Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Bis(5'-adenosyl)-triphosphatase ENPP4

Gene

ENPP4

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

Functioni

Hydrolyzes extracellular Ap3A into AMP and ADP, and Ap4A into AMP and ATP. Ap3A and Ap4A are diadenosine polyphosphates thought to induce proliferation of vascular smooth muscle cells. Acts as a procoagulant, mediating platelet aggregation at the site of nascent thrombus via release of ADP from Ap3A and activation of ADP receptors.2 Publications

Catalytic activityi

P(1)-P(3)-bis(5'-adenosyl) triphosphate + H2O = ADP + AMP.2 Publications

Cofactori

Zn2+1 PublicationNote: Binds 2 Zn2+ ions per subunit.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi34 – 341Zinc 1; catalytic
Active sitei70 – 701AMP-threonine intermediateBy similarity
Metal bindingi70 – 701Zinc 1; catalytic
Binding sitei91 – 911Substrate
Binding sitei154 – 1541Substrate
Metal bindingi189 – 1891Zinc 2; catalytic
Binding sitei189 – 1891Substrate
Metal bindingi193 – 1931Zinc 2; catalytic
Metal bindingi237 – 2371Zinc 1; catalytic
Metal bindingi238 – 2381Zinc 1; catalytic
Metal bindingi336 – 3361Zinc 2; catalytic

GO - Molecular functioni

  • bis(5'-adenosyl)-triphosphatase activity Source: UniProtKB
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

  • blood coagulation Source: UniProtKB-KW
  • positive regulation of blood coagulation Source: UniProtKB
  • purine ribonucleoside catabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Blood coagulation, Hemostasis

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Bis(5'-adenosyl)-triphosphatase ENPP4 (EC:3.6.1.29)
Alternative name(s):
AP3A hydrolase
Short name:
AP3Aase
Ectonucleotide pyrophosphatase/phosphodiesterase family member 4
Short name:
E-NPP 4
Short name:
NPP-4
Gene namesi
Name:ENPP4
Synonyms:KIAA0879, NPP4
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 6

Organism-specific databases

HGNCiHGNC:3359. ENPP4.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini16 – 407392ExtracellularSequence analysisAdd
BLAST
Transmembranei408 – 42821HelicalSequence analysisAdd
BLAST
Topological domaini429 – 45325CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • extracellular exosome Source: UniProtKB
  • integral component of membrane Source: UniProtKB-KW
  • membrane Source: UniProtKB
  • plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA27794.

Polymorphism and mutation databases

BioMutaiENPP4.
DMDMi172045555.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1515Sequence analysisAdd
BLAST
Chaini16 – 453438Bis(5'-adenosyl)-triphosphatase ENPP4PRO_0000324795Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi155 – 1551N-linked (GlcNAc...)1 Publication
Glycosylationi166 – 1661N-linked (GlcNAc...)1 Publication
Disulfide bondi254 ↔ 2871 Publication
Glycosylationi276 – 2761N-linked (GlcNAc...)Sequence analysis
Glycosylationi386 – 3861N-linked (GlcNAc...)1 Publication
Disulfide bondi394 ↔ 4011 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

EPDiQ9Y6X5.
MaxQBiQ9Y6X5.
PaxDbiQ9Y6X5.
PRIDEiQ9Y6X5.

PTM databases

iPTMnetiQ9Y6X5.
PhosphoSiteiQ9Y6X5.

Expressioni

Tissue specificityi

Expressed on the surface of vascular endothelia.1 Publication

Gene expression databases

BgeeiQ9Y6X5.
CleanExiHS_ENPP4.
GenevisibleiQ9Y6X5. HS.

Organism-specific databases

HPAiHPA016594.

Interactioni

Protein-protein interaction databases

BioGridi116542. 9 interactions.
STRINGi9606.ENSP00000318066.

Structurei

Secondary structure

1
453
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi28 – 336Combined sources
Helixi40 – 434Combined sources
Helixi47 – 548Combined sources
Beta strandi56 – 638Combined sources
Helixi70 – 7910Combined sources
Helixi83 – 864Combined sources
Beta strandi90 – 945Combined sources
Turni96 – 983Combined sources
Beta strandi104 – 1063Combined sources
Helixi110 – 1123Combined sources
Turni113 – 1153Combined sources
Helixi119 – 1246Combined sources
Beta strandi130 – 1356Combined sources
Turni137 – 1404Combined sources
Helixi160 – 17213Combined sources
Beta strandi178 – 1858Combined sources
Helixi189 – 1957Combined sources
Helixi200 – 22324Combined sources
Turni227 – 2293Combined sources
Beta strandi231 – 2355Combined sources
Beta strandi247 – 2504Combined sources
Helixi251 – 2533Combined sources
Helixi257 – 2593Combined sources
Beta strandi260 – 2645Combined sources
Beta strandi266 – 27510Combined sources
Helixi277 – 2848Combined sources
Beta strandi291 – 2955Combined sources
Helixi296 – 2983Combined sources
Helixi301 – 3033Combined sources
Beta strandi313 – 3186Combined sources
Beta strandi323 – 3253Combined sources
Beta strandi333 – 3353Combined sources
Helixi343 – 3453Combined sources
Beta strandi349 – 3535Combined sources
Beta strandi358 – 3669Combined sources
Helixi367 – 3693Combined sources
Helixi370 – 3789Combined sources
Helixi389 – 3957Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4LQYX-ray1.54A16-407[»]
4LR2X-ray1.50A16-407[»]
ProteinModelPortaliQ9Y6X5.
SMRiQ9Y6X5. Positions 24-402.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG2645. Eukaryota.
COG1524. LUCA.
GeneTreeiENSGT00760000119157.
HOGENOMiHOG000231018.
HOVERGENiHBG051485.
KOiK18424.
OMAiCLIIIMQ.
OrthoDBiEOG7W153S.
PhylomeDBiQ9Y6X5.
TreeFamiTF330032.

Family and domain databases

Gene3Di3.40.720.10. 1 hit.
InterProiIPR017849. Alkaline_Pase-like_a/b/a.
IPR017850. Alkaline_phosphatase_core.
IPR024873. E-NPP.
IPR029879. ENPP4.
IPR002591. Phosphodiest/P_Trfase.
[Graphical view]
PANTHERiPTHR10151. PTHR10151. 1 hit.
PTHR10151:SF79. PTHR10151:SF79. 1 hit.
PfamiPF01663. Phosphodiest. 1 hit.
[Graphical view]
SUPFAMiSSF53649. SSF53649. 1 hit.

Sequencei

Sequence statusi: Complete.

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

Q9Y6X5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKLLVILLFS GLITGFRSDS SSSLPPKLLL VSFDGFRADY LKNYEFPHLQ
60 70 80 90 100
NFIKEGVLVE HVKNVFITKT FPNHYSIVTG LYEESHGIVA NSMYDAVTKK
110 120 130 140 150
HFSDSNDKDP FWWNEAVPIW VTNQLQENRS SAAAMWPGTD VPIHDTISSY
160 170 180 190 200
FMNYNSSVSF EERLNNITMW LNNSNPPVTF ATLYWEEPDA SGHKYGPEDK
210 220 230 240 250
ENMSRVLKKI DDLIGDLVQR LKMLGLWENL NVIITSDHGM TQCSQDRLIN
260 270 280 290 300
LDSCIDHSYY TLIDLSPVAA ILPKINRTEV YNKLKNCSPH MNVYLKEDIP
310 320 330 340 350
NRFYYQHNDR IQPIILVADE GWTIVLNESS QKLGDHGYDN SLPSMHPFLA
360 370 380 390 400
AHGPAFHKGY KHSTINIVDI YPMMCHILGL KPHPNNGTFG HTKCLLVDQW
410 420 430 440 450
CINLPEAIAI VIGSLLVLTM LTCLIIIMQN RLSVPRPFSR LQLQEDDDDP

LIG
Length:453
Mass (Da):51,641
Last modified:March 18, 2008 - v3
Checksum:iBC82FA36D9B587C4
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti39 – 391D → G in BAF83965 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti144 – 1441H → Q.1 Publication
Corresponds to variant rs7451713 [ dbSNP | Ensembl ].
VAR_039884
Natural varianti255 – 2551I → V.
Corresponds to variant rs9381429 [ dbSNP | Ensembl ].
VAR_039885
Natural varianti439 – 4391S → A.
Corresponds to variant rs16874289 [ dbSNP | Ensembl ].
VAR_039886

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB020686 mRNA. Translation: BAA74902.2.
AK291276 mRNA. Translation: BAF83965.1.
AL035701 Genomic DNA. Translation: CAB56567.1.
BC018054 mRNA. Translation: AAH18054.1.
CCDSiCCDS34468.1.
PIRiA59389.
RefSeqiNP_055751.1. NM_014936.4.
UniGeneiHs.643497.

Genome annotation databases

EnsembliENST00000321037; ENSP00000318066; ENSG00000001561.
GeneIDi22875.
KEGGihsa:22875.
UCSCiuc003oxy.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB020686 mRNA. Translation: BAA74902.2.
AK291276 mRNA. Translation: BAF83965.1.
AL035701 Genomic DNA. Translation: CAB56567.1.
BC018054 mRNA. Translation: AAH18054.1.
CCDSiCCDS34468.1.
PIRiA59389.
RefSeqiNP_055751.1. NM_014936.4.
UniGeneiHs.643497.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4LQYX-ray1.54A16-407[»]
4LR2X-ray1.50A16-407[»]
ProteinModelPortaliQ9Y6X5.
SMRiQ9Y6X5. Positions 24-402.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116542. 9 interactions.
STRINGi9606.ENSP00000318066.

PTM databases

iPTMnetiQ9Y6X5.
PhosphoSiteiQ9Y6X5.

Polymorphism and mutation databases

BioMutaiENPP4.
DMDMi172045555.

Proteomic databases

EPDiQ9Y6X5.
MaxQBiQ9Y6X5.
PaxDbiQ9Y6X5.
PRIDEiQ9Y6X5.

Protocols and materials databases

DNASUi22875.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000321037; ENSP00000318066; ENSG00000001561.
GeneIDi22875.
KEGGihsa:22875.
UCSCiuc003oxy.4. human.

Organism-specific databases

CTDi22875.
GeneCardsiENPP4.
HGNCiHGNC:3359. ENPP4.
HPAiHPA016594.
neXtProtiNX_Q9Y6X5.
PharmGKBiPA27794.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2645. Eukaryota.
COG1524. LUCA.
GeneTreeiENSGT00760000119157.
HOGENOMiHOG000231018.
HOVERGENiHBG051485.
KOiK18424.
OMAiCLIIIMQ.
OrthoDBiEOG7W153S.
PhylomeDBiQ9Y6X5.
TreeFamiTF330032.

Miscellaneous databases

GenomeRNAii22875.
NextBioi43429.
PROiQ9Y6X5.

Gene expression databases

BgeeiQ9Y6X5.
CleanExiHS_ENPP4.
GenevisibleiQ9Y6X5. HS.

Family and domain databases

Gene3Di3.40.720.10. 1 hit.
InterProiIPR017849. Alkaline_Pase-like_a/b/a.
IPR017850. Alkaline_phosphatase_core.
IPR024873. E-NPP.
IPR029879. ENPP4.
IPR002591. Phosphodiest/P_Trfase.
[Graphical view]
PANTHERiPTHR10151. PTHR10151. 1 hit.
PTHR10151:SF79. PTHR10151:SF79. 1 hit.
PfamiPF01663. Phosphodiest. 1 hit.
[Graphical view]
SUPFAMiSSF53649. SSF53649. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Prediction of the coding sequences of unidentified human genes. XII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
    Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
    DNA Res. 5:355-364(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  2. Ohara O., Nagase T., Kikuno R.
    Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION.
  3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT GLN-144.
  4. "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].
  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].
    Tissue: Brain.
  6. "Structural and catalytic similarities between nucleotide pyrophosphatases/phosphodiesterases and alkaline phosphatases."
    Gijsbers R., Ceulemans H., Stalmans W., Bollen M.
    J. Biol. Chem. 276:1361-1368(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION.
  7. Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  8. "The molecular basis of purinergic signal metabolism by ecto-nucleotide pyrophosphatase/phosphodiesterases 4 and 1 and implications in stroke."
    Albright R.A., Ornstein D.L., Cao W., Chang W.C., Robert D., Tehan M., Hoyer D., Liu L., Stabach P., Yang G., De La Cruz E.M., Braddock D.T.
    J. Biol. Chem. 289:3294-3306(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 16-407 IN COMPLEXES WITH ZINC AND AMP, FUNCTION, CATALYTIC ACTIVITY, DISULFIDE BOND, GLYCOSYLATION AT ASN-155; ASN-166 AND ASN-386, ACTIVE SITE, COFACTOR.

Entry informationi

Entry nameiENPP4_HUMAN
AccessioniPrimary (citable) accession number: Q9Y6X5
Secondary accession number(s): A8K5G1, Q7L2N1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: March 18, 2008
Last modified: March 16, 2016
This is version 105 of the entry and version 3 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 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. 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.