlukast.

PTM databases

PhosphoSiteiP12724.

Polymorphism and mutation databases

BioMutaiRNASE3.
DMDMi147744558.

Proteomic databases

PaxDbiP12724.
PRIDEiP12724.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000304639; ENSP00000302324; ENSG00000169397.
GeneIDi6037.
KEGGihsa:6037.
UCSCiuc001vyj.3. human.

Organism-specific databases

CTDi6037.
GeneCardsiGC14P021359.
H-InvDBHIX0037784.
HGNCiHGNC:10046. RNASE3.
HPAiHPA056183.
MIMi131398. gene.
neXtProtiNX_P12724.
PharmGKBiPA34414.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG118739.
GeneTreeiENSGT00390000007840.
HOGENOMiHOG000276882.
HOVERGENiHBG008396.
InParanoidiP12724.
KOiK10787.
OMAiPKCDDAM.
OrthoDBiEOG7KDFCP.
PhylomeDBiP12724.
TreeFamiTF333393.

Miscellaneous databases

EvolutionaryTraceiP12724.
GeneWikiiEosinophil_cationic_protein.
GenomeRNAii6037.
NextBioi23529.
PROiP12724.
SOURCEiSearch...

Gene expression databases

BgeeiP12724.
CleanExiHS_RNASE3.
GenevisibleiP12724. HS.

Family and domain databases

Gene3Di3.10.130.10. 1 hit.
InterProiIPR001427. RNaseA.
IPR023411. RNaseA_AS.
IPR023412. RNaseA_domain.
[Graphical view]
PANTHERiPTHR11437. PTHR11437. 1 hit.
PfamiPF00074. RnaseA. 1 hit.
[Graphical view]
PRINTSiPR00794. RIBONUCLEASE.
ProDomiPD000535. RNaseA. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00092. RNAse_Pc. 1 hit.
[Graphical view]
SUPFAMiSSF54076. SSF54076. 1 hit.
PROSITEiPS00127. RNASE_PANCREATIC. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Human eosinophil cationic protein. Molecular cloning of a cytotoxin and helminthotoxin with ribonuclease activity."
    Rosenberg H.F., Ackerman S.J., Tenen D.G.
    J. Exp. Med. 170:163-176(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ARG-124.
    Tissue: Peripheral blood granulocyte.
  2. "Structure and chromosome localization of the human eosinophil-derived neurotoxin and eosinophil cationic protein genes: evidence for intronless coding sequences in the ribonuclease gene superfamily."
    Hamann K.J., Ten R.M., Loegering D.A., Jenkins R.B., Heise M.T., Schad C.R., Pease L.R., Gleich G.J., Barker R.L.
    Genomics 7:535-546(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ARG-124.
    Tissue: Fetal liver.
  3. "Eosinophil cationic protein cDNA. Comparison with other toxic cationic proteins and ribonucleases."
    Barker R.L., Loegering D.A., Ten R.M., Hamann K.J., Pease L.R., Gleich G.J.
    J. Immunol. 143:952-955(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ARG-124.
  4. Simonsen C.C., Kennedy J., Comstock L., Ashton N., McGrogan M.
    Submitted (OCT-1990) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ARG-124.
    Tissue: Colon.
  5. "Sequence variation at two eosinophil-associated ribonuclease loci in humans."
    Zhang J., Rosenberg H.F.
    Genetics 156:1949-1958(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ARG-124.
  6. "The DNA sequence and analysis of human chromosome 14."
    Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H.
    , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.
    Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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], VARIANT ARG-124.
  8. "Identification of polymorphisms in the ECP gene. Relation to disease activity in Hodgkins lymphoma."
    Bystrom J., Molin D., Jonsson U.B., Enblad G., Sundstrom C., Hogbom E., Venge P.
    Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 20-160, VARIANTS CYS-72 AND ARG-124.
  9. "Biochemical and functional similarities between human eosinophil-derived neurotoxin and eosinophil cationic protein: homology with ribonuclease."
    Gleich G.J., Loegering D.A., Bell M.P., Checkel J.L., Ackerman S.J., McKean D.J.
    Proc. Natl. Acad. Sci. U.S.A. 83:3146-3150(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 28-87.
  10. Cited for: PROTEIN SEQUENCE OF 28-47, FUNCTION AS AN ANTIMICROBIAL PROTEIN.
  11. Cited for: NITRATION AT TYR-60.
  12. "Bactericidal and membrane disruption activities of the eosinophil cationic protein are largely retained in an N-terminal fragment."
    Torrent M., de la Torre B.G., Nogues V.M., Andreu D., Boix E.
    Biochem. J. 421:425-434(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH LPS; LTA AND LIPID BILAYERS.
  13. "Eosinophil cationic protein aggregation: identification of an N-terminus amyloid prone region."
    Torrent M., Odorizzi F., Nogues M.V., Boix E.
    Biomacromolecules 11:1983-1990(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: IN VITRO FORMATION OF AMYLOID-LIKE AGGREGATES, MUTAGENESIS OF ILE-40.
  14. "Crystal structure of eosinophil cationic protein at 2.4 A resolution."
    Boix E., Leonidas D.D., Nikolovski Z., Nogues M.V., Cuchillo C.M., Acharya K.R.
    Biochemistry 38:16794-16801(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 28-160.
  15. "Three-dimensional crystal structure of human eosinophil cationic protein (RNase 3) at 1.75 A resolution."
    Mallorqui-Fernandez G., Pous J., Peracaula R., Aymami J., Maeda T., Tada H., Yamada H., Seno M., de Llorens R., Gomis-Rueth F.-X., Coll M.
    J. Mol. Biol. 300:1297-1307(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 28-160.
  16. "The crystal structure of eosinophil cationic protein in complex with 2',5'-ADP at 2.0 A resolution reveals the details of the ribonucleolytic active site."
    Mohan C.G., Boix E., Evans H.R., Nikolovski Z., Nogues M.V., Cuchillo C.M., Acharya K.R.
    Biochemistry 41:12100-12106(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 28-160.

Entry informationi

Entry nameiECP_HUMAN
AccessioniPrimary (citable) accession number: P12724
Secondary accession number(s): Q4VBC1
, Q8WTP7, Q8WZ62, Q9GZN9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: May 15, 2007
Last modified: June 24, 2015
This is version 154 of the entry and version 2 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 14
    Human chromosome 14: 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

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.